Cloning and characterization of secretory tyrosine phosphatases of Mycobacterium tuberculosis
about
Tyrosine phosphorylation and bacterial virulenceStructural Basis for Selective Inhibition of Mycobacterium tuberculosis Protein Tyrosine Phosphatase PtpBThe Apo-structure of the Low Molecular Weight Protein-tyrosine Phosphatase A (MptpA) from Mycobacterium tuberculosis Allows for Better Target-specific Drug DevelopmentMechanism of phagolysosome biogenesis block by viable Mycobacterium tuberculosis.Mycobacterium tuberculosis PtkA is a novel protein tyrosine kinase whose substrate is PtpAStringent homology-based prediction of H. sapiens-M. tuberculosis H37Rv protein-protein interactions.An arsenate reductase from Synechocystis sp. strain PCC 6803 exhibits a novel combination of catalytic characteristicsDiscovery of Mycobacterium tuberculosis protein tyrosine phosphatase A (MptpA) inhibitors based on natural products and a fragment-based approach.Inhibition of MptpB phosphatase from Mycobacterium tuberculosis impairs mycobacterial survival in macrophages.Fragment-based discovery of selective inhibitors of the Mycobacterium tuberculosis protein tyrosine phosphatase PtpA.A new family of phosphoinositide phosphatases in microorganisms: identification and biochemical analysisMycobacterium tuberculosis supports protein tyrosine phosphorylationSolution structure of a low-molecular-weight protein tyrosine phosphatase from Bacillus subtilisMALDI mass sequencing and biochemical characterization of Setaria cervi protein tyrosine phosphatase.Mycobacterium tuberculosis Serine/Threonine Protein Kinases.Secretory phosphatases deficient mutant of Mycobacterium tuberculosis imparts protection at the primary site of infection in guinea pigs.A low molecular weight protein tyrosine phosphatase from Synechocystis sp. strain PCC 6803: enzymatic characterization and identification of its potential substratesDouble click reaction for the acquisition of a highly potent and selective mPTPB inhibitorProtein tyrosine phosphatase PtpA is not required for Mycobacterium tuberculosis growth in mice.The structure of phosphoinositide phosphatases: Insights into substrate specificity and catalysis.Listeria monocytogenes tyrosine phosphatases affect wall teichoic acid composition and phage resistanceInterplay between mycobacteria and host signalling pathways.Mycobacterial shuttle vectors designed for high-level protein expression in infected macrophages.Systematic Analysis of Mycobacterial Acylation Reveals First Example of Acylation-mediated Regulation of Enzyme Activity of a Bacterial PhosphataseCefsulodin Inspired Potent and Selective Inhibitors of mPTPB, a Virulent Phosphatase from Mycobacterium tuberculosis.Structure/function studies of Ser/Thr and Tyr protein phosphorylation in Mycobacterium tuberculosis.Genetic-and-Epigenetic Interspecies Networks for Cross-Talk Mechanisms in Human Macrophages and Dendritic Cells during MTB Infection.Eukaryote-like serine/threonine kinases and phosphatases in bacteria.New strategies in fighting TB: targeting Mycobacterium tuberculosis-secreted phosphatases MptpA & MptpB.Role of mycobacteria effectors in phagosome maturation blockage and new drug targets discovery.Virulence factors of the Mycobacterium tuberculosis complexElimination of intracellularly residing Mycobacterium tuberculosis through targeting of host and bacterial signaling mechanisms.Agents of change - concepts in Mycobacterium tuberculosis Ser/Thr/Tyr phosphosignalling.An essential tyrosine phosphatase homolog regulates cell separation, outer membrane integrity, and morphology in Caulobacter crescentusSolution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery.The Streptococcus pyogenes orphan protein tyrosine phosphatase, SP-PTP, possesses dual specificity and essential virulence regulatory functions.New potential eukaryotic substrates of the mycobacterial protein tyrosine phosphatase PtpA: hints of a bacterial modulation of macrophage bioenergetics state.Mycobacterium tuberculosis suppresses innate immunity by coopting the host ubiquitin system.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 lineAntimycobacterial and photosynthetic electron transport inhibiting activity of ring-substituted 4-arylamino-7-chloroquinolinium chlorides.
P2860
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P2860
Cloning and characterization of secretory tyrosine phosphatases of Mycobacterium tuberculosis
description
2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2000
@ast
im Oktober 2000 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2000/10/01)
@sk
vědecký článek publikovaný v roce 2000
@cs
wetenschappelijk artikel (gepubliceerd op 2000/10/01)
@nl
наукова стаття, опублікована в жовтні 2000
@uk
مقالة علمية (نشرت في أكتوبر 2000)
@ar
name
Cloning and characterization o ...... of Mycobacterium tuberculosis
@ast
Cloning and characterization o ...... of Mycobacterium tuberculosis
@en
Cloning and characterization o ...... of Mycobacterium tuberculosis
@nl
type
label
Cloning and characterization o ...... of Mycobacterium tuberculosis
@ast
Cloning and characterization o ...... of Mycobacterium tuberculosis
@en
Cloning and characterization o ...... of Mycobacterium tuberculosis
@nl
prefLabel
Cloning and characterization o ...... of Mycobacterium tuberculosis
@ast
Cloning and characterization o ...... of Mycobacterium tuberculosis
@en
Cloning and characterization o ...... of Mycobacterium tuberculosis
@nl
P2093
P2860
P3181
P1476
Cloning and characterization o ...... of Mycobacterium tuberculosis
@en
P2093
A. Choidas
A. K. Tyagi
A. Ullrich
P2860
P304
P3181
P356
10.1128/JB.182.19.5425-5432.2000
P407
P577
2000-10-01T00:00:00Z