Phosphorylation of Mycobacterium tuberculosis Ser/Thr phosphatase by PknA and PknB
about
Ser/Thr phosphorylation as a regulatory mechanism in bacteriaIdentification of Ser/Thr kinase and forkhead associated domains in Mycobacterium ulcerans: characterization of novel association between protein kinase Q and MupFHABiochemical and spatial coincidence in the provisional Ser/Thr protein kinase interaction network of Mycobacterium tuberculosis.Mycobacterium tuberculosis Serine/Threonine Protein Kinases.Interaction of Mycobacterium tuberculosis elongation factor Tu with GTP is regulated by phosphorylation.Comparative Ser/Thr/Tyr phosphoproteomics between two mycobacterial species: the fast growing Mycobacterium smegmatis and the slow growing Mycobacterium bovis BCG.Reciprocal regulation of cephalosporin resistance in Enterococcus faecalis.Unveiling the novel dual specificity protein kinases in Bacillus anthracis: identification of the first prokaryotic dual specificity tyrosine phosphorylation-regulated kinase (DYRK)-like kinase.Systematic Analysis of Mycobacterial Acylation Reveals First Example of Acylation-mediated Regulation of Enzyme Activity of a Bacterial PhosphataseCytoskeletal proteins of actinobacteria.Elimination of intracellularly residing Mycobacterium tuberculosis through targeting of host and bacterial signaling mechanisms.Mycobacterial Growth.Serine/Threonine Protein Phosphatase PstP of Mycobacterium tuberculosis Is Necessary for Accurate Cell Division and Survival of Pathogen.Regulation of homocysteine metabolism by Mycobacterium tuberculosis S-adenosylhomocysteine hydrolaseSer/Thr protein kinase PrkC-mediated regulation of GroEL is critical for biofilm formation in Bacillus anthracis.Ser/Thr Phosphorylation Regulates the Fatty Acyl-AMP Ligase Activity of FadD32, an Essential Enzyme in Mycolic Acid BiosynthesisClose proximity of phosphorylation sites to ligand in the phosphoproteome of the extreme thermophile Thermus thermophilus HB8.Zinc regulates the activity of kinase-phosphatase pair (BasPrkC/BasPrpC) in Bacillus anthracis.The transpeptidase PbpA and non-canonical transglycosylase RodA of Mycobacterium tuberculosis play important roles in regulating bacterial cell lengths.Identification of novel physiological substrates of Mycobacterium Bovis BCG Protein Kinase G (PknG) by label-free quantitative phosphoproteomics.Phosphorylation regulates mycobacterial proteasome.Inhibition of the Protein Phosphatase CppA Alters Development of Chlamydia trachomatis
P2860
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P2860
Phosphorylation of Mycobacterium tuberculosis Ser/Thr phosphatase by PknA and PknB
description
2011 nî lūn-bûn
@nan
2011 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մարտին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Phosphorylation of Mycobacterium tuberculosis Ser/Thr phosphatase by PknA and PknB
@ast
Phosphorylation of Mycobacterium tuberculosis Ser/Thr phosphatase by PknA and PknB
@en
type
label
Phosphorylation of Mycobacterium tuberculosis Ser/Thr phosphatase by PknA and PknB
@ast
Phosphorylation of Mycobacterium tuberculosis Ser/Thr phosphatase by PknA and PknB
@en
prefLabel
Phosphorylation of Mycobacterium tuberculosis Ser/Thr phosphatase by PknA and PknB
@ast
Phosphorylation of Mycobacterium tuberculosis Ser/Thr phosphatase by PknA and PknB
@en
P2093
P2860
P1433
P1476
Phosphorylation of Mycobacterium tuberculosis Ser/Thr phosphatase by PknA and PknB
@en
P2093
Gunjan Arora
Meetu Gupta
Sandeep Upadhyay
Yogendra Singh
P2860
P304
P356
10.1371/JOURNAL.PONE.0017871
P407
P577
2011-03-09T00:00:00Z