2009
Structural and Chemical Basis for Glucosamine 6-Phosphate Binding and Activation of the glmS Ribozyme
Cochrane JC, Lipchock SV, Smith KD, Strobel SA. Structural and Chemical Basis for Glucosamine 6-Phosphate Binding and Activation of the glmS Ribozyme. Biochemistry 2009, 48: 3239-3246. PMID: 19228039, PMCID: PMC2854835, DOI: 10.1021/bi802069p.Peer-Reviewed Original Research
2000
A Single Adenosine with a Neutral pKa in the Ribosomal Peptidyl Transferase Center
Muth G, Ortoleva-Donnelly L, Strobel S. A Single Adenosine with a Neutral pKa in the Ribosomal Peptidyl Transferase Center. Science 2000, 289: 947-950. PMID: 10937997, DOI: 10.1126/science.289.5481.947.Peer-Reviewed Original Research
1999
An important base triple anchors the substrate helix recognition surface within the Tetrahymena ribozyme active site
Szewczak A, Ortoleva-Donnelly L, Zivarts M, Oyelere A, Kazantsev A, Strobel S. An important base triple anchors the substrate helix recognition surface within the Tetrahymena ribozyme active site. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 11183-11188. PMID: 10500151, PMCID: PMC18008, DOI: 10.1073/pnas.96.20.11183.Peer-Reviewed Original ResearchConceptsHelix dockingBase triplesRecognition surfaceGroup I intronActive siteNetwork of interactionsTetrahymena group IP3 helixStructural biologySubstrate bindingI intronCatalytic RNAProduct bindingSuppression analysisFunctional importanceRNA foldingRNA constructsSubstrate helixBiochemical evidenceMutant ribozymesRibozyme active siteSubstantial rearrangementHelixCrystallographic modelRibozyme
1997
Defining the chemical groups essential for Tetrahymena group I intron function by nucleotide analog interference mapping
Strobel S, Shetty K. Defining the chemical groups essential for Tetrahymena group I intron function by nucleotide analog interference mapping. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 2903-2908. PMID: 9096319, PMCID: PMC20295, DOI: 10.1073/pnas.94.7.2903.Peer-Reviewed Original Research
1993
A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
MacDonald M, Ambrose C, Duyao M, Myers R, Lin C, Srinidhi L, Barnes G, Taylor S, James M, Groot N, MacFarlane H, Jenkins B, Anderson M, Wexler N, Gusella J, Bates G, Baxendale S, Hummerich H, Kirby S, North M, Youngman S, Mott R, Zehetner G, Sedlacek Z, Poustka A, Frischauf A, Lehrach H, Buckler A, Church D, Doucette-Stamm L, O'Donovan M, Riba-Ramirez L, Shah M, Stanton V, Strobel S, Draths K, Wales J, Dervan P, Housman D, Altherr M, Shiang R, Thompson L, Fielder T, Wasmuth J, Tagle D, Valdes J, Elmer L, Allard M, Castilla L, Swaroop M, Blanchard K, Collins F, Snell R, Holloway T, Gillespie K, Datson N, Shaw D, Harper P. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 1993, 72: 971-983. PMID: 8458085, DOI: 10.1016/0092-8674(93)90585-e.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceChromosomes, Human, Pair 4Cloning, MolecularExonsGene ExpressionGenesHumansHuntington DiseaseMolecular Sequence DataMutationOligodeoxyribonucleotidesPedigreePolymerase Chain ReactionPolymorphism, GeneticRepetitive Sequences, Nucleic AcidRestriction MappingRNA, MessengerConceptsDisease genesTrinucleotide repeatsUnstable DNA segmentDisease chromosomesFragile X syndromeNew genesNovel genesSpino-bulbar muscular atrophyDNA segmentsHuntington's disease geneDominant phenotypeKD proteinGenesChromosomesLinkage disequilibriumHD chromosomesX syndromeHuntington's disease chromosomesRepeatsHaplotype analysisDisease familiesPolymorphic trinucleotide repeatHD mutationMyotonic dystrophyExons