The Chlamydia type III secretion system C-ring engages a chaperone-effector protein complex.
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Expanded roles for multicargo and class 1B effector chaperones in type III secretionConserved type III secretion system exerts important roles in Chlamydia trachomatisBacterial type III secretion systems: specialized nanomachines for protein delivery into target cellsPolarized Cell Division of Chlamydia trachomatisComposition, formation, and regulation of the cytosolic c-ring, a dynamic component of the type III secretion injectisomeStructure of a bacterial type III secretion system in contact with a host membrane in situStructure and Protein-Protein Interaction Studies on Chlamydia trachomatis Protein CT670 (YscO Homolog)Structure and Interactions of the Cytoplasmic Domain of the Yersinia Type III Secretion Protein YscDTwo Translation Products of Yersinia yscQ Assemble To Form a Complex Essential to Type III SecretionStructure of CT584 fromChlamydia trachomatisrefined to 3.05 Å resolutionThe Chlamydia trachomatis type III secretion chaperone Slc1 engages multiple early effectors, including TepP, a tyrosine-phosphorylated protein required for the recruitment of CrkI-II to nascent inclusions and innate immune signalingStructural characterization of a novel Chlamydia pneumoniae type III secretion-associated protein, Cpn0803The periplasmic HrpB1 protein from Xanthomonas spp. binds to peptidoglycan and to components of the type III secretion system.HrcQ provides a docking site for early and late type III secretion substrates from XanthomonasProtein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria.Genetic variation in Chlamydia trachomatis and their hosts: impact on disease severity and tissue tropismCochaperone interactions in export of the type III needle component PscF of Pseudomonas aeruginosa.Functional and computational analysis of amino acid patterns predictive of type III secretion system substrates in Pseudomonas syringae.A novel C-terminal region within the multicargo type III secretion chaperone CesT contributes to effector secretion.Identification of novel type III secretion chaperone-substrate complexes of Chlamydia trachomatis.Secretion of the chlamydial virulence factor CPAF requires the Sec-dependent pathwayThe Chlamydial Type III Secretion Mechanism: Revealing Cracks in a Tough Nut.Identification of type III secretion substrates of Chlamydia trachomatis using Yersinia enterocolitica as a heterologous system.Scc1 (CP0432) and Scc4 (CP0033) function as a type III secretion chaperone for CopN of Chlamydia pneumoniae.Chlamydia trachomatis secretion of hypothetical protein CT622 into host cell cytoplasm via a secretion pathway that can be inhibited by the type III secretion system inhibitor compound 1.Biochemical and localization analyses of putative type III secretion translocator proteins CopB and CopB2 of Chlamydia trachomatis reveal significant distinctions.A molecular chaperone mediates a two-protein enzyme complex and glycosylation of serine-rich streptococcal adhesins.The Chlamydia effector chlamydial outer protein N (CopN) sequesters tubulin and prevents microtubule assembly.C-ring requirement in flagellar type III secretion is bypassed by FlhDC upregulation.A gatekeeper chaperone complex directs translocator secretion during type three secretion.Chlamydia trachomatis Infection Leads to Defined Alterations to the Lipid Droplet Proteome in Epithelial Cells.Chlamydia trachomatis Slc1 is a type III secretion chaperone that enhances the translocation of its invasion effector substrate TARPQuantitative proteomics reveals metabolic and pathogenic properties of Chlamydia trachomatis developmental formsChlamydia trachomatis In Vivo to In Vitro Transition Reveals Mechanisms of Phase Variation and Down-Regulation of Virulence FactorsApplication of β-lactamase reporter fusions as an indicator of effector protein secretion during infections with the obligate intracellular pathogen Chlamydia trachomatisChlamydia trachomatis Type III Secretion Proteins Regulate Transcription.Multipart Chaperone-Effector Recognition in the Type III Secretion System of Chlamydia trachomatis.A working model for the type III secretion mechanism in Chlamydia.Quantitative Protein Profiling of Chlamydia trachomatis Growth Forms Reveals Defense Strategies Against Tryptophan Starvation.New frontiers in type III secretion biology: the Chlamydia perspective.
P2860
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P2860
The Chlamydia type III secretion system C-ring engages a chaperone-effector protein complex.
description
2009 nî lūn-bûn
@nan
2009 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
The Chlamydia type III secreti ...... rone-effector protein complex.
@ast
The Chlamydia type III secreti ...... rone-effector protein complex.
@en
type
label
The Chlamydia type III secreti ...... rone-effector protein complex.
@ast
The Chlamydia type III secreti ...... rone-effector protein complex.
@en
altLabel
The Chlamydia type III secreti ...... erone-effector protein complex
@en
prefLabel
The Chlamydia type III secreti ...... rone-effector protein complex.
@ast
The Chlamydia type III secreti ...... rone-effector protein complex.
@en
P2093
P2860
P921
P1433
P1476
The Chlamydia type III secreti ...... rone-effector protein complex.
@en
P2093
Kris E Spaeth
Raphael H Valdivia
Yi-Shan Chen
P2860
P304
P356
10.1371/JOURNAL.PPAT.1000579
P407
P577
2009-09-11T00:00:00Z