Mycobacterium tuberculosis ESAT-6 exhibits a unique membrane-interacting activity that is not found in its ortholog from non-pathogenic Mycobacterium smegmatis.
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The ESX-5 System of Pathogenic Mycobacteria Is Involved In Capsule Integrity and Virulence through Its Substrate PPE10Heterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusionsDNA sensor cGAS-mediated immune recognitionThe Disulfide Bond Cys255-Cys279 in the Immunoglobulin-Like Domain of Anthrax Toxin Receptor 2 Is Required for Membrane Insertion of Anthrax Protective Antigen PoreMycobacterium tuberculosis ESAT-6 is a leukocidin causing Ca2+ influx, necrosis and neutrophil extracellular trap formation.A Novel ESAT-6 Secretion System-Secreted Protein EsxX of Community-Associated Staphylococcus aureus Lineage ST398 Contributes to Immune Evasion and Virulence.Identification of a two-component fatty acid kinase responsible for host fatty acid incorporation by Staphylococcus aureusExpression and purification of the functional ectodomain of human anthrax toxin receptor 2 in Escherichia coli Origami B cells with assistance of bacterial Trigger FactorHomeostasis of N-α-terminal acetylation of EsxA correlates with virulence in Mycobacterium marinum.Characterization of Mycobacterium tuberculosis EsxA membrane insertion: roles of N- and C-terminal flexible arms and central helix-turn-helix motifAutophagy-Related Proteins Target Ubiquitin-Free Mycobacterial Compartment to Promote Killing in MacrophagesCharacterization of differential pore-forming activities of ESAT-6 proteins from Mycobacterium tuberculosis and Mycobacterium smegmatisMechanism of ESAT-6 membrane interaction and its roles in pathogenesis of Mycobacterium tuberculosis.EsxA membrane-permeabilizing activity plays a key role in mycobacterial cytosolic translocation and virulence: effects of single-residue mutations at glutamine 5.Disconnecting in vitro ESX-1 secretion from mycobacterial virulence.Secretion of atypical protein substrates by the ESAT-6 secretion system of Staphylococcus aureusMycobacterium tuberculosis evolutionary pathogenesis and its putative impact on drug development.The Cell Wall Lipid PDIM Contributes to Phagosomal Escape and Host Cell Exit of Mycobacterium tuberculosis.Mycobacterium tuberculosis EsxL inhibits MHC-II expression by promoting hypermethylation in class-II transactivator loci in macrophages.Exosomes derived from tumor cells genetically modified to express Mycobacterium tuberculosis antigen: a novel vaccine for cancer therapy.Perspectives on mycobacterial vacuole-to-cytosol translocation: the importance of cytosolic access.Staphylococcal Esx proteins modulate apoptosis and release of intracellular Staphylococcus aureus during infection in epithelial cells.Mycobacterium tuberculosis EspB binds phospholipids and mediates EsxA-independent virulence.Small Molecules That Sabotage Bacterial Virulence.EspC forms a filamentous structure in the cell envelope of Mycobacterium tuberculosis and impacts ESX-1 secretion.Esx Systems and the Mycobacterial Cell Envelope: What's the Connection?cGAS-STING-TBK1-IRF3/7 induced interferon-β contributes to the clearing of non tuberculous mycobacterial infection in mice.Mycobacterial ESX-1 secretion system mediates host cell lysis through bacterium contact-dependent gross membrane disruptions.Cyclic GMP-AMP Synthase Is an Innate Immune DNA Sensor for Mycobacterium tuberculosis.Novel Antitumor Strategy Utilizing a Plasmid Expressing a Mycobacterium tuberculosis Antigen as a "Danger Signal" to Block Immune Escape of Tumor Cells.The ins and outs of the Mycobacterium tuberculosis-containing vacuole.Two distinct conformational states of Mycobacterium tuberculosis virulent factor early secreted antigenic target 6 kDa are behind the discrepancy around its biological functions.Type VII Secretion Systems in Gram-Positive Bacteria.EspH is a hypervirulence factor for Mycobacterium marinum and essential for the secretion of the ESX-1 substrates EspE and EspF
P2860
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P2860
Mycobacterium tuberculosis ESAT-6 exhibits a unique membrane-interacting activity that is not found in its ortholog from non-pathogenic Mycobacterium smegmatis.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
Mycobacterium tuberculosis ESA ...... genic Mycobacterium smegmatis.
@ast
Mycobacterium tuberculosis ESA ...... genic Mycobacterium smegmatis.
@en
type
label
Mycobacterium tuberculosis ESA ...... genic Mycobacterium smegmatis.
@ast
Mycobacterium tuberculosis ESA ...... genic Mycobacterium smegmatis.
@en
prefLabel
Mycobacterium tuberculosis ESA ...... genic Mycobacterium smegmatis.
@ast
Mycobacterium tuberculosis ESA ...... genic Mycobacterium smegmatis.
@en
P2093
P2860
P356
P1476
Mycobacterium tuberculosis ESA ...... ogenic Mycobacterium smegmatis
@en
P2093
Guozhong Jiang
Jianjun Sun
Joaquin De Leon
Sarah Fortune
P2860
P304
44184-44191
P356
10.1074/JBC.M112.420869
P407
P50
P577
2012-11-13T00:00:00Z