Dieter Soll, PhD
Research & Publications
Biography
News
Research Summary
Our major interests focus on the mechanism and evolution of aminoacyl-tRNA synthesis and the expansion of the genetic code. Currently twenty-two cotranslationally inserted amino acids (including selenocysteine and pyrrolysine) are known to occur in proteins. The synthesis of this set of amino-acyl-tRNAs is very diverse in nature, relying on direct acylation of tRNAs by aminoacyl-tRNA synthetases (as predicted by Crick’s adaptor hypothesis) and also on recently discovered, novel mechanisms of pre-translational tRNA-dependent amino acid modification. The latter process is related to tRNA-dependent amino acid biosynthesis (e.g., asparagine and cysteine), the sole route to these amino acids in many bacteria and archaea. These processes also enable us to synthesize proteins containing unusual amino acid (e.g., phosphoserine and pyrrolysine).
Specialized Terms: Aminoacyl-tRNA Synthesis; Functional Genomics; Life Science Biological; Mechanism of Translation
Extensive Research Description
Research in the Söll laboratory centers around functional genomic investigations that explore the translation of the genetic code with canonical and modified amino acids. We are studying archaeal, bacterial and eukaryotic systems in a multidisciplinary approach that includes genetics, biochemistry, enzymology, structural analysis, and molecular biology.
The ancient essential process of ribosomal protein synthesis requires twenty sets of aminoacyl-tRNAs, one for each canonical amino acid, for the correct transmission of the genetic information. Since Crick proposed his adaptor hypothesis it was commonly accepted that all organisms or organelles possess twenty aminoacyl-tRNA synthetases, each enzyme specific for attaching one amino acid to tRNA. It is now clear that aminoacyl-tRNA formation is far more varied, as the biosynthetic routes to asparaginyl-tRNA, glutaminyl-tRNA, lysyl-tRNA and cysteinyl-tRNA vary greatly in nature. For instance, the amide aminoacyl-tRNAs (Asn-tRNA and Gln-tRNA) can be formed by two redundant mechanisms, direct acylation or pre-translational amino acid modification by amidation. Thus, the routes to these tRNAs differ not only in the three domains of life but also vary among organelles. These transamidation enzymes appear to have evolved by recruitment of amino acid metabolizing enzymes. This possible evolutionary link between protein synthesis and amino acid biosynthesis is further highlighted by the discovery that tRNA-dependent amidation of aspartate appears to be the sole route to asparagine synthesis in most bacteria.
The discovery of a non-canonical lysyl-tRNA synthetase gave the first clues on the aminoacylation of pyrrolysine, the 22nd cotranslationally inserted amino acid. Formation of pyrrolysyl-tRNA in the Methanosarcinaceae is catalyzed by an aminoacyl-tRNA synthetase solely specific for a modified amino acid. An analogous enzyme forms O-phosphoseryl-tRNACys, the required intermediate in Cys-tRNA formation in methanogenic archaea. Based on similar enzymology, O-phosphoseryl-tRNASec is the required precursor for synthesis in archaea and eukaryotes of selenocysteine, the 21st cotranslationally inserted amino acid.
New challenges to our understanding of tRNA biosynthesis and the role of the RNA intron emerge from the finding that the deep-rooted organism Nanoarcheaon equitansmakes functional tRNA from encoded half-genes.
Coauthors
Research Interests
Amino Acyl-tRNA Synthetases; Biochemistry; Genetic Code; Transfer RNA Aminoacylation; Synthetic Biology
Selected Publications
- Rational design of the genetic code expansion toolkit for in vivo encoding of D-amino acidsJiang H, Weng J, Wang Y, Tsou J, Chen P, Ko A, Söll D, Tsai M, Wang Y. Rational design of the genetic code expansion toolkit for in vivo encoding of D-amino acids. Frontiers In Genetics 2023, 14: 1277489. PMID: 37904728, PMCID: PMC10613524, DOI: 10.3389/fgene.2023.1277489.
- Creating Selenocysteine-Specific Reporters Using InteinsChung C, Söll D, Krahn N. Creating Selenocysteine-Specific Reporters Using Inteins. 2023, 2676: 69-86. PMID: 37277625, DOI: 10.1007/978-1-0716-3251-2_5.
- Recoding UAG to selenocysteine in Saccharomyces cerevisiaeHoffman K, Chung C, Mukai T, Krahn N, Jiang H, Balasuriya N, O'Donoghue P, Söll D. Recoding UAG to selenocysteine in Saccharomyces cerevisiae. RNA 2023, 29: 1400-1410. PMID: 37279998, PMCID: PMC10573291, DOI: 10.1261/rna.079658.123.
- Mistranslation of the genetic code by a new family of bacterial transfer RNAsSchuntermann D, Fischer J, Bile J, Gaier S, Shelley B, Awawdeh A, Jahn M, Hoffman K, Westhof E, Söll D, Clarke C, Vargas-Rodriguez O. Mistranslation of the genetic code by a new family of bacterial transfer RNAs. Journal Of Biological Chemistry 2023, 299: 104852. PMID: 37224963, PMCID: PMC10404621, DOI: 10.1016/j.jbc.2023.104852.
- Split aminoacyl-tRNA synthetases for proximity-induced stop codon suppressionJiang H, Ambrose N, Chung C, Wang Y, Söll D, Tharp J. Split aminoacyl-tRNA synthetases for proximity-induced stop codon suppression. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2219758120. PMID: 36787361, PMCID: PMC9974479, DOI: 10.1073/pnas.2219758120.
- Dual incorporation of non-canonical amino acids enables production of post-translationally modified selenoproteinsMorosky P, Comyns C, Nunes L, Chung C, Hoffmann P, Söll D, Vargas-Rodriguez O, Krahn N. Dual incorporation of non-canonical amino acids enables production of post-translationally modified selenoproteins. Frontiers In Molecular Biosciences 2023, 10: 1096261. PMID: 36762212, PMCID: PMC9902344, DOI: 10.3389/fmolb.2023.1096261.
- Harnessing selenocysteine to enhance microbial cell factories for hydrogen productionPatel A, Mulder D, Söll D, Krahn N. Harnessing selenocysteine to enhance microbial cell factories for hydrogen production. Frontiers In Catalysis 2022, 2: 1089176. PMID: 36844461, PMCID: PMC9961374, DOI: 10.3389/fctls.2022.1089176.
- Ancestral archaea expanded the genetic code with pyrrolysineGuo LT, Amikura K, Jiang HK, Mukai T, Fu X, Wang YS, O’Donoghue P, Söll D, Tharp JM. Ancestral archaea expanded the genetic code with pyrrolysine. Journal Of Biological Chemistry 2022, 298: 102521. PMID: 36152750, PMCID: PMC9630628, DOI: 10.1016/j.jbc.2022.102521.
- Unconventional genetic code systems in archaeaMeng K, Chung CZ, Söll D, Krahn N. Unconventional genetic code systems in archaea. Frontiers In Microbiology 2022, 13: 1007832. PMID: 36160229, PMCID: PMC9499178, DOI: 10.3389/fmicb.2022.1007832.
- Diversification of aminoacyl-tRNA synthetase activities via genomic duplicationKrahn N, Söll D, Vargas-Rodriguez O. Diversification of aminoacyl-tRNA synthetase activities via genomic duplication. Frontiers In Physiology 2022, 13: 983245. PMID: 36060688, PMCID: PMC9437257, DOI: 10.3389/fphys.2022.983245.
- Uncovering translation roadblocks during the development of a synthetic tRNAPrabhakar A, Krahn N, Zhang J, Vargas-Rodriguez O, Krupkin M, Fu Z, Acosta-Reyes FJ, Ge X, Choi J, Crnković A, Ehrenberg M, Puglisi EV, Söll D, Puglisi J. Uncovering translation roadblocks during the development of a synthetic tRNA. Nucleic Acids Research 2022, 50: 10201-10211. PMID: 35882385, PMCID: PMC9561287, DOI: 10.1093/nar/gkac576.
- The tRNA discriminator base defines the mutual orthogonality of two distinct pyrrolysyl-tRNA synthetase/tRNAPyl pairs in the same organismZhang H, Gong X, Zhao Q, Mukai T, Vargas-Rodriguez O, Zhang H, Zhang Y, Wassel P, Amikura K, Maupin-Furlow J, Ren Y, Xu X, Wolf YI, Makarova KS, Koonin EV, Shen Y, Söll D, Fu X. The tRNA discriminator base defines the mutual orthogonality of two distinct pyrrolysyl-tRNA synthetase/tRNAPyl pairs in the same organism. Nucleic Acids Research 2022, 50: gkac271-. PMID: 35466371, PMCID: PMC9071458, DOI: 10.1093/nar/gkac271.
- Measuring the tolerance of the genetic code to altered codon sizeDeBenedictis EA, Söll D, Esvelt KM. Measuring the tolerance of the genetic code to altered codon size. ELife 2022, 11: e76941. PMID: 35293861, PMCID: PMC9094753, DOI: 10.7554/elife.76941.
- Directed Evolution of Methanomethylophilus alvus Pyrrolysyl-tRNA Synthetase Generates a Hyperactive and Highly Selective VariantFischer JT, Söll D, Tharp JM. Directed Evolution of Methanomethylophilus alvus Pyrrolysyl-tRNA Synthetase Generates a Hyperactive and Highly Selective Variant. Frontiers In Molecular Biosciences 2022, 9: 850613. PMID: 35372501, PMCID: PMC8965510, DOI: 10.3389/fmolb.2022.850613.
- Khorana, Har GobindSöll D, RajBhandary U. Khorana, Har Gobind. 2022 DOI: 10.1016/b978-0-12-822563-9.00089-5.
- Front Cover: Hijacking Translation Initiation for Synthetic Biology (ChemBioChem 10/2020)Tharp J, Krahn N, Varshney U, Söll D. Front Cover: Hijacking Translation Initiation for Synthetic Biology (ChemBioChem 10/2020). ChemBioChem 2020, 21: 1383-1383. DOI: 10.1002/cbic.202000239.
- Initiation of Protein Synthesis with Non‐Canonical Amino Acids In VivoTharp J, Ad O, Amikura K, Ward F, Garcia E, Cate J, Schepartz A, Söll D. Initiation of Protein Synthesis with Non‐Canonical Amino Acids In Vivo. Angewandte Chemie 2020, 132: 3146-3150. DOI: 10.1002/ange.201914671.
- Translation of Diverse Aramid- and 1,3-Dicarbonyl-peptides by Wild Type Ribosomes in VitroAd O, Hoffman KS, Cairns AG, Featherston AL, Miller SJ, Söll D, Schepartz A. Translation of Diverse Aramid- and 1,3-Dicarbonyl-peptides by Wild Type Ribosomes in Vitro. ACS Central Science 2019, 5: 1289-1294. PMID: 31403077, PMCID: PMC6661870, DOI: 10.1021/acscentsci.9b00460.
- Transfer RNA function and evolutionO’Donoghue P, Ling J, Söll D. Transfer RNA function and evolution. RNA Biology 2018, 15: 423-426. PMID: 30099966, PMCID: PMC6103721, DOI: 10.1080/15476286.2018.1478942.
- Overcoming Challenges in Engineering the Genetic CodeLajoie M, Söll D, Church G. Overcoming Challenges in Engineering the Genetic Code. Journal Of Molecular Biology 2015, 428: 1004-1021. PMID: 26348789, PMCID: PMC4779434, DOI: 10.1016/j.jmb.2015.09.003.
- Innentitelbild: Chemische Evolution eines bakteriellen Proteoms (Angew. Chem. 34/2015)Hoesl M, Oehm S, Durkin P, Darmon E, Peil L, Aerni H, Rappsilber J, Rinehart J, Leach D, Söll D, Budisa N. Innentitelbild: Chemische Evolution eines bakteriellen Proteoms (Angew. Chem. 34/2015). Angewandte Chemie 2015, 127: 9862-9862. DOI: 10.1002/ange.201506522.
- Inside Cover: Chemical Evolution of a Bacterial Proteome (Angew. Chem. Int. Ed. 34/2015)Hoesl M, Oehm S, Durkin P, Darmon E, Peil L, Aerni H, Rappsilber J, Rinehart J, Leach D, Söll D, Budisa N. Inside Cover: Chemical Evolution of a Bacterial Proteome (Angew. Chem. Int. Ed. 34/2015). Angewandte Chemie International Edition 2015, 54: 9726-9726. DOI: 10.1002/anie.201506522.
- Chemische Evolution eines bakteriellen ProteomsHoesl M, Oehm S, Durkin P, Darmon E, Peil L, Aerni H, Rappsilber J, Rinehart J, Leach D, Söll D, Budisa N. Chemische Evolution eines bakteriellen Proteoms. Angewandte Chemie 2015, 127: 10168-10172. DOI: 10.1002/ange.201502868.
- Exploring the Substrate Range of Wild‐Type Aminoacyl‐tRNA SynthetasesFan C, Ho JM, Chirathivat N, Söll D, Wang Y. Exploring the Substrate Range of Wild‐Type Aminoacyl‐tRNA Synthetases. ChemBioChem 2014, 15: 1805-1809. PMID: 24890918, PMCID: PMC4133344, DOI: 10.1002/cbic.201402083.
- Cover Picture: Recoding the Genetic Code with Selenocysteine (Angew. Chem. Int. Ed. 1/2014)Bröcker M, Ho J, Church G, Söll D, O'Donoghue P. Cover Picture: Recoding the Genetic Code with Selenocysteine (Angew. Chem. Int. Ed. 1/2014). Angewandte Chemie International Edition 2013, 53: 1-1. DOI: 10.1002/anie.201310509.
- Titelbild: Umkodierung des genetischen Codes mit Selenocystein (Angew. Chem. 1/2014)Bröcker M, Ho J, Church G, Söll D, O'Donoghue P. Titelbild: Umkodierung des genetischen Codes mit Selenocystein (Angew. Chem. 1/2014). Angewandte Chemie 2013, 126: 1-1. DOI: 10.1002/ange.201310509.
- Umkodierung des genetischen Codes mit SelenocysteinBröcker M, Ho J, Church G, Söll D, O'Donoghue P. Umkodierung des genetischen Codes mit Selenocystein. Angewandte Chemie 2013, 126: 325-330. DOI: 10.1002/ange.201308584.
- Aminoacylation of tRNA 2′‐ or 3′‐hydroxyl by phosphoseryl‐ and pyrrolysyl‐tRNA synthetasesEnglert M, Moses S, Hohn M, Ling J, O‧Donoghue P, Söll D. Aminoacylation of tRNA 2′‐ or 3′‐hydroxyl by phosphoseryl‐ and pyrrolysyl‐tRNA synthetases. FEBS Letters 2013, 587: 3360-3364. PMID: 24021645, PMCID: PMC3830498, DOI: 10.1016/j.febslet.2013.08.037.
- Titelbild: A Facile Strategy for Selective Incorporation of Phosphoserine into Histones (Angew. Chem. 22/2013)Lee S, Oh S, Yang A, Kim J, Söll D, Lee D, Park H. Titelbild: A Facile Strategy for Selective Incorporation of Phosphoserine into Histones (Angew. Chem. 22/2013). Angewandte Chemie 2013, 125: 5761-5761. DOI: 10.1002/ange.201303269.
- Cover Picture: A Facile Strategy for Selective Incorporation of Phosphoserine into Histones (Angew. Chem. Int. Ed. 22/2013)Lee S, Oh S, Yang A, Kim J, Söll D, Lee D, Park H. Cover Picture: A Facile Strategy for Selective Incorporation of Phosphoserine into Histones (Angew. Chem. Int. Ed. 22/2013). Angewandte Chemie International Edition 2013, 52: 5651-5651. DOI: 10.1002/anie.201303269.
- A Facile Strategy for Selective Incorporation of Phosphoserine into HistonesLee S, Oh S, Yang A, Kim J, Söll D, Lee D, Park H. A Facile Strategy for Selective Incorporation of Phosphoserine into Histones. Angewandte Chemie International Edition 2013, 52: 5771-5775. PMID: 23533151, PMCID: PMC3775851, DOI: 10.1002/anie.201300531.
- A Facile Strategy for Selective Incorporation of Phosphoserine into HistonesLee S, Oh S, Yang A, Kim J, Söll D, Lee D, Park H. A Facile Strategy for Selective Incorporation of Phosphoserine into Histones. Angewandte Chemie 2013, 125: 5883-5887. DOI: 10.1002/ange.201300531.
- UGA is an additional glycine codon in uncultured SR1 bacteria from the human microbiotaCampbell JH, O’Donoghue P, Campbell AG, Schwientek P, Sczyrba A, Woyke T, Söll D, Podar M. UGA is an additional glycine codon in uncultured SR1 bacteria from the human microbiota. Proceedings Of The National Academy Of Sciences Of The United States Of America 2013, 110: 5540-5545. PMID: 23509275, PMCID: PMC3619370, DOI: 10.1073/pnas.1303090110.
- Back Cover: Rewiring Translation for Elongation Factor Tu‐Dependent Selenocysteine Incorporation (Angew. Chem. Int. Ed. 5/2013)Aldag C, Bröcker M, Hohn M, Prat L, Hammond G, Plummer A, Söll D. Back Cover: Rewiring Translation for Elongation Factor Tu‐Dependent Selenocysteine Incorporation (Angew. Chem. Int. Ed. 5/2013). Angewandte Chemie International Edition 2013, 52: 1596-1596. DOI: 10.1002/anie.201300063.
- Rücktitelbild: Rewiring Translation for Elongation Factor Tu‐Dependent Selenocysteine Incorporation (Angew. Chem. 5/2013)Aldag C, Bröcker M, Hohn M, Prat L, Hammond G, Plummer A, Söll D. Rücktitelbild: Rewiring Translation for Elongation Factor Tu‐Dependent Selenocysteine Incorporation (Angew. Chem. 5/2013). Angewandte Chemie 2013, 125: 1638-1638. DOI: 10.1002/ange.201300063.
- Aminoacyl-tRNA SynthetasesLing J, Söll D. Aminoacyl-tRNA Synthetases. 2013, 57-61. DOI: 10.1007/978-3-642-16712-6_457.
- The genetic code: Yesterday, today, and tomorrowLing J, Söll D. The genetic code: Yesterday, today, and tomorrow. Resonance 2012, 17: 1136-1142. DOI: 10.1007/s12045-012-0130-8.
- Rewiring Translation for Elongation Factor Tu‐Dependent Selenocysteine IncorporationAldag C, Bröcker M, Hohn M, Prat L, Hammond G, Plummer A, Söll D. Rewiring Translation for Elongation Factor Tu‐Dependent Selenocysteine Incorporation. Angewandte Chemie 2012, 125: 1481-1485. DOI: 10.1002/ange.201207567.
- The Mechanism of Pre-transfer Editing in Yeast Mitochondrial Threonyl-tRNA Synthetase*Ling J, Peterson KM, Simonović I, Söll D, Simonović M. The Mechanism of Pre-transfer Editing in Yeast Mitochondrial Threonyl-tRNA Synthetase*. Journal Of Biological Chemistry 2012, 287: 28518-28525. PMID: 22773845, PMCID: PMC3436575, DOI: 10.1074/jbc.m112.372920.
- Yeast mitochondrial threonyl-tRNA synthetase recognizes tRNA isoacceptors by distinct mechanisms and promotes CUN codon reassignmentLing J, Peterson KM, Simonović I, Cho C, Söll D, Simonović M. Yeast mitochondrial threonyl-tRNA synthetase recognizes tRNA isoacceptors by distinct mechanisms and promotes CUN codon reassignment. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: 3281-3286. PMID: 22343532, PMCID: PMC3295322, DOI: 10.1073/pnas.1200109109.
- Rational design of an evolutionary precursor of glutaminyl-tRNA synthetaseO’Donoghue P, Sheppard K, Nureki O, Söll D. Rational design of an evolutionary precursor of glutaminyl-tRNA synthetase. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 20485-20490. PMID: 22158897, PMCID: PMC3251134, DOI: 10.1073/pnas.1117294108.
- tRNA import into mitochondria: many organisms but not so many mechanismsAlfonzo J, Randau L, Söll D. tRNA import into mitochondria: many organisms but not so many mechanisms. The FASEB Journal 2011, 25: 311.3-311.3. DOI: 10.1096/fasebj.25.1_supplement.311.3.
- An unusual tRNAThr derived from tRNAHis reassigns in yeast mitochondria the CUN codons to threonineSu D, Lieberman A, Lang BF, Simonović M, Söll D, Ling J. An unusual tRNAThr derived from tRNAHis reassigns in yeast mitochondria the CUN codons to threonine. Nucleic Acids Research 2011, 39: 4866-4874. PMID: 21321019, PMCID: PMC3113583, DOI: 10.1093/nar/gkr073.
- Mutations Disrupting Selenocysteine Formation Cause Progressive Cerebello-Cerebral AtrophyAgamy O, Zeev B, Lev D, Marcus B, Fine D, Su D, Narkis G, Ofir R, Hoffmann C, Leshinsky-Silver E, Flusser H, Sivan S, Söll D, Lerman-Sagie T, Birk OS. Mutations Disrupting Selenocysteine Formation Cause Progressive Cerebello-Cerebral Atrophy. American Journal Of Human Genetics 2010, 87: 538-544. PMID: 20920667, PMCID: PMC2948803, DOI: 10.1016/j.ajhg.2010.09.007.
- Structure of an archaeal non-discriminating glutamyl-tRNA synthetase: a missing link in the evolution of Gln-tRNAGln formationNureki O, O’Donoghue P, Watanabe N, Ohmori A, Oshikane H, Araiso Y, Sheppard K, Söll D, Ishitani R. Structure of an archaeal non-discriminating glutamyl-tRNA synthetase: a missing link in the evolution of Gln-tRNAGln formation. Nucleic Acids Research 2010, 38: 7286-7297. PMID: 20601684, PMCID: PMC2978374, DOI: 10.1093/nar/gkq605.
- 1SE1020 Genetic code extension and establishment by aminoacyl-tRNA synthetase and tRNA modification enzymes(1SE Recent Advances in Structural Analyses of Funcitonal Mechanisms Based on Dynamics of Biological Reactions,The 48th Annual Meeting of the Biophysical Society of Japan)Nakanishi K, Bonnefond L, Nozawa K, Soll D, Suzuki T, Ishitani R, Nureki O. 1SE1020 Genetic code extension and establishment by aminoacyl-tRNA synthetase and tRNA modification enzymes(1SE Recent Advances in Structural Analyses of Funcitonal Mechanisms Based on Dynamics of Biological Reactions,The 48th Annual Meeting of the Biophysical Society of Japan). Seibutsu Butsuri 2010, 50: s3. DOI: 10.2142/biophys.50.s3_5.
- The Human SepSecS-tRNASec Complex Reveals the Mechanism of Selenocysteine FormationPalioura S, Sherrer RL, Steitz TA, Söll D, Simonović M. The Human SepSecS-tRNASec Complex Reveals the Mechanism of Selenocysteine Formation. Science 2009, 325: 321-325. PMID: 19608919, PMCID: PMC2857584, DOI: 10.1126/science.1173755.
- A Cytidine Deaminase Edits C to U in Transfer RNAs in ArchaeaRandau L, Stanley BJ, Kohlway A, Mechta S, Xiong Y, Söll D. A Cytidine Deaminase Edits C to U in Transfer RNAs in Archaea. Science 2009, 324: 657-659. PMID: 19407206, PMCID: PMC2857566, DOI: 10.1126/science.1170123.
- 1SP7-03 tRNA recognition and molecular evolution of GatCAB(1SP7 Elucidation of Protein Functions at the Atomic Level with X-ray structural, Vibrational spectroscopic, Molecular biological and Theoretical analyses,The 47th Annual Meeting of the Biophysical Society of Japan)Nakamura A, Sheppard K, Yamane J, Yao M, Soll D, Tanaka I. 1SP7-03 tRNA recognition and molecular evolution of GatCAB(1SP7 Elucidation of Protein Functions at the Atomic Level with X-ray structural, Vibrational spectroscopic, Molecular biological and Theoretical analyses,The 47th Annual Meeting of the Biophysical Society of Japan). Seibutsu Butsuri 2009, 49: s9. DOI: 10.2142/biophys.49.s9_1.
- Pyrrolysyl-tRNA synthetase–tRNAPyl structure reveals the molecular basis of orthogonalityNozawa K, O’Donoghue P, Gundllapalli S, Araiso Y, Ishitani R, Umehara T, Söll D, Nureki O. Pyrrolysyl-tRNA synthetase–tRNAPyl structure reveals the molecular basis of orthogonality. Nature 2008, 457: 1163-1167. PMID: 19118381, PMCID: PMC2648862, DOI: 10.1038/nature07611.
- Quality control despite mistranslation caused by an ambiguous genetic codeRuan B, Palioura S, Sabina J, Marvin-Guy L, Kochhar S, LaRossa RA, Söll D. Quality control despite mistranslation caused by an ambiguous genetic code. Proceedings Of The National Academy Of Sciences Of The United States Of America 2008, 105: 16502-16507. PMID: 18946032, PMCID: PMC2575449, DOI: 10.1073/pnas.0809179105.
- Response by Lennart Randau & Dieter SöllRandau L, Söll D. Response by Lennart Randau & Dieter Söll. EMBO Reports 2008, 9: 820-821. PMCID: PMC2529357, DOI: 10.1038/embor.2008.154.
- Stop codon recoding mechanism revealed by the suppressor tRNAPyl/PylS complex structureNureki O, Nozawa K, Araiso Y, Soll D, Ishitani R. Stop codon recoding mechanism revealed by the suppressor tRNAPyl/PylS complex structure. Acta Crystallographica Section A: Foundations And Advances 2008, 64: c25-c26. DOI: 10.1107/s0108767308099224.
- Mammalian mitochondria have the innate ability to import tRNAs by a mechanism distinct from protein importRubio MA, Rinehart JJ, Krett B, Duvezin-Caubet S, Reichert AS, Söll D, Alfonzo JD. Mammalian mitochondria have the innate ability to import tRNAs by a mechanism distinct from protein import. Proceedings Of The National Academy Of Sciences Of The United States Of America 2008, 105: 9186-9191. PMID: 18587046, PMCID: PMC2453747, DOI: 10.1073/pnas.0804283105.
- Life without RNase PRandau L, Schröder I, Söll D. Life without RNase P. Nature 2008, 453: 120-123. PMID: 18451863, DOI: 10.1038/nature06833.
- Characterization and evolutionary history of an archaeal kinase involved in selenocysteinyl-tRNA formationSherrer RL, O’Donoghue P, Söll D. Characterization and evolutionary history of an archaeal kinase involved in selenocysteinyl-tRNA formation. Nucleic Acids Research 2008, 36: 1247-1259. PMID: 18174226, PMCID: PMC2275090, DOI: 10.1093/nar/gkm1134.
- 1P-049 Structural analyses for RNA-dependent eukaryal and archaeal selenocysteine formation(The 46th Annual Meeting of the Biophysical Society of Japan)Araiso Y, Ishitani R, Sherrer L, Soll D, Nureki O. 1P-049 Structural analyses for RNA-dependent eukaryal and archaeal selenocysteine formation(The 46th Annual Meeting of the Biophysical Society of Japan). Seibutsu Butsuri 2008, 48: s28. DOI: 10.2142/biophys.48.s28_4.
- 1P-036 X-ray crystallographic analysis of pyrrolysyl-tRNA synthetase from the eubacteria(The 46th Annual Meeting of the Biophysical Society of Japan)Nozawa K, O'Donoghue P, Araiso Y, Gundllapalli S, Ishitani R, Soll D, Nureki O. 1P-036 X-ray crystallographic analysis of pyrrolysyl-tRNA synthetase from the eubacteria(The 46th Annual Meeting of the Biophysical Society of Japan). Seibutsu Butsuri 2008, 48: s26. DOI: 10.2142/biophys.48.s26_3.
- Features of Aminoacyl‐tRNA Synthesis Unique to ArchaeaPolycarpo C, Sheppard K, Randau L, Ambrogelly A, Cardoso A, Fukai S, Herring S, Hohn M, Nakamura Y, Oshikane H, Palioura S, Salazar J, Yuan J, Nureki O, Söll D. Features of Aminoacyl‐tRNA Synthesis Unique to Archaea. 2007, 198-208. DOI: 10.1128/9781555815516.ch9.
- 3P019 Structural insights into RNA-dependent eukaryal and archaeal selenocysteine formation(Proteins-structure and structure-function relationship,Poster Presentations)Araiso Y, Pailouer S, Ishitani R, Oshikane H, Domae N, Soll D, Nureki O. 3P019 Structural insights into RNA-dependent eukaryal and archaeal selenocysteine formation(Proteins-structure and structure-function relationship,Poster Presentations). Seibutsu Butsuri 2007, 47: s207. DOI: 10.2142/biophys.47.s207_4.
- Aminoacyl‐tRNAs: Deciphering and Defining the Genetic MessageAmbrogelly A, Salazar J, Sheppard K, Polycarpo C, Oshikane H, Nakamura Y, Fukai S, Nureki O, Söll D. Aminoacyl‐tRNAs: Deciphering and Defining the Genetic Message. 2006, 207-215. DOI: 10.1002/9780470750865.ch18.
- Structure of the unusual seryl‐tRNA synthetase reveals a distinct zinc‐dependent mode of substrate recognitionBilokapic S, Maier T, Ahel D, Gruic‐Sovulj I, Söll D, Weygand‐Durasevic I, Ban N. Structure of the unusual seryl‐tRNA synthetase reveals a distinct zinc‐dependent mode of substrate recognition. The EMBO Journal 2006, 25: 2498-2509. PMID: 16675947, PMCID: PMC1478180, DOI: 10.1038/sj.emboj.7601129.
- Saccharomyces cerevisiae imports the cytosolic pathway for Gln‐tRNA synthesis into the mitochondrionKrett B, Rinehart J, Rubio M, Alfonzo J, Söll D. Saccharomyces cerevisiae imports the cytosolic pathway for Gln‐tRNA synthesis into the mitochondrion. The FASEB Journal 2006, 20: a500-a500. DOI: 10.1096/fasebj.20.4.a500-b.
- Recognition in vitro of the suppressor tRNAPyl by the class II‐like Pyrrolsyl‐tRNA SynthetaseHerring S, Li D, Ambrogelly A, Polycarpo C, Soll D. Recognition in vitro of the suppressor tRNAPyl by the class II‐like Pyrrolsyl‐tRNA Synthetase. The FASEB Journal 2006, 20: a503-a503. DOI: 10.1096/fasebj.20.4.a503-b.
- A Molecular Tunnel Required for Cooperation of an Asparaginase and a Glu‐tRNAGln Kinase in Gln‐tRNA FormationSheppard K, Feng L, Oshikane H, Nakamura Y, Fukai S, Nureki O, Söll D. A Molecular Tunnel Required for Cooperation of an Asparaginase and a Glu‐tRNAGln Kinase in Gln‐tRNA Formation. The FASEB Journal 2006, 20: a503-a503. DOI: 10.1096/fasebj.20.4.a503-a.
- RNA‐Dependent Cysteine Biosynthesis in ArchaeaYuan J, Sauerwald A, Zhu W, Major T, Roy H, Palioura S, Jahn D, Whitman W, Yates J, Ibba M, Söll D. RNA‐Dependent Cysteine Biosynthesis in Archaea. The FASEB Journal 2006, 20: a503-a504. DOI: 10.1096/fasebj.20.4.a503-d.
- Mischarging of M. barkeri tRNAPyl with alanine and serine in vitroLi D, Polycarpo C, Ambrogelly A, Söll D. Mischarging of M. barkeri tRNAPyl with alanine and serine in vitro. The FASEB Journal 2006, 20: a503-a503. DOI: 10.1096/fasebj.20.4.a503-c.
- 2P168 Structural Basis of RNA-Dependent Recruitment of Glutamine to the Genetic Code(35. RNA world,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)Oshikane H, Sheppard K, Nakamura Y, Fukai S, Feng L, Numata T, Ishitani R, Soll D, Nureki O. 2P168 Structural Basis of RNA-Dependent Recruitment of Glutamine to the Genetic Code(35. RNA world,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006). Seibutsu Butsuri 2006, 46: s337. DOI: 10.2142/biophys.46.s337_4.
- RNA-Dependent Cysteine Biosynthesis in ArchaeaSauerwald A, Zhu W, Major TA, Roy H, Palioura S, Jahn D, Whitman WB, Yates JR, Ibba M, Söll D. RNA-Dependent Cysteine Biosynthesis in Archaea. Science 2005, 307: 1969-1972. PMID: 15790858, DOI: 10.1126/science.1108329.
- Complete Genome Sequence of the Genetically Tractable Hydrogenotrophic Methanogen Methanococcus maripaludis†Hendrickson E, Kaul R, Zhou Y, Bovee D, Chapman P, Chung J, de Macario E, Dodsworth J, Gillett W, Graham D, Hackett M, Haydock A, Kang A, Land M, Levy R, Lie T, Major T, Moore B, Porat I, Palmeiri A, Rouse G, Saenphimmachak C, Söll D, Van Dien S, Wang T, Whitman W, Xia Q, Zhang Y, Larimer F, Olson M, Leigh J. Complete Genome Sequence of the Genetically Tractable Hydrogenotrophic Methanogen Methanococcus maripaludis†. Journal Of Bacteriology 2004, 186: 6956-6969. PMID: 15466049, PMCID: PMC522202, DOI: 10.1128/jb.186.20.6956-6969.2004.
- Cys-tRNACys formation and cysteine biosynthesis in methanogenic archaea: two faces of the same problem?Ambrogelly A, Kamtekar S, Sauerwald A, Ruan B, Tumbula-Hansen D, Kennedy D, Ahel I, Söll D. Cys-tRNACys formation and cysteine biosynthesis in methanogenic archaea: two faces of the same problem? Cellular And Molecular Life Sciences 2004, 61: 2437-2445. PMID: 15526152, DOI: 10.1007/s00018-004-4194-9.
- The unusual methanogenic seryl‐tRNA synthetase recognizes tRNASer species from all three kingdoms of lifeBilokapic S, Korencic D, Söll D, Weygand‐Durasevic I. The unusual methanogenic seryl‐tRNA synthetase recognizes tRNASer species from all three kingdoms of life. The FEBS Journal 2004, 271: 694-702. PMID: 14764085, DOI: 10.1111/j.1432-1033.2003.03971.x.
- Non-canonical Eukaryotic Glutaminyl- and Glutamyl-tRNA Synthetases Form Mitochondrial Aminoacyl-tRNA in Trypanosoma brucei *Rinehart J, Horn EK, Wei D, Söll D, Schneider A. Non-canonical Eukaryotic Glutaminyl- and Glutamyl-tRNA Synthetases Form Mitochondrial Aminoacyl-tRNA in Trypanosoma brucei *. Journal Of Biological Chemistry 2003, 279: 1161-1166. PMID: 14563839, DOI: 10.1074/jbc.m310100200.
- tRNA‐dependent amino acid discrimination by yeast seryl‐tRNA synthetaseGruic‐Sovulj I, Landeka I, Söll D, Weygand‐Durasevic I. tRNA‐dependent amino acid discrimination by yeast seryl‐tRNA synthetase. The FEBS Journal 2002, 269: 5271-5279. PMID: 12392560, DOI: 10.1046/j.1432-1033.2002.03241.x.
- A one‐step method for in vitro production of tRNA transcriptsKorenčić D, Söll D, Ambrogelly A. A one‐step method for in vitro production of tRNA transcripts. Nucleic Acids Research 2002, 30: e105-e105. PMID: 12384607, PMCID: PMC137149, DOI: 10.1093/nar/gnf104.
- Divergent regulation of the HEMA gene family encoding glutamyl-tRNA reductase in Arabidopsis thaliana: expression of HEMA2 is regulated by sugars, but is independent of light and plastid signallingUjwal ML, McCormac AC, Goulding A, Madan Kumar A, Söll D, Terry MJ. Divergent regulation of the HEMA gene family encoding glutamyl-tRNA reductase in Arabidopsis thaliana: expression of HEMA2 is regulated by sugars, but is independent of light and plastid signalling. Plant Molecular Biology 2002, 50: 81-89. PMID: 12139011, DOI: 10.1023/a:1016081114758.
- Cysteinyl-tRNA synthetase is not essential for viability of the archaeon Methanococcus maripaludisStathopoulos C, Kim W, Li T, Anderson I, Deutsch B, Palioura S, Whitman W, Söll D. Cysteinyl-tRNA synthetase is not essential for viability of the archaeon Methanococcus maripaludis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 14292-14297. PMID: 11717392, PMCID: PMC64675, DOI: 10.1073/pnas.201540498.
- Post-transcriptional modification in archaeal tRNAs: identities and phylogenetic relations of nucleotides from mesophilic and hyperthermophilic MethanococcalesMcCloskey J, Graham D, Zhou S, Crain P, Ibba M, Konisky J, Söll D, Olsen G. Post-transcriptional modification in archaeal tRNAs: identities and phylogenetic relations of nucleotides from mesophilic and hyperthermophilic Methanococcales. Nucleic Acids Research 2001, 29: 4699-4706. PMID: 11713320, PMCID: PMC92529, DOI: 10.1093/nar/29.22.4699.
- A Single Amidotransferase Forms Asparaginyl-tRNA and Glutaminyl-tRNA in Chlamydia trachomatis *Raczniak G, Becker H, Min B, Söll D. A Single Amidotransferase Forms Asparaginyl-tRNA and Glutaminyl-tRNA in Chlamydia trachomatis *. Journal Of Biological Chemistry 2001, 276: 45862-45867. PMID: 11585842, DOI: 10.1074/jbc.m109494200.
- A dual‐specific Glu‐tRNAGln and Asp‐tRNAAsn amidotransferase is involved in decoding glutamine and asparagine codons in Acidithiobacillus ferrooxidansSalazar J, Zúñiga R, Raczniak G, Becker H, Söll D, Orellana O. A dual‐specific Glu‐tRNAGln and Asp‐tRNAAsn amidotransferase is involved in decoding glutamine and asparagine codons in Acidithiobacillus ferrooxidans. FEBS Letters 2001, 500: 129-131. PMID: 11445070, DOI: 10.1016/s0014-5793(01)02600-x.
- Protein synthesis: Twenty three amino acids and countingIbba M, Stathopoulos C, Söll D. Protein synthesis: Twenty three amino acids and counting. Current Biology 2001, 11: r563-r565. PMID: 11509255, DOI: 10.1016/s0960-9822(01)00344-x.
- Genomics and the evolution of aminoacyl-tRNA synthesis.Ruan B, Ahel I, Ambrogelly A, Becker H, Bunjun S, Feng L, Tumbula-Hansen D, Ibba M, Korencic D, Kobayashi H, Jacquin-Becker C, Mejlhede N, Min B, Raczniak G, Rinehart J, Stathopoulos C, Li T, Söll D. Genomics and the evolution of aminoacyl-tRNA synthesis. Acta Biochimica Polonica 2001, 48: 313-21. PMID: 11732603, DOI: 10.18388/abp.2001_3917.
- The renaissance of aminoacyl‐tRNA synthesisIbba M, Söll D. The renaissance of aminoacyl‐tRNA synthesis. EMBO Reports 2001, 2: 382-387. PMID: 11375928, PMCID: PMC1083889, DOI: 10.1093/embo-reports/kve095.
- Conserved amino acids near the carboxy terminus of bacterial tyrosyl‐tRNA synthetase are involved in tRNA and Tyr‐AMP bindingSalazar J, Zuñiga R, Lefimil C, Söll D, Orellana O. Conserved amino acids near the carboxy terminus of bacterial tyrosyl‐tRNA synthetase are involved in tRNA and Tyr‐AMP binding. FEBS Letters 2001, 491: 257-260. PMID: 11240138, DOI: 10.1016/s0014-5793(01)02214-1.
- Genomics-based identification of targets in pathogenic bacteria for potential therapeutic and diagnostic useRaczniak G, Ibba M, Söll D. Genomics-based identification of targets in pathogenic bacteria for potential therapeutic and diagnostic use. Toxicology 2001, 160: 181-189. PMID: 11246138, DOI: 10.1016/s0300-483x(00)00454-6.
- Regulation of HEMA1 expression by phytochrome and a plastid signal during de‐etiolation in Arabidopsis thalianaMcCormac A, Fischer A, Kumar A, Söll D, Terry M. Regulation of HEMA1 expression by phytochrome and a plastid signal during de‐etiolation in Arabidopsis thaliana. The Plant Journal 2001, 25: 549-561. PMID: 11309145, DOI: 10.1046/j.1365-313x.2001.00986.x.
- Protein phosphatase 2A: identification in Oryza sativa of the gene encoding the regulatory A subunitYu S, Lei H, Chang W, Söll D, Hong G. Protein phosphatase 2A: identification in Oryza sativa of the gene encoding the regulatory A subunit. Plant Molecular Biology 2001, 45: 107-112. PMID: 11247601, DOI: 10.1023/a:1006472722500.
- Methanococcus jannaschii Prolyl-Cysteinyl-tRNA Synthetase Possesses Overlapping Amino Acid Binding Sites †Stathopoulos C, Jacquin-Becker C, Becker H, Li T, Ambrogelly A, Longman R, Söll D. Methanococcus jannaschii Prolyl-Cysteinyl-tRNA Synthetase Possesses Overlapping Amino Acid Binding Sites †. Biochemistry 2000, 40: 46-52. PMID: 11141055, DOI: 10.1021/bi002108x.
- A Mutant Escherichia coli Tyrosyl-tRNA Synthetase Utilizes the Unnatural Amino Acid Azatyrosine More Efficiently than Tyrosine*Hamano-Takaku F, Iwama T, Saito-Yano S, Takaku K, Monden Y, Kitabatake M, Söll D, Nishimura S. A Mutant Escherichia coli Tyrosyl-tRNA Synthetase Utilizes the Unnatural Amino Acid Azatyrosine More Efficiently than Tyrosine*. Journal Of Biological Chemistry 2000, 275: 40324-40328. PMID: 11006270, DOI: 10.1074/jbc.m003696200.
- A dual-specificity aminoacyl-tRNA synthetase in the deep-rooted eukaryote Giardia lambliaBunjun S, Stathopoulos C, Graham D, Min B, Kitabatake M, Wang A, Wang C, Vivarès C, Weiss L, Söll D. A dual-specificity aminoacyl-tRNA synthetase in the deep-rooted eukaryote Giardia lamblia. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 12997-13002. PMID: 11078517, PMCID: PMC27167, DOI: 10.1073/pnas.230444397.
- Ancient Adaptation of the Active Site of Tryptophanyl-tRNA Synthetase for Tryptophan Binding †Ibba M, Stange-Thomann N, Kitabatake M, Ali K, Söll I, Carter, C, Michael Ibba, and, Söll D. Ancient Adaptation of the Active Site of Tryptophanyl-tRNA Synthetase for Tryptophan Binding †. Biochemistry 2000, 39: 13136-13143. PMID: 11052665, DOI: 10.1021/bi001512t.
- Domain-specific recruitment of amide amino acids for protein synthesisTumbula D, Becker H, Chang W, Söll D. Domain-specific recruitment of amide amino acids for protein synthesis. Nature 2000, 407: 106-110. PMID: 10993083, DOI: 10.1038/35024120.
- Author CorrectionIbba M, Becker H, Stathopoulos C, Tumbula D, Soll D. Author Correction. Trends In Biochemical Sciences 2000, 25: 380. PMID: 10916157, DOI: 10.1016/s0968-0004(00)01648-0.
- The heterotrimeric Thermus thermophilus Asp‐tRNAAsn amidotransferase can also generate Gln‐tRNAGlnBecker H, Min B, Jacobi C, Raczniak G, Pelaschier J, Roy H, Klein S, Kern D, Söll D. The heterotrimeric Thermus thermophilus Asp‐tRNAAsn amidotransferase can also generate Gln‐tRNAGln. FEBS Letters 2000, 476: 140-144. PMID: 10913601, DOI: 10.1016/s0014-5793(00)01697-5.
- The Adaptor hypothesis revisitedIbba M, Becker H, Stathopoulos C, Tumbula D, Söll D, Ibba M, Becker H, Stathopoulos C, Tumbula D, Söll D. The Adaptor hypothesis revisited. Trends In Biochemical Sciences 2000, 25: 311-316. PMID: 10871880, DOI: 10.1016/s0968-0004(00)01600-5.
- AMINOACYL-tRNA SYNTHESISIbba M, Söll D. AMINOACYL-tRNA SYNTHESIS. Annual Review Of Biochemistry 2000, 69: 617-650. PMID: 10966471, DOI: 10.1146/annurev.biochem.69.1.617.
- Aminoacyl-tRNA Synthetases, the Genetic Code, and the Evolutionary ProcessWoese C, Olsen G, Ibba M, Söll D. Aminoacyl-tRNA Synthetases, the Genetic Code, and the Evolutionary Process. Microbiology And Molecular Biology Reviews 2000, 64: 202-236. PMID: 10704480, PMCID: PMC98992, DOI: 10.1128/mmbr.64.1.202-236.2000.
- Transfer RNA Identity Change in Anticodon Variants of E. coli tRNAPhe in VivoKim H, Kim I, Söll D, Lee Y. Transfer RNA Identity Change in Anticodon Variants of E. coli tRNAPhe in Vivo. Molecules And Cells 2000, 10: 76-82. PMID: 10774751, DOI: 10.1007/s10059-000-0076-7.
- One Polypeptide with Two Aminoacyl-tRNA Synthetase ActivitiesStathopoulos C, Li T, Longman R, Vothknecht U, Becker H, Ibba M, Söll D. One Polypeptide with Two Aminoacyl-tRNA Synthetase Activities. Science 2000, 287: 479-482. PMID: 10642548, DOI: 10.1126/science.287.5452.479.
- Cysteine Biosynthesis Pathway in the ArchaeonMethanosarcina barkeri Encoded by Acquired Bacterial Genes?Kitabatake M, So M, Tumbula D, Söll D. Cysteine Biosynthesis Pathway in the ArchaeonMethanosarcina barkeri Encoded by Acquired Bacterial Genes? Journal Of Bacteriology 2000, 182: 143-145. PMID: 10613873, PMCID: PMC94250, DOI: 10.1128/jb.182.1.143-145.2000.
- Antisense HEMA1 RNA Expression Inhibits Heme and Chlorophyll Biosynthesis in ArabidopsisKumar A, Söll D. Antisense HEMA1 RNA Expression Inhibits Heme and Chlorophyll Biosynthesis in Arabidopsis. Plant Physiology 2000, 122: 49-56. PMID: 10631248, PMCID: PMC58843, DOI: 10.1104/pp.122.1.49.
- Mutations in a new Arabidopsis cyclophilin disrupt its interaction with protein phosphatase 2AJackson K, Söll D. Mutations in a new Arabidopsis cyclophilin disrupt its interaction with protein phosphatase 2A. Molecular Genetics And Genomics 1999, 262: 830-838. PMID: 10628867, DOI: 10.1007/s004380051147.
- Cysteinyl‐tRNA formation: the last puzzle of aminoacyl‐tRNA synthesisLi T, Graham D, Stathopoulos C, Haney P, Kim H, Vothknecht U, Kitabatake M, Hong K, Eggertsson G, Curnow A, Lin W, Celic I, Whitman W, Söll D. Cysteinyl‐tRNA formation: the last puzzle of aminoacyl‐tRNA synthesis. FEBS Letters 1999, 462: 302-306. PMID: 10622715, DOI: 10.1016/s0014-5793(99)01550-1.
- The RCN1‐encoded A subunit of protein phosphatase 2A increases phosphatase activity in vivoDeruère J, Jackson K, Garbers C, Söll D, DeLong A. The RCN1‐encoded A subunit of protein phosphatase 2A increases phosphatase activity in vivo. The Plant Journal 1999, 20: 389-399. PMID: 10607292, DOI: 10.1046/j.1365-313x.1999.00607.x.
- Transfer RNA identity contributes to transition state stabilization during aminoacyl-tRNA synthesisIbba M, Sever S, Praetorius-Ibba M, Söll D. Transfer RNA identity contributes to transition state stabilization during aminoacyl-tRNA synthesis. Nucleic Acids Research 1999, 27: 3631-3637. PMID: 10471730, PMCID: PMC148616, DOI: 10.1093/nar/27.18.3631.
- Archaeal aminoacyl-tRNA synthesis: diversity replaces dogma.Tumbula D, Vothknecht U, Kim H, Ibba M, Min B, Li T, Pelaschier J, Stathopoulos C, Becker H, Söll D. Archaeal aminoacyl-tRNA synthesis: diversity replaces dogma. Genetics 1999, 152: 1269-76. PMID: 10430557, PMCID: PMC1460689, DOI: 10.1093/genetics/152.4.1269.
- Selective inhibition of HEMA gene expression by photooxidation in Arabidopsis thalianaKumar M, Chaturvedi S, Söll D. Selective inhibition of HEMA gene expression by photooxidation in Arabidopsis thaliana. Phytochemistry 1999, 51: 847-851. PMID: 10423858, DOI: 10.1016/s0031-9422(99)00114-4.
- Archaeal aminoacyl-tRNA synthesis: unique determinants of a universal genetic code?Ibba M, Curnow A, Bono J, Rosa P, Woese C, Söll D. Archaeal aminoacyl-tRNA synthesis: unique determinants of a universal genetic code? Biological Bulletin 1999, 196: 335-6; discussion 336-7. PMID: 10390832, DOI: 10.2307/1542964.
- Substrate recognition by class I lysyl-tRNA synthetases: A molecular basis for gene displacementIbba M, Losey H, Kawarabayasi Y, Kikuchi H, Bunjun S, Söll D. Substrate recognition by class I lysyl-tRNA synthetases: A molecular basis for gene displacement. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 418-423. PMID: 9892648, PMCID: PMC15151, DOI: 10.1073/pnas.96.2.418.
- Recognition of One tRNA by Two Classes of Aminoacyl-tRNA SynthetaseIbba M, Bunjun S, Losey H, Min B, Söll D. Recognition of One tRNA by Two Classes of Aminoacyl-tRNA Synthetase. 1999, 143-148. DOI: 10.1007/978-94-011-4485-8_11.
- 6.01 OverviewMoore P, Nishimura S, Söll D. 6.01 Overview. 1999, 1-2. DOI: 10.1016/b978-0-08-091283-7.00201-0.
- Sequence divergence of seryl-tRNA synthetases in archaea.Kim H, Vothknecht U, Hedderich R, Celic I, Söll D. Sequence divergence of seryl-tRNA synthetases in archaea. Journal Of Bacteriology 1998, 180: 6446-9. PMID: 9851985, PMCID: PMC107743, DOI: 10.1128/jb.180.24.6446-6449.1998.
- Root-Growth Behavior of the Arabidopsis Mutantrgr1 Roles of Gravitropism and Circumnutation in the Waving/Coiling PhenomenonMullen J, Turk E, Johnson K, Wolverton C, Ishikawa H, Simmons C, Söll D, Evans M. Root-Growth Behavior of the Arabidopsis Mutantrgr1 Roles of Gravitropism and Circumnutation in the Waving/Coiling Phenomenon. Plant Physiology 1998, 118: 1139-1145. PMID: 9847088, PMCID: PMC34730, DOI: 10.1104/pp.118.4.1139.
- C‐terminal truncation of yeast SerRS is toxic for Saccharomyces cerevisiae due to altered mechanism of substrate recognitionLenhard B, Prætorius-Ibba M, Filipic S, Söll D, Weygand-Durasevic I. C‐terminal truncation of yeast SerRS is toxic for Saccharomyces cerevisiae due to altered mechanism of substrate recognition. FEBS Letters 1998, 439: 235-240. PMID: 9845329, DOI: 10.1016/s0014-5793(98)01376-3.
- Glutamyl-tRNAGln amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesisCurnow A, Tumbula D, Pelaschier J, Min B, Söll D. Glutamyl-tRNAGln amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 12838-12843. PMID: 9789001, PMCID: PMC23620, DOI: 10.1073/pnas.95.22.12838.
- Maize mitochondrial seryl-tRNA synthetase recognizes Escherichia coli tRNASer in vivo and in vitroRokov J, Söll D, Weygand-Durašević I. Maize mitochondrial seryl-tRNA synthetase recognizes Escherichia coli tRNASer in vivo and in vitro. Plant Molecular Biology 1998, 38: 497-502. PMID: 9747857, DOI: 10.1023/a:1006088516228.
- Retracing the evolution of amino acid specificity in glutaminyl‐tRNA synthetaseHong K, Ibba M, Söll D. Retracing the evolution of amino acid specificity in glutaminyl‐tRNA synthetase. FEBS Letters 1998, 434: 149-154. PMID: 9738468, DOI: 10.1016/s0014-5793(98)00968-5.
- Major Identity Element of Glutamine tRNAs from Bacillus subtilis and Escherichia coli in the Reaction with B. subtilis Glutamyl-tRNA SynthetaseKim S, Söll D. Major Identity Element of Glutamine tRNAs from Bacillus subtilis and Escherichia coli in the Reaction with B. subtilis Glutamyl-tRNA Synthetase. Molecules And Cells 1998, 8: 459-465. PMID: 9749534, DOI: 10.1016/s1016-8478(23)13451-0.
- The Terminal Adenosine of tRNAGln Mediates tRNA-Dependent Amino Acid Recognition by Glutaminyl-tRNA Synthetase †Liu J, Ibba M, Hong K, Söll D. The Terminal Adenosine of tRNAGln Mediates tRNA-Dependent Amino Acid Recognition by Glutaminyl-tRNA Synthetase †. Biochemistry 1998, 37: 9836-9842. PMID: 9657697, DOI: 10.1021/bi980704+.
- Archaeal-type lysyl-tRNA synthetase in the Lyme disease spirochete Borrelia burgdorferiIbba M, Bono J, Rosa P, Söll D. Archaeal-type lysyl-tRNA synthetase in the Lyme disease spirochete Borrelia burgdorferi. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 14383-14388. PMID: 9405621, PMCID: PMC24988, DOI: 10.1073/pnas.94.26.14383.
- A Euryarchaeal Lysyl-tRNA Synthetase: Resemblance to Class I SynthetasesIbba M, Morgan S, Curnow A, Pridmore D, Vothknecht U, Gardner W, Lin W, Woese C, Söll D. A Euryarchaeal Lysyl-tRNA Synthetase: Resemblance to Class I Synthetases. Science 1997, 278: 1119-1122. PMID: 9353192, DOI: 10.1126/science.278.5340.1119.
- Glutamyl-tRNA sythetase.Freist W, Gauss D, Söll D, Lapointe J. Glutamyl-tRNA sythetase. Biological Chemistry 1997, 378: 1313-29. PMID: 9426192.
- Glu-tRNAGln amidotransferase: A novel heterotrimeric enzyme required for correct decoding of glutamine codons during translationCurnow A, Hong K, Yuan R, Kim S, Martins O, Winkler W, Henkin T, Söll D. Glu-tRNAGln amidotransferase: A novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 11819-11826. PMID: 9342321, PMCID: PMC23611, DOI: 10.1073/pnas.94.22.11819.
- Glutaminyl-tRNA synthetase.Freist W, Gauss D, Ibba M, Söll D. Glutaminyl-tRNA synthetase. Biological Chemistry 1997, 378: 1103-17. PMID: 9372179.
- When protein engineering confronts the tRNA worldSchimmel P, Söll D. When protein engineering confronts the tRNA world. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 10007-10009. PMID: 9294151, PMCID: PMC33764, DOI: 10.1073/pnas.94.19.10007.
- A nuclear genetic lesion affecting Saccharomyces cerevisiae mitochondrial translation is complemented by a homologous Bacillus gene.Kim S, Stange-Thomann N, Martins O, Hong K, Söll D, Fox T. A nuclear genetic lesion affecting Saccharomyces cerevisiae mitochondrial translation is complemented by a homologous Bacillus gene. Journal Of Bacteriology 1997, 179: 5625-5627. PMID: 9287027, PMCID: PMC179443, DOI: 10.1128/jb.179.17.5625-5627.1997.
- Aminoacyl-tRNA synthesis: divergent routes to a common goalIbba M, Curnow A, Söll D. Aminoacyl-tRNA synthesis: divergent routes to a common goal. Trends In Biochemical Sciences 1997, 22: 39-42. PMID: 9048478, DOI: 10.1016/s0968-0004(96)20033-7.
- tRNA-dependent amino acid transformations.Curnow A, Hong K, Yuan R, Söll D. tRNA-dependent amino acid transformations. Nucleic Acids Symposium Series 1997, 2-4. PMID: 9478189.
- Aminoacyl-tRNA synthesis in Archaea.Ibba M, Celic I, Curnow A, Kim H, Pelaschier J, Tumbula D, Vothknecht U, Woese C, Söll D. Aminoacyl-tRNA synthesis in Archaea. Nucleic Acids Symposium Series 1997, 305-6. PMID: 9586121.
- Defining the Active Site of Yeast Seryl-tRNA Synthetase MUTATIONS IN MOTIF 2 LOOP RESIDUES AFFECT tRNA-DEPENDENT AMINO ACID RECOGNITION*Lenhard B, Filipić S, Landeka I, Škrtić I, Söll D, Weygand-Durašević I. Defining the Active Site of Yeast Seryl-tRNA Synthetase MUTATIONS IN MOTIF 2 LOOP RESIDUES AFFECT tRNA-DEPENDENT AMINO ACID RECOGNITION*. Journal Of Biological Chemistry 1997, 272: 1136-1141. PMID: 8995413, DOI: 10.1074/jbc.272.2.1136.
- 'Distorted' RNA helix recognitionIbba M, Söll D. 'Distorted' RNA helix recognition. Nature 1996, 384: 422-422. DOI: 10.1038/384422b0.
- Glutamyl-transfer RNA: at the crossroad between chlorophyll and protein biosynthesisKumar A, Schaub U, Söll D, Ujwal M. Glutamyl-transfer RNA: at the crossroad between chlorophyll and protein biosynthesis. Trends In Plant Science 1996, 1: 371-376. DOI: 10.1016/s1360-1385(96)80311-6.
- Genetic analysis of functional connectivity between substrate recognition domains ofEscherichia coli glutaminyl-tRNA synthetaseKitabatake M, Inokuchi H, Ibba M, Hong K, Söll D. Genetic analysis of functional connectivity between substrate recognition domains ofEscherichia coli glutaminyl-tRNA synthetase. Molecular Genetics And Genomics 1996, 252: 717-722. PMID: 8917315, DOI: 10.1007/bf02173978.
- tRNA-dependent asparagine formationCurnow A, Ibba M, Söll D. tRNA-dependent asparagine formation. Nature 1996, 382: 589-590. PMID: 8757127, DOI: 10.1038/382589b0.
- Interactions between tRNA identity nucleotides and their recognition sites in glutaminyl-tRNA synthetase determine the cognate amino acid affinity of the enzyme.Ibba M, Hong K, Sherman J, Sever S, Söll D. Interactions between tRNA identity nucleotides and their recognition sites in glutaminyl-tRNA synthetase determine the cognate amino acid affinity of the enzyme. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 6953-6958. PMID: 8692925, PMCID: PMC38915, DOI: 10.1073/pnas.93.14.6953.
- Protein-RNA molecular recognitionIbba M, Söll D. Protein-RNA molecular recognition. Nature 1996, 381: 656-656. PMID: 8649510, DOI: 10.1038/381656a0.
- A mutation in protein phosphatase 2A regulatory subunit A affects auxin transport in Arabidopsis.Garbers C, DeLong A, Deruére J, Bernasconi P, Söll D. A mutation in protein phosphatase 2A regulatory subunit A affects auxin transport in Arabidopsis. The EMBO Journal 1996, 15: 2115-2124. PMID: 8641277, PMCID: PMC450134, DOI: 10.1002/j.1460-2075.1996.tb00565.x.
- Glutaminyl‐tRNA synthetase: from genetics to molecular recognitionIbba M, Hong K, Söll D. Glutaminyl‐tRNA synthetase: from genetics to molecular recognition. Genes To Cells 1996, 1: 421-427. PMID: 9078373, DOI: 10.1046/j.1365-2443.1996.d01-255.x.
- Transfer RNA-dependent cognate amino acid recognition by an aminoacyl-tRNA synthetase.Hong K, Ibba M, Weygand-Durasevic I, Rogers M, Thomann H, Söll D. Transfer RNA-dependent cognate amino acid recognition by an aminoacyl-tRNA synthetase. The EMBO Journal 1996, 15: 1983-91. PMID: 8617245, PMCID: PMC450117, DOI: 10.1002/j.1460-2075.1996.tb00549.x.
- Lactobacillus bulgaricus asparagine synthetase and asparaginyl-tRNA synthetase: coregulation by transcription antitermination?Kim S, Germond J, Pridmore D, Söll D. Lactobacillus bulgaricus asparagine synthetase and asparaginyl-tRNA synthetase: coregulation by transcription antitermination? Journal Of Bacteriology 1996, 178: 2459-2461. PMID: 8636057, PMCID: PMC177964, DOI: 10.1128/jb.178.8.2459-2461.1996.
- A second and differentially expressed glutamyl-tRNA reductase gene from Arabidopsis thalianaKumar A, Csankovszki G, Söll D. A second and differentially expressed glutamyl-tRNA reductase gene from Arabidopsis thaliana. Plant Molecular Biology 1996, 30: 419-426. PMID: 8605295, DOI: 10.1007/bf00049321.
- Glutamate transfer RNA: a cofactor for heme and chlorophyll biosynthesis.Madan Kumar A, Söll D. Glutamate transfer RNA: a cofactor for heme and chlorophyll biosynthesis. Indian Journal Of Biochemistry And Biophysics 1996, 33: 30-4. PMID: 8744830.
- The C-terminal Extension of Yeast Seryl-tRNA Synthetase Affects Stability of the Enzyme and Its Substrate Affinity (*)Weygand-Durasevic I, Lenhard B, Filipic S, Söll D. The C-terminal Extension of Yeast Seryl-tRNA Synthetase Affects Stability of the Enzyme and Its Substrate Affinity (*). Journal Of Biological Chemistry 1996, 271: 2455-2461. PMID: 8576207, DOI: 10.1074/jbc.271.5.2455.
- Genetic analysis of functional connectivity between substrate recognition domains ofKitabatake M, Ibba M, Hong K, Söll D, Inokuchi H. Genetic analysis of functional connectivity between substrate recognition domains of. Molecular Genetics And Genomics 1996, 252: 717. DOI: 10.1007/s004380050281.
- Aminoacyl-tRNA Synthetases Optimize Both Cognate tRNA Recognition and Discrimination against Noncognate tRNAs †Sherman J, Söll D. Aminoacyl-tRNA Synthetases Optimize Both Cognate tRNA Recognition and Discrimination against Noncognate tRNAs †. Biochemistry 1996, 35: 601-607. PMID: 8555233, DOI: 10.1021/bi951602b.
- Escherichia coli Tryptophanyl-tRNA Synthetase Mutants Selected for Tryptophan Auxotrophy Implicate the Dimer Interface in Optimizing Amino Acid Binding †Sever S, Rogers K, Rogers M, Carter C, Söll D. Escherichia coli Tryptophanyl-tRNA Synthetase Mutants Selected for Tryptophan Auxotrophy Implicate the Dimer Interface in Optimizing Amino Acid Binding †. Biochemistry 1996, 35: 32-40. PMID: 8555191, DOI: 10.1021/bi952103d.
- Homologous Expression and Purification of Mutants of an Essential Protein by Reverse Epitope-TaggingThomann H, Ibba M, Hong K, Söll D. Homologous Expression and Purification of Mutants of an Essential Protein by Reverse Epitope-Tagging. Bio/Technology 1996, 14: 50-55. PMID: 9636312, DOI: 10.1038/nbt0196-50.
- Divergence of glutamate and glutamine aminoacylation pathways: Providing the evolutionary rationale for mischargingRogers K, Söll D. Divergence of glutamate and glutamine aminoacylation pathways: Providing the evolutionary rationale for mischarging. Journal Of Molecular Evolution 1995, 40: 476-481. PMID: 7783222, DOI: 10.1007/bf00166615.
- A novel root gravitropism mutant of Arabidopsis thaliana exhibiting altered auxin physiologySimmons C, Migliaccio F, Masson P, Caspar T, Soll D. A novel root gravitropism mutant of Arabidopsis thaliana exhibiting altered auxin physiology. Physiologia Plantarum 1995, 93: 790-798. DOI: 10.1034/j.1399-3054.1995.930431.x.
- A novel root gravitropism mutant of Arabidopsis thaliana exhibiting altered auxin physiologySimmons C, Migliaccio F, Masson P, Caspar T, Söll D. A novel root gravitropism mutant of Arabidopsis thaliana exhibiting altered auxin physiology. Physiologia Plantarum 1995, 93: 790-798. PMID: 11540162, DOI: 10.1111/j.1399-3054.1995.tb05133.x.
- A broadly applicable continuous spectrophotometric assay for measuring aminoacyl-tRNA synthetase activityLloyd A, Thomann H, Ibba M, Soöll D. A broadly applicable continuous spectrophotometric assay for measuring aminoacyl-tRNA synthetase activity. Nucleic Acids Research 1995, 23: 2886-2892. PMID: 7659511, PMCID: PMC307126, DOI: 10.1093/nar/23.15.2886.
- Circumnutation and gravitropism cause root waving in Arabidopsis thalianaSimmons C, Söll D, Migliaccio F. Circumnutation and gravitropism cause root waving in Arabidopsis thaliana. Journal Of Experimental Botany 1995, 46: 143-150. DOI: 10.1093/jxb/46.1.143.
- Substrate selection by aminoacyl-tRNA synthetases.Ibba M, Thomann H, Hong K, Sherman J, Weygand-Durasevic I, Sever S, Stange-Thomann N, Praetorius M, Söll D. Substrate selection by aminoacyl-tRNA synthetases. Nucleic Acids Symposium Series 1995, 40-2. PMID: 8643392.
- Aminoacylation of transfer RNAs with 2-thiouridine derivatives in the wobble position of the anticodonRogers K, Crescenzo A, Söll D. Aminoacylation of transfer RNAs with 2-thiouridine derivatives in the wobble position of the anticodon. Biochimie 1995, 77: 66-74. PMID: 7541255, DOI: 10.1016/0300-9084(96)88106-5.
- Transfer RNA in Its Fourth DecadeRajBhandary U, Söll D. Transfer RNA in Its Fourth Decade. 1994, 1-4. DOI: 10.1128/9781555818333.ch1.
- Recognition in the Glutamine tRNA System: from Structure to FunctionSherman J, Rogers M, Söll D. Recognition in the Glutamine tRNA System: from Structure to Function. 1994, 395-409. DOI: 10.1128/9781555818333.ch19.
- Glutamyl‐tRNA as an Intermediate in Glutamate ConversionsVerkamp E, Kumar A, Lloyd A, Martins O, Stange‐Thomann N, Söll D. Glutamyl‐tRNA as an Intermediate in Glutamate Conversions. 1994, 545-550. DOI: 10.1128/9781555818333.ch27.
- A point mutation in Euglena gracilis chloroplast tRNA(Glu) uncouples protein and chlorophyll biosynthesis.Stange-Thomann N, Thomann H, Lloyd A, Lyman H, Söll D. A point mutation in Euglena gracilis chloroplast tRNA(Glu) uncouples protein and chlorophyll biosynthesis. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 7947-7951. PMID: 8058739, PMCID: PMC44521, DOI: 10.1073/pnas.91.17.7947.
- Identity switches between tRNAs aminoacylated by class I glutaminyl- and class II aspartyl-tRNA synthetases.Frugier M, Söll D, Giegé R, Florentz C. Identity switches between tRNAs aminoacylated by class I glutaminyl- and class II aspartyl-tRNA synthetases. Biochemistry 1994, 33: 9912-21. PMID: 8060999, DOI: 10.1021/bi00199a013.
- Thiobacillus ferrooxidans tyrosyl-tRNA synthetase functions in vivo in Escherichia coli.Salazar O, Sagredo B, Jedlicki E, Söll D, Weygand-Durasevic I, Orellana O. Thiobacillus ferrooxidans tyrosyl-tRNA synthetase functions in vivo in Escherichia coli. Journal Of Bacteriology 1994, 176: 4409-4415. PMID: 7517395, PMCID: PMC205654, DOI: 10.1128/jb.176.14.4409-4415.1994.
- Domains of E. Coli Glutaminyl-tRNA Synthetase Disordered in the Crystal Structure Are Essential for Function or StabilityConley J, Sherman J, Thomann H, Söill D. Domains of E. Coli Glutaminyl-tRNA Synthetase Disordered in the Crystal Structure Are Essential for Function or Stability. Nucleosides Nucleotides & Nucleic Acids 1994, 13: 1581-1595. DOI: 10.1080/15257779408012173.
- Connecting Anticodon Recognition with the Active Site of Escherichia coli Glutaminyl-tRNA SynthetaseWeygand-Duraševic I, Rogers M, Söll D. Connecting Anticodon Recognition with the Active Site of Escherichia coli Glutaminyl-tRNA Synthetase. Journal Of Molecular Biology 1994, 240: 111-118. PMID: 8027995, DOI: 10.1006/jmbi.1994.1425.
- Light regulation of chlorophyll biosynthesis at the level of 5-aminolevulinate formation in Arabidopsis.Ilag L, Kumar A, Söll D. Light regulation of chlorophyll biosynthesis at the level of 5-aminolevulinate formation in Arabidopsis. The Plant Cell 1994, 6: 265-275. PMID: 7908550, PMCID: PMC160432, DOI: 10.1105/tpc.6.2.265.
- Light Regulation of Chlorophyll Biosynthesis at the Level of 5-Aminolevulinate Formation in ArabidopsisIlag L, Kumar A, Soll D. Light Regulation of Chlorophyll Biosynthesis at the Level of 5-Aminolevulinate Formation in Arabidopsis. The Plant Cell 1994, 6: 265. DOI: 10.2307/3869644.
- Functional communication in the recognition of tRNA by Escherichia coli glutaminyl-tRNA synthetase.Rogers M, Adachi T, Inokuchi H, Söll D. Functional communication in the recognition of tRNA by Escherichia coli glutaminyl-tRNA synthetase. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 291-295. PMID: 7506418, PMCID: PMC42933, DOI: 10.1073/pnas.91.1.291.
- Coexpression of eukaryotic tRNASer and yeast seryl-tRNA synthetase leads to functional amber suppression in Escherichia coli.Weygand-Durasević I, Nalaskowska M, Söll D. Coexpression of eukaryotic tRNASer and yeast seryl-tRNA synthetase leads to functional amber suppression in Escherichia coli. Journal Of Bacteriology 1994, 176: 232-239. PMID: 8282701, PMCID: PMC205035, DOI: 10.1128/jb.176.1.232-239.1994.
- A Lactobacillus nifS-like gene suppresses an Escherichia coli transaminase B mutationLeong-Morgenthaler P, Oliver S, Hottinger H, Söll D. A Lactobacillus nifS-like gene suppresses an Escherichia coli transaminase B mutation. Biochimie 1994, 76: 45-49. PMID: 8031904, DOI: 10.1016/0300-9084(94)90061-2.
- The ERabp Gene Family: Structural and Physiological AnalysesPalme K, Hesse T, Garbers C, Simmons C, Söll D. The ERabp Gene Family: Structural and Physiological Analyses. 1994, 62: 155-161. PMID: 8147818, DOI: 10.1007/978-1-4757-9492-2_12.
- Selection of a 'minimal' glutaminyl-tRNA synthetase and the evolution of class I synthetases.Schwob E, Söll D. Selection of a 'minimal' glutaminyl-tRNA synthetase and the evolution of class I synthetases. The EMBO Journal 1993, 12: 5201-8. PMID: 7505222, PMCID: PMC413784, DOI: 10.1002/j.1460-2075.1993.tb06215.x.
- Incomplete citric acid cycle obliges aminolevulinic acid synthesis via the C5 pathway in a methylotrophLloyd A, Weitzman P, Söll D. Incomplete citric acid cycle obliges aminolevulinic acid synthesis via the C5 pathway in a methylotroph. Microbiology 1993, 139: 2931-2938. DOI: 10.1099/00221287-139-12-2931.
- Discrimination among tRNAs intermediate in glutamate and glutamine acceptor identity.Rogers K, Söll D. Discrimination among tRNAs intermediate in glutamate and glutamine acceptor identity. Biochemistry 1993, 32: 14210-9. PMID: 7505112, DOI: 10.1021/bi00214a021.
- Two members of the ERabp gene family are expressed differentially in reproductive organs but to similar levels in the coleoptile of maizeHesse T, Garbers C, Brzobohaty B, Kreimer G, Söll D, Melkonian M, Schell J, Palme K. Two members of the ERabp gene family are expressed differentially in reproductive organs but to similar levels in the coleoptile of maize. Plant Molecular Biology 1993, 23: 57-66. PMID: 8219056, DOI: 10.1007/bf00021419.
- Identification of a 100‐kDa protein associated with nuclear ribonuclease P activity in Schizosaccharomyces pombeZIMMERLY S, DRAINAS D, SYLVERS L, Dieter S. Identification of a 100‐kDa protein associated with nuclear ribonuclease P activity in Schizosaccharomyces pombe. The FEBS Journal 1993, 217: 501-507. PMID: 8223594, DOI: 10.1111/j.1432-1033.1993.tb18270.x.
- Molecular analysis of three maize 22 kDa auxin‐binding protein genes — transient promoter expression and regulatory regionsSchwob E, Choi S, Simmons C, Migliaccio F, Ilag L, Hesse T, Palme K, Söll D. Molecular analysis of three maize 22 kDa auxin‐binding protein genes — transient promoter expression and regulatory regions. The Plant Journal 1993, 4: 423-432. PMID: 7693132, DOI: 10.1046/j.1365-313x.1993.04030423.x.
- Yeast seryl‐tRNA synthetase expressed in Escherichia coli recognizes bacterial serine‐specific tRNAs in vivoWEYGAND‐DURAŠEVIĆ I, Nenad B, Dieter J, Dieter S. Yeast seryl‐tRNA synthetase expressed in Escherichia coli recognizes bacterial serine‐specific tRNAs in vivo. The FEBS Journal 1993, 214: 869-877. PMID: 7686490, DOI: 10.1111/j.1432-1033.1993.tb17990.x.
- A 2-thiouridine derivative in tRNAGlu is a positive determinant for aminoacylation by Escherichia coli glutamyl-tRNA synthetase.Sylvers L, Rogers K, Shimizu M, Ohtsuka E, Söll D. A 2-thiouridine derivative in tRNAGlu is a positive determinant for aminoacylation by Escherichia coli glutamyl-tRNA synthetase. Biochemistry 1993, 32: 3836-41. PMID: 8385989, DOI: 10.1021/bi00066a002.
- SPL1-1, a Saccharomyces cerevisiae mutation affecting tRNA splicing.Kolman C, Söll D. SPL1-1, a Saccharomyces cerevisiae mutation affecting tRNA splicing. Journal Of Bacteriology 1993, 175: 1433-1442. PMID: 8444805, PMCID: PMC193230, DOI: 10.1128/jb.175.5.1433-1442.1993.
- The periplasmic dipeptide permease system transports 5-aminolevulinic acid in Escherichia coli.Verkamp E, Backman V, Björnsson J, Söll D, Eggertsson G. The periplasmic dipeptide permease system transports 5-aminolevulinic acid in Escherichia coli. Journal Of Bacteriology 1993, 175: 1452-1456. PMID: 8444807, PMCID: PMC193232, DOI: 10.1128/jb.175.5.1452-1456.1993.
- Acceptor end binding domain interactions ensure correct aminoacylation of transfer RNA.Weygand-Durasević I, Schwob E, Söll D. Acceptor end binding domain interactions ensure correct aminoacylation of transfer RNA. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 2010-2014. PMID: 7680483, PMCID: PMC46010, DOI: 10.1073/pnas.90.5.2010.
- The recognition of E. coli glutamine tRNA by glutaminyl-tRNA synthetase.Rogers M, Weygand-Durasević I, Schwob E, Sherman J, Rogers K, Thomann H, Sylvers L, Ohtsuka E, Inokuchi H, Söll D. The recognition of E. coli glutamine tRNA by glutaminyl-tRNA synthetase. Nucleic Acids Symposium Series 1993, 211-3. PMID: 7504247.
- Selectivity and specificity in the recognition of tRNA by E coli glutaminyl-tRNA synthetaseRogers M, Weygand-Durašević I, Schwob E, Sherman J, Rogers K, Adachi T, Inokuchi H, Söll D. Selectivity and specificity in the recognition of tRNA by E coli glutaminyl-tRNA synthetase. Biochimie 1993, 75: 1083-1090. PMID: 8199243, DOI: 10.1016/0300-9084(93)90007-f.
- Specificity in RNA: Protein Interactions; the Recognition of Escherichia Coli Glutamine tRNARogers M, Weygand-Durašević I, Schwob E, Sherman J, Rogers K, Thomann H, Sylvers L, Jahn M, Inokuchi H, Ohtsuka E, Söll D. Specificity in RNA: Protein Interactions; the Recognition of Escherichia Coli Glutamine tRNA. 1993, 47-58. DOI: 10.1007/978-1-4615-2407-6_5.
- Acceptor stem and anticodon RNA hairpin helix interactions with glutamine tRNA synthetaseWright D, Martinis S, Jahn M, Söll D, Schimmel P. Acceptor stem and anticodon RNA hairpin helix interactions with glutamine tRNA synthetase. Biochimie 1993, 75: 1041-1049. PMID: 8199240, DOI: 10.1016/0300-9084(93)90003-b.
- Synthetase competition and tRNA context determine the in vivo identity of tRNA discriminator mutantsSherman J, Rogers K, Rogers M, Söll D. Synthetase competition and tRNA context determine the in vivo identity of tRNA discriminator mutants. Journal Of Molecular Biology 1992, 228: 1055-1062. PMID: 1474577, DOI: 10.1016/0022-2836(92)90314-a.
- Arabidopsis alternative oxidase sustains Escherichia coli respiration.Kumar A, Söll D. Arabidopsis alternative oxidase sustains Escherichia coli respiration. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 10842-10846. PMID: 1438286, PMCID: PMC50438, DOI: 10.1073/pnas.89.22.10842.
- Recognition of bases in Escherichia coli tRNA(Gln) by glutaminyl-tRNA synthetase: a complete identity set.Hayase Y, Jahn M, Rogers M, Sylvers L, Koizumi M, Inoue H, Ohtsuka E, Söll D. Recognition of bases in Escherichia coli tRNA(Gln) by glutaminyl-tRNA synthetase: a complete identity set. The EMBO Journal 1992, 11: 4159-65. PMID: 1396597, PMCID: PMC556926, DOI: 10.1002/j.1460-2075.1992.tb05509.x.
- Chloroplast tRNAAsp: nucleotide sequence and variation of in vivo levels during plastid maturationSchön A, Gough S, Söll D. Chloroplast tRNAAsp: nucleotide sequence and variation of in vivo levels during plastid maturation. Plant Molecular Biology 1992, 20: 601-607. PMID: 1450377, DOI: 10.1007/bf00046445.
- Organization and nucleotide sequence of the glutamine synthetase (glnA) gene from Lactobacillus delbrueckii subsp. bulgaricus.Ishino Y, Morgenthaler P, Hottinger H, Söll D. Organization and nucleotide sequence of the glutamine synthetase (glnA) gene from Lactobacillus delbrueckii subsp. bulgaricus. Applied And Environmental Microbiology 1992, 58: 3165-9. PMID: 1359838, PMCID: PMC183065, DOI: 10.1128/aem.58.9.3165-3169.1992.
- Switching tRNA(Gln) identity from glutamine to tryptophan.Rogers M, Adachi T, Inokuchi H, Söll D. Switching tRNA(Gln) identity from glutamine to tryptophan. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 3463-3467. PMID: 1565639, PMCID: PMC48888, DOI: 10.1073/pnas.89.8.3463.
- Glutamyl-tRNA reductase from Escherichia coli and Synechocystis 6803. Gene structure and expression.Verkamp E, Jahn M, Jahn D, Kumar A, Söll D. Glutamyl-tRNA reductase from Escherichia coli and Synechocystis 6803. Gene structure and expression. Journal Of Biological Chemistry 1992, 267: 8275-8280. PMID: 1569081, DOI: 10.1016/s0021-9258(18)42438-6.
- Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylationSherman J, Ropers M, Söll D. Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation. Nucleic Acids Research 1992, 20: 2931-2931. DOI: 10.1093/nar/20.11.2931-a.
- Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylationSherman J, Rogers M, Söll D. Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation. Nucleic Acids Research 1992, 20: 1547-1552. PMID: 16617497, PMCID: PMC312236, DOI: 10.1093/nar/20.7.1547.
- Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylationSherman J, Rogers M, Söll D. Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation. Nucleic Acids Research 1992, 20: 2847-2852. PMID: 1377381, PMCID: PMC336931, DOI: 10.1093/nar/20.11.2847.
- Aminoacyl-tRNA synthetase-induced cleavage of tRNABeresten S, Jahn M, Söll D. Aminoacyl-tRNA synthetase-induced cleavage of tRNA. Nucleic Acids Research 1992, 20: 1523-1530. PMID: 1579445, PMCID: PMC312233, DOI: 10.1093/nar/20.7.1523.
- Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. I. Purification and physical properties.Pande S, Jahn D, Söll D. Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. I. Purification and physical properties. Journal Of Biological Chemistry 1991, 266: 22826-22831. PMID: 1660461, DOI: 10.1016/s0021-9258(18)54428-8.
- Mutant enzymes and tRNAs as probes of the glutaminyl-tRNA synthetase: tRNAGln interactionEnlisch-Peters S, Conley J, Plumbridge J, Leptak C, Söll D, Rogers M. Mutant enzymes and tRNAs as probes of the glutaminyl-tRNA synthetase: tRNAGln interaction. Biochimie 1991, 73: 1501-1508. PMID: 1725262, DOI: 10.1016/0300-9084(91)90184-3.
- Anticodon and acceptor stem nucleotides in tRNAGln are major recognition elements for E. coli glutaminyl-tRNA synthetaseJahn M, Rogers M, Söll D. Anticodon and acceptor stem nucleotides in tRNAGln are major recognition elements for E. coli glutaminyl-tRNA synthetase. Nature 1991, 352: 258-260. PMID: 1857423, DOI: 10.1038/352258a0.
- The Escherichia coli hemL gene encodes glutamate 1-semialdehyde aminotransferase.Ilag L, Jahn D, Eggertsson G, Söll D. The Escherichia coli hemL gene encodes glutamate 1-semialdehyde aminotransferase. Journal Of Bacteriology 1991, 173: 3408-3413. PMID: 2045363, PMCID: PMC207952, DOI: 10.1128/jb.173.11.3408-3413.1991.
- Mono Q chromatography permits recycling of DNA template and purification of RNA transcripts after T7 RNA polymerase reactionJahn M, Jahn D, Kumar A, Söll D. Mono Q chromatography permits recycling of DNA template and purification of RNA transcripts after T7 RNA polymerase reaction. Nucleic Acids Research 1991, 19: 2786-2786. PMID: 1710347, PMCID: PMC328209, DOI: 10.1093/nar/19.10.2786.
- Two glutamyl-tRNA reductase activities in Escherichia coliJahn D, Michelsen U, Söll D. Two glutamyl-tRNA reductase activities in Escherichia coli. Journal Of Biological Chemistry 1991, 266: 2542-2548. PMID: 1990004, DOI: 10.1016/s0021-9258(18)52279-1.
- Purification and functional characterization of glutamate-1-semialdehyde aminotransferase from Chlamydomonas reinhardtii.Jahn D, Chen M, Söll D. Purification and functional characterization of glutamate-1-semialdehyde aminotransferase from Chlamydomonas reinhardtii. Journal Of Biological Chemistry 1991, 266: 161-167. PMID: 1985889, DOI: 10.1016/s0021-9258(18)52416-9.
- The Human Genome Project: a paradigm for information management in the life sciencesPearson M, Söll D. The Human Genome Project: a paradigm for information management in the life sciences. The FASEB Journal 1991, 5: 35-39. PMID: 1991581, DOI: 10.1096/fasebj.5.1.1991581.
- delta-Aminolevulinic acid dehydratase deficiency can cause delta-aminolevulinate auxotrophy in Escherichia coli.O'Neill G, Thorbjarnardóttir S, Michelsen U, Pálsson S, Söll D, Eggertsson G. delta-Aminolevulinic acid dehydratase deficiency can cause delta-aminolevulinate auxotrophy in Escherichia coli. Journal Of Bacteriology 1991, 173: 94-100. PMID: 1987138, PMCID: PMC207161, DOI: 10.1128/jb.173.1.94-100.1991.
- Transfer RNA Involvement in Chlorophyll BiosynthesisO’Neill G, Jahn D, Söll D. Transfer RNA Involvement in Chlorophyll Biosynthesis. 1991, 17: 235-264. PMID: 1796486, DOI: 10.1007/978-1-4613-9365-8_11.
- Isolation and Sequence of a tRNAGly (CCC) from Streptomyces coelicolor A3(2)Rokem J, Schön A, Söll D. Isolation and Sequence of a tRNAGly (CCC) from Streptomyces coelicolor A3(2). 1991, 47-52. DOI: 10.1007/978-1-4684-5922-7_7.
- The accuracy of aminoacylation — ensuring the fidelity of the genetic codeSöll D. The accuracy of aminoacylation — ensuring the fidelity of the genetic code. Cellular And Molecular Life Sciences 1990, 46: 1089-1096. PMID: 2253707, DOI: 10.1007/bf01936918.
- Expression of the Synechocystis sp. strain PCC 6803 tRNA(Glu) gene provides tRNA for protein and chlorophyll biosynthesis.O'Neill G, Söll D. Expression of the Synechocystis sp. strain PCC 6803 tRNA(Glu) gene provides tRNA for protein and chlorophyll biosynthesis. Journal Of Bacteriology 1990, 172: 6363-6371. PMID: 2121711, PMCID: PMC526821, DOI: 10.1128/jb.172.11.6363-6371.1990.
- Transfer RNA and the formation of the heme and chlorophyll precursor, 5-aminolevulinic acid.O'Neill G, Söll D. Transfer RNA and the formation of the heme and chlorophyll precursor, 5-aminolevulinic acid. BioFactors 1990, 2: 227-35. PMID: 2282139.
- The RNA component of RNase P in Schizosaccharomyces speciesZimmerly S, Gamulin V, Burkard U, Söll D. The RNA component of RNase P in Schizosaccharomyces species. FEBS Letters 1990, 271: 189-193. PMID: 2226803, DOI: 10.1016/0014-5793(90)80403-6.
- Purification and functional characterization of the Glu-tRNA(Gln) amidotransferase from Chlamydomonas reinhardtii.Jahn D, Kim Y, Ishino Y, Chen M, Söll D. Purification and functional characterization of the Glu-tRNA(Gln) amidotransferase from Chlamydomonas reinhardtii. Journal Of Biological Chemistry 1990, 265: 8059-8064. PMID: 1970821, DOI: 10.1016/s0021-9258(19)39038-6.
- Purification and characterization of Chlamydomonas reinhardtii chloroplast glutamyl-tRNA synthetase, a natural misacylating enzyme.Chen M, Jahn D, Schön A, O'Neill G, Söll D. Purification and characterization of Chlamydomonas reinhardtii chloroplast glutamyl-tRNA synthetase, a natural misacylating enzyme. Journal Of Biological Chemistry 1990, 265: 4054-4057. PMID: 2303494, DOI: 10.1016/s0021-9258(19)39701-7.
- Purification of the glutamyl-tRNA reductase from Chlamydomonas reinhardtii involved in delta-aminolevulinic acid formation during chlorophyll biosynthesis.Chen M, Jahn D, O'Neill G, Söll D. Purification of the glutamyl-tRNA reductase from Chlamydomonas reinhardtii involved in delta-aminolevulinic acid formation during chlorophyll biosynthesis. Journal Of Biological Chemistry 1990, 265: 4058-4063. PMID: 2303495, DOI: 10.1016/s0021-9258(19)39702-9.
- Sequence of a tRNA Gly from Streptomyces coelicolorRokem J, Schön A, Söll D. Sequence of a tRNA Gly from Streptomyces coelicolor. Nucleic Acids Research 1990, 18: 3988-3988. PMID: 2374719, PMCID: PMC331104, DOI: 10.1093/nar/18.13.3988.
- Enzymatic addition of guanylate to histidine transfer RNAWilliams J, Cooley L, Söll D. Enzymatic addition of guanylate to histidine transfer RNA. 1990, 181: 451-462. PMID: 2166216, DOI: 10.1016/0076-6879(90)81143-i.
- Inaccuracy and the Recognition of †RNARogers M, Soll D. Inaccuracy and the Recognition of †RNA. 1990, 39: 185-208. PMID: 2247608, DOI: 10.1016/s0079-6603(08)60627-3.
- Sequence of tRNAGlu and its genes from the chloroplast genome of Chlamydomonas reinhardtiiO'Neill G, Schön A, Chow H, Chen M, Kim Y, Söll D. Sequence of tRNAGlu and its genes from the chloroplast genome of Chlamydomonas reinhardtii. Nucleic Acids Research 1990, 18: 5893-5893. PMID: 2216788, PMCID: PMC332342, DOI: 10.1093/nar/18.19.5893.
- Introduction and OverviewSöll D. Introduction and Overview. 1990, 45: b1-b11. DOI: 10.1016/s0301-4770(08)61486-4.
- Yeast suppressor mutations and transfer RNA processingNichols M, Willis I, Söll D. Yeast suppressor mutations and transfer RNA processing. 1990, 181: 377-394. PMID: 2199758, DOI: 10.1016/0076-6879(90)81137-j.
- A selection for mutants of the RNA polymerase III transcription apparatus: PCF1 stimulates transcription of tRNA and 5S RNA genes.Willis I, Schmidt P, Söll D. A selection for mutants of the RNA polymerase III transcription apparatus: PCF1 stimulates transcription of tRNA and 5S RNA genes. The EMBO Journal 1989, 8: 4281-4288. PMID: 2686985, PMCID: PMC401634, DOI: 10.1002/j.1460-2075.1989.tb08614.x.
- Structure of E. coli Glutaminyl-tRNA Synthetase Complexed with tRNAGln and ATP at 2.8 Å ResolutionRould M, Perona J, Söll D, Steitz T. Structure of E. coli Glutaminyl-tRNA Synthetase Complexed with tRNAGln and ATP at 2.8 Å Resolution. Science 1989, 246: 1135-1142. PMID: 2479982, DOI: 10.1126/science.2479982.
- Structural Basis for Misaminoacylation by Mutant E. coli Glutaminyl-tRNA Synthetase EnzymesPerona J, Swanson R, Rould M, Steitz T, Söll D. Structural Basis for Misaminoacylation by Mutant E. coli Glutaminyl-tRNA Synthetase Enzymes. Science 1989, 246: 1152-1154. PMID: 2686030, DOI: 10.1126/science.2686030.
- Multiple Mutations of the First Gene of a Dimeric tRNA Gene Abolish in Vitro tRNA Gene TranscriptionNichols M, Bell J, Klekamp M, Weil P, Söll D. Multiple Mutations of the First Gene of a Dimeric tRNA Gene Abolish in Vitro tRNA Gene Transcription. Journal Of Biological Chemistry 1989, 264: 17084-17090. PMID: 2676999, DOI: 10.1016/s0021-9258(18)71462-2.
- delta-Aminolevulinic acid biosynthesis in Escherichia coli and Bacillus subtilis involves formation of glutamyl-tRNA.O'Neill G, Chen M, Söll D. delta-Aminolevulinic acid biosynthesis in Escherichia coli and Bacillus subtilis involves formation of glutamyl-tRNA. FEMS Microbiology Letters 1989, 51: 255-9. PMID: 2511063, DOI: 10.1016/0378-1097(89)90406-0.
- δ‐Aminolevulinic acid biosynthesis in Escherichia coli and Bacillus subtilis involves formation of glutamyl‐tRNAO'Neill G, Chen M, Söll D. δ‐Aminolevulinic acid biosynthesis in Escherichia coli and Bacillus subtilis involves formation of glutamyl‐tRNA. FEMS Microbiology Letters 1989, 60: 255-260. DOI: 10.1111/j.1574-6968.1989.tb03482.x.
- Substrate structural requirements of Schizosaccharomyces pombe RNase PDrainas D, Zimmerly S, Willis I, Söll D. Substrate structural requirements of Schizosaccharomyces pombe RNase P. FEBS Letters 1989, 251: 84-88. PMID: 2666172, DOI: 10.1016/0014-5793(89)81433-4.
- Characterization of cis-acting mutations which increase expression of a glnS-lacZ fusion in Escherichia coliPlumbridge J, Söll D. Characterization of cis-acting mutations which increase expression of a glnS-lacZ fusion in Escherichia coli. Molecular Genetics And Genomics 1989, 216: 113-119. PMID: 2471922, DOI: 10.1007/bf00332238.
- Specificity of sRNA for Recognition of Codons as Studied by the Ribosomal Binding Technique††This is paper LVII in the series “Studies on Polynucleotides”. Paper LVI is by D. S. Jones, S. Nishimura & H. G. Khorana (1966), J. Mol. Biol. 16, 454.SÖLL D, JONES D, OHTSUKA E, FAULKNER R, LOHRMANN R, HAYATSU H, KHORANA H, CHERAYIL J, HAMPEL A, BOCK R. Specificity of sRNA for Recognition of Codons as Studied by the Ribosomal Binding Technique††This is paper LVII in the series “Studies on Polynucleotides”. Paper LVI is by D. S. Jones, S. Nishimura & H. G. Khorana (1966), J. Mol. Biol. 16, 454. 1989, 378-395. DOI: 10.1016/b978-0-12-131200-8.50027-7.
- 3 Informational Suppression, Transfer RNA, and Intergenic ConversionKOHLI J, MUNZ P, SÖLL D. 3 Informational Suppression, Transfer RNA, and Intergenic Conversion. 1989, 75-96. DOI: 10.1016/b978-0-12-514085-0.50008-7.
- The selenocysteine-inserting opal suppressor serine tRNA from E.coli is highly unusual in structure and modificationSchön A, Böck A, Ott G, Sprinzl M, Söll D. The selenocysteine-inserting opal suppressor serine tRNA from E.coli is highly unusual in structure and modification. Nucleic Acids Research 1989, 17: 7159-7165. PMID: 2529478, PMCID: PMC334795, DOI: 10.1093/nar/17.18.7159.
- Accuracy of in Vivo Aminoacylation Requires Proper Balance of tRNA and Aminoacyl-tRNA SynthetaseSwanson R, Hoben P, Sumner-Smith M, Uemura H, Watson L, Söll D. Accuracy of in Vivo Aminoacylation Requires Proper Balance of tRNA and Aminoacyl-tRNA Synthetase. Science 1988, 242: 1548-1551. PMID: 3144042, DOI: 10.1126/science.3144042.
- Site-directed mutagenesis to fine-tune enzyme specificityUemura H, Rogers M, Swanson R, Watson L, Söll D. Site-directed mutagenesis to fine-tune enzyme specificity. Protein Engineering Design And Selection 1988, 2: 293-296. PMID: 3150543, DOI: 10.1093/protein/2.4.293.
- Genomic organization of tRNA and aminoacyl-tRNA synthetase genes for two amino acids in Saccharomyces cerevisiaeKolman C, Snyder M, Söll D. Genomic organization of tRNA and aminoacyl-tRNA synthetase genes for two amino acids in Saccharomyces cerevisiae. Genomics 1988, 3: 201-206. PMID: 3066745, DOI: 10.1016/0888-7543(88)90080-8.
- Transfer ribonucleic acid-mediated suppression of termination codons in Escherichia coli.Eggertsson G, Söll D. Transfer ribonucleic acid-mediated suppression of termination codons in Escherichia coli. Microbiology And Molecular Biology Reviews 1988, 52: 354-74. PMID: 3054467, PMCID: PMC373150, DOI: 10.1128/mr.52.3.354-374.1988.
- Formation of the chlorophyll precursor delta-aminolevulinic acid in cyanobacteria requires aminoacylation of a tRNAGlu species.O'Neill G, Peterson D, Schön A, Chen M, Söll D. Formation of the chlorophyll precursor delta-aminolevulinic acid in cyanobacteria requires aminoacylation of a tRNAGlu species. Journal Of Bacteriology 1988, 170: 3810-3816. PMID: 2900830, PMCID: PMC211375, DOI: 10.1128/jb.170.9.3810-3816.1988.
- Discrimination between glutaminyl-tRNA synthetase and seryl-tRNA synthetase involves nucleotides in the acceptor helix of tRNA.Rogers M, Söll D. Discrimination between glutaminyl-tRNA synthetase and seryl-tRNA synthetase involves nucleotides in the acceptor helix of tRNA. Proceedings Of The National Academy Of Sciences Of The United States Of America 1988, 85: 6627-6631. PMID: 3045821, PMCID: PMC282030, DOI: 10.1073/pnas.85.18.6627.
- The 5′-terminal guanylate of chloroplast histidine tRNA is encoded in its gene.Burkard U, Söll D. The 5′-terminal guanylate of chloroplast histidine tRNA is encoded in its gene. Journal Of Biological Chemistry 1988, 263: 9578-9581. PMID: 2838471, DOI: 10.1016/s0021-9258(19)81555-7.
- Overproduction and purification of Escherichia coli tRNAGln2 and its use in crystallization of the glutaminyl-tRNA synthetase-tRNAGln complexPerona J, Swanson R, Steitz T, Söll D. Overproduction and purification of Escherichia coli tRNAGln2 and its use in crystallization of the glutaminyl-tRNA synthetase-tRNAGln complex. Journal Of Molecular Biology 1988, 202: 121-126. PMID: 2459391, DOI: 10.1016/0022-2836(88)90524-4.
- The nucleotide sequences of barley cytoplasmic glutamate transfer RNAs and structural features essential for formation of δ-aminolevulinic acidPeterson D, Schön A, Söll D. The nucleotide sequences of barley cytoplasmic glutamate transfer RNAs and structural features essential for formation of δ-aminolevulinic acid. Plant Molecular Biology 1988, 11: 293-299. PMID: 24272342, DOI: 10.1007/bf00027386.
- DNA Databases MonitoredSoll D, Kirschstein R, Philipson L, Uchida H. DNA Databases Monitored. Science 1988, 240: 375-375. PMID: 3358119, DOI: 10.1126/science.3358119.
- Misaminoacylation and transamidation are required for protein biosynthesis in lactobacillus bulgaricusSchön A, Hottinger H, Söll D. Misaminoacylation and transamidation are required for protein biosynthesis in lactobacillus bulgaricus. Biochimie 1988, 70: 391-394. PMID: 3139057, DOI: 10.1016/0300-9084(88)90212-x.
- Yeast RNase P: catalytic activity and substrate binding are separate functions.Nichols M, Söll D, Willis I. Yeast RNase P: catalytic activity and substrate binding are separate functions. Proceedings Of The National Academy Of Sciences Of The United States Of America 1988, 85: 1379-1383. PMID: 3278310, PMCID: PMC279774, DOI: 10.1073/pnas.85.5.1379.
- tRNA specificity of a mischarging aminoacyl‐tRNA synthetase: Glutamyl‐tRNA synthetase from barley chloroplastsSchön A, Söll D. tRNA specificity of a mischarging aminoacyl‐tRNA synthetase: Glutamyl‐tRNA synthetase from barley chloroplasts. FEBS Letters 1988, 228: 241-244. DOI: 10.1016/0014-5793(88)80007-3.
- Processing of histidine transfer RNA precursors. Abnormal cleavage site for RNase P.Burkard U, Willis I, Söll D. Processing of histidine transfer RNA precursors. Abnormal cleavage site for RNase P. Journal Of Biological Chemistry 1988, 263: 2447-2451. PMID: 3276688, DOI: 10.1016/s0021-9258(18)69227-0.
- Escherichia coli glutaminyl-tRNA synthetase: a single amino acid replacement relaxes rRNA specificity.Uemura H, Conley J, Yamao F, Rogers J, Söll D. Escherichia coli glutaminyl-tRNA synthetase: a single amino acid replacement relaxes rRNA specificity. Protein Sequences And Data Analysis 1988, 1: 479-85. PMID: 2464170.
- The unusually long amino acid acceptor stem of Escherichia coli selenocysteine tRNA results from abnormal cleavage by RNase PBurkard U, Söll D. The unusually long amino acid acceptor stem of Escherichia coli selenocysteine tRNA results from abnormal cleavage by RNase P. Nucleic Acids Research 1988, 16: 11617-11624. PMID: 3062578, PMCID: PMC339093, DOI: 10.1093/nar/16.24.11617.
- Transfer ribonucleic acid-mediated suppression of termination codons in Escherichia coli.Eggertsson G, Söll D. Transfer ribonucleic acid-mediated suppression of termination codons in Escherichia coli. Microbiology And Molecular Biology Reviews 1988, 52: 354-374. DOI: 10.1128/mmbr.52.3.354-374.1988.
- EditorialBeynon R, Modelevsky J, Roberts R, Söll D. Editorial. Nucleic Acids Research 1988, 16: 1655-1655. PMID: 16617485, PMCID: PMC338159, DOI: 10.1093/nar/16.5.1655.
- Protein biosynthesis in organelles requires misaminoacylation of tRNASchön A, Kannangara C, Cough S, SÖll D. Protein biosynthesis in organelles requires misaminoacylation of tRNA. Nature 1988, 331: 187-190. PMID: 3340166, DOI: 10.1038/331187a0.
- The effect of dam methylation on the expression of glnS in E. coliPlumbridge J, Söll D. The effect of dam methylation on the expression of glnS in E. coli. Biochimie 1987, 69: 539-541. PMID: 2960382, DOI: 10.1016/0300-9084(87)90091-5.
- Simplified in vitro synthesis of mutated RNA moleculesKrupp G, Söll D. Simplified in vitro synthesis of mutated RNA molecules. FEBS Letters 1987, 212: 271-275. PMID: 3545903, DOI: 10.1016/0014-5793(87)81359-5.
- Substrate Recognition and Identification of Splice Sites by the tRNA-Splicing Endonuclease and Ligase from Saccharomyces cerevisiaeGreer C, Söll D, Willis I. Substrate Recognition and Identification of Splice Sites by the tRNA-Splicing Endonuclease and Ligase from Saccharomyces cerevisiae. Molecular And Cellular Biology 1987, 7: 76-84. DOI: 10.1128/mcb.7.1.76-84.1987.
- Substrate recognition and identification of splice sites by the tRNA-splicing endonuclease and ligase from Saccharomyces cerevisiae.Greer C, Söll D, Willis I. Substrate recognition and identification of splice sites by the tRNA-splicing endonuclease and ligase from Saccharomyces cerevisiae. Molecular And Cellular Biology 1987, 7: 76-84. PMID: 3550427, PMCID: PMC365043, DOI: 10.1128/mcb.7.1.76.
- Allele-specific complementation of an Escherichia coli leuB mutation by a Lactobacillus bulgaricus tRNA geneHottinger H, Ohgi T, Zwahlen M, Dhamija S, Söll D. Allele-specific complementation of an Escherichia coli leuB mutation by a Lactobacillus bulgaricus tRNA gene. Gene 1987, 60: 75-83. PMID: 3326787, DOI: 10.1016/0378-1119(87)90215-0.
- Cloning and characterization of the gene coding for cytoplasmic seryl-tRNA synthetase from Saccharomyces cerevisiaeWeygand-Durasevic I, johnson-Burke D, Söll D. Cloning and characterization of the gene coding for cytoplasmic seryl-tRNA synthetase from Saccharomyces cerevisiae. Nucleic Acids Research 1987, 15: 1887-1904. PMID: 3031581, PMCID: PMC340606, DOI: 10.1093/nar/15.5.1887.
- 19 A New Role for Transfer RNA: A Chloroplast Transfer RNA Is a Cofactor in the Conversion of Glutamate to Delta-Aminolevulinic AcidSCHÖN A, KRUPP G, SÖLL D, GOUGH S, KANNANGARA C. 19 A New Role for Transfer RNA: A Chloroplast Transfer RNA Is a Cofactor in the Conversion of Glutamate to Delta-Aminolevulinic Acid. 1987, 295-303. DOI: 10.1016/b978-0-12-372483-0.50022-3.
- Functional complementation between mutations in a yeast suppressor tRNA gene reveals potential for evolution of tRNA sequences.Willis I, Nichols M, Chisholm V, Söll D, Heyer W, Szankasi P, Amstutz H, Munz P, Kohli J. Functional complementation between mutations in a yeast suppressor tRNA gene reveals potential for evolution of tRNA sequences. Proceedings Of The National Academy Of Sciences Of The United States Of America 1986, 83: 7860-7864. PMID: 3532123, PMCID: PMC386822, DOI: 10.1073/pnas.83.20.7860.
- Two RNA species co‐purify with RNase P from the fission yeast Schizosaccharomyces pombe.Krupp G, Cherayil B, Frendewey D, Nishikawa S, Söll D. Two RNA species co‐purify with RNase P from the fission yeast Schizosaccharomyces pombe. The EMBO Journal 1986, 5: 1697-1703. PMID: 3743551, PMCID: PMC1166996, DOI: 10.1002/j.1460-2075.1986.tb04413.x.
- The RNA required in the first step of chlorophyll biosynthesis is a chloroplast glutamate tRNASchön A, Krupp G, Gough S, Berry-Lowe S, Kannangara C, Söll D. The RNA required in the first step of chlorophyll biosynthesis is a chloroplast glutamate tRNA. Nature 1986, 322: 281-284. PMID: 3637637, DOI: 10.1038/322281a0.
- A single base change in the intron of a serine tRNA affects the rate of RNase P cleavage in vitro and suppressor activity in vivo in Saccharomyces cerevisiae.Willis I, Frendewey D, Nichols M, Hottinger-Werlen A, Schaack J, Söll D. A single base change in the intron of a serine tRNA affects the rate of RNase P cleavage in vitro and suppressor activity in vivo in Saccharomyces cerevisiae. Journal Of Biological Chemistry 1986, 261: 5878-5885. PMID: 3516987, DOI: 10.1016/s0021-9258(17)38465-x.
- Inactivation of nonsense suppressor transfer RNA genes in Schizosaccharomyces pombe Intergenic conversion and hot spots of mutationHeyer W, Münz P, Amstutz H, Aebi R, Gysler C, Schuchert P, Szankasi P, Leupold U, Kohli J, Gamulin V, Söll D. Inactivation of nonsense suppressor transfer RNA genes in Schizosaccharomyces pombe Intergenic conversion and hot spots of mutation. Journal Of Molecular Biology 1986, 188: 343-353. PMID: 3735426, DOI: 10.1016/0022-2836(86)90159-2.
- The Additional Guanylate at the 5′ Terminus of Escherichia coli tRNAHis is the Result of Unusual Processing by RNase POrellana O, Cooley L, Söll D. The Additional Guanylate at the 5′ Terminus of Escherichia coli tRNAHis is the Result of Unusual Processing by RNase P. Molecular And Cellular Biology 1986, 6: 525-529. DOI: 10.1128/mcb.6.2.525-529.1986.
- The additional guanylate at the 5' terminus of Escherichia coli tRNAHis is the result of unusual processing by RNase P.Orellana O, Cooley L, Söll D. The additional guanylate at the 5' terminus of Escherichia coli tRNAHis is the result of unusual processing by RNase P. Molecular And Cellular Biology 1986, 6: 525-529. PMID: 3023854, PMCID: PMC367542, DOI: 10.1128/mcb.6.2.525.
- The nucleotide sequence of a wheat γ-gliadin genomic cloneSugiyama T, Rafalski A, Söll D. The nucleotide sequence of a wheat γ-gliadin genomic clone. Plant Science 1986, 44: 205-209. DOI: 10.1016/0168-9452(86)90092-0.
- The nucleotide sequence, localization and transcriptional properties of a tRNACUGLeu gene from Drosophila melanogasterGlew L, Lo R, Recce T, Nichols M, Söll D, Bell J. The nucleotide sequence, localization and transcriptional properties of a tRNACUGLeu gene from Drosophila melanogaster. Gene 1986, 44: 307-314. PMID: 2946625, DOI: 10.1016/0378-1119(86)90195-2.
- Proton NMR Studies of RNA’S and Related Enzymes Using Isotope LabelsRedfield A, Choi B, Griffey R, Jarema M, Rosevear P, Hoben P, Swanson R, Soll D. Proton NMR Studies of RNA’S and Related Enzymes Using Isotope Labels. 1986, 99-112. DOI: 10.1007/978-1-4684-5173-3_9.
- supN ochre suppressor gene in Escherichia coli codes for tRNALys.Uemura H, Thorbjarnardóttir S, Gamulin V, Yano J, Andrésson O, Söll D, Eggertsson G. supN ochre suppressor gene in Escherichia coli codes for tRNALys. Journal Of Bacteriology 1985, 163: 1288-9. PMID: 3897192, PMCID: PMC219277, DOI: 10.1128/jb.163.3.1288-1289.1985.
- First identification of an amber nonsense mutation in Schizosaccharomyces pombe: major differences in the efficiency of homologous versus heterologous yeast suppressor tRNA genesKrupp G, Thuriaux P, Willis I, Gamulin V, Söll D. First identification of an amber nonsense mutation in Schizosaccharomyces pombe: major differences in the efficiency of homologous versus heterologous yeast suppressor tRNA genes. Molecular Genetics And Genomics 1985, 201: 82-87. PMID: 3903436, DOI: 10.1007/bf00397990.
- Preface.Roberts R, Söll D. Preface. Nucleic Acids Research 1985, 14: nil25. PMID: 16617478, PMCID: PMC339346, DOI: 10.1146/annurev.bb.14.111006.100001.
- Mutations Preventing Expression of sup3 tRNASer Nonsense Suppressors of Schizosaccharomyces pombePearson D, Willis I, Hottinger H, Bell J, Kumar A, Leupold U, Söll D. Mutations Preventing Expression of sup3 tRNASer Nonsense Suppressors of Schizosaccharomyces pombe. Molecular And Cellular Biology 1985, 5: 808-815. DOI: 10.1128/mcb.5.4.808-815.1985.
- Mutations preventing expression of sup3 tRNASer nonsense suppressors of Schizosaccharomyces pombe.Pearson D, Willis I, Hottinger H, Bell J, Kumar A, Leupold U, Söll D. Mutations preventing expression of sup3 tRNASer nonsense suppressors of Schizosaccharomyces pombe. Molecular And Cellular Biology 1985, 5: 808-815. PMID: 3921825, PMCID: PMC366785, DOI: 10.1128/mcb.5.4.808.
- Leucine tRNA family of Escherichia coli: nucleotide sequence of the supP(Am) suppressor gene.Thorbjarnardóttir S, Dingermann T, Rafnar T, Andrésson O, Söll D, Eggertsson G. Leucine tRNA family of Escherichia coli: nucleotide sequence of the supP(Am) suppressor gene. Journal Of Bacteriology 1985, 161: 219-22. PMID: 2981802, PMCID: PMC214859, DOI: 10.1128/jb.161.1.219-222.1985.
- Escherichia coli supH suppressor: temperature-sensitive missense suppression caused by an anticodon change in tRNASer2.Thorbjarnardóttir S, Uemura H, Dingermann T, Rafnar T, Thorsteinsdóttir S, Söll D, Eggertsson G. Escherichia coli supH suppressor: temperature-sensitive missense suppression caused by an anticodon change in tRNASer2. Journal Of Bacteriology 1985, 161: 207-11. PMID: 3155715, PMCID: PMC214857, DOI: 10.1128/jb.161.1.207-211.1985.
- Processing of precursor tRNAs in Drosophila. Processing of the 3‘ end involves an endonucleolytic cleavage and occurs after 5‘ end maturation.Frendewey D, Dingermann T, Cooley L, Söll D. Processing of precursor tRNAs in Drosophila. Processing of the 3‘ end involves an endonucleolytic cleavage and occurs after 5‘ end maturation. Journal Of Biological Chemistry 1985, 260: 449-454. PMID: 3843841, DOI: 10.1016/s0021-9258(18)89752-6.
- Two control systems modulate the level of glutaminyl-tRNA synthetase in Escherichia coli.Cheung A, Watson L, Söll D. Two control systems modulate the level of glutaminyl-tRNA synthetase in Escherichia coli. Journal Of Bacteriology 1985, 161: 212-8. PMID: 2578447, PMCID: PMC214858, DOI: 10.1128/jb.161.1.212-218.1985.
- Functional analysis of fractionated Drosophila Kc cell tRNA gene transcription components.Burke D, Söll D. Functional analysis of fractionated Drosophila Kc cell tRNA gene transcription components. Journal Of Biological Chemistry 1985, 260: 816-823. PMID: 3844013, DOI: 10.1016/s0021-9258(20)71171-3.
- Dimeric tRNA gene arrangement in Schizosaccharomyces pombe allows increased expression of the downstream geneHottinger-Werlen A, Schaack J, Lapointe J, Mao J, Nichols M, Söll D. Dimeric tRNA gene arrangement in Schizosaccharomyces pombe allows increased expression of the downstream gene. Nucleic Acids Research 1985, 13: 8739-8747. PMID: 3936021, PMCID: PMC318948, DOI: 10.1093/nar/13.24.8739.
- [8] Glutaminyl-tRNA synthetase of Escherichia coliHoben P, Söll D. [8] Glutaminyl-tRNA synthetase of Escherichia coli. 1985, 113: 55-59. PMID: 3911010, DOI: 10.1016/s0076-6879(85)13011-9.
- A wheat HMW glutenin subunit gene reveals a highly repeated structureSugiyama T, Rafalski A, Peterson D, Söll D. A wheat HMW glutenin subunit gene reveals a highly repeated structure. Nucleic Acids Research 1985, 13: 8729-8737. PMID: 3001648, PMCID: PMC318947, DOI: 10.1093/nar/13.24.8729.
- Heptapeptide repeat structure of a wheat γ-gliadinScheets K, Rafalski J, Hedgcoth C, Söll D. Heptapeptide repeat structure of a wheat γ-gliadin. Plant Science 1985, 37: 221-225. DOI: 10.1016/0304-4211(85)90008-2.
- Nucleotide sequences of two serine tRNAs with a GGA anticodon: the structure-function relationships in the serine family of E. coli tRNAsGrosjean H, Nicoghosian K, Haumont E, Söll D, Cedergren R. Nucleotide sequences of two serine tRNAs with a GGA anticodon: the structure-function relationships in the serine family of E. coli tRNAs. Nucleic Acids Research 1985, 13: 5697-5706. PMID: 3898020, PMCID: PMC321899, DOI: 10.1093/nar/13.15.5697.
- Conservation and variability of wheat α/β-gliadin genesSumner-Smith M, Rafalski J, Sugiyama T, Stoll M, Sōll D. Conservation and variability of wheat α/β-gliadin genes. Nucleic Acids Research 1985, 13: 3905-3916. PMID: 3839304, PMCID: PMC341285, DOI: 10.1093/nar/13.11.3905.
- Transcription of a Drosophila tRNAArg gene in yeast extract: 5′-flanking sequence dependence for transcription in a heterologous systemSchaack J, Söll D. Transcription of a Drosophila tRNAArg gene in yeast extract: 5′-flanking sequence dependence for transcription in a heterologous system. Nucleic Acids Research 1985, 13: 2803-2814. PMID: 3889849, PMCID: PMC341195, DOI: 10.1093/nar/13.8.2803.
- Misaminoacylation by glutaminyl-tRNA synthetase: relaxed specificity in wild-type and mutant enzymes.Hoben P, Uemura H, Yamao F, Cheung A, Swanson R, Sumner-Smith M, Söll D. Misaminoacylation by glutaminyl-tRNA synthetase: relaxed specificity in wild-type and mutant enzymes. The FASEB Journal 1984, 43: 2972-6. PMID: 6389180.
- Transcription Factor Binding Is Limited by the 5′-Flanking Regions of a Drosophila tRNAHis Gene and a tRNAHis PseudogeneCooley L, Schaack J, Burke D, Thomas B, Söll D. Transcription Factor Binding Is Limited by the 5′-Flanking Regions of a Drosophila tRNAHis Gene and a tRNAHis Pseudogene. Molecular And Cellular Biology 1984, 4: 2714-2722. DOI: 10.1128/mcb.4.12.2714-2722.1984.
- Transcription factor binding is limited by the 5'-flanking regions of a Drosophila tRNAHis gene and a tRNAHis pseudogene.Cooley L, Schaack J, Burke DJ, Thomas B, Söll D. Transcription factor binding is limited by the 5'-flanking regions of a Drosophila tRNAHis gene and a tRNAHis pseudogene. Molecular And Cellular Biology 1984, 4: 2714-2722. PMID: 6570190, PMCID: PMC369281, DOI: 10.1128/mcb.4.12.2714.
- The sup8 tRNALeu gene of Schizosaccharomyces pombe has an unusual intervening sequence and reduced pairing in the anticodon stemSumner-Smith M, Hottinger H, Willis I, Koch T, Arentzen R, Söll D. The sup8 tRNALeu gene of Schizosaccharomyces pombe has an unusual intervening sequence and reduced pairing in the anticodon stem. Molecular Genetics And Genomics 1984, 197: 447-452. PMID: 6597338, DOI: 10.1007/bf00329941.
- Transfer RNA mischarging mediated by a mutant Escherichia coli glutaminyl-tRNA synthetase.Inokuchi H, Hoben P, Yamao F, Ozeki H, Söll D. Transfer RNA mischarging mediated by a mutant Escherichia coli glutaminyl-tRNA synthetase. Proceedings Of The National Academy Of Sciences Of The United States Of America 1984, 81: 5076-5080. PMID: 6382258, PMCID: PMC391640, DOI: 10.1073/pnas.81.16.5076.
- In vivo and in vitro transcription of the Escherichia coli glutaminyl-tRNA synthetase gene.Cheung A, Söll D. In vivo and in vitro transcription of the Escherichia coli glutaminyl-tRNA synthetase gene. Journal Of Biological Chemistry 1984, 259: 9953-9958. PMID: 6086662, DOI: 10.1016/s0021-9258(17)42791-8.
- Mutations affecting excision of the intron from a eukaryotic dimeric tRNA precursor.Willis I, Hottinger H, Pearson D, Chisholm V, Leupold U, Söll D. Mutations affecting excision of the intron from a eukaryotic dimeric tRNA precursor. The EMBO Journal 1984, 3: 1573-1580. PMID: 6430697, PMCID: PMC557561, DOI: 10.1002/j.1460-2075.1984.tb02013.x.
- Developmentally regulated plant genes: the nucleotide sequence of a wheat gliadin genomic clone.Rafalski J, Scheets K, Metzler M, Peterson D, Hedgcoth C, Söll D. Developmentally regulated plant genes: the nucleotide sequence of a wheat gliadin genomic clone. The EMBO Journal 1984, 3: 1409-15. PMID: 6204862, PMCID: PMC557531, DOI: 10.1002/j.1460-2075.1984.tb01985.x.
- The Schizosaccharomyces pombe sup3-i suppressor recognizes ochre, but not amber codons in vitro and in vivo.Hottinger H, Stadelmann B, Pearson D, Frendewey D, Kohli J, Söll D. The Schizosaccharomyces pombe sup3-i suppressor recognizes ochre, but not amber codons in vitro and in vivo. The EMBO Journal 1984, 3: 423-8. PMID: 6370683, PMCID: PMC557361, DOI: 10.1002/j.1460-2075.1984.tb01823.x.
- The extent of a eukaryotic tRNA gene. 5‘- and 3‘-flanking sequence dependence for transcription and stable complex formation.Schaack J, Sharp S, Dingermann T, Burke DJ, Cooley L, Söll D. The extent of a eukaryotic tRNA gene. 5‘- and 3‘-flanking sequence dependence for transcription and stable complex formation. Journal Of Biological Chemistry 1984, 259: 1461-1467. PMID: 6693417, DOI: 10.1016/s0021-9258(17)43429-6.
- Interallelic and intergenic conversion in three serine tRNA genes of Schizosaccharomyces pombe.Kohli J, Munz P, Aebi R, Amstutz H, Gysler C, Heyer W, Lehmann L, Schuchert P, Szankasi P, Thuriaux P, Leupold U, Bell J, Gamulin V, Hottinger H, Pearson D, Soll D. Interallelic and intergenic conversion in three serine tRNA genes of Schizosaccharomyces pombe. Cold Spring Harbor Symposia On Quantitative Biology 1984, 49: 31-40. PMID: 6597758, DOI: 10.1101/sqb.1984.049.01.006.
- Transcriptionally active and inactive gene repeats within the D. meianogaster 5S RNA gene clusterSharp S, Garcia A, Cooley L, Söll D. Transcriptionally active and inactive gene repeats within the D. meianogaster 5S RNA gene cluster. Nucleic Acids Research 1984, 12: 7617-7632. PMID: 6093044, PMCID: PMC320189, DOI: 10.1093/nar/12.20.7617.
- Partial purification of Drosophila Kc cell RNA polymerase III transcription components. Evidence for shared 5 S RNA and tRNA gene factors.Burke D, Schaack J, Sharp S, Söll D. Partial purification of Drosophila Kc cell RNA polymerase III transcription components. Evidence for shared 5 S RNA and tRNA gene factors. Journal Of Biological Chemistry 1983, 258: 15224-15231. PMID: 6197413, DOI: 10.1016/s0021-9258(17)43797-5.
- Stable transcription complex formation of eukaryotic tRNA genes is dependent on a limited separation of the two intragenic control regions.Dingermann T, Sharp S, Schaack J, Söll D. Stable transcription complex formation of eukaryotic tRNA genes is dependent on a limited separation of the two intragenic control regions. Journal Of Biological Chemistry 1983, 258: 10395-10402. PMID: 6309803, DOI: 10.1016/s0021-9258(17)44470-x.
- Preface.Roberts R, Söll D. Preface. Nucleic Acids Research 1983, 12: nil17. PMID: 16617477, PMCID: PMC321058, DOI: 10.1146/annurev.bb.12.111006.100001.
- Organization of ribosomal DNA in yellow lupine (Lupinus luteus) and sequence of the 5.8 S RNA geneRafalski J, Wiewiórowski M, Söll D. Organization of ribosomal DNA in yellow lupine (Lupinus luteus) and sequence of the 5.8 S RNA gene. FEBS Letters 1983, 152: 241-246. DOI: 10.1016/0014-5793(83)80388-3.
- Transcription of eukaryotic tRNA genes in vitro. I. Analysis of control regions using a competition assay.Sharp S, Dingermann T, Schaack J, DeFranco D, Söll D. Transcription of eukaryotic tRNA genes in vitro. I. Analysis of control regions using a competition assay. Journal Of Biological Chemistry 1983, 258: 2440-2446. PMID: 6549757, DOI: 10.1016/s0021-9258(18)32945-4.
- Transcription of eukaryotic tRNA genes in vitro. II. Formation of stable complexes.Schaack J, Sharp S, Dingermann T, Söll D. Transcription of eukaryotic tRNA genes in vitro. II. Formation of stable complexes. Journal Of Biological Chemistry 1983, 258: 2447-2453. PMID: 6549758, DOI: 10.1016/s0021-9258(18)32946-6.
- The structure and regulation of Escherichia coli glutaminyl-tRNA synthetase.Cheung A, Hoben P, Inokuchi H, Ozeki H, Sumner-Smith M, Swanson R, Uemura H, Yamao F, Söll D. The structure and regulation of Escherichia coli glutaminyl-tRNA synthetase. Nucleic Acids Symposium Series 1983, 221-2. PMID: 6364044.
- PrefaceRoberts R, Söll D. Preface. 1983, 12: ix. PMID: 16617476, PMCID: PMC320978, DOI: 10.1016/s0099-5428(08)60161-6.
- Organization and Expression of tRNA Genes in Drosophila MelanogasterSharp S, Cooley L, DeFranco D, Dingermann T, Söll D. Organization and Expression of tRNA Genes in Drosophila Melanogaster. 1983, 84: 1-14. PMID: 6405456, DOI: 10.1007/978-3-642-81947-6_1.
- Each element of the Drosophila tRNA Arg gene split promoter directs transcription in Xenopus oocytesSharp S, Dingermann T, Schaack J, Sharp J, Burke D, DeRobertis E, Söll D. Each element of the Drosophila tRNA Arg gene split promoter directs transcription in Xenopus oocytes. Nucleic Acids Research 1983, 11: 8677-8690. PMID: 6561520, PMCID: PMC326616, DOI: 10.1093/nar/11.24.8677.
- Six Schizosaccharomyces pombe tRNA genes including a gene for a tRNA Lys with an intervening sequence which cannot base-pair with the anticodonGamulin V, Mao J, Appel B, Sumner-Smith M, Yamao F, Söll D. Six Schizosaccharomyces pombe tRNA genes including a gene for a tRNA Lys with an intervening sequence which cannot base-pair with the anticodon. Nucleic Acids Research 1983, 11: 8537-8546. PMID: 6561518, PMCID: PMC326605, DOI: 10.1093/nar/11.24.8537.
- The 5- flanking sequences of Drosophila tRNAArg genes control their in vitro transcription in a Drosophila cell extract.Dingermann T, Burke D, Sharp S, Schaack J, Söll D. The 5- flanking sequences of Drosophila tRNAArg genes control their in vitro transcription in a Drosophila cell extract. Journal Of Biological Chemistry 1982, 257: 14738-14744. PMID: 6924656, DOI: 10.1016/s0021-9258(18)33342-8.
- Nonsense suppression in Schizosaccharomyces pombe: The S. pombe Sup3-e tRNASerUGA gene is active in S. cerevisiaeHottinger H, Pearson D, Yamao F, Gamulin V, Colley L, Cooper T, Söll D. Nonsense suppression in Schizosaccharomyces pombe: The S. pombe Sup3-e tRNASerUGA gene is active in S. cerevisiae. Molecular Genetics And Genomics 1982, 188: 219-224. PMID: 6818425, DOI: 10.1007/bf00332678.
- Post-transcriptional nucleotide addition is responsible for the formation of the 5' terminus of histidine tRNA.Cooley L, Appel B, Söll D. Post-transcriptional nucleotide addition is responsible for the formation of the 5' terminus of histidine tRNA. Proceedings Of The National Academy Of Sciences Of The United States Of America 1982, 79: 6475-6479. PMID: 6292903, PMCID: PMC347149, DOI: 10.1073/pnas.79.21.6475.
- Escherichia coli glutaminyl-tRNA synthetase. I. Isolation and DNA sequence of the glnS gene.Yamao F, Inokuchi H, Cheung A, Ozeki H, Söll D. Escherichia coli glutaminyl-tRNA synthetase. I. Isolation and DNA sequence of the glnS gene. Journal Of Biological Chemistry 1982, 257: 11639-11643. PMID: 6288695, DOI: 10.1016/s0021-9258(18)33810-9.
- Escherichia coli glutaminyl-tRNA synthetase. II. Characterization of the glnS gene product.Hoben P, Royal N, Cheung A, Yamao F, Biemann K, Söll D. Escherichia coli glutaminyl-tRNA synthetase. II. Characterization of the glnS gene product. Journal Of Biological Chemistry 1982, 257: 11644-11650. PMID: 6749844, DOI: 10.1016/s0021-9258(18)33811-0.
- Arrangement of the ribosomal RNA genes in Schizosaccharomyces pombeBarnitz J, Cramer J, Rownd R, Cooley L, Söll D. Arrangement of the ribosomal RNA genes in Schizosaccharomyces pombe. FEBS Letters 1982, 143: 129-132. PMID: 6288447, DOI: 10.1016/0014-5793(82)80288-3.
- Recent developments in the chemical synthesis of polynucleotidesOhtsuka E, Ikehara M, Söll D. Recent developments in the chemical synthesis of polynucleotides. Nucleic Acids Research 1982, 10: 6553-6570. PMID: 6757865, PMCID: PMC326948, DOI: 10.1093/nar/10.21.6553.
- Eukaryotic tRNA gene transcription is controlled by signals within and outside the mature coding sequence.DeFranco D, Dingermann T, Johnson D, Sharp S, Söll D. Eukaryotic tRNA gene transcription is controlled by signals within and outside the mature coding sequence. Princess Takamatsu Symposia 1982, 12: 63-72. PMID: 7166550.
- CONCLUDING REMARKSSöLL D. CONCLUDING REMARKS. 1982, 515-517. DOI: 10.1016/b978-0-444-00760-5.50041-1.
- STRUCTURE AND REGULATION OF E. COLI GLUTAMINYL-tRNA SYNTHETASECHEUNG A, HOBEN P, MORGAN S, YAMAO F, SöLL D, LOW K, ROYAL N. STRUCTURE AND REGULATION OF E. COLI GLUTAMINYL-tRNA SYNTHETASE. 1982, 57-68. DOI: 10.1016/b978-0-444-00760-5.50009-5.
- The minimum intragenic sequences required for promotion of eukaryotic tRNA gene transcriptionSharp S, Dingermann T, Söll D. The minimum intragenic sequences required for promotion of eukaryotic tRNA gene transcription. Nucleic Acids Research 1982, 10: 5393-5406. PMID: 6924209, PMCID: PMC320884, DOI: 10.1093/nar/10.18.5393.
- Organization and nucleotide sequence of nuclear 5S rRNA genes in yellow lupin ( Lupinus lutens )Rafalski J, Wiewiorowski M, SÖll D. Organization and nucleotide sequence of nuclear 5S rRNA genes in yellow lupin ( Lupinus lutens ). Nucleic Acids Research 1982, 10: 7635-7642. PMID: 7155897, PMCID: PMC327035, DOI: 10.1093/nar/10.23.7635.
- 18 RNA MethylationSöll D, Kline L. 18 RNA Methylation. 1982, 15: 557-566. DOI: 10.1016/s1874-6047(08)60290-5.
- THE IN VITRO TRANSCRIPTION OF DROSOPHILA tRNA GENESDingermann T, Sharp S, Schaack J, DeFranco D, Johnson D, Cooley L, Söll D. THE IN VITRO TRANSCRIPTION OF DROSOPHILA tRNA GENES. 1982, 219-234. DOI: 10.1016/b978-0-12-525960-6.50021-3.
- Genes for tRNA 5Lys from Drosophila melanogasterDeFranco D, Burke K, Hayashi S, Tener G, Miller R, Söll D. Genes for tRNA 5Lys from Drosophila melanogaster. Nucleic Acids Research 1982, 10: 5799-5808. PMID: 6292853, PMCID: PMC320931, DOI: 10.1093/nar/10.19.5799.
- The 5S RNA genes of Schizosaccharomyces pombeMao J, Appel B, Schaack J, Sharp S, Yamada H, Söll D. The 5S RNA genes of Schizosaccharomyces pombe. Nucleic Acids Research 1982, 10: 487-500. PMID: 6278416, PMCID: PMC326152, DOI: 10.1093/nar/10.2.487.
- E. coli initiator tRNA analogs with different nucleotides in the discriminator base positionUemura H, Imai M, Ohtsuka E, Ikehara M, Söll D. E. coli initiator tRNA analogs with different nucleotides in the discriminator base position. Nucleic Acids Research 1982, 10: 6531-6539. PMID: 6294608, PMCID: PMC326942, DOI: 10.1093/nar/10.20.6531.
- The 5.8S RNA gene sequence and the ribosomal repeat of Schizosaccharomyces pombeSchaak J, Mao J, Söll D. The 5.8S RNA gene sequence and the ribosomal repeat of Schizosaccharomyces pombe. Nucleic Acids Research 1982, 10: 2851-2864. PMID: 6285312, PMCID: PMC320660, DOI: 10.1093/nar/10.9.2851.
- 19 Nucleotide Modification in RNAKline L, Söll D. 19 Nucleotide Modification in RNA. 1982, 15: 567-582. DOI: 10.1016/s1874-6047(08)60291-7.
- Identification of regulatory sequences contained in the 5'-flanking region of Drosophila lysine tRNA2 genes.DeFranco D, Sharp S, Söll D. Identification of regulatory sequences contained in the 5'-flanking region of Drosophila lysine tRNA2 genes. Journal Of Biological Chemistry 1981, 256: 12424-12429. PMID: 6913581, DOI: 10.1016/s0021-9258(18)43290-5.
- Internal control regions for transcription of eukaryotic tRNA genes.Sharp S, DeFranco D, Dingermann T, Farrell P, Söll D. Internal control regions for transcription of eukaryotic tRNA genes. Proceedings Of The National Academy Of Sciences Of The United States Of America 1981, 78: 6657-6661. PMID: 6947245, PMCID: PMC349108, DOI: 10.1073/pnas.78.11.6657.
- Gene Expression- The Production of RNA's Cell Biology: A Comprehensive Treatise, Volume 3. Lester Goldstein , David M. PrescottSoll D. Gene Expression- The Production of RNA's Cell Biology: A Comprehensive Treatise, Volume 3. Lester Goldstein , David M. Prescott. The Quarterly Review Of Biology 1981, 56: 333-334. DOI: 10.1086/412354.
- Preface.Roberts R, Söll D. Preface. Nucleic Acids Research 1981, 10: nil15. PMID: 16617472, PMCID: PMC326107, DOI: 10.1146/annurev.bb.10.111006.100001.
- Partial purification of RNase P from Schizosaccharomyces pombe.Kline L, Nishikawa S, Söll D. Partial purification of RNase P from Schizosaccharomyces pombe. Journal Of Biological Chemistry 1981, 256: 5058-5063. PMID: 6262315, DOI: 10.1016/s0021-9258(19)69366-x.
- Transcription of cloned tRNA and 5S RNA genes in a Drosophila cell free extractDingermann T, Sharp S, Appel B, DeFranco D, Mount S, Heiermann R, Pongs O, Söll D. Transcription of cloned tRNA and 5S RNA genes in a Drosophila cell free extract. Nucleic Acids Research 1981, 9: 3907-3918. PMID: 6170932, PMCID: PMC327404, DOI: 10.1093/nar/9.16.3907.
- A conversational system for the computer analysis of nucleic acid sequencesSege R, Söll D, Ruddle F, Queen C. A conversational system for the computer analysis of nucleic acid sequences. Nucleic Acids Research 1981, 9: 437-444. PMID: 6163137, PMCID: PMC326703, DOI: 10.1093/nar/9.2.437.
- The initiator tRNA genes of Drosophila melanogaster: evidence for a tRNA pseudogeneSharp S, DeFranco D, Silberklang M, Hosbach H, Schmidt T, Kubli E, Gergen J, Wensink P, Söll D. The initiator tRNA genes of Drosophila melanogaster: evidence for a tRNA pseudogene. Nucleic Acids Research 1981, 9: 5867-5882. PMID: 6273811, PMCID: PMC327570, DOI: 10.1093/nar/9.22.5867.
- ARRANGEMENT AND TRANSCRIPTION OF EUKARYOTIC tRNA GENES11This work was supported by grants from the National Institutes of Health and from the National Science Foundation.Schmidt O, Sharp S, Mao J, DeFranco D, Söll D. ARRANGEMENT AND TRANSCRIPTION OF EUKARYOTIC tRNA GENES11This work was supported by grants from the National Institutes of Health and from the National Science Foundation. 1981, 61-85. DOI: 10.1016/b978-0-12-641820-0.50008-x.
- Dimeric tRNA precursors in yeastSchmidt O, Mao J, Ogden R, Beckmann J, Sakano H, Abelson J, Söll D. Dimeric tRNA precursors in yeast. Nature 1980, 287: 750-752. PMID: 6253814, DOI: 10.1038/287750a0.
- Dimeric transfer RNA precursors in S. pombeMao J, Schmidt O, Söll D. Dimeric transfer RNA precursors in S. pombe. Cell 1980, 21: 509-516. PMID: 7407924, DOI: 10.1016/0092-8674(80)90488-2.
- Two control regions for eukaryotic tRNA gene transcription.DeFranco D, Schmidt O, Söll D. Two control regions for eukaryotic tRNA gene transcription. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 3365-3368. PMID: 6774336, PMCID: PMC349616, DOI: 10.1073/pnas.77.6.3365.
- Analysis of a drosophila tRNA gene clusterHovemann B, Sharp S, Yamada H, Söll D. Analysis of a drosophila tRNA gene cluster. Cell 1980, 19: 889-895. PMID: 6769590, DOI: 10.1016/0092-8674(80)90080-x.
- IN VITRO TRANSCRIPTION OF CLONED EUKARYOTIC tRNA GENESSchmidt O, Hovemann B, Silverman S, Yamada H, Mao J, Söll D. IN VITRO TRANSCRIPTION OF CLONED EUKARYOTIC tRNA GENES. 1980, 179-188. DOI: 10.1016/b978-0-08-024417-4.50021-4.
- Regulation of biosynthesis of aminoacyl-transfer RNA synthetases and of transfer-RNA in Escherichia coli.Morgan S, Larossa R, Cheung A, Low B, Söll D. Regulation of biosynthesis of aminoacyl-transfer RNA synthetases and of transfer-RNA in Escherichia coli. Biological Research 1979, 12: 415-26. PMID: 45219.
- The nucleotide sequence of a cloned Drosophila arginine tRNA gene and its in vitro transcription in Xenopus germinal vesicle extracts.Silverman S, Schmidt O, Söll D, Hovemann B. The nucleotide sequence of a cloned Drosophila arginine tRNA gene and its in vitro transcription in Xenopus germinal vesicle extracts. Journal Of Biological Chemistry 1979, 254: 10290-10294. PMID: 114522, DOI: 10.1016/s0021-9258(19)86707-8.
- Regulation of the biosynthesis of aminoacyl-transfer ribonucleic acid synthetases and of transfer ribonucleic acid in Escherichia coli. VI. Mutants with increased levels of glutaminyl-transfer ribonucleic acid synthetase and of glutamine transfer ribonucleic acid.Cheung A, Morgan S, Low K, Söll D. Regulation of the biosynthesis of aminoacyl-transfer ribonucleic acid synthetases and of transfer ribonucleic acid in Escherichia coli. VI. Mutants with increased levels of glutaminyl-transfer ribonucleic acid synthetase and of glutamine transfer ribonucleic acid. Journal Of Bacteriology 1979, 139: 176-84. PMID: 378954, PMCID: PMC216843, DOI: 10.1128/jb.139.1.176-184.1979.
- Regulation of the biosynthesis of aminoacyl-transfer ribonucleic acid synthetases and of transfer ribonucleic acid in Escherichia coli. V. Mutants with increased levels of valyl-transfer ribonucleic acid synthetase.Baer M, Low K, Söll D. Regulation of the biosynthesis of aminoacyl-transfer ribonucleic acid synthetases and of transfer ribonucleic acid in Escherichia coli. V. Mutants with increased levels of valyl-transfer ribonucleic acid synthetase. Journal Of Bacteriology 1979, 139: 165-75. PMID: 378953, PMCID: PMC216842, DOI: 10.1128/jb.139.1.165-175.1979.
- Aminoacyl-tRNA Synthetases: General Features and Recognition of Transfer RNAsSchimmel P, Söll D. Aminoacyl-tRNA Synthetases: General Features and Recognition of Transfer RNAs. Annual Review Of Biochemistry 1979, 48: 601-648. PMID: 382994, DOI: 10.1146/annurev.bi.48.070179.003125.
- In vitro transcription and processing of a yeast tRNA gene containing an intervening sequenceOgden R, Beckman J, Abelson J, Kang H, Söll D, Schmidt O. In vitro transcription and processing of a yeast tRNA gene containing an intervening sequence. Cell 1979, 17: 399-406. PMID: 378410, DOI: 10.1016/0092-8674(79)90166-1.
- Characterization of a UGA-suppressing serine tRNA from Schizosaccharomyces pombe with the help of a new in vitro assay system for eukaryotic suppressor tRNAs.Kohli J, Kwong T, Altruda F, Söll D, Wahl G. Characterization of a UGA-suppressing serine tRNA from Schizosaccharomyces pombe with the help of a new in vitro assay system for eukaryotic suppressor tRNAs. Journal Of Biological Chemistry 1979, 254: 1546-1551. PMID: 762155, DOI: 10.1016/s0021-9258(17)37806-7.
- Glutamyl-γ-methyl ester acts as a methionine analogue in Escherichia coli: analogue resistant mutants map at the metJ and metK lociKraus J, Soll D, Low K. Glutamyl-γ-methyl ester acts as a methionine analogue in Escherichia coli: analogue resistant mutants map at the metJ and metK loci. Genetics Research 1979, 33: 49-55. PMID: 383574, DOI: 10.1017/s0016672300018152.
- The nucleotide sequence of the initiator tRNA from Drosophila melanogasterSilverman S, Heckman J, Cowling G, Delaney A, Dunn R, Gillani I, Tener G, Söll D, RajBhandary U. The nucleotide sequence of the initiator tRNA from Drosophila melanogaster. Nucleic Acids Research 1979, 6: 421-434. PMID: 106370, PMCID: PMC327704, DOI: 10.1093/nar/6.2.421.
- ERRATUMWong T, McCutchan T, Kohli J, Söll D. ERRATUM. Nucleic Acids Research 1979, 7: 289-289. DOI: 10.1093/nar/7.1.289.
- The nucleotide sequence of the major glutamate transfer RNA from Schizosaccharomyces pombeWong T, McCutchan T, Kohli J, Söll D. The nucleotide sequence of the major glutamate transfer RNA from Schizosaccharomyces pombe. Nucleic Acids Research 1979, 6: 2057-2068. PMID: 379816, PMCID: PMC327836, DOI: 10.1093/nar/6.6.2057.
- The nucleotide sequence of lysine tRNA 2 from DrosophilaSilverman S, Gillam I, Tener G, Söll D. The nucleotide sequence of lysine tRNA 2 from Drosophila. Nucleic Acids Research 1979, 6: 435-442. PMID: 106371, PMCID: PMC327705, DOI: 10.1093/nar/6.2.435.
- Specific chemical labeling of DNA fragmentsEshaghpour H, Söll D, Crothers D. Specific chemical labeling of DNA fragments. Nucleic Acids Research 1979, 7: 1485-1495. PMID: 228251, PMCID: PMC342322, DOI: 10.1093/nar/7.6.1485.
- Regulation of the biosynthesis of aminoacyl-tRNA synthetases and of tRNA in Escherichia coliTheall G, Low K, Söll D. Regulation of the biosynthesis of aminoacyl-tRNA synthetases and of tRNA in Escherichia coli. Molecular Genetics And Genomics 1979, 169: 205-211. PMID: 375009, DOI: 10.1007/bf00271672.
- SuppressionSteege D, Söll D. Suppression. 1979, 433-485. DOI: 10.1007/978-1-4684-3417-0_11.
- Identification and nucleotide sequence of the sup8-e UGA-suppressor leucine tRNA from Schizosaccharomyces pombeWetzel R, Kohli J, Altruda F, Söll D. Identification and nucleotide sequence of the sup8-e UGA-suppressor leucine tRNA from Schizosaccharomyces pombe. Molecular Genetics And Genomics 1979, 172: 221-228. PMID: 289895, DOI: 10.1007/bf00268286.
- The nucleotide sequence of a UGA suppressor serine tRNA from Schizosaccharomyces pombeRafalski A, Kohli J, Agris P, Söll D. The nucleotide sequence of a UGA suppressor serine tRNA from Schizosaccharomyces pombe. Nucleic Acids Research 1979, 6: 2683-2695. PMID: 461200, PMCID: PMC327885, DOI: 10.1093/nar/6.8.2683.
- Specific transcription of eukaryotic tRNA genes in Xenopus germinal vesicle extracts.Schmidt O, Mao J, Silverman S, Hovemann B, Söll D. Specific transcription of eukaryotic tRNA genes in Xenopus germinal vesicle extracts. Proceedings Of The National Academy Of Sciences Of The United States Of America 1978, 75: 4819-4823. PMID: 105357, PMCID: PMC336212, DOI: 10.1073/pnas.75.10.4819.
- Nucleotide sequence of phenylalanine transfer RNA from Schizosaccharomyces pombe: implications for transfer RNA recognition by yeast phenylalanyl-tRNA synthetase.McCutchan T, Silverman S, Kohli J, Soell D. Nucleotide sequence of phenylalanine transfer RNA from Schizosaccharomyces pombe: implications for transfer RNA recognition by yeast phenylalanyl-tRNA synthetase. Biochemistry 1978, 17: 1622-8. PMID: 247991, DOI: 10.1021/bi00602a007.
- Regulation of the Biosynthesis of Aminoacid:tRNA Ligases and of †RNAMorgan S, Söll D. Regulation of the Biosynthesis of Aminoacid:tRNA Ligases and of †RNA. 1978, 21: 181-207. PMID: 358278, DOI: 10.1016/s0079-6603(08)60270-6.
- Regulation of biosynthesis of aminoacyl-tRNA synthetases and of tRNA in Escherichia coli I. Isolation and characterization of a mutant with elevated levels of tRNAGln1Morgan S, Körner A, Low K, Söll D. Regulation of biosynthesis of aminoacyl-tRNA synthetases and of tRNA in Escherichia coli I. Isolation and characterization of a mutant with elevated levels of tRNAGln1. Journal Of Molecular Biology 1977, 117: 1013-1031. PMID: 24122, DOI: 10.1016/s0022-2836(77)80010-7.
- Regulation of biosynthesis of aminoacyl-tRNA synthetases and of tRNA in Escherichia coli II. Isolation of regulatory mutants affecting leucyl-tRNA synthetase levelsLaRossa R, Vögeli G, Low K, Söll D. Regulation of biosynthesis of aminoacyl-tRNA synthetases and of tRNA in Escherichia coli II. Isolation of regulatory mutants affecting leucyl-tRNA synthetase levels. Journal Of Molecular Biology 1977, 117: 1033-1048. PMID: 342703, DOI: 10.1016/s0022-2836(77)80011-9.
- Regulation of biosynthesis of aminoacyl-tRNA synthetases and of tRNA in Escherichia coli III. Biochemical characterization of regulatory mutants affecting leucyl-tRNA synthetase levelsLaRossa R, Mao J, Low K, Söll D. Regulation of biosynthesis of aminoacyl-tRNA synthetases and of tRNA in Escherichia coli III. Biochemical characterization of regulatory mutants affecting leucyl-tRNA synthetase levels. Journal Of Molecular Biology 1977, 117: 1049-1059. PMID: 342704, DOI: 10.1016/s0022-2836(77)80012-0.
- Isolation of Escherichia coli precursor tRNAs containing modified nucleoside Q.Vögeli G, Stewart T, McCutchan T, Söll D. Isolation of Escherichia coli precursor tRNAs containing modified nucleoside Q. Journal Of Biological Chemistry 1977, 252: 2311-2318. PMID: 321455, DOI: 10.1016/s0021-9258(17)40556-4.
- Studies of the complex between transfer RNA's with complementary anticodons : a direct approach to the "wobble" problem [proceedings].Grosjean H, Söll D, Crothers D. Studies of the complex between transfer RNA's with complementary anticodons : a direct approach to the "wobble" problem [proceedings]. Archives Of Physiology And Biochemistry 1977, 85: 414-5. PMID: 71115.
- Analogs of methionyl-tRNA synthetase substrates containing photolabile groupsWetzel R, Soöll D. Analogs of methionyl-tRNA synthetase substrates containing photolabile groups. Nucleic Acids Research 1977, 4: 1681-1694. PMID: 331263, PMCID: PMC343781, DOI: 10.1093/nar/4.5.1681.
- A rapid method for preparation of calf spleen exonucleaseSilverman S, Sōll D. A rapid method for preparation of calf spleen exonuclease. Nucleic Acids Research 1977, 4: 3511-3517. PMID: 200894, PMCID: PMC342668, DOI: 10.1093/nar/4.10.3511.
- The Modified Nucleosides in Transfer RNAAGRIS P, SÖLL D. The Modified Nucleosides in Transfer RNA. 1977, 321-344. DOI: 10.1016/b978-0-12-722560-9.50024-x.
- Suppression of a defective alanyl-tRNA synthetase in Escherichia coli: A compensatory mutation to high alanine affinityTheall G, Low K, Söll D. Suppression of a defective alanyl-tRNA synthetase in Escherichia coli: A compensatory mutation to high alanine affinity. Molecular Genetics And Genomics 1977, 156: 221-227. PMID: 340903, DOI: 10.1007/bf00283495.
- The nucleotide sequence of asparagine tRNA from Escherichia coliOhashi K, Harada F, Ohashi Z, Nishimura S, Stewart T, Vögeli G, McCutchan T, Söll D. The nucleotide sequence of asparagine tRNA from Escherichia coli. Nucleic Acids Research 1976, 3: 3369-3376. PMID: 794837, PMCID: PMC343181, DOI: 10.1093/nar/3.12.3369.
- Studies of the complex between transfer RNAs with complementary anticodons I. Origins of enhanced affinity between complementary tripletsGrosjean H, Söll D, Crothers D. Studies of the complex between transfer RNAs with complementary anticodons I. Origins of enhanced affinity between complementary triplets. Journal Of Molecular Biology 1976, 103: 499-519. PMID: 781277, DOI: 10.1016/0022-2836(76)90214-x.
- Proceedings: Studies of the complex between transfer RNA'S with complementary anticodons: origins of enhanced affinity between complementary triplets.Grosjean H, Söll D, Crothers D. Proceedings: Studies of the complex between transfer RNA'S with complementary anticodons: origins of enhanced affinity between complementary triplets. Archives Of Physiology And Biochemistry 1976, 84: 163-4. PMID: 60940.
- Studies of the complex between transfer RNA molecules and complementary anticodons: kinetic and thermodynamic aspects.Grosjean H, Söll D, Crothers D. Studies of the complex between transfer RNA molecules and complementary anticodons: kinetic and thermodynamic aspects. Archives Of Physiology And Biochemistry 1975, 83: 970-1. PMID: 58627.
- A method for the isolation of specific tRNA precursors.Vögeli G, Grosjean H, Söll D. A method for the isolation of specific tRNA precursors. Proceedings Of The National Academy Of Sciences Of The United States Of America 1975, 72: 4790-4794. PMID: 1108001, PMCID: PMC388817, DOI: 10.1073/pnas.72.12.4790.
- Isolation and partial characterization of three Escherichia coli mutants with altered transfer ribonucleic acid methylases.Marinus M, Morris N, Söll D, Kwong T. Isolation and partial characterization of three Escherichia coli mutants with altered transfer ribonucleic acid methylases. Journal Of Bacteriology 1975, 122: 257-65. PMID: 1091626, PMCID: PMC235665, DOI: 10.1128/jb.122.1.257-265.1975.
- Maturation of a hypermodified nucleoside in transfer RNAAgris P, Armstrong D, Schäfer K, Söll D. Maturation of a hypermodified nucleoside in transfer RNA. Nucleic Acids Research 1975, 2: 691-699. PMID: 49880, PMCID: PMC343621, DOI: 10.1093/nar/2.5.691.
- An Improved method for the purification of tRNA by chromatography on dlhydroxyboryl substituted celluloseMcCutchan T, Gilham P, Söll D. An Improved method for the purification of tRNA by chromatography on dlhydroxyboryl substituted cellulose. Nucleic Acids Research 1975, 2: 853-864. PMID: 1096084, PMCID: PMC343472, DOI: 10.1093/nar/2.6.853.
- Bacteriophage λ induction causes increased production of E. coli lysine transfer RNAKwong T, Steege D, Lawler D, Söll D. Bacteriophage λ induction causes increased production of E. coli lysine transfer RNA. Archives Of Biochemistry And Biophysics 1975, 170: 651-658. PMID: 1103738, DOI: 10.1016/0003-9861(75)90161-7.
- The phenylalanine tRNA from Mycoplasma sp. (Kid): a tRNA lacking hypermodified nucleosides functional in protein synthesis.Kimball M, Soll D. The phenylalanine tRNA from Mycoplasma sp. (Kid): a tRNA lacking hypermodified nucleosides functional in protein synthesis. Nucleic Acids Research 1974, 1: 1713-20. PMID: 4615304, PMCID: PMC343450.
- Nuclear magnetic resonance studies of protein-nucleic acid interactions II. The E. coli tRNAGlu complex with glutamyl-tRNA synthetaseShulman R, Hilbers C, Söll D, Yang S. Nuclear magnetic resonance studies of protein-nucleic acid interactions II. The E. coli tRNAGlu complex with glutamyl-tRNA synthetase. Journal Of Molecular Biology 1974, 90: 609-611. PMID: 4615173, DOI: 10.1016/0022-2836(74)90238-1.
- Isolation and partial characterization of a temperature-sensitive Escherichia coli mutant with altered glutaminyl-transfer ribonucleic acid synthetase.Körner A, Magee B, Liska B, Low K, Adelberg E, Söll D. Isolation and partial characterization of a temperature-sensitive Escherichia coli mutant with altered glutaminyl-transfer ribonucleic acid synthetase. Journal Of Bacteriology 1974, 120: 154-8. PMID: 4153616, PMCID: PMC245744, DOI: 10.1128/jb.120.1.154-158.1974.
- New aspects in tRNA biosynthesisSchäfer K, Söll D. New aspects in tRNA biosynthesis. Biochimie 1974, 56: 795-804. PMID: 4614860, DOI: 10.1016/s0300-9084(74)80500-6.
- Covalent attachment of fluorescent groups to transfer ribonucleic acid. Reactions with 4-bromomethyl-7-methoxy-2-oxo-2H-benzopyran.Yang C, Soell D. Covalent attachment of fluorescent groups to transfer ribonucleic acid. Reactions with 4-bromomethyl-7-methoxy-2-oxo-2H-benzopyran. Biochemistry 1974, 13: 3615-21. PMID: 4367729, DOI: 10.1021/bi00714a033.
- Studies of Transfer RNA Tertiary Structure by Singlet-Singlet Energy TransferYang C, Söll D. Studies of Transfer RNA Tertiary Structure by Singlet-Singlet Energy Transfer. Proceedings Of The National Academy Of Sciences Of The United States Of America 1974, 71: 2838-2842. PMID: 4527991, PMCID: PMC388567, DOI: 10.1073/pnas.71.7.2838.
- Involvement of the anticodon region of Escherichia coli tRNAGln and tRNAGlu in the specific interaction with cognate aminoacyl-tRNA synthetase Alteration of the 2-thiouridine derivatives located in the anticodon of the tRNAs by BrCN or sulfur deprivationSeno T, Agris P, Söll D. Involvement of the anticodon region of Escherichia coli tRNAGln and tRNAGlu in the specific interaction with cognate aminoacyl-tRNA synthetase Alteration of the 2-thiouridine derivatives located in the anticodon of the tRNAs by BrCN or sulfur deprivation. Biochimica Et Biophysica Acta 1974, 349: 328-338. PMID: 4366808, DOI: 10.1016/0005-2787(74)90120-8.
- N‐(purin‐6‐ylcarbamoyl)threonine: Biosynthesis in vitro in transfer RNA by an enzyme purified from Escherichia coliKörner A, Söll D. N‐(purin‐6‐ylcarbamoyl)threonine: Biosynthesis in vitro in transfer RNA by an enzyme purified from Escherichia coli. FEBS Letters 1974, 39: 301-306. PMID: 4604806, DOI: 10.1016/0014-5793(74)80135-3.
- Fingerprinting nonradioactive ribonucleic acid with the aid of polynucleotide phosphorylaseSzeto K, Söll D. Fingerprinting nonradioactive ribonucleic acid with the aid of polynucleotide phosphorylase. Nucleic Acids Research 1974, 1: 171-182. PMID: 10793669, PMCID: PMC343333, DOI: 10.1093/nar/1.1.171.
- Sequence studies of nonradioactive Mycoplasma tRNA Phe with the aid of polynucleotide phosphorylase and polynucleotide kinaseSzeto K, Söll D. Sequence studies of nonradioactive Mycoplasma tRNA Phe with the aid of polynucleotide phosphorylase and polynucleotide kinase. Nucleic Acids Research 1974, 1: 1733-1738. PMID: 4449733, PMCID: PMC343452, DOI: 10.1093/nar/1.12.1733.
- 15. Aminoacyl-tRNA SynthetasesSöll D, Schimmel P. 15. Aminoacyl-tRNA Synthetases. 1974, 10: 489-538. DOI: 10.1016/s1874-6047(08)60147-x.
- Nucleotide Modification In Vitro of the Precursor of Transfer RNATyr of Escherichia coliSchaefer K, Altman S, Söll D. Nucleotide Modification In Vitro of the Precursor of Transfer RNATyr of Escherichia coli. Proceedings Of The National Academy Of Sciences Of The United States Of America 1973, 70: 3626-3630. PMID: 4587257, PMCID: PMC427294, DOI: 10.1073/pnas.70.12.3626.
- Biological function of 2-thiouridine in Escherichia coli glutamic acid transfer ribonucleic acid.Agris P, Soell D, Seno T. Biological function of 2-thiouridine in Escherichia coli glutamic acid transfer ribonucleic acid. Biochemistry 1973, 12: 4331-7. PMID: 4584321, DOI: 10.1021/bi00746a005.
- Guidelines for DNA Hybrid MoleculesSinger M, Soll D. Guidelines for DNA Hybrid Molecules. Science 1973, 181: 1114-1120. DOI: 10.1126/science.181.4105.1114-a.
- Guidelines for DNA Hybrid MoleculesSinger M, Soll D. Guidelines for DNA Hybrid Molecules. Science 1973, 181: 1114-1114. DOI: 10.1126/science.181.4105.1114.a.
- Covalent attachment of a fluorescent group to 4-thiouridine in transfer RNA.YANG C, SÖLL D. Covalent attachment of a fluorescent group to 4-thiouridine in transfer RNA. The Journal Of Biochemistry 1973, 73: 1243-7. PMID: 4579541, DOI: 10.1093/oxfordjournals.jbchem.a130197.
- NUCLEIC ACIDSSinger M, Söll D, Leder P, Gefter M. NUCLEIC ACIDS. Photochemistry And Photobiology 1973, 17: 356-356. DOI: 10.1111/j.1751-1097.1973.tb06366.x.
- Covalent attachment of fluorescent groups to the 5′-end of transfer RNAYang C, Söll D. Covalent attachment of fluorescent groups to the 5′-end of transfer RNA. Archives Of Biochemistry And Biophysics 1973, 155: 70-81. PMID: 4351348, DOI: 10.1016/s0003-9861(73)80010-4.
- The effect of growth temperatures on the in vivo ribose methylation of Bacillus stearothermophilus transfer RNAAgris P, Koh H, Söll D. The effect of growth temperatures on the in vivo ribose methylation of Bacillus stearothermophilus transfer RNA. Archives Of Biochemistry And Biophysics 1973, 154: 277-282. PMID: 4689778, DOI: 10.1016/0003-9861(73)90058-1.
- Leucine tRNA1 from HisT mutant of Salmonella typhimurium lacks two pseudouridinesAllaudeen H, Yang S, Söll D. Leucine tRNA1 from HisT mutant of Salmonella typhimurium lacks two pseudouridines. FEBS Letters 1972, 28: 205-208. PMID: 11946859, DOI: 10.1016/0014-5793(72)80713-0.
- Is There a Discriminator Site in Transfer RNA?Crothers D, Seno T, Söll D. Is There a Discriminator Site in Transfer RNA? Proceedings Of The National Academy Of Sciences Of The United States Of America 1972, 69: 3063-3067. PMID: 4562753, PMCID: PMC389707, DOI: 10.1073/pnas.69.10.3063.
- Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli I. PURIFICATION AND PROPERTIESLapointe J, Söll D. Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli I. PURIFICATION AND PROPERTIES. Journal Of Biological Chemistry 1972, 247: 4966-4974. PMID: 4341531, DOI: 10.1016/s0021-9258(19)44925-9.
- Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli II. INTERACTION WITH INTACT GLUTAMYL TRANSFER RIBONUCLEIC ACIDLapointe J, Söll D. Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli II. INTERACTION WITH INTACT GLUTAMYL TRANSFER RIBONUCLEIC ACID. Journal Of Biological Chemistry 1972, 247: 4975-4981. PMID: 4341532, DOI: 10.1016/s0021-9258(19)44926-0.
- Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli III. INFLUENCE OF THE 46K PROTEIN ON THE AFFINITY OF THE 56K GLUTAMYL TRANSFER RIBONUCLEIC ACID SYNTHETASE FOR ITS SUBSTRATESLapointe J, Söll D. Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli III. INFLUENCE OF THE 46K PROTEIN ON THE AFFINITY OF THE 56K GLUTAMYL TRANSFER RIBONUCLEIC ACID SYNTHETASE FOR ITS SUBSTRATES. Journal Of Biological Chemistry 1972, 247: 4982-4985. PMID: 4560497, DOI: 10.1016/s0021-9258(19)44927-2.
- Properties of a dimer of tRNA I Tyr 1 (Escherichia coli).Yang S, Söll D, Crothers D. Properties of a dimer of tRNA I Tyr 1 (Escherichia coli). Biochemistry 1972, 11: 2311-20. PMID: 4555033, DOI: 10.1021/bi00762a016.
- Investigation of adenovirus-directed 4S RNAKline L, Weissman S, Söll D. Investigation of adenovirus-directed 4S RNA. Virology 1972, 48: 291-296. PMID: 5017153, DOI: 10.1016/0042-6822(72)90142-0.
- N6 - (Δ2 - Isopentenyl) Adenosine: Biosynthesis in vitro in transfer RNA by an enzyme purified from Eschericha coliBartz J, Söll D. N6 - (Δ2 - Isopentenyl) Adenosine: Biosynthesis in vitro in transfer RNA by an enzyme purified from Eschericha coli. Biochimie 1972, 54: 31-39. PMID: 4346747, DOI: 10.1016/s0300-9084(72)80035-x.
- Isolation and partial characterization of temperature-sensitive Escherichia coli mutants with altered leucyl- and seryl-transfer ribonucleic acid synthetases.Low B, Gates F, Goldstein T, Söll D. Isolation and partial characterization of temperature-sensitive Escherichia coli mutants with altered leucyl- and seryl-transfer ribonucleic acid synthetases. Journal Of Bacteriology 1971, 108: 742-50. PMID: 4942762, PMCID: PMC247134, DOI: 10.1128/jb.108.2.742-750.1971.
- Temperature dependence of the aminoacylation of tRNA by bacillus stearothermophilus aminoacyl‐tRNA synthetasesJohnson L, Söll D. Temperature dependence of the aminoacylation of tRNA by bacillus stearothermophilus aminoacyl‐tRNA synthetases. Biopolymers 1971, 10: 2209-2221. PMID: 4940767, DOI: 10.1002/bip.360101114.
- Purification of Five Leucine Transfer Ribonucleic Acid Species from Escherichia coli and Their Acylation by Heterologous Leucyl-Transfer Ribonucleic Acid SynthetaseBlank H, Söll D. Purification of Five Leucine Transfer Ribonucleic Acid Species from Escherichia coli and Their Acylation by Heterologous Leucyl-Transfer Ribonucleic Acid Synthetase. Journal Of Biological Chemistry 1971, 246: 4947-4950. PMID: 4936719, DOI: 10.1016/s0021-9258(18)61954-4.
- A Comparative Study of the Interactions of Escherichia coli Leucyl-, Seryl-, and Valyl-Transfer Ribonucleic Acid Synthetases with Their Cognate Transfer Ribonucleic AcidsMyers G, Blank H, Söll D. A Comparative Study of the Interactions of Escherichia coli Leucyl-, Seryl-, and Valyl-Transfer Ribonucleic Acid Synthetases with Their Cognate Transfer Ribonucleic Acids. Journal Of Biological Chemistry 1971, 246: 4955-4964. PMID: 4936720, DOI: 10.1016/s0021-9258(18)61956-8.
- Purification of an Escherichia coli Leucine Suppressor Transfer Ribonucleic Acid and Its Aminoacylation by the Homologous Leucyl-Transfer Ribonucleic Acid SynthetaseHayashi H, Söll D. Purification of an Escherichia coli Leucine Suppressor Transfer Ribonucleic Acid and Its Aminoacylation by the Homologous Leucyl-Transfer Ribonucleic Acid Synthetase. Journal Of Biological Chemistry 1971, 246: 4951-4954. PMID: 4941862, DOI: 10.1016/s0021-9258(18)61955-6.
- Enzymatic Modification of Transfer RNASöll D. Enzymatic Modification of Transfer RNA. Science 1971, 173: 293-299. PMID: 4934576, DOI: 10.1126/science.173.3994.293.
- The nucleotide sequence of two leucine tRNA species from Escherichia coli K12Blank H, Sőll D. The nucleotide sequence of two leucine tRNA species from Escherichia coli K12. Biochemical And Biophysical Research Communications 1971, 43: 1192-1197. PMID: 4936129, DOI: 10.1016/0006-291x(71)90589-4.
- Identification of the Cytokinin-Active Ribonucleosides in Pure Escherichia coli tRNA SpeciesBartz J, Söll D, Burrows W, Skoog F. Identification of the Cytokinin-Active Ribonucleosides in Pure Escherichia coli tRNA Species. Proceedings Of The National Academy Of Sciences Of The United States Of America 1970, 67: 1448-1453. PMID: 4922291, PMCID: PMC283372, DOI: 10.1073/pnas.67.3.1448.
- In Vitro Biosynthesis of Pseudouridine at the Polynucleotide Level by an Enzyme Extract from Escherichia coliJohnson L, Söll D. In Vitro Biosynthesis of Pseudouridine at the Polynucleotide Level by an Enzyme Extract from Escherichia coli. Proceedings Of The National Academy Of Sciences Of The United States Of America 1970, 67: 943-950. PMID: 4943184, PMCID: PMC283296, DOI: 10.1073/pnas.67.2.943.
- N6-(Δ2-isopentenyl)adenosine: Biosynthesis in vitro in transfer RNA by an enzyme purified from escherichia coliBartz J, Kline L, Söll D. N6-(Δ2-isopentenyl)adenosine: Biosynthesis in vitro in transfer RNA by an enzyme purified from escherichia coli. Biochemical And Biophysical Research Communications 1970, 40: 1481-1487. PMID: 4326583, DOI: 10.1016/0006-291x(70)90035-5.
- Isolation and properties of a transfer ribonucleic acid deficient in ribothymidine.Johnson L, Hayashi H, Soell D. Isolation and properties of a transfer ribonucleic acid deficient in ribothymidine. Biochemistry 1970, 9: 2823-31. PMID: 4918123, DOI: 10.1021/bi00816a011.
- Purification of Five Serine Transfer Ribonucleic Acid Species from Escherichia coli and Their Acylation by Homologous and Heterologous Seryl Transfer Ribonucleic Acid SynthetasesRoy K, Söll D. Purification of Five Serine Transfer Ribonucleic Acid Species from Escherichia coli and Their Acylation by Homologous and Heterologous Seryl Transfer Ribonucleic Acid Synthetases. Journal Of Biological Chemistry 1970, 245: 1394-1400. PMID: 4910052, DOI: 10.1016/s0021-9258(18)63249-1.
- The Interaction of Seryl and of Leucyl Transfer Ribonucleic Acid Synthetases with Their Cognate Transfer Ribonucleic AcidsKnowles J, Katze J, Konigsberg W, Söll D. The Interaction of Seryl and of Leucyl Transfer Ribonucleic Acid Synthetases with Their Cognate Transfer Ribonucleic Acids. Journal Of Biological Chemistry 1970, 245: 1407-1415. PMID: 4910800, DOI: 10.1016/s0021-9258(18)63251-x.
- Purification of Leucyl Transfer Ribonucleic Acid Synthetase from Escherichia coliHayashi H, Knowles J, Katze J, Lapointe J, Söll D. Purification of Leucyl Transfer Ribonucleic Acid Synthetase from Escherichia coli. Journal Of Biological Chemistry 1970, 245: 1401-1406. PMID: 4986473, DOI: 10.1016/s0021-9258(18)63250-8.
- Transfer ribonucleic acid from Mycoplasma.Hayashi H, Fisher H, Soell D. Transfer ribonucleic acid from Mycoplasma. Biochemistry 1969, 8: 3680-6. PMID: 4897946, DOI: 10.1021/bi00837a028.
- CYTOKININS: DISTRIBUTION IN TRANSFER RNA SPECIES OF Escherichia coli*Armstrong D, Burrows W, Skoog F, Roy K, Söll D. CYTOKININS: DISTRIBUTION IN TRANSFER RNA SPECIES OF Escherichia coli*. Proceedings Of The National Academy Of Sciences Of The United States Of America 1969, 63: 834-841. PMID: 4899879, PMCID: PMC223528, DOI: 10.1073/pnas.63.3.834.
- Mechanism of protein biosynthesis.Lengyel P, Söll D. Mechanism of protein biosynthesis. Microbiology And Molecular Biology Reviews 1969, 33: 264-301. PMID: 4896351, PMCID: PMC378322, DOI: 10.1128/br.33.2.264-301.1969.
- Mechanism of protein biosynthesis.Lengyel P, Söll D. Mechanism of protein biosynthesis. Microbiology And Molecular Biology Reviews 1969, 33: 264-301. DOI: 10.1128/mmbr.33.2.264-301.1969.
- On the recognition of serine transfer RNA's specific for unrelated codons by the same seryl-transfer RNA synthetase.Sundharadas G, Katze J, Söll D, Konigsberg W, Lengyel P. On the recognition of serine transfer RNA's specific for unrelated codons by the same seryl-transfer RNA synthetase. Proceedings Of The National Academy Of Sciences Of The United States Of America 1968, 61: 693-700. PMID: 4879401, PMCID: PMC225215, DOI: 10.1073/pnas.61.2.693.
- Structure and function of Escherichia coli ribosomes II. Translational fidelity and efficiency in protein synthesis of a protein-deficient subribosomal particleTraub P, Söll D, Nomura M. Structure and function of Escherichia coli ribosomes II. Translational fidelity and efficiency in protein synthesis of a protein-deficient subribosomal particle. Journal Of Molecular Biology 1968, 34: 595-608. PMID: 4938559, DOI: 10.1016/0022-2836(68)90183-6.
- Studies on polynucleotides LXXXV. Partial purification of an amber supressor tRNA and studies on in vitro suppressionSöll D. Studies on polynucleotides LXXXV. Partial purification of an amber supressor tRNA and studies on in vitro suppression. Journal Of Molecular Biology 1968, 34: 175-187. PMID: 4938541, DOI: 10.1016/0022-2836(68)90243-x.
- Biosynthesis of the Peptidoglycan of Bacterial Cell Walls X. Further Study of the Glycyl Transfer Ribonucleic Acids Active in Peptidoglycan Synthesis in Staphylococcus AureusBumsted R, Dahl J, Söll D, Strominger J. Biosynthesis of the Peptidoglycan of Bacterial Cell Walls X. Further Study of the Glycyl Transfer Ribonucleic Acids Active in Peptidoglycan Synthesis in Staphylococcus Aureus. Journal Of Biological Chemistry 1968, 243: 779-782. PMID: 4867040, DOI: 10.1016/s0021-9258(19)81733-7.
- Biosynthesis of the Peptidoglycan of Bacterial Cell Walls VI. Incorporation Of l-Threonine Into Interpeptide Bridges in Micrococcus RoseusRoberts W, Strominger J, Söll D. Biosynthesis of the Peptidoglycan of Bacterial Cell Walls VI. Incorporation Of l-Threonine Into Interpeptide Bridges in Micrococcus Roseus. Journal Of Biological Chemistry 1968, 243: 749-756. PMID: 5638591, DOI: 10.1016/s0021-9258(19)81729-5.
- Biosynthesis of the Peptidoglycan of Bacterial Cell Walls VII. Incorporation of Serine and Glycine into Interpeptide Bridges in Staphylococcus EpidermidisPetit J, Strominger J, Söll D. Biosynthesis of the Peptidoglycan of Bacterial Cell Walls VII. Incorporation of Serine and Glycine into Interpeptide Bridges in Staphylococcus Epidermidis. Journal Of Biological Chemistry 1968, 243: 757-767. PMID: 5638592, DOI: 10.1016/s0021-9258(19)81730-1.
- Fractionation of Escherichia coli transfer RNA on benzoylated DEAE-celluloseRoy K, Söll D. Fractionation of Escherichia coli transfer RNA on benzoylated DEAE-cellulose. Biochimica Et Biophysica Acta 1968, 161: 572-574. PMID: 4875424, DOI: 10.1016/0005-2787(68)90137-8.
- Studies on polynucleotides LXXVI. Specificity of transfer RNA for codon recognition as studied by amino acid incorporationSöll D, RajBhandary U. Studies on polynucleotides LXXVI. Specificity of transfer RNA for codon recognition as studied by amino acid incorporation. Journal Of Molecular Biology 1967, 29: 113-124. PMID: 4861608, DOI: 10.1016/0022-2836(67)90184-2.
- Studies on polynucleotides LXXV. Specificity of tRNA for codon recognition as studied by the ribosomal binding techniqueSöll D, Cherayil J, Bock R. Studies on polynucleotides LXXV. Specificity of tRNA for codon recognition as studied by the ribosomal binding technique. Journal Of Molecular Biology 1967, 29: 97-112. PMID: 4861614, DOI: 10.1016/0022-2836(67)90183-0.
- Studies on polynucleotides LXVII. Initiation of protein synthesis in vitro as studied by using ribopolynucleotides with repeating nucleotide sequences as messengersGhosh H, Söll D, Khorana H. Studies on polynucleotides LXVII. Initiation of protein synthesis in vitro as studied by using ribopolynucleotides with repeating nucleotide sequences as messengers. Journal Of Molecular Biology 1967, 25: 275-298. PMID: 5340533, DOI: 10.1016/0022-2836(67)90142-8.
- An analysis of arginine codon multiplicity in rabbit hemoglobinWeisblum B, Cherayil J, Bock R, Söll D. An analysis of arginine codon multiplicity in rabbit hemoglobin. Journal Of Molecular Biology 1967, 28: 275-280. PMID: 4861175, DOI: 10.1016/s0022-2836(67)80009-3.
- Specificity of sRNA for recognition of codons as studied by the ribosomal binding techniqueSöll D, Jones D, Ohtsuka E, Faulkner R, Lohrmann R, Hayatsu H, Khorana H, Cherayil J, Hampel A, Bock R. Specificity of sRNA for recognition of codons as studied by the ribosomal binding technique. Journal Of Molecular Biology 1966, 19: 556-573. PMID: 5338858, DOI: 10.1016/s0022-2836(66)80023-2.
- Studies on polynucleotides. LI. Syntheses of the 64 possible ribotrinucleotides derived from the four major ribomononucleotides.Lohrmann R, Söll D, Hayatsu H, Ohtsuka E, Khorana H. Studies on polynucleotides. LI. Syntheses of the 64 possible ribotrinucleotides derived from the four major ribomononucleotides. Journal Of The American Chemical Society 1966, 88: 819-29. PMID: 5902563, DOI: 10.1021/ja00956a039.
- sRNA specificity for codon recognition as studied by the ribosomal binding technique.Söll D, Cherayil J, Jones D, Faulkner R, Hapel A, Bock R, Khorana H. sRNA specificity for codon recognition as studied by the ribosomal binding technique. Cold Spring Harbor Symposia On Quantitative Biology 1966, 31: 51-61. PMID: 4866399, DOI: 10.1101/sqb.1966.031.01.011.
- Studies on polynucleotides, XLIX. Stimulation of the binding of aminoacyl-sRNA's to ribosomes by ribotrinucleotides and a survey of codon assignments for 20 amino acids.Söll D, Ohtsuka E, Jones D, Lohrmann R, Hayatsu H, Nishimura S, Khorana H. Studies on polynucleotides, XLIX. Stimulation of the binding of aminoacyl-sRNA's to ribosomes by ribotrinucleotides and a survey of codon assignments for 20 amino acids. Proceedings Of The National Academy Of Sciences Of The United States Of America 1965, 54: 1378-1385. PMID: 5325653, PMCID: PMC219908, DOI: 10.1073/pnas.54.5.1378.
- STUDIES ON POLYNUCLEOTIDES. XXXVI. THE SPECIFIC SYNTHESIS OF C3'-C5'-LINKED RIBOOLIGONUCLEOTIDES. IX. THE SYNTHESIS OF RIBODINUCLEOTIDES BEARING 3'-PHOSPHOMONOESTER GROUPS.Söll D, Khorana H. STUDIES ON POLYNUCLEOTIDES. XXXVI. THE SPECIFIC SYNTHESIS OF C3'-C5'-LINKED RIBOOLIGONUCLEOTIDES. IX. THE SYNTHESIS OF RIBODINUCLEOTIDES BEARING 3'-PHOSPHOMONOESTER GROUPS. Journal Of The American Chemical Society 1965, 87: 360-7. PMID: 14228462, DOI: 10.1021/ja01080a037.
- STUDIES ON POLYNUCLEOTIDES. XXXV. THE SPECIFIC SYNTHESIS OF C3'-C5'-LINKED RIBOOLIGONUCLEOTIDES. 8. THE SYNTHESIS OF RIBODINUCLEOTIDES BEARING 3'-PHOSPHOMONOESTER GROUPS.Söll D, Khorana H. STUDIES ON POLYNUCLEOTIDES. XXXV. THE SPECIFIC SYNTHESIS OF C3'-C5'-LINKED RIBOOLIGONUCLEOTIDES. 8. THE SYNTHESIS OF RIBODINUCLEOTIDES BEARING 3'-PHOSPHOMONOESTER GROUPS. Journal Of The American Chemical Society 1965, 87: 350-9. PMID: 14228461, DOI: 10.1021/ja01080a036.
- Synthese von Ribodinucleotiden mit 3′‐endständiger PhosphatgruppeSöll D, Khorana H. Synthese von Ribodinucleotiden mit 3′‐endständiger Phosphatgruppe. Angewandte Chemie 1964, 76: 435-436. DOI: 10.1002/ange.19640761014.
- Synthesis of Ribodinucleotides with Terminal 3′‐Phosphate GroupsSöll D, Khorana H. Synthesis of Ribodinucleotides with Terminal 3′‐Phosphate Groups. Angewandte Chemie International Edition 1964, 3: 374-375. DOI: 10.1002/anie.196403742.
- Pteridine, XXVIII. Über die Synthese und Struktur von 4‐Amino‐6‐hydroxy‐ und 4‐Amino‐7‐hydroxy‐ pteridinenSöll D, Pfleiderer W. Pteridine, XXVIII. Über die Synthese und Struktur von 4‐Amino‐6‐hydroxy‐ und 4‐Amino‐7‐hydroxy‐ pteridinen. Chemische Berichte 1963, 96: 2977-2991. DOI: 10.1002/cber.19630961120.