2024
PilY1 regulates the dynamic architecture of the type IV pilus machine in Pseudomonas aeruginosa
Guo S, Chang Y, Brun Y, Howell P, Burrows L, Liu J. PilY1 regulates the dynamic architecture of the type IV pilus machine in Pseudomonas aeruginosa. Nature Communications 2024, 15: 9382. PMID: 39477930, PMCID: PMC11525922, DOI: 10.1038/s41467-024-53638-y.Peer-Reviewed Original ResearchConceptsPilus extensionCell envelopeType IV piliPathogen Pseudomonas aeruginosaBacterial cell envelopeP. aeruginosa cellsCryo-electron tomographyPilus dynamicsPilin subunitSecretin channelSurface motilityPriming complexOuter membraneBiofilm formationT4PPilY1P. aeruginosaPseudomonas aeruginosaCentral poreMolecular mechanismsSubtomogram averagingPotential therapeutic targetDynamic assemblyTherapeutic targetMolecular framework
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 ResearchHIDE Probes: A New Toolkit for Visualizing Organelle Dynamics, Longer and at Super-Resolution
Thompson AD, Bewersdorf J, Toomre D, Schepartz A. HIDE Probes: A New Toolkit for Visualizing Organelle Dynamics, Longer and at Super-Resolution. Biochemistry 2017, 56: 5194-5201. PMID: 28792749, PMCID: PMC5854879, DOI: 10.1021/acs.biochem.7b00545.Peer-Reviewed Original ResearchConceptsLive cellsOrganelle dynamicsDiscrete organellesMultiple organellesLive-cell nanoscopyPlasma membraneDiverse processesEndoplasmic reticulumDynamic assemblyLiving cellsDynamic reorganizationOrganellesSingle-molecule switchingMembrane probeCellsMembraneMitochondriaReticulumRegulationHigh densityProbeAssemblyNew toolkitLong time periodsDivision
2016
α-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix Bundle
Ma L, Kang Y, Jiao J, Rebane AA, Keun HK, Xi Z, Qu H, Zhang Y. α-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix Bundle. Cell Reports 2016, 15: 531-539. PMID: 27068468, PMCID: PMC4838522, DOI: 10.1016/j.celrep.2016.03.050.Peer-Reviewed Original ResearchConceptsSoluble N-ethylmaleimide-sensitive factor attachment protein receptorsC-terminal domainN-terminal domainMembrane fusionLinker domainΑ-SNAPSynaptic soluble N-ethylmaleimide-sensitive factor attachment protein receptorN-ethylmaleimide-sensitive factor attachment protein receptorsFactor attachment protein receptorsIntracellular membrane fusionAttachment protein receptorsConformational selection mechanismFour-helix bundleSNARE assemblySNARE complexProtein receptorsDynamic assemblyStepwise assemblyAssemblyDomainFusionZipperingOptical tweezersRecent experimentsReceptors
2013
How cells get the message: dynamic assembly and function of mRNA–protein complexes
Müller-McNicoll M, Neugebauer KM. How cells get the message: dynamic assembly and function of mRNA–protein complexes. Nature Reviews Genetics 2013, 14: 275-287. PMID: 23478349, DOI: 10.1038/nrg3434.Peer-Reviewed Original Research
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