Chlamydial entry involves TARP binding of guanine nucleotide exchange factors.
about
The lipid transfer protein CERT interacts with the Chlamydia inclusion protein IncD and participates to ER-Chlamydia inclusion membrane contact sitesHost Organelle Hijackers: a similar modus operandi for Toxoplasma gondii and Chlamydia trachomatis: co-infection model as a tool to investigate pathogenesisConserved type III secretion system exerts important roles in Chlamydia trachomatisRho GTPases as pathogen targets: Focus on curable sexually transmitted infectionsA C. trachomatis cloning vector and the generation of C. trachomatis strains expressing fluorescent proteins under the control of a C. trachomatis promoterActin recruitment to the Chlamydia inclusion is spatiotemporally regulated by a mechanism that requires host and bacterial factorsHijacking Host Cell Highways: Manipulation of the Host Actin Cytoskeleton by Obligate Intracellular Bacterial PathogensContrasting Lifestyles Within the Host CellThe 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, Cpn0803Tarp regulates early Chlamydia-induced host cell survival through interactions with the human adaptor protein SHC1The Chlamydia effector TarP mimics the mammalian leucine-aspartic acid motif of paxillin to subvert the focal adhesion kinase during invasionSmall molecule inhibitors of the Yersinia type III secretion system impair the development of Chlamydia after entry into host cellsHuman 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 ChlamydiaeInteractions 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 pneumoniaeThe 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 severityEndocytosis of viruses and bacteria.Specific chlamydial inclusion membrane proteins associate with active Src family kinases in microdomains that interact with the host microtubule networkPhylogenetic 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 TARPSubversion of membrane transport pathways by vacuolar pathogensHost-pathogen reorganisation during host cell entry by Chlamydia trachomatis.Chlamydia trachomatis Tarp cooperates with the Arp2/3 complex to increase the rate of actin polymerizationProgesterone 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 muridarumChlamydial 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 MembraneConjunctival 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
Q21131416-09CF1C00-CD97-4B4E-8704-173E36B57CF8Q26825487-22535394-4175-4126-A15D-7C3CB2D7FBD3Q26998512-5CAE299E-26AC-45AB-A993-5BDABDDAC8F0Q27000265-603A29FD-1188-4FED-ABD3-C4844FF03392Q27313656-AE175B24-2A0B-4B99-8A94-FBD70A491C8AQ27315371-8D7D4800-E79F-4AFA-B45C-DB0CEA2222A0Q28066074-7245070F-6B18-4EAC-91E8-C05CF381C330Q28078686-BD279C9F-2AAE-4DE1-B9A6-884E22241960Q28539981-611B1D79-656F-4F07-8457-8829E106A6E4Q28732757-F48825FF-FAC6-4382-B202-6AC1E9B3D4FCQ28902456-060EDB54-F56F-4D86-A05B-928B1C2FC4ECQ30409633-D33E6176-D188-4BF6-8C5F-A5720769B6DDQ33433231-39189F11-363A-44BD-9FEC-9E0854D517C7Q33490124-1D2220AB-AE69-4F0F-B201-02DD16882408Q33521095-4414FC1D-1A54-43BA-A87B-86B54C3AF00FQ33526048-7C837615-0347-4056-B9BF-033E19EB1CC3Q33548679-4D7078A1-59C5-497E-AA8F-8EFD504C5393Q33570163-2500E8D2-36E7-48B2-9DFD-AB8B17A3B6FBQ33640294-1CF62EE7-9821-4152-AE4A-1AF7ED8FD3C6Q33806902-9D29C657-22C0-4A31-A4D8-8B9FF72E4848Q33885417-6EE844F1-4A84-4579-8C3D-8A4AB52C8193Q33938568-B9F886B7-415E-4F50-8385-49EC52011383Q34073220-11DCC81E-AA30-471D-9E18-1A138F07709EQ34119391-8AFE2911-D42A-4E74-8B83-97E1A675185CQ34150358-14A82C84-A3BA-4963-A21C-0592E2F60083Q34160717-A2A8ADBC-8F21-4C06-BEE8-EF00A67777A9Q34595020-3C1A0AA8-A663-4957-8CD7-DB1B6FBA0AE4Q34980175-D36B4B04-85CE-4DA2-BB1A-F216E58BA273Q35095777-5BD188C6-F942-4C2D-BF80-799DAB5CD9D6Q35216604-7D41287C-2A69-41CD-9EF9-50A79A93A0E1Q35545495-17812855-CBAE-4682-B57F-8526CE464185Q35621027-3A66FD3E-5075-4FD1-89BC-3B251A7BAF35Q35759757-8711DB20-86C1-4E0E-B02F-4EAFB4604FB0Q35907102-854404D5-759E-42A6-9BEE-D34DC086F0A0Q35974555-0ED0C13C-3DEB-46FE-B6E4-9DC12DE9C320Q36040993-2B53619B-9E45-461F-85B1-A054848A813DQ36318962-D79AEEB2-644C-4719-AE18-431A98008B54Q36328807-9FAAEE48-6481-42A1-BB73-E2D26A32967EQ36329527-9D3E199D-E3AF-40E7-9C2D-C87E8BED3C1FQ36672137-A6C99225-1F23-4B1B-866A-8F3A60582780
P2860
Chlamydial entry involves TARP binding of guanine nucleotide exchange factors.
description
2008 nî lūn-bûn
@nan
2008 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի մարտին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
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
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
P2093
P2860
P1433
P1476
Chlamydial entry involves TARP binding of guanine nucleotide exchange factors.
@en
P2093
B Josh Lane
Charla Mutchler
Scott S Grieshaber
P2860
P304
P356
10.1371/JOURNAL.PPAT.1000014
P577
2008-03-01T00:00:00Z