2018
Dynamic functional assembly of the Torsin AAA+ ATPase and its modulation by LAP1: a novel mode of regulation for AAA+ ATPases
Chase A, Laudermilch E, Wang J, Shigematsu H, Yokoyama T, Schlieker C. Dynamic functional assembly of the Torsin AAA+ ATPase and its modulation by LAP1: a novel mode of regulation for AAA+ ATPases. The FASEB Journal 2018, 32: 114.1-114.1. DOI: 10.1096/fasebj.2018.32.1_supplement.114.1.Peer-Reviewed Original ResearchOligomeric stateNuclear envelope defectsRobust ATPase activityExperimental Biology 2018 MeetingPresence of ATPEnvelope defectsCofactor assemblyHomotypic oligomersCellular cofactorsATP hydrolysisDynamic assemblyFunctional assemblyMolecular etiologyATPase activationLAP1Novel modeATPase activityCofactorFASEB JournalATPasesCofactor systemATPaseAssemblyDYT1 dystoniaKey role
2017
Dynamic functional assembly of the Torsin AAA+ ATPase and its modulation by LAP1
Chase AR, Laudermilch E, Wang J, Shigematsu H, Yokoyama T, Schlieker C. Dynamic functional assembly of the Torsin AAA+ ATPase and its modulation by LAP1. Molecular Biology Of The Cell 2017, 28: 2765-2772. PMID: 28814508, PMCID: PMC5638581, DOI: 10.1091/mbc.e17-05-0281.Peer-Reviewed Original Research
2003
Modifying the oligomeric state of cyclic amidase and its effect on enzymatic catalysis
Yoon J, Oh B, Kim K, Park JE, Wang J, Kim HS, Kim Y. Modifying the oligomeric state of cyclic amidase and its effect on enzymatic catalysis. Biochemical And Biophysical Research Communications 2003, 310: 651-659. PMID: 14521961, DOI: 10.1016/j.bbrc.2003.09.056.Peer-Reviewed Original ResearchConceptsCyclic amidasesD-hydantoinaseCatalytic propertiesHydrophobic interaction domainCatalytic activityEnzymatic catalysisHydrophobic interactionsCyclic ureidesReversible hydrolysisDimeric formHydrophobic patchDimeric interactionsOligomeric stateSpecific activityTetramerKinetic propertiesCatalysisLow specific activityDihydropyrimidinesPropertiesHydantoinsDimersDihydroorotaseHydrolysisInteraction