Phosphoprotein phosphatase of Mycobacterium tuberculosis dephosphorylates serine-threonine kinases PknA and PknB
about
The Sorcerer II Global Ocean Sampling expedition: expanding the universe of protein familiesGenome sequence of the Fleming strain of Micrococcus luteus, a simple free-living actinobacteriumMass Spectrometry Offers Insight into the Role of Ser/Thr/Tyr Phosphorylation in the MycobacteriaUnderstanding the role of PknJ in Mycobacterium tuberculosis: biochemical characterization and identification of novel substrate pyruvate kinase ATranscriptional control of the mycobacterial embCAB operon by PknH through a regulatory protein, EmbR, in vivoThe condensing activities of the Mycobacterium tuberculosis type II fatty acid synthase are differentially regulated by phosphorylationLoss of kinase activity in Mycobacterium tuberculosis multidomain protein Rv1364cPhosphorylation of Mycobacterium tuberculosis Ser/Thr phosphatase by PknA and PknBMolecular structure of EmbR, a response element of Ser/Thr kinase signaling in Mycobacterium tuberculosis.Bacterial growth and cell division: a mycobacterial perspective.Comparative Ser/Thr/Tyr phosphoproteomics between two mycobacterial species: the fast growing Mycobacterium smegmatis and the slow growing Mycobacterium bovis BCG.Recent advances towards identification of new drug targets for Mycobacterium tuberculosis.Structure/function studies of Ser/Thr and Tyr protein phosphorylation in Mycobacterium tuberculosis.Phosphorylation Modulates Catalytic Activity of Mycobacterial Sirtuins.Pathogens hijack the epigenome: a new twist on host-pathogen interactions.Eukaryote-like serine/threonine kinases and phosphatases in bacteria.New strategies in fighting TB: targeting Mycobacterium tuberculosis-secreted phosphatases MptpA & MptpB.Elimination of intracellularly residing Mycobacterium tuberculosis through targeting of host and bacterial signaling mechanisms.Serine/Threonine Protein Phosphatase PstP of Mycobacterium tuberculosis Is Necessary for Accurate Cell Division and Survival of Pathogen.Zinc regulates the activity of kinase-phosphatase pair (BasPrkC/BasPrpC) in Bacillus anthracis.Integrated gene co-expression network analysis in the growth phase of Mycobacterium tuberculosis reveals new potential drug targets.
P2860
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P2860
Phosphoprotein phosphatase of Mycobacterium tuberculosis dephosphorylates serine-threonine kinases PknA and PknB
description
2003 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2003
@ast
im November 2003 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2003/11/07)
@sk
vědecký článek publikovaný v roce 2003
@cs
wetenschappelijk artikel (gepubliceerd op 2003/11/07)
@nl
наукова стаття, опублікована в листопаді 2003
@uk
مقالة علمية (نشرت في 7-11-2003)
@ar
name
Phosphoprotein phosphatase of ...... hreonine kinases PknA and PknB
@ast
Phosphoprotein phosphatase of ...... hreonine kinases PknA and PknB
@en
Phosphoprotein phosphatase of ...... hreonine kinases PknA and PknB
@nl
type
label
Phosphoprotein phosphatase of ...... hreonine kinases PknA and PknB
@ast
Phosphoprotein phosphatase of ...... hreonine kinases PknA and PknB
@en
Phosphoprotein phosphatase of ...... hreonine kinases PknA and PknB
@nl
prefLabel
Phosphoprotein phosphatase of ...... hreonine kinases PknA and PknB
@ast
Phosphoprotein phosphatase of ...... hreonine kinases PknA and PknB
@en
Phosphoprotein phosphatase of ...... hreonine kinases PknA and PknB
@nl
P2093
P3181
P1476
Phosphoprotein phosphatase of ...... hreonine kinases PknA and PknB
@en
P2093
Anil K. Tyagi
Bhuminder Singh
Harshavardhan Koduri
Laxman S. Meena
Megha Ghildiyal
Parampal Deol
Puneet Chopra
Ramandeep Singh
Reena Vohra
P304
P3181
P356
10.1016/J.BBRC.2003.09.173
P407
P577
2003-11-07T00:00:00Z