2024
Structural study for substrate recognition of human N‐terminal glutamine amidohydrolase 1 in the arginine N‐degron pathway
Kang J, Park J, Lee J, Jang J, Han B. Structural study for substrate recognition of human N‐terminal glutamine amidohydrolase 1 in the arginine N‐degron pathway. Protein Science 2024, 33: e5067. PMID: 38864716, PMCID: PMC11168063, DOI: 10.1002/pro.5067.Peer-Reviewed Original ResearchConceptsN-degron pathwaySubstrate recognitionN-degronSubstrate-binding conformationHalf-life of proteinsProtein degradation machineryTargeted protein therapyDegradation machinerySubstrate specificityProtein regulationBackbone of proteinsGln residuesCharged residuesNT residuesDegradation systemProteinBiochemical analysisResiduesPathwayStructural studiesGlnProtein therapyArginineSide chainsShed light
2019
Structural basis of antagonism of human APOBEC3F by HIV-1 Vif
Hu Y, Desimmie BA, Nguyen HC, Ziegler SJ, Cheng TC, Chen J, Wang J, Wang H, Zhang K, Pathak VK, Xiong Y. Structural basis of antagonism of human APOBEC3F by HIV-1 Vif. Nature Structural & Molecular Biology 2019, 26: 1176-1183. PMID: 31792451, PMCID: PMC6899190, DOI: 10.1038/s41594-019-0343-6.Peer-Reviewed Original ResearchConceptsHIV-1 VifProtein degradation machineryCryo-EM structureHuman immunodeficiency virus type 1 (HIV-1) replicationCore-binding factor betaUbiquitin-proteasome pathwayRole of CbfβHIV-1 virion infectivity factorType 1 replicationVif-A3 interactionsViral immune evasionDegradation machineryAntiviral APOBEC3Terminal domainVirion infectivity factorStructural basisMolecular mechanismsViral restrictionA3 proteinsMolecular determinantsImmune evasionInfectivity factorFactor betaCellular studiesAntiviral therapeutics
2017
A Method for the Acute and Rapid Degradation of Endogenous Proteins
Clift D, McEwan W, Labzin L, Konieczny V, Mogessie B, James L, Schuh M. A Method for the Acute and Rapid Degradation of Endogenous Proteins. Cell 2017, 171: 1692-1706.e18. PMID: 29153837, PMCID: PMC5733393, DOI: 10.1016/j.cell.2017.10.033.Peer-Reviewed Original ResearchConceptsTrim-AwayProtein functionSystematic characterization of genesDisruption of protein functionEndogenous proteinsStudy of protein functionCharacterization of genesDisrupt protein functionCellular protein degradation machineryProtein degradation machineryEndogenous protein levelsDiverse cell typesDegradation of endogenous proteinsDegradation machineryMammalian cellsRNA interferenceTarget proteinsNative proteinTargeted disruptionGenomeCell typesProteinPrimary cellsRapid degradationProtein levels
2015
Systematic Protein Level Regulation via Degradation Machinery Induced by Genotoxic Drugs
Kume K, Ishida K, Ikeda M, Takemoto K, Shimura T, Young L, Nishizuka SS. Systematic Protein Level Regulation via Degradation Machinery Induced by Genotoxic Drugs. Journal Of Proteome Research 2015, 15: 205-215. PMID: 26625007, DOI: 10.1021/acs.jproteome.5b00759.Peer-Reviewed Original ResearchConceptsDegradation machineryGenotoxic drugsProtein dynamicsProtein-level regulationProtein degradation systemProtein levelsDistinct proteinsApoptosis-related proteinsDegradation systemProtein arraysProteinLevel regulationProteasome inhibitorsMachineryComprehensive insightRegulationMG132Similar dynamicsPairsInhibitorsDynamicsDifferent concentrationsResponseSimilarityLevels
2012
The Prolyl Isomerase Pin1 Targets Stem-Loop Binding Protein (SLBP) To Dissociate the SLBP-Histone mRNA Complex Linking Histone mRNA Decay with SLBP Ubiquitination
Krishnan N, Lam TT, Fritz A, Rempinski D, O'Loughlin K, Minderman H, Berezney R, Marzluff WF, Thapar R. The Prolyl Isomerase Pin1 Targets Stem-Loop Binding Protein (SLBP) To Dissociate the SLBP-Histone mRNA Complex Linking Histone mRNA Decay with SLBP Ubiquitination. Molecular And Cellular Biology 2012, 32: 4306-4322. PMID: 22907757, PMCID: PMC3486140, DOI: 10.1128/mcb.00382-12.Peer-Reviewed Original ResearchMeSH KeywordsCell CycleCell Line, TumorCell NucleusDown-RegulationHEK293 CellsHeLa CellsHistonesHumansmRNA Cleavage and Polyadenylation FactorsNIMA-Interacting Peptidylprolyl IsomeraseNuclear ProteinsPeptidylprolyl IsomeraseProtein Phosphatase 2RNA InterferenceRNA StabilityRNA-Binding ProteinsRNA, MessengerRNA, Small InterferingUbiquitinationConceptsStem-loop binding proteinHistone mRNADegradation of SLBPMRNA stabilityBinding proteinHistone mRNA stabilityRNA degradation machineryHistone mRNA decayS phaseProtein phosphatase 2AHistone mRNA degradationCore histone mRNAsExosome-mediated degradationDownregulation of Pin1Ubiquitin-proteasome systemMRNA 3' endsProlyl isomerase Pin1Phosphatase 2ADegradation machineryMRNA decayMRNA degradationProteasome systemIsomerase Pin1MRNA complexesUntranslated region
1997
AU-rich elements target small nuclear RNAs as well as mRNAs for rapid degradation
Fan X, Myer V, Steitz J. AU-rich elements target small nuclear RNAs as well as mRNAs for rapid degradation. Genes & Development 1997, 11: 2557-2568. PMID: 9334320, PMCID: PMC316563, DOI: 10.1101/gad.11.19.2557.Peer-Reviewed Original ResearchMeSH KeywordsAntigens, SurfaceBase SequenceELAV ProteinsELAV-Like Protein 1Gene Expression RegulationGenes, ReporterGlobinsHerpesvirus 2, SaimiriineMolecular Sequence DataMutationRepetitive Sequences, Nucleic AcidRibonucleasesRNA, MessengerRNA, Small NuclearRNA, ViralRNA-Binding ProteinsTranscription, GeneticTransfectionConceptsAU-rich elementsMRNA degradation machinerySmall nuclear RNAHSUR 1Host RNA moleculesDegradation machineryMammalian mRNAsNuclear RNARNA moleculesMutational analysisSequence requirementsTarget RNAHuR proteinOngoing translationRNA 1MRNARapid degradationRNASimilar mechanismDegradation activityDeadenylationSnRNAMachineryProteinDegradation
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