2024
Tetrameric PilZ protein stabilizes stator ring in complex flagellar motor and is required for motility in Campylobacter jejuni
Chen Y, Tachiyama S, Li Y, Feng X, Zhao H, Wu Y, Guo Y, Lara-Tejero M, Hua C, Liu J, Gao B. Tetrameric PilZ protein stabilizes stator ring in complex flagellar motor and is required for motility in Campylobacter jejuni. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 122: e2412594121. PMID: 39793078, PMCID: PMC11725899, DOI: 10.1073/pnas.2412594121.Peer-Reviewed Original ResearchConceptsFlagellar motorPilZ domain-containing proteinsBound cyclic di-GMPCyclic di-GMPC-di-GMPDomain-containing proteinsStator unitsDi-GMPFamily proteinsSuperfamily proteinsBacterial flagellaRing assemblyCellular pathwaysCampylobacter jejuniCryoelectron tomographyCampylobacter jejuni</i>.Subtomogram averagingPilZProteinFlagellaPhylumAncestorMotilityJejuniStructural components
2015
Functions of Kinesin Superfamily Proteins in Neuroreceptor Trafficking
Wang N, Xu J. Functions of Kinesin Superfamily Proteins in Neuroreceptor Trafficking. BioMed Research International 2015, 2015: 639301. PMID: 26075252, PMCID: PMC4449888, DOI: 10.1155/2015/639301.Peer-Reviewed Original ResearchConceptsKinesin superfamily proteinsSuperfamily proteinsSynaptic plasticityTransport various cargoesGlutamate receptorsKainate receptorsGABA receptorsAdaptor proteinTrafficking of NMDA receptorsN-methyl-D-aspartate-Cellular basis of learningMolecular mechanismsMolecular eventsTraffickingProteinNMDA receptorsAMPA receptorsSynaptic transmissionCellular basisNeuronal activityReceptorsBasis of learningKainateGABAAdaptor
2012
Catalysis of Disulfide Bond Formation by the Quiescin Sulfhydryl Oxidases
Alon A, Fass D. Catalysis of Disulfide Bond Formation by the Quiescin Sulfhydryl Oxidases. 2012 DOI: 10.1002/9780470015902.a0024168.Peer-Reviewed Original ResearchQuiescin sulfhydryl oxidase enzymesQuiescin sulfhydryl oxidaseDisulfide bond formationSubstrate proteinsProtein disulfide isomerase family proteinsSulfhydryl oxidaseProtein disulfide isomerase familyCatalysis of disulfide bond formationDithiol/disulfide exchange reactionsRedox-active disulfideDisulfide isomerase familyExtracellular matrix assemblyHigh-resolution viewSecretory pathwayFamily proteinsSuperfamily proteinsCatalytic machineryDomain duplicationExtracellular environmentMatrix assemblyRedox relayEnzymeProteinSide-chain dynamicsDisulfide bonds
2006
The Inner Loop of Tetraspanins CD82 and CD81 Mediates Interactions with Human T Cell Lymphotrophic Virus Type 1 Gag Protein*
Mazurov D, Heidecker G, Derse D. The Inner Loop of Tetraspanins CD82 and CD81 Mediates Interactions with Human T Cell Lymphotrophic Virus Type 1 Gag Protein*. Journal Of Biological Chemistry 2006, 282: 3896-3903. PMID: 17166843, DOI: 10.1074/jbc.m607322200.Peer-Reviewed Original ResearchConceptsTetraspanin-enriched microdomainsC-terminusN-terminusTetraspanin superfamily proteinsSite-directed mutationsMembrane protein complexesExtracellular loopCytoplasmic N-terminusHTLV-1T cell adhesionIntegrin functionPalmitoylated cysteinesSuperfamily proteinsProtein complexesTetraspanin CD82Cytoplasmic facePlasma membraneHTLV-1 GagColocalization approachesAmino acidsCD82IntegrinTetraspaninMutationsCD81
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