Survival of pathogenic mycobacteria in macrophages is mediated through autophosphorylation of protein kinase G
about
Crosstalk between Mycobacterium tuberculosis and the host cellIdentification of Ser/Thr kinase and forkhead associated domains in Mycobacterium ulcerans: characterization of novel association between protein kinase Q and MupFHAInflammatory stimuli reprogram macrophage phagocytosis to macropinocytosis for the rapid elimination of pathogensProteins with complex architecture as potential targets for drug design: a case study of Mycobacterium tuberculosisEstablishment and validation of whole-cell based fluorescence assays to identify anti-mycobacterial compounds using the Acanthamoeba castellanii-Mycobacterium marinum host-pathogen systemExploring prospects of novel drugs for tuberculosis.Mycobacterium tuberculosis protein kinase K confers survival advantage during early infection in mice and regulates growth in culture and during persistent infection: implications for immune modulation.Protein kinase A (PknA) of Mycobacterium tuberculosis is independently activated and is critical for growth in vitro and survival of the pathogen in the host.Nontuberculous mycobacterial osteomyelitis.Key residues in Mycobacterium tuberculosis protein kinase G play a role in regulating kinase activity and survival in the host.Bacterial serine/threonine protein kinases in host-pathogen interactions.Virulence factors of the Mycobacterium tuberculosis complexElimination of intracellularly residing Mycobacterium tuberculosis through targeting of host and bacterial signaling mechanisms.Cytokine-induced macropinocytosis in macrophages is regulated by 14-3-3ζ through its interaction with serine-phosphorylated coronin 1.Oxidative Unfolding of the Rubredoxin Domain and the Natively Disordered N-terminal Region Regulate the Catalytic Activity of Mycobacterium tuberculosis Protein Kinase G.New Test System for Serine/Threonine Protein Kinase Inhibitors Screening: E. coli APHVIII/Pk25 designPknG supports mycobacterial adaptation in acidic environment.Chemical shift assignment of the intrinsically disordered N-terminus and the rubredoxin domain in the folded metal bound and unfolded oxidized state of mycobacterial protein kinase G.Identification of novel physiological substrates of Mycobacterium Bovis BCG Protein Kinase G (PknG) by label-free quantitative phosphoproteomics.Analysis of SecA2-dependent substrates in Mycobacterium marinum identifies protein kinase G (PknG) as a virulence effector.
P2860
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P2860
Survival of pathogenic mycobacteria in macrophages is mediated through autophosphorylation of protein kinase G
description
2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2009
@ast
im Juli 2009 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2009/07/01)
@sk
vědecký článek publikovaný v roce 2009
@cs
wetenschappelijk artikel (gepubliceerd op 2009/07/01)
@nl
наукова стаття, опублікована в липні 2009
@uk
مقالة علمية (نشرت في يوليو 2009)
@ar
name
Survival of pathogenic mycobac ...... horylation of protein kinase G
@ast
Survival of pathogenic mycobac ...... horylation of protein kinase G
@en
Survival of pathogenic mycobac ...... horylation of protein kinase G
@nl
type
label
Survival of pathogenic mycobac ...... horylation of protein kinase G
@ast
Survival of pathogenic mycobac ...... horylation of protein kinase G
@en
Survival of pathogenic mycobac ...... horylation of protein kinase G
@nl
prefLabel
Survival of pathogenic mycobac ...... horylation of protein kinase G
@ast
Survival of pathogenic mycobac ...... horylation of protein kinase G
@en
Survival of pathogenic mycobac ...... horylation of protein kinase G
@nl
P2093
P2860
P356
P1476
Survival of pathogenic mycobac ...... horylation of protein kinase G
@en
P2093
Benoît Combaluzier
Damir Perisa
Nicole Scherr
Philipp Müller
P2860
P304
P356
10.1128/JB.00245-09
P407
P50
P577
2009-05-15T00:00:00Z