2024
Development of a Shigella conjugate vaccine targeting Shigella flexneri 6 that is immunogenic and provides protection against virulent challenge
Kelly M, Janardhanan J, Wagh C, Verma S, Charles R, Leung D, Kamruzzaman M, Pansuriya R, Chowdhury F, Vann W, Kaminski R, Khan A, Bhuiyan T, Qadri F, Kováč P, Xu P, Ryan E. Development of a Shigella conjugate vaccine targeting Shigella flexneri 6 that is immunogenic and provides protection against virulent challenge. Vaccine 2024, 42: 126263. PMID: 39217775, PMCID: PMC11409015, DOI: 10.1016/j.vaccine.2024.126263.Peer-Reviewed Original ResearchS. flexneri 6O-specific polysaccharideS. flexneri 3aShigella flexneri 2aShigella flexneri 6Component of lipopolysaccharideSerotype-specific monoclonal antibodiesS. sonneiShigella speciesFlexneri 2aShigella infectionShigella vaccineCarrier proteinHeavy chainBactericidal antibody responsesShigellaShigellosisVaccinated miceConjugate vaccineSerum of humansIgG responsesImmune responseLethal challengeAntibody responseIgM responseEmerging Cerebrospinal Fluid Biomarkers of Disease Activity and Progression in Multiple Sclerosis
Cross A, Gelfand J, Thebault S, Bennett J, von Büdingen H, Cameron B, Carruthers R, Edwards K, Fallis R, Gerstein R, Giacomini P, Greenberg B, Hafler D, Ionete C, Kaunzner U, Kodama L, Lock C, Longbrake E, Musch B, Pardo G, Piehl F, Weber M, Yuen S, Ziemssen T, Bose G, Freedman M, Anania V, Ramesh A, Winger R, Jia X, Herman A, Harp C, Bar-Or A. Emerging Cerebrospinal Fluid Biomarkers of Disease Activity and Progression in Multiple Sclerosis. JAMA Neurology 2024, 81: 373-383. PMID: 38466277, PMCID: PMC10928543, DOI: 10.1001/jamaneurol.2024.0017.Peer-Reviewed Original ResearchPrimary progressive MSGlial fibrillary acidic proteinNeurofilament heavy chainRelapsing MSCerebrospinal fluidTest cohortMultiple sclerosisDisease-modifying MS therapyMulticenter study of patientsBiomarkers of disease activityAnti-CD20 treatmentCentral nervous system biologyClinical follow-upConfirmation cohortT2 lesion volumeStudy of patientsHeavy chainCSF-GFAP levelsMS disease progressionMagnetic resonance imaging measuresNeurofilament light chainActivated glial markersStudy assessed dataFibrillary acidic proteinAnti-CD20
2023
Discovery of the first unconventional myosin: Acanthamoeba myosin-I
Pollard T, Korn E. Discovery of the first unconventional myosin: Acanthamoeba myosin-I. Frontiers In Physiology 2023, 14: 1324623. PMID: 38046947, PMCID: PMC10693453, DOI: 10.3389/fphys.2023.1324623.Peer-Reviewed Original ResearchUnconventional myosinActin filamentsMyosin heavy chain kinaseFirst unconventional myosinsEvolution of eukaryotesClass I MyosinHeavy chain kinaseNovel unconventional myosinPhylogenetic analysisSlime moldMembrane lipidsChain kinaseProteolytic fragmentsHeavy chainMuscle myosinMyosinCofactorEnzymeMg-ATPaseMg-ATPase activityEukaryotesFilamentsCrude enzymeKinaseActin
2022
SARS-CoV-2 accessory proteins ORF7a and ORF3a use distinct mechanisms to down-regulate MHC-I surface expression
Arshad N, Laurent-Rolle M, Ahmed W, Hsu J, Mitchell S, Pawlak J, Sengupta D, Biswas K, Cresswell P. SARS-CoV-2 accessory proteins ORF7a and ORF3a use distinct mechanisms to down-regulate MHC-I surface expression. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 120: e2208525120. PMID: 36574644, PMCID: PMC9910621, DOI: 10.1073/pnas.2208525120.Peer-Reviewed Original ResearchConceptsMHC-I expressionSARS-CoV-2Major histocompatibility complex (MHC) class I moleculesT cell recognitionVirus-infected cellsClass I moleculesAntigen presentationOngoing COVID-19 pandemicHeavy chainImmune evasionViral peptidesSecretory pathwayDistinct mechanismsMHCI moleculesPeptide-MHCInfected cellsCausative agentCell recognitionCD8COVID-19 pandemicViral proteinsEndoplasmic reticulumHuman MHCORF7a
2021
Cryo‐EM Structures of Outer‐arm Dynein Array Bound to Microtubule Doublet Reveal a Mechanism for Motor Coordination
Rao Q, Wang Y, Chai P, Kuo Y, Han L, Yang R, Yang Y, Howard J, Zhang K. Cryo‐EM Structures of Outer‐arm Dynein Array Bound to Microtubule Doublet Reveal a Mechanism for Motor Coordination. The FASEB Journal 2021, 35 DOI: 10.1096/fasebj.2021.35.s1.03099.Peer-Reviewed Original ResearchOuter arm dyneinMicrotubule-bound stateInner arm dyneinsCentral pair complexMicrotubule-binding domainMicrotubule doubletsIntermediate chainATP hydrolysisFundamental cellular processesHeavy chainCryo-EM structureCryo-EM analysisCryo-electron tomographyKey motor proteinCryo-electron microscopyLight chainCellular processesEukaryotic ciliaT. thermophilaEmbryonic developmentAdjacent microtubule doubletsCellular motilityMotor proteinsAxonemal dyneinsMotile cilia
2018
Expression and clinical significance of antigen presentation components beta-2 microglobulin, HLA class I heavy chains, and HLA class II in non-small cell lung cancer (NSCLC).
Datar I, Villarroel-Espindola F, Henick B, Syrigos K, Toki M, Rimm D, Ferrone S, Herbst R, Schalper K. Expression and clinical significance of antigen presentation components beta-2 microglobulin, HLA class I heavy chains, and HLA class II in non-small cell lung cancer (NSCLC). Journal Of Clinical Oncology 2018, 36: 12015-12015. DOI: 10.1200/jco.2018.36.15_suppl.12015.Peer-Reviewed Original Research
2014
Chemokine-coupled β2 integrin–induced macrophage Rac2–Myosin IIA interaction regulates VEGF-A mRNA stability and arteriogenesis
Morrison AR, Yarovinsky TO, Young BD, Moraes F, Ross TD, Ceneri N, Zhang J, Zhuang ZW, Sinusas AJ, Pardi R, Schwartz MA, Simons M, Bender JR. Chemokine-coupled β2 integrin–induced macrophage Rac2–Myosin IIA interaction regulates VEGF-A mRNA stability and arteriogenesis. Journal Of Experimental Medicine 2014, 211: 1957-1968. PMID: 25180062, PMCID: PMC4172219, DOI: 10.1084/jem.20132130.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsArteriesCD18 AntigensDNA PrimersFlow CytometryHumansMiceMice, Inbred C57BLMonocytesNeovascularization, PhysiologicNonmuscle Myosin Type IIArac GTP-Binding ProteinsReal-Time Polymerase Chain ReactionReceptors, CCR2RNA StabilityVascular Endothelial Growth Factor AX-Ray MicrotomographyConceptsMyosin IIASignal transduction eventsHuR translocationRapid nuclearTransduction eventsProteomic analysisProtein HuR.Induction of arteriogenesisMRNA stabilityMRNA stabilizationNovel roleCytosolic translocationMyosin-9ICAM-1 adhesionReceptor engagementDevelopmental vasculogenesisCellular effectorsMolecular triggersTranslocationHeavy chainGrowth factorMyeloid cellsVascular endothelial growth factorKey molecular triggerCCL2 stimulation
2010
Contribution of Amino Acid Region 659−663 of Factor Va Heavy Chain to the Activity of Factor Xa within Prothrombinase,
Hirbawi J, Vaughn J, Bukys M, Vos H, Kalafatis M. Contribution of Amino Acid Region 659−663 of Factor Va Heavy Chain to the Activity of Factor Xa within Prothrombinase,. Biochemistry 2010, 49: 8520-8534. PMID: 20722419, PMCID: PMC2946813, DOI: 10.1021/bi101097t.Peer-Reviewed Original ResearchRegulation of CD1 Antigen-presenting Complex Stability*
Odyniec A, Barral D, Garg S, Tatituri R, Besra G, Brenner M. Regulation of CD1 Antigen-presenting Complex Stability*. Journal Of Biological Chemistry 2010, 285: 11937-11947. PMID: 20133943, PMCID: PMC2852931, DOI: 10.1074/jbc.m109.077933.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigen PresentationAntigens, CD1beta 2-MicroglobulinCell LineCell MembraneEndosomesHeLa CellsHistocompatibility Antigens Class IHistocompatibility Antigens Class IIHumansHydrogen-Ion ConcentrationLysosomesMiceMultiprotein ComplexesProtein IsoformsProtein StabilityRecombinant ProteinsTransfectionConceptsCD1 heavy chainsCell surfaceHeavy chainEndosomal pHQuality control mechanismsCD1 proteinsCell surface pHCD1 isoformsLipid antigensAcidic endosomal pHAntigen-loading complexesPH optimaAcidic pHIntracellular compartmentsMildly acidic pHLipid exchangeAntigen bindingNeutral pHTraffickingPeptide antigensCellsBindingCD1LipidBeta(2)-microglobulin
2009
A PH domain within OCRL bridges clathrin‐mediated membrane trafficking to phosphoinositide metabolism
Mao Y, Balkin DM, Zoncu R, Erdmann KS, Tomasini L, Hu F, Jin MM, Hodsdon ME, De Camilli P. A PH domain within OCRL bridges clathrin‐mediated membrane trafficking to phosphoinositide metabolism. The EMBO Journal 2009, 28: 1831-1842. PMID: 19536138, PMCID: PMC2711190, DOI: 10.1038/emboj.2009.155.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesClathrinCoated VesiclesEndocytosisHeLa CellsHumansModels, MolecularMolecular Sequence DataMutationNuclear Magnetic Resonance, BiomolecularPhosphatidylinositolsPhospholipidsPhosphoric Monoester HydrolasesProtein ConformationProtein Structure, TertiaryRatsSequence AlignmentConceptsPH domainNH2-terminal portionEndocytic clathrin-coated pitsClathrin-binding siteClathrin-coated pitsNMR structure determinationNH2-terminal regionCOOH-terminal regionClathrin-box motifsMembrane traffickingEvolutionary pressureSimilar proteinsINPP5BOCRLSpecialized functionsSequence dissimilarityLowe syndromePhosphoinositide metabolismDent's diseaseHeavy chainMutationsRecruitment efficiencyStructure determinationMetabolismDomain
2006
Peptide motifs of the single dominantly expressed class I molecule explain the striking MHC-determined response to Rous sarcoma virus in chickens
Wallny H, Avila D, Hunt L, Powell T, Riegert P, Salomonsen J, Skjødt K, Vainio O, Vilbois F, Wiles M, Kaufman J. Peptide motifs of the single dominantly expressed class I molecule explain the striking MHC-determined response to Rous sarcoma virus in chickens. Proceedings Of The National Academy Of Sciences Of The United States Of America 2006, 103: 1434-1439. PMID: 16432226, PMCID: PMC1360531, DOI: 10.1073/pnas.0507386103.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsAntigen PresentationAvian Sarcoma VirusesChickensDNA, ComplementaryElectrophoresis, Gel, Two-DimensionalFlow CytometryGenes, DominantGenes, MHC Class IHaplotypesModels, MolecularMolecular Sequence DataPeptidesPoultry DiseasesSarcoma, AvianSequence Homology, Amino AcidTime FactorsConceptsExpressed class I moleculeRous sarcoma virusPeptide motifsB12 haplotypeSarcoma virusMinimal essential MHCB15 haplotypePulse-labeled cellsLevels of RNAClass I genesClass I moleculesAbundant cDNAPooled sequencingI geneChicken MHCHaplotypesCDNAI moleculesMotifHeavy chainMHC functionSusceptibility to Rous sarcoma virusMHC haplotypesIndividual peptidesMammals
2002
Ly-6 Superfamily Members Ly-6A/E, Ly-6C, and Ly-6I Recognize Two Potential Ligands Expressed by B Lymphocytes
Pflugh DL, Maher SE, Bothwell AL. Ly-6 Superfamily Members Ly-6A/E, Ly-6C, and Ly-6I Recognize Two Potential Ligands Expressed by B Lymphocytes. The Journal Of Immunology 2002, 169: 5130-5136. PMID: 12391229, DOI: 10.4049/jimmunol.169.9.5130.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDAntigens, Differentiation, B-LymphocyteAntigens, LyB-Lymphocyte SubsetsCD59 AntigensCell Adhesion MoleculesCHO CellsCOS CellsCricetinaeGenetic VariationImmunoglobulin Constant RegionsImmunoglobulin mu-ChainsLectinsLigandsMembrane ProteinsMiceMice, Inbred C57BLMultigene FamilyMyeloid CellsProtein BindingRecombinant Fusion ProteinsSialic Acid Binding Ig-like Lectin 2TransfectionTumor Cells, CulturedConceptsLy-6 proteinsLy-6A/EChimeric proteinLy-6 moleculesMost hemopoietic cellsGlycosylphosphatidylinositol-linked proteinsMature B cellsMembrane proteinsLipid raftsLy-6ECell adhesion moleculeStages of differentiationMature B lymphocytesAnalysis of variantsIgM heavy chainSupergene familyCH27 cellsProteinHemopoietic cellsLigand activityLy-6CHeavy chainPotential ligandsB lymphocytesAdhesion moleculesAnalysis of structure and function relationships of an autoantigenic peptide of insulin bound to H-2Kd that stimulates CD8 T cells in insulin-dependent diabetes mellitus
Wong F, Moustakas A, Wen L, Papadopoulos G, Janeway C. Analysis of structure and function relationships of an autoantigenic peptide of insulin bound to H-2Kd that stimulates CD8 T cells in insulin-dependent diabetes mellitus. Proceedings Of The National Academy Of Sciences Of The United States Of America 2002, 99: 5551-5556. PMID: 11943852, PMCID: PMC122807, DOI: 10.1073/pnas.072037299.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAutoantigensCD8-Positive T-LymphocytesCell DivisionCell LineChromium RadioisotopesDiabetes Mellitus, Type 1Dose-Response Relationship, DrugH-2 AntigensInsulinInterferon-gammaMiceMice, Inbred NODModels, MolecularPeptidesProtein BindingReceptor, InsulinStructure-Activity RelationshipTime FactorsConceptsT cellsCD8 T cell clonesInsulin-dependent diabetes mellitusInduction of CD8CD8 T cellsPathogenic T cellsT cell clonesT cell stimulationSmall glycine residueMHC-peptide complexesDiabetes mellitusAutoantigenic peptidesH-2KdCell clonesGlutamate residuesHydrophobic residuesGlycine residueReceptor interaction sitesCell stimulationFunctional assaysInteraction sitesFunction relationshipsPeptide substitutionProductive interactionHeavy chain
2000
Distinct Domains of CD98hc Regulate Integrins and Amino Acid Transport*
Fenczik C, Zent R, Dellos M, Calderwood D, Satriano J, Kelly C, Ginsberg M. Distinct Domains of CD98hc Regulate Integrins and Amino Acid Transport*. Journal Of Biological Chemistry 2000, 276: 8746-8752. PMID: 11121428, DOI: 10.1074/jbc.m011239200.Peer-Reviewed Original ResearchConceptsAmino acid transportIntegrin functionAcid transportDistinct domainsType II transmembrane proteinIsoleucine transportAmino acid transportersCD98 heavy chainCell surface heterodimersTransmembrane domainCytoplasmic domainTransmembrane proteinSurface heterodimersExtracellular domainAcid transportersCD98hcHeavy chainProteinIntegrinsCovalent linkageDifferent light chainsLight chainDomainMutantsHeterodimers
1999
Insulin-like growth factor I stimulates cardiac myosin heavy chain and actin synthesis in the awake rat
Young L, Renfu Y, Hu X, Chong S, Hasan S, Jacob R, Sherwin R. Insulin-like growth factor I stimulates cardiac myosin heavy chain and actin synthesis in the awake rat. American Journal Of Physiology 1999, 276: e143-e150. PMID: 9886960, DOI: 10.1152/ajpendo.1999.276.1.e143.Peer-Reviewed Original ResearchConceptsInsulin-like growth factor IGrowth factor IAwake ratsMyosin heavy chainFactor IContractile protein synthesisIGF-I infusionLow-dose IGFMixed cardiac proteinsCardiac myosin heavy chainMyosin synthesisBlood pressureOvernight fastIntravenous infusionRight ventricleHeavy chainHeart rateHypoglycemic effectFed ratsIGFRatsDirect actionProtein synthesisSalineCardiac proteins
1998
Assembly of MHC class I molecules with biosynthesized endoplasmic reticulum-targeted peptides is inefficient in insect cells and can be enhanced by protease inhibitors.
Deng Y, Gibbs J, Bačík I, Porgador A, Copeman J, Lehner P, Ortmann B, Cresswell P, Bennink J, Yewdell J. Assembly of MHC class I molecules with biosynthesized endoplasmic reticulum-targeted peptides is inefficient in insect cells and can be enhanced by protease inhibitors. The Journal Of Immunology 1998, 161: 1677-85. PMID: 9712031, DOI: 10.4049/jimmunol.161.4.1677.Peer-Reviewed Original ResearchMeSH KeywordsAedesAnimalsAntibodies, MonoclonalAntiportersCell LineEndoplasmic ReticulumH-2 AntigensHeLa CellsHumansImmunoglobulinsLymphocyte ActivationMacromolecular SubstancesMembrane Transport ProteinsMiceOligopeptidesOvalbuminPeptide FragmentsProtease InhibitorsRecombinant ProteinsT-LymphocytesVaccinia virusConceptsInsect cellsEndoplasmic reticulumVertebrate cellsHuman cellsHuman tapasinVaccinia virus-mediated expressionCell surface expressionProtease inhibitorsInefficient assemblyKbMHC class IMouse betaInsectsEfficient assemblyImmediate precursorSurface expressionAntigenic peptidesHeavy chainClass IRecombinant vaccinia virusVirus-mediated expressionAssemblyExpressionCellsVaccinia virus
1997
Regulation of Distinct Stages of Skeletal Muscle Differentiation by Mitogen-Activated Protein Kinases
Bennett A, Tonks N. Regulation of Distinct Stages of Skeletal Muscle Differentiation by Mitogen-Activated Protein Kinases. Science 1997, 278: 1288-1291. PMID: 9360925, DOI: 10.1126/science.278.5341.1288.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium-Calmodulin-Dependent Protein KinasesCell Cycle ProteinsCell DifferentiationCell DivisionCell LineCloning, MolecularCulture MediaCyclin D1Dual Specificity Phosphatase 1Gene Expression Regulation, DevelopmentalImmediate-Early ProteinsJNK Mitogen-Activated Protein KinasesMiceMitogen-Activated Protein Kinase 1Mitogen-Activated Protein KinasesMitogensMuscle ProteinsMuscle, SkeletalPhosphoprotein PhosphatasesPhosphorylationProtein Phosphatase 1Protein Tyrosine PhosphatasesRecombinant Fusion ProteinsSignal TransductionTetracyclineTranscription, GeneticConceptsMuscle-specific gene expressionMAPK phosphatase-1Skeletal muscle differentiationMuscle differentiationGene expressionMitogen-activated protein kinaseMuscle-specific genesSignal transduction pathwaysMKP-1 overexpressionPhosphatase 1Extracellular signalsProtein kinaseTransduction pathwaysMitogen withdrawalC2C12 myoblastsDifferentiated myocytesMyotube formationEndogenous expressionMyosin heavy chainMyogenesisDifferentiationHeavy chainExpressionOverexpressionAppropriate expressionMisfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome
Hughes E, Hammond C, Cresswell P. Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 1896-1901. PMID: 9050876, PMCID: PMC20014, DOI: 10.1073/pnas.94.5.1896.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcysteinebeta 2-MicroglobulinBlotting, WesternCysteine EndopeptidasesCysteine Proteinase InhibitorsCytoplasmEndoplasmic ReticulumEnzyme InhibitorsGlycosylationHistocompatibility Antigens Class IHumansKineticsLeupeptinsMultienzyme ComplexesProteasome Endopeptidase ComplexProtein FoldingSolubilityTransfectionTumor Cells, CulturedConceptsClass I heavy chainsMHC class I heavy chainMajor histocompatibility complex class I heavy chainsBeta2-microglobulinHeavy chainMHC class ICell linesCell line DaudiTAP-deficient cell linesSpecific irreversible inhibitorClass IHerpes simplex virus proteinDaudiVirus proteinsEndoplasmic reticulumIrreversible inhibitorSimilar accumulationLactacystinPeriod of hours
1995
The mouse Snell's waltzer deafness gene encodes an unconventional myosin required for structural integrity of inner ear hair cells
Avraham K, Hasson T, Steel K, Kingsley D, Russell L, Mooseker M, Copeland N, Jenkins N. The mouse Snell's waltzer deafness gene encodes an unconventional myosin required for structural integrity of inner ear hair cells. Nature Genetics 1995, 11: 369-375. PMID: 7493015, DOI: 10.1038/ng1295-369.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceChromosome InversionCloning, MolecularDeafnessDNA Mutational AnalysisGenes, RecessiveHair Cells, Auditory, InnerHumansMiceMice, Inbred C57BLMice, Mutant StrainsMolecular Sequence DataMyosin Heavy ChainsOrgan of CortiRestriction MappingRNA, MessengerSequence DeletionConceptsMyosin VIUnconventional myosin heavy chainPositional cloning approachInner ear hair cellsHuman deafness disordersExcellent model systemEar hair cellsSensory hair cellsHair cellsDeafness disordersCloning approachUnconventional myosinDeafness mutationsDeafness mutantsDeafness genesMyosin heavy chainGenesGenetic deafnessModel systemHeavy chainStructural integrityWaltzerInner earCellsMutants
1993
Calcium-calmodulin and regulation of brush border myosin-I MgATPase and mechanochemistry
Wolenski J, Hayden S, Forscher P, Mooseker. Calcium-calmodulin and regulation of brush border myosin-I MgATPase and mechanochemistry. Journal Of Cell Biology 1993, 122: 613-621. PMID: 8335688, PMCID: PMC2119657, DOI: 10.1083/jcb.122.3.613.Peer-Reviewed Original Research
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