Tyrosine phosphatase MptpA of Mycobacterium tuberculosis inhibits phagocytosis and increases actin polymerization in macrophages
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Tyrosine phosphorylation and bacterial virulenceEvidence for oxidative stress and defective antioxidant response in guinea pigs with tuberculosisInhibition of MptpB phosphatase from Mycobacterium tuberculosis impairs mycobacterial survival in macrophages.Alterporriol-type dimers from the mangrove endophytic fungus, Alternaria sp. (SK11), and their MptpB inhibitionsAsperlones A and B, dinaphthalenone derivatives from a mangrove endophytic fungus Aspergillus sp. 16-5C.Protein tyrosine phosphatase PtpA is not required for Mycobacterium tuberculosis growth in mice.Bicyclic benzofuran and indole-based salicylic acids as protein tyrosine phosphatase inhibitorsRole of protein phosphorylation on serine/threonine and tyrosine in the virulence of bacterial pathogens.Actin-binding protein regulation by microRNAs as a novel microbial strategy to modulate phagocytosis by host cells: the case of N-Wasp and miR-142-3pProtein tyrosine phosphatases: structure-function relationships.Mycobacterial Protein Tyrosine Phosphatases A and B Inhibitors Augment the Bactericidal Activity of the Standard Anti-tuberculosis RegimenNew strategies in fighting TB: targeting Mycobacterium tuberculosis-secreted phosphatases MptpA & MptpB.Protein tyrosine phosphatase structure-function relationships in regulation and pathogenesis.Reactive nitrogen species and hydrogen sulfide as regulators of protein tyrosine phosphatase activity.The tyrosine kinase BceF and the phosphotyrosine phosphatase BceD of Burkholderia contaminans are required for efficient invasion and epithelial disruption of a cystic fibrosis lung epithelial cell lineMycobacterium avium subsp. paratuberculosis PtpA is an endogenous tyrosine phosphatase secreted during infectionMptpB, a virulence factor from Mycobacterium tuberculosis, exhibits triple-specificity phosphatase activityIdentification and characterization of a protein-tyrosine phosphatase in Leishmania: Involvement in virulence.The solution structure of Escherichia coli Wzb reveals a novel substrate recognition mechanism of prokaryotic low molecular weight protein-tyrosine phosphatases.Bacillus Calmette-Guérin induces rapid gene expression changes in human bladder cancer cell lines that may modulate its survival.
P2860
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P2860
Tyrosine phosphatase MptpA of Mycobacterium tuberculosis inhibits phagocytosis and increases actin polymerization in macrophages
description
2005 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2005
@ast
scientific journal article
@en
vedecký článok (publikovaný 2005/12/01)
@sk
vědecký článek publikovaný v roce 2005
@cs
wetenschappelijk artikel (gepubliceerd op 2005/12/01)
@nl
наукова стаття, опублікована в грудні 2005
@uk
مقالة علمية (نشرت في ديسمبر 2005)
@ar
name
Tyrosine phosphatase MptpA of ...... polymerization in macrophages
@ast
Tyrosine phosphatase MptpA of ...... polymerization in macrophages
@en
Tyrosine phosphatase MptpA of ...... polymerization in macrophages
@nl
type
label
Tyrosine phosphatase MptpA of ...... polymerization in macrophages
@ast
Tyrosine phosphatase MptpA of ...... polymerization in macrophages
@en
Tyrosine phosphatase MptpA of ...... polymerization in macrophages
@nl
prefLabel
Tyrosine phosphatase MptpA of ...... polymerization in macrophages
@ast
Tyrosine phosphatase MptpA of ...... polymerization in macrophages
@en
Tyrosine phosphatase MptpA of ...... polymerization in macrophages
@nl
P2093
P50
P921
P1476
Tyrosine phosphatase MptpA of ...... polymerization in macrophages
@en
P2093
Alain J. Cozzone
Gareth Griffiths
Jean-François Prost
Jérôme Castandet
Pascale Peyron
P304
P356
10.1016/J.RESMIC.2005.05.013
P577
2005-12-01T00:00:00Z