2023
Lysine Demethylation in Pathogenesis
Cao J, Yan Q. Lysine Demethylation in Pathogenesis. Advances In Experimental Medicine And Biology 2023, 1433: 1-14. PMID: 37751133, DOI: 10.1007/978-3-031-38176-8_1.ChaptersConceptsLysine demethylasesLSD1/KDM1AHistone lysine methylationHistone lysine methyltransferasesMajor epigenetic mechanismsNormal developmentNon-histone substratesSpecific small molecule inhibitorsSmall molecule inhibitorsLysine methylationLysine methyltransferasesHistone methylationHistone lysineLysine demethylationEpigenetic mechanismsDNA repairArginine residuesHuman diseasesMore subfamiliesMolecule inhibitorsLysine modificationDemethylasesMethylationTreatment of cancerEnzyme
2020
The GTPase-activating protein p120RasGAP has an evolutionarily conserved “FLVR-unique” SH2 domain
Jaber Chehayeb R, Wang J, Stiegler AL, Boggon TJ. The GTPase-activating protein p120RasGAP has an evolutionarily conserved “FLVR-unique” SH2 domain. Journal Of Biological Chemistry 2020, 295: 10511-10521. PMID: 32540970, PMCID: PMC7397115, DOI: 10.1074/jbc.ra120.013976.Peer-Reviewed Original ResearchConceptsC-terminal SH2 domainSH2 domainFLVR motifSrc homology 2 domainArginine residuesSalt bridgePhosphotyrosine motifsPeptide-bound formsPhosphopeptide bindingUnrecognized diversityDirect salt bridgeIntramolecular salt bridgeIsothermal titration calorimetryPhosphotyrosineP120RasGAPMotifX-ray crystal structureTitration calorimetryAspartic acidTandem substitutionsResiduesBindingDomainGTPaseP190RhoGAP
2015
Identification of Multiple Structurally Distinct, Nonpeptidic Small Molecule Inhibitors of Protein Arginine Deiminase 3 Using a Substrate-Based Fragment Method
Jamali H, Khan HA, Stringer JR, Chowdhury S, Ellman JA. Identification of Multiple Structurally Distinct, Nonpeptidic Small Molecule Inhibitors of Protein Arginine Deiminase 3 Using a Substrate-Based Fragment Method. Journal Of The American Chemical Society 2015, 137: 3616-3621. PMID: 25742366, PMCID: PMC4447334, DOI: 10.1021/jacs.5b00095.Peer-Reviewed Original ResearchConceptsProtein arginine deiminasesExhibit tissue-specific expressionTissue-specific expressionNonpeptidic small-molecule inhibitorsFamily of enzymesSmall molecule inhibitorsDistinct inhibitorsArginine residuesMolecule inhibitorsPAD inhibitorsArginine deiminasesLow molecular weightPAD3Selective inhibitorPotent inhibitorReliable discoveryInhibitorsMolecular weightFragment method
2014
Structural models of the membrane anchors of envelope glycoproteins E1 and E2 from pestiviruses
Wang J, Li Y, Modis Y. Structural models of the membrane anchors of envelope glycoproteins E1 and E2 from pestiviruses. Virology 2014, 454: 93-101. PMID: 24725935, PMCID: PMC3986810, DOI: 10.1016/j.virol.2014.02.015.Peer-Reviewed Original Research
2013
Tdrkh is essential for spermatogenesis and participates in primary piRNA biogenesis in the germline
Saxe JP, Chen M, Zhao H, Lin H. Tdrkh is essential for spermatogenesis and participates in primary piRNA biogenesis in the germline. The EMBO Journal 2013, 32: 1869-1885. PMID: 23714778, PMCID: PMC3981179, DOI: 10.1038/emboj.2013.121.Peer-Reviewed Original ResearchConceptsPrimary piRNA biogenesisPiRNA biogenesisKH domain-containing proteinPiRNA biogenesis pathwayPing-pong cycleDomain-containing proteinsMature piRNAsPIWI proteinsBiogenesis pathwayMitochondrial proteinsEpigenetic programmingNuclear localizationCytoplasmic localizationZygotene stageBiogenesisTDRKHArginine residuesMeiotic arrestMIWI2MIWIDistinct populationsProteinMutantsGermlineRNA
2012
Binding of the Heterogeneous Ribonucleoprotein K (hnRNP K) to the Epstein-Barr Virus Nuclear Antigen 2 (EBNA2) Enhances Viral LMP2A Expression
Gross H, Hennard C, Masouris I, Cassel C, Barth S, Stober-Grässer U, Mamiani A, Moritz B, Ostareck D, Ostareck-Lederer A, Neuenkirchen N, Fischer U, Deng W, Leonhardt H, Noessner E, Kremmer E, Grässer FA. Binding of the Heterogeneous Ribonucleoprotein K (hnRNP K) to the Epstein-Barr Virus Nuclear Antigen 2 (EBNA2) Enhances Viral LMP2A Expression. PLOS ONE 2012, 7: e42106. PMID: 22879910, PMCID: PMC3411732, DOI: 10.1371/journal.pone.0042106.Peer-Reviewed Original ResearchMeSH KeywordsAntibodies, MonoclonalAntibody SpecificityArginineCell LineDNAEpstein-Barr Virus InfectionsEpstein-Barr Virus Nuclear AntigensGene Expression Regulation, ViralHerpesvirus 4, HumanHeterogeneous-Nuclear Ribonucleoprotein KHumansImmunoprecipitationMethylationMolecular Sequence DataMultiprotein ComplexesMutant ProteinsPromoter Regions, GeneticProtein BindingProtein TransportRepetitive Sequences, Amino AcidsnRNP Core ProteinsTransfectionViral Matrix ProteinsViral ProteinsConceptsEpstein-Barr virus nuclear antigen 2Survival motor neuron (SMN) proteinHnRNP KHeterogeneous ribonucleoprotein KRG repeatsCellular proteinsSDMA-specific antibodyGel shift experimentsMotor neuron proteinHnRNP K.Cellular homologueCellular processesSequence motifsNp9 proteinsHuman endogenous retrovirus KArginine residuesNeuron proteinEBNA2 proteinShift experimentsLMP2A expressionNuclear antigen 2ProteinUnknown mechanismE. coliArginine-Glycine
2011
PAPI, a novel TUDOR-domain protein, complexes with AGO3, ME31B and TRAL in the nuage to silence transposition
Liu L, Qi H, Wang J, Lin H. PAPI, a novel TUDOR-domain protein, complexes with AGO3, ME31B and TRAL in the nuage to silence transposition. Development 2011, 138: 1863-1873. PMID: 21447556, PMCID: PMC3074456, DOI: 10.1242/dev.059287.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, Genetically ModifiedArgonaute ProteinsCarrier ProteinsDEAD-box RNA HelicasesDNA Transposable ElementsDrosophila melanogasterDrosophila ProteinsEmbryo, NonmammalianFemaleGene Expression Regulation, DevelopmentalGene SilencingGerm CellsMaleModels, BiologicalMutagenesis, InsertionalPeptide Initiation FactorsProtein BindingRibonucleoproteinsRNA-Binding ProteinsRNA-Induced Silencing ComplexConceptsPiRNA pathway componentsPIWI-interacting RNAsArgonaute 3PiRNA pathwayPIWI proteinsTransposon activationPathway componentsPIWI protein AubergineTudor domain proteinsP-body componentsN-terminal domainNuage componentsPiRNA mutantsTransposon controlGermline developmentTudor domainMutant ovariesArginine methyltransferaseGermline genomeEpigenetic regulationPerinuclear structuresNuageAdult ovariesArginine residuesFunctional interaction
2010
Arginine methylation in subunits of mammalian pre-mRNA cleavage factor I
Martin G, Ostareck-Lederer A, Chari A, Neuenkirchen N, Dettwiler S, Blank D, Rüegsegger U, Fischer U, Keller W. Arginine methylation in subunits of mammalian pre-mRNA cleavage factor I. RNA 2010, 16: 1646-1659. PMID: 20562214, PMCID: PMC2905762, DOI: 10.1261/rna.2164210.Peer-Reviewed Original ResearchConceptsProtein arginine methyltransferasesCleavage factor IMammalian cleavage factor IProcessing complexMessenger RNA precursorsPost-translational modificationsHeLa cell extractsRecombinant protein substratesSite of methylationS-adenosyl methionineBinding protein 1GAR motifArginine methylationArginine methyltransferasesRNA exportSecond methyltransferaseAsymmetric dimethylationRNA precursorsThird polypeptideC-terminusSuch enzymesArginine residuesCell extractsPolypeptide chainMethylation
2009
Protein arginine methyltransferase 1 regulates herpes simplex virus replication through ICP27 RGG-box methylation
Yu J, Shin B, Park E, Yang S, Choi S, Kang M, Rho J. Protein arginine methyltransferase 1 regulates herpes simplex virus replication through ICP27 RGG-box methylation. Biochemical And Biophysical Research Communications 2009, 391: 322-328. PMID: 19913501, DOI: 10.1016/j.bbrc.2009.11.057.Peer-Reviewed Original ResearchConceptsProtein arginine methyltransferase 1ICP27 RGG boxProtein arginine methylationArginine methylationRGG boxHerpes simplex virus type 1Arginine residuesRNA-binding activityArginine substitution mutantsArginine methyltransferase 1Gene expression in vivoRNA metabolismMethylation sitesSubcellular localizationSubstitution mutantsCellular processesCellular regulationExpression in vivoHerpes simplex virus replicationArginine mutationPRMT inhibitorsICP27Methyltransferase 1Cytokine signalingCellular mediators
2008
Methylation of RUNX1 by PRMT1 abrogates SIN3A binding and potentiates its transcriptional activity
Zhao X, Jankovic V, Gural A, Huang G, Pardanani A, Menendez S, Zhang J, Dunne R, Xiao A, Erdjument-Bromage H, Allis CD, Tempst P, Nimer SD. Methylation of RUNX1 by PRMT1 abrogates SIN3A binding and potentiates its transcriptional activity. Genes & Development 2008, 22: 640-653. PMID: 18316480, PMCID: PMC2259033, DOI: 10.1101/gad.1632608.Peer-Reviewed Original ResearchMeSH KeywordsAntigens, CD34ArginineCell Line, TumorCore Binding Factor Alpha 2 SubunitDNA-Binding ProteinsGene Expression RegulationHematopoiesisHumansMethylationMutationPlatelet Membrane Glycoprotein IIbProtein-Arginine N-MethyltransferasesProto-Oncogene ProteinsRepressor ProteinsRNA, Small InterferingRUNX1 Translocation Partner 1 ProteinSin3 Histone Deacetylase and Corepressor ComplexTrans-ActivatorsTranscription FactorsTranscription, GeneticConceptsRUNX1 functionArginine residuesRUNX1-ETO fusion proteinArginine methyltransferase PRMT1Arginine methylation sitesPRMT1-dependent methylationRUNX1 target genesProtein-protein interactionsPost-translational modificationsRUNX1/AML1Dominant inhibitory activityDefinitive hematopoiesisMethyltransferase PRMT1Corepressor Sin3ATranscriptional coactivatorPRMT1Target genesMethylation sitesDynamic regulationTranscriptional activityCorepressor bindingHuman acute leukemiaFusion proteinChromosome translocationRUNX1
2004
Structure-based mechanism of photosynthetic water oxidation
McEvoy J, Brudvig G. Structure-based mechanism of photosynthetic water oxidation. Physical Chemistry Chemical Physics 2004, 6: 4754-4763. DOI: 10.1039/b407500e.Peer-Reviewed Original ResearchOxygen-evolving complexO bond-forming stepSubstrate water moleculesX-ray crystal structureBond-forming stepPhotosynthetic water oxidationWater splitting reactionResolution X-ray crystal structureCyanobacterial photosystem IIÅ resolution X-ray crystal structureCP43-Arg357Water oxidationStructure-based mechanismWater moleculesCertain amino acid residuesAmino acid residuesCrystal structureMechanistic functionPhotosystem IIArginine residuesCrystallographic informationLends weightResiduesNucleophilesOxidation
1995
Structural specificity of substrate for S-adenosylmethionine protein arginine N-methyltransferases
Rawal N, Rajpurohit R, Lischwe M, Williams K, Paik W, Kim S. Structural specificity of substrate for S-adenosylmethionine protein arginine N-methyltransferases. Biochimica Et Biophysica Acta 1995, 1248: 11-18. PMID: 7536038, DOI: 10.1016/0167-4838(94)00213-z.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsMethylationMolecular Sequence DataMyelin Basic ProteinOligopeptidesPeptide FragmentsProtein-Arginine N-MethyltransferasesRatsRibonucleoproteinsS-AdenosylmethionineSubstrate SpecificityTrypsinConceptsProtein methylase IArginine residuesProtein A1Protein arginine N-methyltransferasesEnzymatic methylationPreferred amino acid sequencesArginine-methylated proteinsProtein arginine N-methyltransferaseHnRNP protein A1Arginine-rich motifAmino acid sequenceArginine N-methyltransferaseN-methyltransferasesRich motifN-terminal fragmentHPLC amino acid analysisC-terminusMethyl acceptorAmino acid analysisDisulfide bridgesS-adenosylmethionineProtein moleculesTrypsin digestionNG-monomethylarginineGood substrate
1993
Human SR proteins and isolation of a cDNA encoding SRp75.
Zahler A, Neugebauer K, Stolk J, Roth M. Human SR proteins and isolation of a cDNA encoding SRp75. Molecular And Cellular Biology 1993, 13: 4023-4028. PMID: 8321209, PMCID: PMC359951, DOI: 10.1128/mcb.13.7.4023.Peer-Reviewed Original ResearchConceptsRNA recognition motifSR proteinsN-terminal RNA recognition motifLong C-terminal domainPolymerase II transcriptionHuman SR proteinsSR family membersC-terminal domainFamily of proteinsGlycine-rich regionApparent molecular massCDNA clonesRecognition motifSRp75Mobility shiftArginine residuesMolecular massSR domainProteinInternal regionSerineCommon epitopesActive siteFamily membersSRp55Human SR Proteins and Isolation of a cDNA Encoding SRp75
Zahler A, Neugebauer K, Stolk J, Roth M. Human SR Proteins and Isolation of a cDNA Encoding SRp75. Molecular And Cellular Biology 1993, 13: 4023-4028. DOI: 10.1128/mcb.13.7.4023-4028.1993.Peer-Reviewed Original ResearchRNA recognition motifSR proteinsN-terminal RNA recognition motifLong C-terminal domainPolymerase II transcriptionHuman SR proteinsSR family membersC-terminal domainFamily of proteinsGlycine-rich regionApparent molecular massCDNA clonesRecognition motifSRp75Mobility shiftArginine residuesMolecular massSR domainProteinInternal regionSerineCommon epitopesActive siteFamily membersSRp55
1989
Molecular basis of mouse Himalayan mutation
Kwon B, Halaban R, Chintamaneni C. Molecular basis of mouse Himalayan mutation. Biochemical And Biophysical Research Communications 1989, 161: 252-260. PMID: 2567165, DOI: 10.1016/0006-291x(89)91588-x.Peer-Reviewed Original ResearchConceptsAmino acid 420Histidine residuesAmino acidsTemperature-sensitive tyrosinaseCDNA libraryHimalayan miceMouse tyrosinaseInteresting mutantsNucleotide sequenceB proteinMolecular basisTyrosinase geneTyrosinase cDNAArginine residuesTyrosinase moleculesHuman tyrosinaseG changeResiduesMutationsTyrosinaseMutantsCDNAGenesMiceTyrosinase inhibitors
1986
Coding sequence of the precursor of the beta subunit of rat propionyl-CoA carboxylase.
Kraus J, Firgaira F, Novotný J, Kalousek F, Williams K, Williamson C, Ohura T, Rosenberg L. Coding sequence of the precursor of the beta subunit of rat propionyl-CoA carboxylase. Proceedings Of The National Academy Of Sciences Of The United States Of America 1986, 83: 8049-8053. PMID: 3464942, PMCID: PMC386864, DOI: 10.1073/pnas.83.21.8049.Peer-Reviewed Original ResearchConceptsPropionyl-CoA carboxylaseNH2-terminal leader peptideAmino acid sequenceBeta subunitBeta-subunit precursorMature subunitAcid sequenceLeader peptideMitochondrial enzyme propionyl-CoA carboxylaseAmino acidsSubunit precursorOpen reading frameAlpha-helical segmentsEnzyme propionyl-CoA carboxylaseCarboxylaseNH2-terminal residuesFirst helixReading frameDNA sequencesPrecursorsCytoplasmic precursorMRNA sequencesArginine residuesHydrophobic momentMRNA transcripts
1985
Arginine in the leader peptide is required for both import and proteolytic cleavage of a mitochondrial precursor.
Horwich A, Kalousek F, Rosenberg L. Arginine in the leader peptide is required for both import and proteolytic cleavage of a mitochondrial precursor. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 4930-4933. PMID: 3895227, PMCID: PMC390471, DOI: 10.1073/pnas.82.15.4930.Peer-Reviewed Original ResearchConceptsLeader peptideOrnithine transcarbamoylaseImport of precursorsMost mitochondrial proteinsMitochondrial matrix fractionOverall amino acid compositionMitochondrial matrix enzymeMitochondrial precursorsMitochondrial proteinsSubunit precursorAmino acid compositionBasic arginine residuesBasic residuesMatrix enzymeGlycine residueLarger precursorArginine residuesMatrix fractionIntact mitochondriaNH2-terminalDependent proteaseProteolytic cleavageTranscarbamoylaseResiduesMitochondriaExpression of amplified DNA sequences for ornithine transcarbamylase in HeLa cells: arginine residues may be required for mitochondrial import of enzyme precursor.
Horwich A, Fenton W, Firgaira F, Fox J, Kolansky D, Mellman I, Rosenberg L. Expression of amplified DNA sequences for ornithine transcarbamylase in HeLa cells: arginine residues may be required for mitochondrial import of enzyme precursor. Journal Of Cell Biology 1985, 100: 1515-1521. PMID: 3988798, PMCID: PMC2113848, DOI: 10.1083/jcb.100.5.1515.Peer-Reviewed Original ResearchConceptsMitochondrial importOTC precursorsHeLa cellsOrnithine transcarbamylaseArginine residuesMouse dihydrofolate reductaseNH2-terminal leader sequenceRate of importArginine analog canavanineViral regulatory elementsImmunoprecipitation of extractsMitochondrial localizationCDNA sequenceRegulatory elementsLeader sequenceDNA sequencesEnzyme precursorsMitochondrial enzymesCell extractsDihydrofolate reductaseEnzymatic activityBlot analysisNormal precursorsResiduesSubunits
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply