Expression and translocation of chlamydial protease during acute and persistent infection of the epithelial HEp-2 cells with Chlamydophila (Chlamydia) pneumoniae.
about
Chlamydia pneumoniae induces aponecrosis in human aortic smooth muscle cellsChlamydia psittaci: update on an underestimated zoonotic agentPenicillin kills Chlamydia following the fusion of bacteria with lysosomes and prevents genital inflammatory lesions in C. muridarum-infected miceLead Discovery Strategies for Identification of Chlamydia pneumoniae InhibitorsTarp regulates early Chlamydia-induced host cell survival through interactions with the human adaptor protein SHC1Characterization of hypothetical proteins Cpn0146, 0147, 0284 & 0285 that are predicted to be in the Chlamydia pneumoniae inclusion membrane.Gene expression profiles of Chlamydophila pneumoniae during the developmental cycle and iron depletion-mediated persistenceProduction of a proteolytically active protein, chlamydial protease/proteasome-like activity factor, by five different Chlamydia species.Membrane vesicle production by Chlamydia trachomatis as an adaptive responseTargeting of a chlamydial protease impedes intracellular bacterial growthAutoprocessing and self-activation of the secreted protease CPAF in Chlamydia-infected cellsImproved plaque assay identifies a novel anti-Chlamydia ceramide derivative with altered intracellular localizationIntramolecular dimerization is required for the chlamydia-secreted protease CPAF to degrade host transcriptional factors.Localization of Chlamydia trachomatis hypothetical protein CT311 in host cell cytoplasm.Treatment of Chlamydia trachomatis with a small molecule inhibitor of the Yersinia type III secretion system disrupts progression of the chlamydial developmental cycle.Golgi fragmentation and sphingomyelin transport to Chlamydia trachomatis during penicillin-induced persistence do not depend on the cytosolic presence of the chlamydial protease CPAFLocalization of the hypothetical protein Cpn0797 in the cytoplasm of Chlamydia pneumoniae-infected host cells.Characterization of CPAF critical residues and secretion during Chlamydia trachomatis infection.Persistent Chlamydia trachomatis infection of HeLa cells mediates apoptosis resistance through a Chlamydia protease-like activity factor-independent mechanism and induces high mobility group box 1 release.Chlamydial persistence: beyond the biphasic paradigm.Altered protein secretion of Chlamydia trachomatis in persistently infected human endocervical epithelial cellsChlamydial effector proteins localized to the host cell cytoplasmic compartmentCoxiella type IV secretion and cellular microbiology.Identifying catalytic residues in CPAF, a Chlamydia-secreted protease.Human antibody responses to a Chlamydia-secreted protease factorAnalysis of CPAF mutants: new functions, new questions (the ins and outs of a chlamydial protease).Analysis of Chlamydia pneumoniae infection in mononuclear cells by reverse transcription-PCR targeted to chlamydial gene transcripts.Secretion of Cpn0796 from Chlamydia pneumoniae into the host cell cytoplasm by an autotransporter mechanism.Activation of Raf/MEK/ERK/cPLA2 signaling pathway is essential for chlamydial acquisition of host glycerophospholipids.
P2860
Q24798576-1EEF09E3-31BF-44DB-A8A1-8B9D2423A3EAQ26823750-E984CBD0-2171-4A2D-91EC-95D0BA034099Q27339732-AFD051CB-3F60-4141-85FA-A028DC89E443Q28069433-CD82A61C-AC69-4085-85C9-D8A3D07E4B81Q28902456-3ABBD8FA-FC57-4686-82FA-F65C10338270Q33284727-BD750ADF-8B19-4422-B811-D841973B104FQ33288727-6D7AE96C-1C37-4C58-ACBC-ECB6ABC07D70Q33716094-E41FCE09-ABA0-417E-B897-C30CA6D2D027Q33730339-66951946-AE06-4A21-81EA-ACEFDBC19520Q34047005-7275E74A-10A8-46C9-A0D7-3B7CB9152F43Q34049916-F634F960-D309-458A-B649-00CF68EB201CQ34057486-511AC59C-8259-4FF2-92DE-A3A776827E12Q34756931-3B357600-FCF6-4BF7-81E9-377A7DD668CBQ35061773-AEC5F66A-F3D8-4575-AEBF-B451A6F4D60FQ35099063-CF05F620-7CF4-4DE0-8755-B78002E4517CQ35214207-48EF83A5-39F1-4E7A-9F10-96FA1ED8B1E4Q35217607-37B7EF52-CD0B-4DE2-92BE-76C0F1B12126Q35609380-1F736A9D-4C96-48BB-8923-68902C47D460Q35665397-A22E5595-E267-4338-B203-EA816DA00BA9Q35708475-103691FB-9CF9-4895-8D44-C1D00207E0B0Q35963835-390CB6C1-8032-4E72-825A-70F763E86746Q36950073-01B1D9FF-7AA8-4E41-B319-DD471159FCCFQ37162198-DEC3D681-0C09-4CE0-A63D-D3E8FA7B12B8Q37401433-0DCFE71A-9955-4283-97EB-9BCC465261CDQ37623832-A1399706-7774-4AD2-98D5-F9B20F37404FQ37844146-22CAA035-FF56-4440-8B2E-04C09D3758D9Q37851467-FCA065AE-E169-4017-BC75-864E36AA979BQ37864878-D869B7C7-5BD3-43CB-B2BD-9E0BA4EF0BB6Q37868030-F2977C4B-7FAD-4B22-9756-763216BED1D8
P2860
Expression and translocation of chlamydial protease during acute and persistent infection of the epithelial HEp-2 cells with Chlamydophila (Chlamydia) pneumoniae.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on May 2003
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Expression and translocation o ...... ophila (Chlamydia) pneumoniae.
@en
Expression and translocation o ...... HEp-2 cells with Chlamydophila
@nl
type
label
Expression and translocation o ...... ophila (Chlamydia) pneumoniae.
@en
Expression and translocation o ...... HEp-2 cells with Chlamydophila
@nl
prefLabel
Expression and translocation o ...... ophila (Chlamydia) pneumoniae.
@en
Expression and translocation o ...... HEp-2 cells with Chlamydophila
@nl
P2860
P1476
Expression and translocation o ...... ophila (Chlamydia) pneumoniae.
@en
P2093
Dagmar Heuer
Volker Brinkmann
P2860
P304
P356
10.1046/J.1462-5822.2003.00278.X
P577
2003-05-01T00:00:00Z