The conserved Tarp actin binding domain is important for chlamydial invasion. - Wikidata - awgldk - TriplyDB

The conserved Tarp actin binding domain is important for chlamydial invasion.

The conserved Tarp actin binding domain is important for chlamydial invasion.

http://www.wikidata.org/entity/Q33640294

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Rickettsia Sca2 is a bacterial formin-like mediator of actin-based motility Chlamydia psittaci: update on an underestimated zoonotic agent Actin recruitment to the Chlamydia inclusion is spatiotemporally regulated by a mechanism that requires host and bacterial factors 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 Interplay of recombination and selection in the genomes of Chlamydia trachomatis.'Cand. Actinochlamydia clariae' gen. nov., sp. nov., a unique intracellular bacterium causing epitheliocystis in catfish (Clarias gariepinus) in Uganda.Chlamydia trachomatis co-opts the FGF2 signaling pathway to enhance infection Genetic variation in Chlamydia trachomatis and their hosts: impact on disease severity and tissue tropism The Chlamydia trachomatis type III secretion substrates CT142, CT143, and CT144 are secreted into the lumen of the inclusion.Endocytosis of viruses and bacteria.Phylogenetic analysis of Chlamydia trachomatis Tarp and correlation with clinical phenotype.Identification of novel type III secretion chaperone-substrate complexes of Chlamydia trachomatis.Profiling antibody responses to infections by Chlamydia abortus enables identification of potential virulence factors and candidates for serodiagnosis 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.Quantitative proteomics reveals metabolic and pathogenic properties of Chlamydia trachomatis developmental forms Chlamydia trachomatis In Vivo to In Vitro Transition Reveals Mechanisms of Phase Variation and Down-Regulation of Virulence Factors Chlamydia trachomatis Tarp cooperates with the Arp2/3 complex to increase the rate of actin polymerization Analysis of Humoral Immune Responses to Surface and Virulence-Associated Chlamydia abortus Proteins in Ovine and Human Abortions by Use of a Newly Developed Line Immunoassay Domain analyses reveal that Chlamydia trachomatis CT694 protein belongs to the membrane-localized family of type III effector proteins.Directional evolution of Chlamydia trachomatis towards niche-specific adaptation.The molecular basis for disease phenotype in chronic Chlamydia-induced arthritis.Chlamydia trachomatis from Australian Aboriginal people with trachoma are polyphyletic composed of multiple distinctive lineages.Chlamydial intracellular survival strategies.Targeted Disruption of Chlamydia trachomatis Invasion by in Trans Expression of Dominant Negative Tarp Effectors New frontiers in type III secretion biology: the Chlamydia perspective.The Effector TepP Mediates Recruitment and Activation of Phosphoinositide 3-Kinase on Early Chlamydia trachomatis Vacuoles.Common Themes in Cytoskeletal Remodeling by Intracellular Bacterial Effectors.Chlamydia-host cell interaction not only from a bird's eye view: some lessons from Chlamydia psittaci.Manipulation of the Host Cell Cytoskeleton by Chlamydia.One Face of Chlamydia trachomatis: The Infectious Elementary Body.Identification of linear B-cell epitopes within Tarp of Chlamydia trachomatis.Recent advances in Chlamydia subversion of host cytoskeletal and membrane trafficking pathways.Modulation of host signaling and cellular responses by Chlamydia Chlamydia trachomatis Tarp harbors distinct G and F actin binding domains that bundle actin filaments.Bacterial nucleators: actin' on actin.Fluorescence-Reported Allelic Exchange Mutagenesis Reveals a Role for Chlamydia trachomatis TmeA in Invasion That Is Independent of Host AHNAK.Actin-based motility of bacterial pathogens: mechanistic diversity and its impact on virulence.Taking control: reorganization of the host cytoskeleton by Chlamydia.The intrinsically disordered Tarp protein from chlamydia binds actin with a partially preformed helix.

P2860

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P2860

The conserved Tarp actin binding domain is important for chlamydial invasion.

http://www.wikidata.org/entity/Q33640294

description

2010 nî lūn-bûn

@nan

2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հուլիսին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

@zh-hk

2010年論文

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2010年論文

@zh-tw

2010年论文

@wuu

name

The conserved Tarp actin binding domain is important for chlamydial invasion.

@ast

The conserved Tarp actin binding domain is important for chlamydial invasion.

@en

type

label

The conserved Tarp actin binding domain is important for chlamydial invasion.

@ast

The conserved Tarp actin binding domain is important for chlamydial invasion.

@en

prefLabel

The conserved Tarp actin binding domain is important for chlamydial invasion.

@ast

The conserved Tarp actin binding domain is important for chlamydial invasion.

@en

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JOURNAL.PPAT.1000997

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The conserved Tarp actin binding domain is important for chlamydial invasion.

@en

P2093

Cheryl A Dooley

http://www.w3.org/2001/XMLSchema#string

Natalie J Miller

http://www.w3.org/2001/XMLSchema#string

Ted Hackstadt

http://www.w3.org/2001/XMLSchema#string

Travis J Jewett

http://www.w3.org/2001/XMLSchema#string

P2860

Comparative Genomic Analysis of Chlamydia trachomatis Oculotropic and Genitotropic Strains

Genome Sequence of an Obligate Intracellular Pathogen of Humans: Chlamydia trachomatis

Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): examining the role of niche-specific genes in the evolution of the Chlamydiaceae

Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39.

Comparative genomes of Chlamydia pneumoniae and C. trachomatis

Type III protein secretion systems in bacterial pathogens of animals and plants

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

Crystal structure of Arp2/3 complex

Leiomodin is an actin filament nucleator in muscle cells.

Mechanism and function of formins in the control of actin assembly

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e1000997

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scholarly article

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10.1371/JOURNAL.PPAT.1000997

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7

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2904776

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