2008
Widely Distributed Residues in Thymosin β4 Are Critical for Actin Binding
Au JK, Olivares AO, Henn A, Cao W, Safer D, De La Cruz EM. Widely Distributed Residues in Thymosin β4 Are Critical for Actin Binding. Biochemistry 2008, 47: 4181-4188. PMID: 18327913, PMCID: PMC2587058, DOI: 10.1021/bi701769u.Peer-Reviewed Original ResearchConceptsActin Binding AffinityActin bindingProline residuesHydrophobic residuesAlanine residuesLysine residuesPro27Thymosin beta4Actin monomersPro29MutagenesisHydrophobic contactsLeu28Slow association rateResiduesLys19Thymosin β4Ile34Tbeta4Lys18Binding affinitiesTwo-step mechanismAssociation ratePro4Cis-trans isomerization
2005
Proteomic Patterns and Prediction of Glomerulosclerosis and Its Mechanisms
Xu BJ, Shyr Y, Liang X, Ma LJ, Donnert EM, Roberts JD, Zhang X, Kon V, Brown NJ, Caprioli RM, Fogo AB. Proteomic Patterns and Prediction of Glomerulosclerosis and Its Mechanisms. Journal Of The American Society Of Nephrology 2005, 16: 2967-2975. PMID: 16079267, DOI: 10.1681/asn.2005030262.Peer-Reviewed Original ResearchConceptsThymosin beta4Proteomic patternsProtein expression profilesSuch early eventsPlasminogen activator inhibitor-1 expressionMatrix-assisted laser desorption/ionization timeLaser desorption/ionization timeDesorption/ionization timeLaser capture microdissectionEndothelial cellsExpression profilesProtein profilesCapture microdissectionBeta4Cultured glomerular endothelial cellsPlasminogen activator inhibitor-1Early eventsFlight mass spectrometryIonization timeActivator inhibitor-1Inhibitor-1ProteinEarly activationMass spectrometryCells
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