Structural basis for activation and inhibition of the secreted chlamydia protease CPAF - Wikidata - wikimedia - TriplyDB

Structural basis for activation and inhibition of the secreted chlamydia protease CPAF

Structural basis for activation and inhibition of the secreted chlamydia protease CPAF

http://www.wikidata.org/entity/Q27653088

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Intrinsic evolutionary constraints on protease structure, enzyme acylation, and the identity of the catalytic triad A path forward for the chlamydial virulence factor CPAF Structures of an ATP-independent Lon-like protease and its complexes with covalent inhibitors Chlamydial protease-like activity factor--insights into immunity and vaccine development Multinucleation during C. trachomatis infections is caused by the contribution of two effector pathways The chlamydial periplasmic stress response serine protease cHtrA is secreted into host cell cytosol Targeting of a chlamydial protease impedes intracellular bacterial growth Autoprocessing and self-activation of the secreted protease CPAF in Chlamydia-infected cells Characterization of Pgp3, a Chlamydia trachomatis plasmid-encoded immunodominant antigen CPAF: a Chlamydial protease in search of an authentic substrate.Cleavage of the NF-κB family protein p65/RelA by the chlamydial protease-like activity factor (CPAF) impairs proinflammatory signaling in cells infected with Chlamydiae Vaccination against Chlamydia genital infection utilizing the murine C. muridarum model.Secretion of the chlamydial virulence factor CPAF requires the Sec-dependent pathway Chlamydia trachomatis secretion of proteases for manipulating host signaling pathways.Localization of Chlamydia trachomatis hypothetical protein CT311 in host cell cytoplasm.A Chlamydia trachomatis OmcB C-terminal fragment is released into the host cell cytoplasm and is immunogenic in humans Chlamydia trachomatis secretion of an immunodominant hypothetical protein (CT795) into host cell cytoplasm.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.The Chlamydia protease CPAF regulates host and bacterial proteins to maintain pathogen vacuole integrity and promote virulence Characterization of CPAF critical residues and secretion during Chlamydia trachomatis infection.Insight into the Mechanism of Intramolecular Inhibition of the Catalytic Activity of Sirtuin 2 (SIRT2).The Chlamydia trachomatis Protease CPAF Contains a Cryptic PDZ-Like Domain with Similarity to Human Cell Polarity and Tight Junction PDZ-Containing Proteins Identification of Protease Specificity by Combining Proteome-Derived Peptide Libraries and Quantitative Proteomics Chlamydial infection induces host cytokinesis failure at abscission.Chlamydial plasmid-encoded virulence factor Pgp3 neutralizes the antichlamydial activity of human cathelicidin LL-37.Chlamydia trachomatis outer membrane complex protein B (OmcB) is processed by the protease CPAF.Chlamydia protease-like activity factor (CPAF): characterization of proteolysis activity in vitro and development of a nanomolar affinity CPAF zymogen-derived inhibitor.Fold conservation and proteolysis in zebrafish IRBP structure: Clues to possible enzymatic function?The Chlamydia-Secreted Protease CPAF Promotes Chlamydial Survival in the Mouse Lower Genital Tract Chlamydial Protease-Like Activity Factor and Type III Secreted Effectors Cooperate in Inhibition of p65 Nuclear Translocation.Killing me softly: chlamydial use of proteolysis for evading host defenses.Identifying catalytic residues in CPAF, a Chlamydia-secreted protease.Pathogenic Bacterial Proteins and their Anti-Inflammatory Effects in the Eukaryotic Host.In silico functional elucidation of uncharacterized proteins of Chlamydia abortus strain LLG.Bacterial proteases from the intracellular vacuole niche; protease conservation and adaptation for pathogenic advantage.Update on Chlamydia trachomatis Vaccinology.Chlamydial Plasmid-Dependent Pathogenicity.Structural basis of the proteolytic and chaperone activity of Chlamydia trachomatis CT441.Analysis of CPAF mutants: new functions, new questions (the ins and outs of a chlamydial protease).Exploiting nature's rich source of proteasome inhibitors as starting points in drug development.

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P2860

Structural basis for activation and inhibition of the secreted chlamydia protease CPAF

http://www.wikidata.org/entity/Q27653088

description

2008 nî lūn-bûn

@nan

2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի դեկտեմբերին 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

Structural basis for activation and inhibition of the secreted chlamydia protease CPAF

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Structural basis for activation and inhibition of the secreted chlamydia protease CPAF

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Structural basis for activation and inhibition of the secreted chlamydia protease CPAF

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Structural basis for activation and inhibition of the secreted chlamydia protease CPAF

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Structural basis for activation and inhibition of the secreted chlamydia protease CPAF

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Structural basis for activation and inhibition of the secreted chlamydia protease CPAF

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Structural basis for activation and inhibition of the secreted chlamydia protease CPAF

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Structural basis for activation and inhibition of the secreted chlamydia protease CPAF

@en

Structural basis for activation and inhibition of the secreted chlamydia protease CPAF

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J.CHOM.2008.10.005

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Cell Host & Microbe

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Structural basis for activation and inhibition of the secreted chlamydia protease CPAF

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Ding Chen

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Guangming Zhong

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Jijie Chai

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Lichuan Gu

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Siyang Huang

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Xiaojing Wu

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Xiaojun Wang

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Xingguo Xiao

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Yingcai Feng

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Zhiwei Huang

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