Chlamydial TARP is a bacterial nucleator of actin - Wikidata - awgldk - TriplyDB

Chlamydial TARP is a bacterial nucleator of actin

Chlamydial TARP is a bacterial nucleator of actin

http://www.wikidata.org/entity/Q35108349

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Molecular and cellular pathobiology of Ehrlichia infection: targets for new therapeutics and immunomodulation strategies Chlamydia psittaci: update on an underestimated zoonotic agent Host Organelle Hijackers: a similar modus operandi for Toxoplasma gondii and Chlamydia trachomatis: co-infection model as a tool to investigate pathogenesis Conserved type III secretion system exerts important roles in Chlamydia trachomatis Actin recruitment to the Chlamydia inclusion is spatiotemporally regulated by a mechanism that requires host and bacterial factors Mechanism of actin filament nucleation by the bacterial effector VopL Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation Structure of the formin-interaction domain of the actin nucleation-promoting factor Bud6 Hijacking Host Cell Highways: Manipulation of the Host Actin Cytoskeleton by Obligate Intracellular Bacterial Pathogens Contrasting Lifestyles Within the Host Cell Why are bacteria different from eukaryotes?Tarp regulates early Chlamydia-induced host cell survival through interactions with the human adaptor protein SHC1 Arp2/3-independent assembly of actin by Vibrio type III effector VopL.The Chlamydia effector TarP mimics the mammalian leucine-aspartic acid motif of paxillin to subvert the focal adhesion kinase during invasion 'Cand. Actinochlamydia clariae' gen. nov., sp. nov., a unique intracellular bacterium causing epitheliocystis in catfish (Clarias gariepinus) in Uganda.Exploration of chlamydial type III secretion system reconstitution in Escherichia coli.RNA interference screen identifies Abl kinase and PDGFR signaling in Chlamydia trachomatis entry.Chlamydial entry involves TARP binding of guanine nucleotide exchange factors.Small molecule inhibitors of the Yersinia type III secretion system impair the development of Chlamydia after entry into host cells Comprehensive in silico prediction and analysis of chlamydial outer membrane proteins reflects evolution and life style of the Chlamydiae Actin re-organization induced by Chlamydia trachomatis serovar D--evidence for a critical role of the effector protein CT166 targeting Rac.Genetic variation in Chlamydia trachomatis and their hosts: impact on disease severity and tissue tropism Chlamydia Hijacks ARF GTPases To Coordinate Microtubule Posttranslational Modifications and Golgi Complex Positioning Bacillus anthracis spore entry into epithelial cells is an actin-dependent process requiring c-Src and PI3K.The conserved Tarp actin binding domain is important for chlamydial invasion.Lipopolysaccharide-binding alkylpolyamine DS-96 inhibits Chlamydia trachomatis infection by blocking attachment and entry.Novel molecular markers of Chlamydia pecorum genetic diversity in the koala (Phascolarctos cinereus).Chlamydia trachomatis strains and virulence: rethinking links to infection prevalence and disease severity Phylogenetic analysis of Chlamydia trachomatis Tarp and correlation with clinical phenotype.Amoebal endosymbiont Protochlamydia induces apoptosis to human immortal HEp-2 cells Immunodominant regions of a Chlamydia trachomatis type III secretion effector protein, Tarp.The Legionella pneumophila effector VipA is an actin nucleator that alters host cell organelle trafficking.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.Approach to discover T- and B-cell antigens of intracellular pathogens applied to the design of Chlamydia trachomatis vaccines Identification of motifs of Burkholderia pseudomallei BimA required for intracellular motility, actin binding, and actin polymerization.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 TARP Unity in variety--the pan-genome of the Chlamydiae Host-pathogen reorganisation during host cell entry by Chlamydia trachomatis.Genetic diversity in the plasticity zone and the presence of the chlamydial plasmid differentiates Chlamydia pecorum strains from pigs, sheep, cattle, and koalas

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Chlamydial TARP is a bacterial nucleator of actin

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description

2006 nî lūn-bûn

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2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2006 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Chlamydial TARP is a bacterial nucleator of actin

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Chlamydial TARP is a bacterial nucleator of actin

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Chlamydial TARP is a bacterial nucleator of actin

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Chlamydial TARP is a bacterial nucleator of actin

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Chlamydial TARP is a bacterial nucleator of actin

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Chlamydial TARP is a bacterial nucleator of actin

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Chlamydial TARP is a bacterial nucleator of actin

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P2093

David J Mead

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Elizabeth R Fischer

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Ted Hackstadt

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Travis J Jewett

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P2860

WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac

Comparative Genomic Analysis of Chlamydia trachomatis Oculotropic and Genitotropic Strains

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

Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP

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

Effects of cytochalasin and phalloidin on actin

Role of formins in actin assembly: nucleation and barbed-end association.

Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex

Actin polymerization. The mechanism of action of cytochalasin D

Actin-dependent movement of bacterial pathogens

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103

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