Polar localization of virulence-related Esx-1 secretion in mycobacteria. - Test2 - elhamkhani - TriplyDB

Polar localization of virulence-related Esx-1 secretion in mycobacteria.

Polar localization of virulence-related Esx-1 secretion in mycobacteria.

http://www.wikidata.org/entity/Q33404091

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ESX-1 secreted virulence factors are recognized by multiple cytosolic AAA ATPases in pathogenic mycobacteria Modular Organization of the ESX-5 Secretion System in Mycobacterium tuberculosis The ESX-5 System of Pathogenic Mycobacteria Is Involved In Capsule Integrity and Virulence through Its Substrate PPE10 Mycobacterium tuberculosis proteins involved in mycolic acid synthesis and transport localize dynamically to the old growing pole and septum High levels of DegU-P activate an Esat-6-like secretion system in Bacillus subtilis Systematic genetic nomenclature for type VII secretion systems.A novel ESX-1 locus reveals that surface-associated ESX-1 substrates mediate virulence in Mycobacterium marinum.Direct visualization by cryo-EM of the mycobacterial capsular layer: a labile structure containing ESX-1-secreted proteins.To catch a killer. What can mycobacterial models teach us about Mycobacterium tuberculosis pathogenesis?Polar localization of the Coxiella burnetii type IVB secretion system.Direct detection of bacterial protein secretion using whole colony proteomics.Mycobacterium tuberculosis PE25/PPE41 protein complex induces necrosis in macrophages: Role in virulence and disease reactivation?Correlation of phenotypic profiles using targeted proteomics identifies mycobacterial esx-1 substrates.Impact of protein domains on PE_PGRS30 polar localization in Mycobacteria Poles apart: prokaryotic polar organelles and their spatial regulation Homeostasis of N-α-terminal acetylation of EsxA correlates with virulence in Mycobacterium marinum.Deciphering the growth behaviour of Mycobacterium africanum.Conserved Pro-Glu (PE) and Pro-Pro-Glu (PPE) protein domains target LipY lipases of pathogenic mycobacteria to the cell surface via the ESX-5 pathway.Revealing of Mycobacterium marinum transcriptome by RNA-seq The autophagic machinery ensures nonlytic transmission of mycobacteria.Bacteriophage infection in rod-shaped gram-positive bacteria: evidence for a preferential polar route for phage SPP1 entry in Bacillus subtilis.Structure of EspB, a secreted substrate of the ESX-1 secretion system of Mycobacterium tuberculosis.The conserved polarity factor podJ1 impacts multiple cell envelope-associated functions in Sinorhizobium meliloti.General secretion signal for the mycobacterial type VII secretion pathway.A Duplicated ESAT-6 Region of ESX-5 Is Involved in Protein Export and Virulence of Mycobacteria.Specific chaperones for the type VII protein secretion pathway.Systematic review on the proteomic profile of Mycobacterium tuberculosis exposed to drugs.Prison break: pathogens' strategies to egress from host cells.EsxA membrane-permeabilizing activity plays a key role in mycobacterial cytosolic translocation and virulence: effects of single-residue mutations at glutamine 5.The Mycobacterium avium ESX-5 PPE protein, PPE25-MAV, interacts with an ESAT-6 family Protein, MAV_2921, and localizes to the bacterial surface A Nonsense Mutation in Mycobacterium marinum That Is Suppressible by a Novel Mechanism VgrG-5 is a Burkholderia type VI secretion system-exported protein required for multinucleated giant cell formation and virulence.The ins and outs of Mycobacterium tuberculosis protein export.Compartmentalization and spatiotemporal organization of macromolecules in bacteria.Virulence factors of the Mycobacterium tuberculosis complex Release of mycobacterial antigens.Esx Systems and the Mycobacterial Cell Envelope: What's the Connection?Polar assembly and scaffolding proteins of the virulence-associated ESX-1 secretory apparatus in mycobacteria.Unexpected link between lipooligosaccharide biosynthesis and surface protein release in Mycobacterium marinum.Zebrafish embryo screen for mycobacterial genes involved in the initiation of granuloma formation reveals a newly identified ESX-1 component.

P2860

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P2860

Polar localization of virulence-related Esx-1 secretion in mycobacteria.

http://www.wikidata.org/entity/Q33404091

description

2009 nî lūn-bûn

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2009 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հունվարին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Polar localization of virulence-related Esx-1 secretion in mycobacteria.

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Polar localization of virulence-related Esx-1 secretion in mycobacteria.

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type

label

Polar localization of virulence-related Esx-1 secretion in mycobacteria.

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Polar localization of virulence-related Esx-1 secretion in mycobacteria.

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prefLabel

Polar localization of virulence-related Esx-1 secretion in mycobacteria.

@ast

Polar localization of virulence-related Esx-1 secretion in mycobacteria.

@en

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JOURNAL.PPAT.1000285

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Polar localization of virulence-related Esx-1 secretion in mycobacteria.

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Eric J Brown

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

Linda Rangell

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Shilpa A Joshi

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P2860

Mechanism of polarization of Listeria monocytogenes surface protein ActA

Tuberculous granuloma formation is enhanced by a mycobacterium virulence determinant

Individual RD1-region genes are required for export of ESAT-6/CFP-10 and for virulence of Mycobacterium tuberculosis

A mycobacterium ESX-1-secreted virulence factor with unique requirements for export

Mutually dependent secretion of proteins required for mycobacterial virulence.

Acute infection and macrophage subversion by Mycobacterium tuberculosis require a specialized secretion system

Genetic requirements for mycobacterial survival during infection

Spatial location and requirements for the assembly of the Agrobacterium tumefaciens type IV secretion apparatus.

Cytoplasmic targeting of IpaC to the bacterial pole directs polar type III secretion in Shigella

A mycobacterial virulence gene cluster extending RD1 is required for cytolysis, bacterial spreading and ESAT-6 secretion.

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e1000285

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scholarly article

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10.1371/JOURNAL.PPAT.1000285

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5

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Fredric Carlsson

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