Chlamydial entry involves TARP binding of guanine nucleotide exchange factors. - Test2 - elhamkhani - TriplyDB

Chlamydial entry involves TARP binding of guanine nucleotide exchange factors.

Chlamydial entry involves TARP binding of guanine nucleotide exchange factors.

http://www.wikidata.org/entity/Q33326689

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The lipid transfer protein CERT interacts with the Chlamydia inclusion protein IncD and participates to ER-Chlamydia inclusion membrane contact sites Host Organelle Hijackers: a similar modus operandi for Toxoplasma gondii and Chlamydia trachomatis: co-infection model as a tool to investigate pathogenesis Conserved type III secretion system exerts important roles in Chlamydia trachomatis Rho GTPases as pathogen targets: Focus on curable sexually transmitted infections A C. trachomatis cloning vector and the generation of C. trachomatis strains expressing fluorescent proteins under the control of a C. trachomatis promoter Actin recruitment to the Chlamydia inclusion is spatiotemporally regulated by a mechanism that requires host and bacterial factors Hijacking Host Cell Highways: Manipulation of the Host Actin Cytoskeleton by Obligate Intracellular Bacterial Pathogens Contrasting Lifestyles Within the Host Cell The 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 signaling Structural characterization of a novel Chlamydia pneumoniae type III secretion-associated protein, Cpn0803 Tarp regulates early Chlamydia-induced host cell survival through interactions with the human adaptor protein SHC1 The Chlamydia effector TarP mimics the mammalian leucine-aspartic acid motif of paxillin to subvert the focal adhesion kinase during invasion Small molecule inhibitors of the Yersinia type III secretion system impair the development of Chlamydia after entry into host cells Human guanylate binding proteins potentiate the anti-chlamydia effects of interferon-gamma.Comprehensive in silico prediction and analysis of chlamydial outer membrane proteins reflects evolution and life style of the Chlamydiae Interactions between flagellar and type III secretion proteins in Chlamydia pneumoniae.Actin re-organization induced by Chlamydia trachomatis serovar D--evidence for a critical role of the effector protein CT166 targeting Rac.Evolution to a chronic disease niche correlates with increased sensitivity to tryptophan availability for the obligate intracellular bacterium Chlamydia pneumoniae The conserved Tarp actin binding domain is important for chlamydial invasion.The Chlamydia trachomatis type III secretion substrates CT142, CT143, and CT144 are secreted into the lumen of the inclusion.Chlamydia trachomatis strains and virulence: rethinking links to infection prevalence and disease severity Endocytosis of viruses and bacteria.Specific chlamydial inclusion membrane proteins associate with active Src family kinases in microdomains that interact with the host microtubule network Phylogenetic analysis of Chlamydia trachomatis Tarp and correlation with clinical phenotype.Immunodominant regions of a Chlamydia trachomatis type III secretion effector protein, Tarp.Bacterial factors exploit eukaryotic Rho GTPase signaling cascades to promote invasion and proliferation within their host.Identification of novel type III secretion chaperone-substrate complexes of Chlamydia trachomatis.A chlamydial type III-secreted effector protein (Tarp) is predominantly recognized by antibodies from humans infected with Chlamydia trachomatis and induces protective immunity against upper genital tract pathologies in mice.Identification of type III secretion substrates of Chlamydia trachomatis using Yersinia enterocolitica as a heterologous system.Bacterial subversion of host actin dynamics at the plasma membrane.Chlamydia trachomatis Slc1 is a type III secretion chaperone that enhances the translocation of its invasion effector substrate TARP Subversion of membrane transport pathways by vacuolar pathogens Host-pathogen reorganisation during host cell entry by Chlamydia trachomatis.Chlamydia trachomatis Tarp cooperates with the Arp2/3 complex to increase the rate of actin polymerization Progesterone antagonizes the positive influence of estrogen on Chlamydia trachomatis serovar E in an Ishikawa/SHT-290 co-culture model.Mapping immunodominant antigens and H-2-linked antibody responses in mice urogenitally infected with Chlamydia muridarum Chlamydial Lytic Exit from Host Cells Is Plasmid Regulated.Vinculin Interacts with the Chlamydia Effector TarP Via a Tripartite Vinculin Binding Domain to Mediate Actin Recruitment and Assembly at the Plasma Membrane Conjunctival fibrosis and the innate barriers to Chlamydia trachomatis intracellular infection: a genome wide association study.Chlamydia trachomatis tarp is phosphorylated by src family tyrosine kinases

P2860

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P2860

Chlamydial entry involves TARP binding of guanine nucleotide exchange factors.

http://www.wikidata.org/entity/Q33326689

description

2008 nî lūn-bûn

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2008 թուականի Մարտին հրատարակուած գիտական յօդուած

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2008 թվականի մարտին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Chlamydial entry involves TARP binding of guanine nucleotide exchange factors.

@ast

Chlamydial entry involves TARP binding of guanine nucleotide exchange factors.

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Chlamydial entry involves TARP binding of guanine nucleotide exchange factors.

@nl

type

label

Chlamydial entry involves TARP binding of guanine nucleotide exchange factors.

@ast

Chlamydial entry involves TARP binding of guanine nucleotide exchange factors.

@en

Chlamydial entry involves TARP binding of guanine nucleotide exchange factors.

@nl

prefLabel

Chlamydial entry involves TARP binding of guanine nucleotide exchange factors.

@ast

Chlamydial entry involves TARP binding of guanine nucleotide exchange factors.

@en

Chlamydial entry involves TARP binding of guanine nucleotide exchange factors.

@nl

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JOURNAL.PPAT.1000014

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Chlamydial entry involves TARP binding of guanine nucleotide exchange factors.

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B Josh Lane

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Charla Mutchler

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Scott S Grieshaber

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P2860

Comparative Genomic Analysis of Chlamydia trachomatis Oculotropic and Genitotropic Strains

Structure of the PH domain and Btk motif from Bruton's tyrosine kinase: molecular explanations for X-linked agammaglobulinaemia

Identification and analysis of PH domain-containing targets of phosphatidylinositol 3-kinase using a novel in vivo assay in yeast.

Critical but distinct roles for the pleckstrin homology and cysteine-rich domains as positive modulators of Vav2 signaling and transformation

A chlamydial type III translocated protein is tyrosine-phosphorylated at the site of entry and associated with recruitment of actin

An effector region in Eps8 is responsible for the activation of the Rac-specific GEF activity of Sos-1 and for the proper localization of the Rac-based actin-polymerizing machine

SH2 domains recognize specific phosphopeptide sequences

Phosphatidylinositol 3-kinase-dependent membrane association of the Bruton's tyrosine kinase pleckstrin homology domain visualized in single living cells

Eps8 in the midst of GTPases

Mechanism of epidermal growth factor regulation of Vav2, a guanine nucleotide exchange factor for Rac

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e1000014

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scholarly article

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10.1371/JOURNAL.PPAT.1000014

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3

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4

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Souhaila Al-Khodor

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2008-03-01T00:00:00Z

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5468301

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18383626

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2279300

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