2024
Development of a High-Throughput Platform for Quantitation of Histone Modifications on a New QTOF Instrument
Zahn E, Xie Y, Liu X, Karki R, Searfoss R, de Luna Vitorino F, Lempiäinen J, Gongora J, Lin Z, Zhao C, Yuan Z, Garcia B. Development of a High-Throughput Platform for Quantitation of Histone Modifications on a New QTOF Instrument. Molecular & Cellular Proteomics 2024, 24: 100897. PMID: 39708910, PMCID: PMC11787651, DOI: 10.1016/j.mcpro.2024.100897.Peer-Reviewed Original ResearchMeSH KeywordsChromatography, LiquidHigh-Throughput Screening AssaysHistone Deacetylase InhibitorsHistonesHumansMass SpectrometryPeptidesProtein Processing, Post-TranslationalProteomicsConceptsData-independent acquisitionModified histone peptidesLC-MSMass spectrometry (MS)-based approachesMicroflow liquid chromatographyNanoflow LC-MSPost-translational modificationsIsobaric peptidesQTOF instrumentLC gradientSequential window acquisitionHistone post-translational modificationsMass spectrometerHistone peptidesTransforming growth factor beta 1Histone deacetylase inhibitorsHistone samplesWindow acquisitionOrbitrapLow stoichiometryLiquid chromatographyCharacterization of histone PTMsHigh-throughput methodDeacetylase inhibitorsInstrumentation timeIdentification of coilin interactors reveals coordinated control of Cajal body number and structure
Escayola D, Zhang C, Nischwitz E, Schärfen L, Dörner K, Straube K, Kutay U, Butter F, Neugebauer K. Identification of coilin interactors reveals coordinated control of Cajal body number and structure. Journal Of Cell Biology 2024, 224: e202305081. PMID: 39602297, PMCID: PMC11602656, DOI: 10.1083/jcb.202305081.Peer-Reviewed Original ResearchMeSH KeywordsCell NucleusCoiled BodiesCytoskeletal ProteinsHeLa CellsHumansNuclear ProteinsProtein BindingProtein Processing, Post-TranslationalRibosomal ProteinsRibosome Subunits, Large, EukaryoticSMN Complex ProteinsConceptsCajal bodiesSurvival motor neuron proteinCB assemblyModulating posttranslational modificationsRegulate RNA processingProtein interactorsProximity biotinylationRNA processingGenetic lociPosttranslational modificationsGene activationTranscription factorsFunctional screeningBiomolecular condensatesCoilinNeuronal proteinsCell nucleiProteinNuclear levelsNuclear positivityCB componentsCB numberBody numberAssemblyRibosomeA proteogenomic analysis of cervical cancer reveals therapeutic and biological insights
Yu J, Gui X, Zou Y, Liu Q, Yang Z, An J, Guo X, Wang K, Guo J, Huang M, Zhou S, Zuo J, Chen Y, Deng L, Yuan G, Li N, Song Y, Jia J, Zeng J, Zhao Y, Liu X, Du X, Liu Y, Wang P, Zhang B, Ding L, Robles A, Rodriguez H, Zhou H, Shao Z, Wu L, Gao D. A proteogenomic analysis of cervical cancer reveals therapeutic and biological insights. Nature Communications 2024, 15: 10114. PMID: 39578447, PMCID: PMC11584810, DOI: 10.1038/s41467-024-53830-0.Peer-Reviewed Original ResearchMeSH KeywordsAcetylationAdultBiomarkers, TumorCell Line, TumorCell ProliferationE1A-Associated p300 ProteinFemaleGene Expression Regulation, NeoplasticHumansMiddle AgedPapillomaviridaePapillomavirus InfectionsPrognosisProtein Kinase C betaProtein Processing, Post-TranslationalProteogenomicsProto-Oncogene Proteins c-fosUterine Cervical NeoplasmsConceptsCervical cancerIncidence of cervical cancerIntegrative proteogenomic analysisMulti-omic changesHuman papillomavirusImmune infiltrationSignificant public health issueProteogenomic analysisGenetic alterationsCC patientsPatient subgroupsMalignant proliferationAnalysis of cervical cancerCC tumorsChinese womenPost-translational modifications regulationPublic health issuePotential treatmentScreening strategiesClinical practiceProliferation of CC cellsPatientsWomen's healthCancerLow-income countriesBalancing acts: The posttranslational modification tightrope of flavivirus replication
Boytz R, Laurent-Rolle M. Balancing acts: The posttranslational modification tightrope of flavivirus replication. PLOS Pathogens 2024, 20: e1012626. PMID: 39466723, PMCID: PMC11516179, DOI: 10.1371/journal.ppat.1012626.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsMeSH KeywordsAnimalsFlavivirusFlavivirus InfectionsHumansImmunity, InnateProtein Processing, Post-TranslationalSumoylationUbiquitinationViral ProteinsVirus ReplicationOrganization of a functional glycolytic metabolon on mitochondria for metabolic efficiency
Wang H, Vant J, Zhang A, Sanchez R, Wu Y, Micou M, Luczak V, Whiddon Z, Carlson N, Yu S, Jabbo M, Yoon S, Abushawish A, Ghassemian M, Masubuchi T, Gan Q, Watanabe S, Griffis E, Hammarlund M, Singharoy A, Pekkurnaz G. Organization of a functional glycolytic metabolon on mitochondria for metabolic efficiency. Nature Metabolism 2024, 6: 1712-1735. PMID: 39261628, DOI: 10.1038/s42255-024-01121-9.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsGlucoseGlycolysisHexokinaseHumansMiceMitochondriaN-AcetylglucosaminyltransferasesNeuronsOxidative PhosphorylationProtein Processing, Post-TranslationalConceptsO-GlcNAc transferaseO-GlcNAcylation sitesGlycolytic metabolonO-GlcNAcylationEnzyme O-GlcNAc transferaseOuter mitochondrial membraneDynamic O-GlcNAcylationPost-translational modificationsReduced ATP generationMitochondrial ATP productionMetabolic efficiencyEnergy-demanding tissuesCellular energy sourceOGT activityMitochondrial associationRegulatory domainMitochondrial membraneMultiple cell typesATP generationATP productionMitochondrial functionMitochondrial couplingMetabolonCell typesGlucose fluxPTMoreR-enabled cross-species PTM mapping and comparative phosphoproteomics across mammals
Wang S, Di Y, Yang Y, Salovska B, Li W, Hu L, Yin J, Shao W, Zhou D, Cheng J, Liu D, Yang H, Liu Y. PTMoreR-enabled cross-species PTM mapping and comparative phosphoproteomics across mammals. Cell Reports Methods 2024, 4: 100859. PMID: 39255793, PMCID: PMC11440062, DOI: 10.1016/j.crmeth.2024.100859.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsHumansMammalsMicePhosphoproteinsPhosphorylationProtein Processing, Post-TranslationalProteomeProteomicsSoftwareSpecies SpecificityConceptsP-siteSurrounding amino acid sequenceKinase-substrate networkQuantitative phosphoproteomic analysisFunctional enrichment analysisPhosphoproteomic resultsKinase motifsComparative phosphoproteomicsPTM sitesPhosphorylation eventsPhosphoproteomic analysisProteomic analysisEnrichment analysisMammalian speciesSpeciesEvolutionary anglePhosphoproteomeMotifEnvironmental factorsNon-human speciesPTMProteomicsKinaseMammalsProteinGlycoproteomics: Charting new territory in mass spectrometry and glycobiology
Malaker S. Glycoproteomics: Charting new territory in mass spectrometry and glycobiology. Journal Of Mass Spectrometry 2024, 59: e5034. PMID: 38726698, DOI: 10.1002/jms.5034.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsGlycomicsGlycopeptidesGlycoproteinsGlycosylationHumansMass SpectrometryPolysaccharidesProtein Processing, Post-TranslationalProteomicsSoftware
2023
The SysteMHC Atlas v2.0, an updated resource for mass spectrometry-based immunopeptidomics
Huang X, Gan Z, Cui H, Lan T, Liu Y, Caron E, Shao W. The SysteMHC Atlas v2.0, an updated resource for mass spectrometry-based immunopeptidomics. Nucleic Acids Research 2023, 52: d1062-d1071. PMID: 38000392, PMCID: PMC10767952, DOI: 10.1093/nar/gkad1068.Peer-Reviewed Original ResearchAnimalsDatabases, ProteinHumansInternetMass SpectrometryPeptidesProtein Processing, Post-TranslationalProteomicsNatural isoaspartyl protein modification of ZAP70 alters T cell responses in lupus
Yang M, Lam T, Kanyo J, Kang I, Zhou Z, Clarke S, Mamula M. Natural isoaspartyl protein modification of ZAP70 alters T cell responses in lupus. Autoimmunity 2023, 56: 2282945. PMID: 37994408, PMCID: PMC10897934, DOI: 10.1080/08916934.2023.2282945.Peer-Reviewed Original ResearchAutoimmunityHumansOxidative StressProtein D-Aspartate-L-Isoaspartate MethyltransferaseProtein Processing, Post-TranslationalT-LymphocytesZAP-70 Protein-Tyrosine KinaseAcetyl-methyllysine marks chromatin at active transcription start sites
Lu-Culligan W, Connor L, Xie Y, Ekundayo B, Rose B, Machyna M, Pintado-Urbanc A, Zimmer J, Vock I, Bhanu N, King M, Garcia B, Bleichert F, Simon M. Acetyl-methyllysine marks chromatin at active transcription start sites. Nature 2023, 622: 173-179. PMID: 37731000, PMCID: PMC10845139, DOI: 10.1038/s41586-023-06565-9.Peer-Reviewed Original ResearchMeSH KeywordsAcetylationAnimalsChromatinHistone DeacetylasesHistonesHumansLysineMethylationPeptidesProtein Processing, Post-TranslationalTranscription Initiation SiteConceptsPost-translational modificationsLysine residuesActive transcription start sitesTranscription start siteRange of speciesChromatin biologyChromatin proteinsLysine methylationActive chromatinProteins BRD2Transcriptional initiationLysine acetylationHistone H4Start siteMammalian tissuesHuman diseasesSame residuesMethylationAcetylationChromatinResiduesProteinBiological signalsHistonesBRD2System‐wide optimization of an orthogonal translation system with enhanced biological tolerance
Mohler K, Moen J, Rogulina S, Rinehart J. System‐wide optimization of an orthogonal translation system with enhanced biological tolerance. Molecular Systems Biology 2023, 19: msb202110591. PMID: 37477096, PMCID: PMC10407733, DOI: 10.15252/msb.202110591.Peer-Reviewed Original ResearchConceptsOrthogonal translation systemHost interactionsNon-standard amino acidsPost-translational modificationsSystems-level biologyStress response activationTranslation systemSynthetic biological systemsCellular physiologyProtein phosphorylationOTS performanceHost physiologyCellular environmentAmino acidsCellular mechanismsDeleterious interactionsResponse activationBiological systemsPhysiologyOTS developmentUnparalleled accessPhosphorylationHost toxicityBiologyInteractionAcetylation of MLH1 by CBP increases cellular DNA mismatch repair activity
Zhang M, Zhao J, Glazer P, Bai W, Bepler G, Zhang X. Acetylation of MLH1 by CBP increases cellular DNA mismatch repair activity. The Journal Of Biochemistry 2023, 174: 183-191. PMID: 37094360, DOI: 10.1093/jb/mvad034.Peer-Reviewed Original ResearchMeSH KeywordsAcetylationCREB-Binding ProteinDNADNA Mismatch RepairDNA RepairProtein Processing, Post-TranslationalConceptsMutLα complexMMR activityUbiquitin-proteasome degradation pathwayDNA mismatch repair activityDNA damage responsePost-translational modificationsCell cycle checkpointsOverexpression of CBPMismatch repair activityDNA base pair mismatchesInsertions/deletionsDNA mismatch repair proteinsGenomic integrityDamage responseDNA replicationCycle checkpointsRepair proteinsTrichostatin ABase pair mismatchesNovel roleMismatch repair proteinsRepair activityCBPProteinDeacetylase inhibitorsUncovering biology by single-cell proteomics
Mansuri M, Williams K, Nairn A. Uncovering biology by single-cell proteomics. Communications Biology 2023, 6: 381. PMID: 37031277, PMCID: PMC10082756, DOI: 10.1038/s42003-023-04635-2.Peer-Reviewed Original ResearchCurrent landscape of translational and clinical research in myelodysplastic syndromes/neoplasms (MDS): Proceedings from the 1st International Workshop on MDS (iwMDS) Of the International Consortium for MDS (icMDS)
Bewersdorf J, Xie Z, Bejar R, Borate U, Boultwood J, Brunner A, Buckstein R, Carraway H, Churpek J, Daver N, Porta M, DeZern A, Fenaux P, Figueroa M, Gore S, Griffiths E, Halene S, Hasserjian R, Hourigan C, Kim T, Komrokji R, Kuchroo V, List A, Loghavi S, Majeti R, Odenike O, Patnaik M, Platzbecker U, Roboz G, Sallman D, Santini V, Sanz G, Sekeres M, Stahl M, Starczynowski D, Steensma D, Taylor J, Abdel-Wahab O, Xu M, Savona M, Wei A, Zeidan A. Current landscape of translational and clinical research in myelodysplastic syndromes/neoplasms (MDS): Proceedings from the 1st International Workshop on MDS (iwMDS) Of the International Consortium for MDS (icMDS). Blood Reviews 2023, 60: 101072. PMID: 36934059, DOI: 10.1016/j.blre.2023.101072.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsMeSH KeywordsAnimalsCell- and Tissue-Based TherapyEpigenomicsHumansMyelodysplastic SyndromesNeoplasmsProtein Processing, Post-TranslationalConceptsImmune checkpoint inhibitorsSpecific molecular alterationsNovel animal modelInnate immune systemCheckpoint inhibitorsImmune dysregulationMDS patientsClinical trialsNovel therapiesTherapeutic strategiesAnimal modelsGermline predispositionImmune systemMolecular alterationsClinical researchInternational ConsortiumNeoplasmsClinical workGenetic landscapeInternational WorkshopPatientsCurrent landscapePathogenesisTherapyDiseasePost‐translational modification and phenotype
Salovska B, Liu Y. Post‐translational modification and phenotype. Proteomics 2023, 23: e2200535. PMID: 36799530, DOI: 10.1002/pmic.202200535.Peer-Reviewed Original ResearchPhenotypeProtein Processing, Post-Translational
2022
Mechanistic insight into female predominance in Alzheimer’s disease based on aberrant protein S-nitrosylation of C3
Yang H, Oh C, Amal H, Wishnok J, Lewis S, Schahrer E, Trudler D, Nakamura T, Tannenbaum S, Lipton S. Mechanistic insight into female predominance in Alzheimer’s disease based on aberrant protein S-nitrosylation of C3. Science Advances 2022, 8: eade0764. PMID: 36516243, PMCID: PMC9750152, DOI: 10.1126/sciadv.ade0764.Peer-Reviewed Original ResearchConceptsAlzheimer's diseaseAD brainPostmortem Alzheimer's diseaseComplement component 3Sex-dependent mannerConsequent cognitive declineSynaptic phagocytosisΒ-estradiol levelsFemale predominanceAberrant protein S-nitrosylationSynaptic damageAD pathogenesisSNO proteinsCognitive declineProtein SDiseaseRobust alterationsBrainComponent 3Protein S-nitrosylationHuman brainS-nitrosylationS-nitrosoproteomePatientsPathogenesisToward a hypothesis‐free understanding of how phosphorylation dynamically impacts protein turnover
Li W, Salovska B, Fornasiero E, Liu Y. Toward a hypothesis‐free understanding of how phosphorylation dynamically impacts protein turnover. Proteomics 2022, 23: e2100387. PMID: 36422574, PMCID: PMC10964180, DOI: 10.1002/pmic.202100387.Peer-Reviewed Original ResearchMeSH KeywordsIsotope LabelingMass SpectrometryPhosphorylationProtein Processing, Post-TranslationalProteolysisProteomeConceptsPost-translational modificationsProtein turnoverDynamic stable isotope labelingCell starvationStable isotope labelingData-independent acquisition mass spectrometryAcquisition mass spectrometryProteome levelTurnover diversityPhosphoproteomic datasetsPhosphorylation stoichiometryMetabolic labelingIsotope labelingMass spectrometryPhosphorylationAmino acidsCell culturesBiological perspectiveStarvationTurnoverTurnover measurementsRecent studiesSILACProteoformsPeptidoformsCarbonyl Posttranslational Modification Associated With Early-Onset Type 1 Diabetes Autoimmunity.
Yang ML, Connolly SE, Gee RJ, Lam TT, Kanyo J, Peng J, Guyer P, Syed F, Tse HM, Clarke SG, Clarke CF, James EA, Speake C, Evans-Molina C, Arvan P, Herold KC, Wen L, Mamula MJ. Carbonyl Posttranslational Modification Associated With Early-Onset Type 1 Diabetes Autoimmunity. Diabetes 2022, 71: 1979-1993. PMID: 35730902, PMCID: PMC9450849, DOI: 10.2337/db21-0989.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAutoantigensAutoimmunityDiabetes Mellitus, Type 1HumansInsulinIslets of LangerhansMiceMice, Inbred NODProinsulinProtein Processing, Post-TranslationalProteinsConceptsType 1 diabetesNOD miceMurine type 1 diabetesHuman type 1 diabetesDecreased glucose-stimulated insulin secretionAnti-insulin autoimmunityPrediabetic NOD miceGlucose-stimulated insulin secretionOnset Type 1T cell responsesOnset of hyperglycemiaCirculation of patientsAutoreactive CD4Insulin ratioInsulin secretionDiabetesPancreatic isletsType 1Islet proteinsOxidative stressAutoimmunitySelect groupMiceCarbonyl modificationOnsetChromatin profiling in human neurons reveals aberrant roles for histone acetylation and BET family proteins in schizophrenia
Farrelly L, Zheng S, Schrode N, Topol A, Bhanu N, Bastle R, Ramakrishnan A, Chan J, Cetin B, Flaherty E, Shen L, Gleason K, Tamminga C, Garcia B, Li H, Brennand K, Maze I. Chromatin profiling in human neurons reveals aberrant roles for histone acetylation and BET family proteins in schizophrenia. Nature Communications 2022, 13: 2195. PMID: 35459277, PMCID: PMC9033776, DOI: 10.1038/s41467-022-29922-0.Peer-Reviewed Original ResearchMeSH KeywordsAcetylationCell Cycle ProteinsChromatinHistonesHumansInduced Pluripotent Stem CellsNerve Tissue ProteinsNeuronsNuclear ProteinsProtein Processing, Post-TranslationalReceptors, Cell SurfaceSchizophreniaTranscription FactorsConceptsHistone posttranslational modificationsPosttranslational modificationsUnbiased proteomic approachPluripotent stem cellsPatient-derived neuronsH2A.Z acetylationChromatin profilingHyperacetylated histonesFamily proteinsProteomic approachProtein interactionsHistone acetylationTranscriptional abnormalitiesEpigenetic factorsExtraterminal (BET) proteinsSZ casesRisk variantsHuman neuronsStem cellsAberrant roleProtein inhibitionBona fideTreatment of schizophreniaPostmortem human brainCritical role
2021
A peptidoform based proteomic strategy for studying functions of post‐translational modifications
Liu Y. A peptidoform based proteomic strategy for studying functions of post‐translational modifications. Proteomics 2021, 22: e2100316. PMID: 34878717, PMCID: PMC8959388, DOI: 10.1002/pmic.202100316.Peer-Reviewed Original Research
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