2023
Linear motif specificity in signaling through p38α and ERK2 mitogen–activated protein kinases
Robles J, Lou H, Shi G, Pan P, Turk B. Linear motif specificity in signaling through p38α and ERK2 mitogen–activated protein kinases. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2316599120. PMID: 37988460, PMCID: PMC10691213, DOI: 10.1073/pnas.2316599120.Peer-Reviewed Original ResearchConceptsExtracellular signal-regulated kinase 2Docking motifERK2 mitogen-activated protein kinaseSignal-regulated kinase 2Protein kinase cascadeMitogen-activated protein kinaseFull-length proteinMAPK substratesEukaryotic cellsKinase cascadeMAPK networkLinear motifsProtein kinaseMotif specificityProteomic librariesDocking siteAcidic residuesKinase 2Diverse stimuliCellular responsesP38αDocking interfaceHigh net chargeMotifSelective interaction
2012
Structural Insights into the Substrate Specificity of Human Granzyme H: The Functional Roles of a Novel RKR Motif
Wang L, Zhang K, Wu L, Liu S, Zhang H, Zhou Q, Tong L, Sun F, Fan Z. Structural Insights into the Substrate Specificity of Human Granzyme H: The Functional Roles of a Novel RKR Motif. The Journal Of Immunology 2012, 188: 765-773. PMID: 22156497, DOI: 10.4049/jimmunol.1101381.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsCatalytic DomainCatsCell LineCell Line, TransformedCrystallography, X-RayCytotoxicity, ImmunologicDogsGranzymesHumansHydrogen-Ion ConcentrationK562 CellsMolecular Sequence DataPan troglodytesProtein BindingSerine Proteinase InhibitorsSubstrate SpecificityConceptsRKR motifHuman granzyme HStructural insightsSubstrate recognition mechanismChymotrypsin-like serine proteaseGranzyme HSubstrate recognitionSubstrate specificitySubstrate preferenceChloromethylketone inhibitorAcidic residuesInnate immune responseAromatic residuesFunctional roleP1 positionSerine proteasesS1 pocketRecognition mechanismMotifGzmHResiduesProteolytic activityDecapeptide substrateImportant roleMutants
1999
The Bovine Papillomavirus E5 Protein Requires a Juxtamembrane Negative Charge for Activation of the Platelet-Derived Growth Factor β Receptor and Transformation of C127 Cells
Klein O, Kegler-Ebo D, Su J, Smith S, DiMaio D. The Bovine Papillomavirus E5 Protein Requires a Juxtamembrane Negative Charge for Activation of the Platelet-Derived Growth Factor β Receptor and Transformation of C127 Cells. Journal Of Virology 1999, 73: 3264-3272. PMID: 10074180, PMCID: PMC104090, DOI: 10.1128/jvi.73.4.3264-3272.1999.Peer-Reviewed Original ResearchConceptsPlatelet-derived growth factor beta receptorPDGF beta receptorGrowth factor beta receptorE5 proteinBovine papillomavirus E5 proteinCell transformationHomodimeric transmembrane proteinSustained receptor activationC127 mouse fibroblastsExtracellular juxtamembrane regionBeta receptorsE5 dimerE5 mutantsDouble mutantJuxtamembrane regionTransmembrane proteinC127 cellsC-terminusAcidic residuesE5 geneMutantsPosition 33Mouse fibroblastsProteinSalt bridge
1997
Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation
Arendt C, Hochstrasser M. Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 7156-7161. PMID: 9207060, PMCID: PMC23776, DOI: 10.1073/pnas.94.14.7156.Peer-Reviewed Original ResearchConceptsActive siteN-terminal threonineBeta subunitDistinct peptidase activitiesMost minor effectsSubunit ringDifferent beta subunitsCorresponding threonineActive site formationUbiquitin-dependent proteolysisDegradation of substratesProteasome active sitesYeast proteasomeArchaeal proteasomeDifferent eukaryotesActive-site nucleophileUbiquitin pathwayHeptameric ringsBasic residuesSubunit interactionsAcidic residuesAlpha subunitSubstrateProteasomePeptide substrates
1995
Phosphorylation of DARPP-32, a Dopamine- and cAMP-regulated Phosphoprotein, by Casein Kinase I in Vitro and in Vivo *
Desdouits F, Cohen D, Nairn A, Greengard P, Girault J. Phosphorylation of DARPP-32, a Dopamine- and cAMP-regulated Phosphoprotein, by Casein Kinase I in Vitro and in Vivo *. Journal Of Biological Chemistry 1995, 270: 8772-8778. PMID: 7721783, DOI: 10.1074/jbc.270.15.8772.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCasein KinasesCattleCorpus StriatumCyclic AMPDNA PrimersDopamineDopamine and cAMP-Regulated Phosphoprotein 32Electrophoresis, Polyacrylamide GelHumansMolecular Sequence DataMutagenesis, Site-DirectedNerve Tissue ProteinsNeuronsPeptide MappingPhosphoproteinsPhosphorylationProtein KinasesRabbitsRatsSubstantia NigraConceptsCasein kinase IProtein phosphatase 1Kinase ISer-137Phosphatase 1Ser-189DARPP-32CAMP-dependent protein kinasePhosphatase-1 inhibitorStoichiometry of phosphorylationSite-directed mutagenesisSpecific cell populationsProtein kinaseProtein sequencingSeryl residuesAcidic residuesThr-34PhosphorylationPhosphate/Presence of SDSChoroid plexus epithelial cellsResiduesCell populationsElectrophoretic mobilityEpithelial cells
1984
Structure and Expression of a Complementary DNA for the Nuclear Coded Precursor of Human Mitochondrial Ornithine Transcarbamylase
Horwich A, Fenton W, Williams K, Kalousek F, Kraus J, Doolittle R, Konigsberg W, Rosenberg L. Structure and Expression of a Complementary DNA for the Nuclear Coded Precursor of Human Mitochondrial Ornithine Transcarbamylase. Science 1984, 224: 1068-1074. PMID: 6372096, DOI: 10.1126/science.6372096.Peer-Reviewed Original ResearchConceptsComplementary DNALeader peptideOrnithine transcarbamylaseAmino-terminal leader peptideMost mitochondrial proteinsComplete primary structureHuman ornithine transcarbamylaseFree cytoplasmic ribosomesMitochondrial matrix enzymeCultured HeLa cellsMitochondrial proteinsCytoplasmic ribosomesRegulatory elementsNucleotide sequenceStable transformantsMatrix enzymeAsparagine residuesAcidic residuesLarger precursorMature formPrimary structureProtein occursHeLa cellsEscherichia coliAmino acids
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