Infection with Chlamydia trachomatis alters the tyrosine phosphorylation and/or localization of several host cell proteins including cortactin.
about
Cortactin signalling and dynamic actin networksA chlamydial type III translocated protein is tyrosine-phosphorylated at the site of entry and associated with recruitment of actinCortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex.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 signalingProtein kinase Cdelta and calmodulin regulate epidermal growth factor receptor recycling from early endosomes through Arp2/3 complex and cortactinRNA interference screen identifies Abl kinase and PDGFR signaling in Chlamydia trachomatis entry.Coincubation of human spermatozoa with Chlamydia trachomatis in vitro causes increased tyrosine phosphorylation of sperm proteins.Chlamydial infection induces pathobiotype-specific protein tyrosine phosphorylation in epithelial cells.Nitropropenyl benzodioxole, an anti-infective agent with action as a protein tyrosine phosphatase inhibitorTyrosine phosphorylation of the chlamydial effector protein Tarp is species specific and not required for recruitment of actin.Significance of host cell kinesin in the development of Chlamydia psittaci.Eukaryotic cell uptake of heparin-coated microspheres: a model of host cell invasion by Chlamydia trachomatisSpecific chlamydial inclusion membrane proteins associate with active Src family kinases in microdomains that interact with the host microtubule networkTarp and Arp: How Chlamydia induces its own entry.Diverse requirements for SRC-family tyrosine kinases distinguish chlamydial speciesActivation of epidermal growth factor receptor is required for Chlamydia trachomatis development.Diagnosis and assessment of trachoma.Mechanisms of Chlamydia trachomatis entry into nonphagocytic cells.Chlamydia-infected cells continue to undergo mitosis and resist induction of apoptosis.Chlamydia trachomatis species-specific induction of ezrin tyrosine phosphorylation functions in pathogen entry.Lipid raft-mediated entry is not required for Chlamydia trachomatis infection of cultured epithelial cells.Inhibiting the Arp2/3 complex limits infection of both intracellular mature vaccinia virus and primate lentiviruses.Characterization and intracellular localization of putative Chlamydia pneumoniae effector proteins.Chlamydophila pneumoniae PknD exhibits dual amino acid specificity and phosphorylates Cpn0712, a putative type III secretion YscD homologcDNA array analysis of altered gene expression in human endothelial cells in response to Chlamydia pneumoniae infection.Rapid, transient phosphatidylserine externalization induced in host cells by infection with Chlamydia spp.Chlamydia pneumoniae infection of human endothelial cells induces proliferation of smooth muscle cells via an endothelial cell-derived soluble factor(s).Legionella pneumophila invasion of MRC-5 cells induces tyrosine protein phosphorylation.Interaction of enteropathogenic or enterohemorrhagic Escherichia coli with HeLa cells results in translocation of cortactin to the bacterial adherence site.The Loss of Expression of a Single Type 3 Effector (CT622) Strongly Reduces Chlamydia trachomatis Infectivity and Growth.
P2860
Q24528115-FCEA21E3-B927-4E48-89F6-72416FBFEC64Q24564460-65E75527-13D4-4D7D-8923-BCE97EB98612Q24681508-7D7A4CF4-A66E-44BA-BC55-A4E2F809FAF5Q28539981-5718475F-74BA-4137-9629-4BF3E83E6B8AQ28581952-6C1A31A1-E592-43CB-A1E1-0BBF290DC8F8Q33325917-D4CE510A-69C5-42E5-980D-79A920D4CF86Q33596882-02622534-4A70-4C76-AD5D-30FDF37B2DD7Q33769391-A9489AA7-4692-42E8-83B1-9654F8778130Q33815443-14E24127-C39F-426B-8354-745B10BEDCCBQ33883293-C67E14AA-C6C0-4F9E-9D96-73159F4BB0D5Q34002219-F0C1CA1E-C2D7-41C4-BB45-4C08845A9CAEQ34003448-E3515371-A00B-4D25-9C80-08E3A059550CQ34073220-DBFE8CFB-969C-45CB-B5AD-47E956063A3DQ34330210-ECF369A5-E77F-41D1-989B-3D72D1D5B841Q34713788-CE5E82A7-39F2-474C-81EF-64F9C3C991C1Q34727996-9DF291DA-D38A-48F1-B2FE-5F5E11DF2E6CQ35920659-81665F47-C951-4CF3-B65C-06B60A739211Q35949838-0BDCFA61-47D6-4984-A4C1-9D35150FDBDEQ36227486-76B0EC34-1E71-427E-847B-3F9080405641Q36313951-5D4C2387-4E0C-4526-93BB-AAC779C4F84AQ37623436-9BF15E16-4A19-450C-9753-E39368DEFCB2Q37657108-40E0EC4C-7033-4A80-B3C7-A42A5E2EE50CQ37857565-AA94C62F-2ABA-4B50-8E3D-1F57F8AEED5BQ37859124-5CC8729C-E0E8-4545-9AD8-C8B6F44B96E0Q37874954-3096D51A-A2CD-4413-A37F-79208CE55B4DQ37875003-523544E1-4C15-4154-9348-B13E30969B88Q37878378-7C0C5BBF-9B39-4B90-8DF4-26546D9191A3Q39511722-1286A0EF-4015-47D6-9E6D-585D7BB4B980Q39513832-756EAA74-5A32-484D-9249-FB31686125C7Q55344798-5F4E3E95-C606-4640-B285-562A31F2752C
P2860
Infection with Chlamydia trachomatis alters the tyrosine phosphorylation and/or localization of several host cell proteins including cortactin.
description
1997 nî lūn-bûn
@nan
1997 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Infection with Chlamydia trach ...... proteins including cortactin.
@ast
Infection with Chlamydia trach ...... proteins including cortactin.
@en
type
label
Infection with Chlamydia trach ...... proteins including cortactin.
@ast
Infection with Chlamydia trach ...... proteins including cortactin.
@en
prefLabel
Infection with Chlamydia trach ...... proteins including cortactin.
@ast
Infection with Chlamydia trach ...... proteins including cortactin.
@en
P2093
P2860
P1476
Infection with Chlamydia trach ...... l proteins including cortactin
@en
P2093
P2860
P304
P407
P577
1997-12-01T00:00:00Z