Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition
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Modular Organization of the ESX-5 Secretion System in Mycobacterium tuberculosisThe pup-proteasome system of Mycobacterium tuberculosisThe Pup-Proteasome System of MycobacteriaNonclassical T cells and their antigens in tuberculosisDiscovery of a Siderophore Export System Essential for Virulence of Mycobacterium tuberculosisStructure of the Mycosin-1 Protease from the Mycobacterial ESX-1 Protein Type VII Secretion SystemMycobacterium tuberculosis Rv3406 is a type II alkyl sulfatase capable of sulfate scavengingUnderstanding specificity of the mycosin proteases in ESX/type VII secretion by structural and functional analysisHeterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusionsBacterial Secretion Systems: An OverviewSimultaneous analysis of multiple Mycobacterium tuberculosis knockdown mutants in vitro and in vivoA β-Lactamase based reporter system for ESX dependent protein translocation in mycobacteria4'-Phosphopantetheinyl transferase PptT, a new drug target required for Mycobacterium tuberculosis growth and persistence in vivoA novel copper-responsive regulon in Mycobacterium tuberculosisEspA acts as a critical mediator of ESX1-dependent virulence in Mycobacterium tuberculosis by affecting bacterial cell wall integrityThe crystal structure of the Mycobacterium tuberculosis Rv3019c-Rv3020c ESX complex reveals a domain-swapped heterotetramerIdentification of new drug targets and resistance mechanisms in Mycobacterium tuberculosisRegulation of mycolactone, the Mycobacterium ulcerans toxin, depends on nutrient sourceLipidomic analysis links mycobactin synthase K to iron uptake and virulence in M. tuberculosisThe Complete Genome Sequence of the Emerging Pathogen Mycobacterium haemophilum Explains Its Unique Culture RequirementsStructures of EccB1 and EccD1 from the core complex of the mycobacterial ESX-1 type VII secretion system.Iron Homeostasis in Mycobacterium tuberculosis: Mechanistic Insights into Siderophore-Mediated Iron UptakeMycobacterial Esx-3 requires multiple components for iron acquisition.Dimer recognition and secretion by the ESX secretion system in Bacillus subtilisPrimary transcriptomes of Mycobacterium avium subsp. paratuberculosis reveal proprietary pathways in tissue and macrophages.Iron-sparing response of Mycobacterium avium subsp. paratuberculosis is strain dependent.Mycobacterium tuberculosis EsxH inhibits ESCRT-dependent CD4+ T-cell activationTo catch a killer. What can mycobacterial models teach us about Mycobacterium tuberculosis pathogenesis?Direct detection of bacterial protein secretion using whole colony proteomics.Structure of the Mycobacterium tuberculosis type VII secretion system chaperone EspG5 in complex with PE25-PPE41 dimer.Manipulation of the mononuclear phagocyte system by Mycobacterium tuberculosis.Role of porins in iron uptake by Mycobacterium smegmatis.Mycobacterium tuberculosis acquires iron by cell-surface sequestration and internalization of human holo-transferrin.The ESX-5 associated eccB-EccC locus is essential for Mycobacterium tuberculosis viability.Regulated Expression Systems for Mycobacteria and Their ApplicationsGenetics of Capsular Polysaccharides and Cell Envelope (Glyco)lipids.Depletion of antibiotic targets has widely varying effects on growthProtein inactivation in mycobacteria by controlled proteolysis and its application to deplete the beta subunit of RNA polymerase.Mycobacterium tuberculosis can utilize heme as an iron source.The ESX-3 secretion system is necessary for iron and zinc homeostasis in Mycobacterium tuberculosis.
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P2860
Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition
description
2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
article publié dans les Procee ...... f the United States of America
@fr
artículu científicu espublizáu en 2009
@ast
im November 2009 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2009/11/03)
@sk
vědecký článek publikovaný v roce 2009
@cs
wetenschappelijk artikel (gepubliceerd op 2009/11/03)
@nl
наукова стаття, опублікована в листопаді 2009
@uk
name
Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition
@ast
Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition
@en
Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition
@nl
type
label
Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition
@ast
Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition
@en
Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition
@nl
prefLabel
Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition
@ast
Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition
@en
Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition
@nl
P2093
P2860
P3181
P356
P1476
Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition
@en
P2093
D. Branch Moody
Eric J. Rubin
M. Sloan Siegrist
Mark Borowsky
Matthew J. McConnell
Meera Unnikrishnan
Noman Siddiqi
Sarah M. Fortune
Tan-Yun Cheng
P2860
P304
18792–18797
P3181
P356
10.1073/PNAS.0900589106
P407
P577
2009-11-03T00:00:00Z