Extensive phosphorylation with overlapping specificity by Mycobacterium tuberculosis serine/threonine protein kinases - Wikidata - awgldk - TriplyDB

Extensive phosphorylation with overlapping specificity by Mycobacterium tuberculosis serine/threonine protein kinases

Extensive phosphorylation with overlapping specificity by Mycobacterium tuberculosis serine/threonine protein kinases

http://www.wikidata.org/entity/Q33841901

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Role of Protein Phosphorylation in the Regulation of Cell Cycle and DNA-Related Processes in Bacteria Mass Spectrometry Offers Insight into the Role of Ser/Thr/Tyr Phosphorylation in the Mycobacteria Elucidating Host-Pathogen Interactions Based on Post-Translational Modifications Using Proteomics Approaches Bacterial phosphoproteomic analysis reveals the correlation between protein phosphorylation and bacterial pathogenicity Identification of Ser/Thr kinase and forkhead associated domains in Mycobacterium ulcerans: characterization of novel association between protein kinase Q and MupFHA Phosphorylation of the Peptidoglycan Synthase PonA1 Governs the Rate of Polar Elongation in Mycobacteria A Phosphorylated Pseudokinase Complex Controls Cell Wall Synthesis in Mycobacteria Evidence that phosphorylation of threonine in the GT motif triggers activation of PknA, a eukaryotic-type serine/threonine kinase from Mycobacterium tuberculosis Crystal structures of the transpeptidase domain of the Mycobacterium tuberculosis penicillin-binding protein PonA1 reveal potential mechanisms of antibiotic resistance Mycobacterium tuberculosis protein kinase K enables growth adaptation through translation control Characterisation of ATP-dependent Mur ligases involved in the biogenesis of cell wall peptidoglycan in Mycobacterium tuberculosis The Escherichia coli phosphotyrosine proteome relates to core pathways and virulence Mycobacterium tuberculosis Ser/Thr protein kinase B mediates an oxygen-dependent replication switch Phosphorylation of KasB regulates virulence and acid-fastness in Mycobacterium tuberculosis Biochemical analysis of the NAD+-dependent malate dehydrogenase, a substrate of several serine/threonine protein kinases of Mycobacterium tuberculosis Mycobacterial gene cuvA is required for optimal nutrient utilization and virulence Protein kinase B (PknB) of Mycobacterium tuberculosis is essential for growth of the pathogen in vitro as well as for survival within the host.Mycobacterium tuberculosis supports protein tyrosine phosphorylation Phosphorylation of Mycobacterium tuberculosis Ser/Thr phosphatase by PknA and PknB A novel protein kinase inhibitor IMB-YH-8 with anti-tuberculosis activity Biochemical and spatial coincidence in the provisional Ser/Thr protein kinase interaction network of Mycobacterium tuberculosis.The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr kinase PknB binds specific muropeptides and is required for PknB localization A eukaryotic-type signalling system of Pseudomonas aeruginosa contributes to oxidative stress resistance, intracellular survival and virulence.Quantitative phosphoproteome analysis of Bacillus subtilis reveals novel substrates of the kinase PrkC and phosphatase PrpC Toward Understanding the Essence of Post-Translational Modifications for the Mycobacterium tuberculosis Immunoproteome The eukaryotic-type serine/threonine protein kinase Stk is required for biofilm formation and virulence in Staphylococcus epidermidis Role of Mycobacterium tuberculosis pknD in the pathogenesis of central nervous system tuberculosis.Using bacteria to determine protein kinase specificity and predict target substrates Mycobacterium tuberculosis Serine/Threonine Protein Kinases.Phosphoproteomics analysis of a clinical Mycobacterium tuberculosis Beijing isolate: expanding the mycobacterial phosphoproteome catalog.Forkhead-associated (FHA) domain containing ABC transporter Rv1747 is positively regulated by Ser/Thr phosphorylation in Mycobacterium tuberculosis.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.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.Rapid and reproducible single-stage phosphopeptide enrichment of complex peptide mixtures: application to general and phosphotyrosine-specific phosphoproteomics experiments.The Eukaryotic-Like Ser/Thr Kinase PrkC Regulates the Essential WalRK Two-Component System in Bacillus subtilis Site-Specific Ser/Thr/Tyr Phosphoproteome of Sinorhizobium meliloti at Stationary Phase.Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium.Shotgun proteomics of bacterial pathogens: advances, challenges and clinical implications.RD-1 encoded EspJ protein gets phosphorylated prior to affect the growth and intracellular survival of mycobacteria.

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P2860

Extensive phosphorylation with overlapping specificity by Mycobacterium tuberculosis serine/threonine protein kinases

http://www.wikidata.org/entity/Q33841901

description

2010 nî lūn-bûn

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2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Extensive phosphorylation with ...... rine/threonine protein kinases

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Extensive phosphorylation with ...... rine/threonine protein kinases

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Extensive phosphorylation with ...... rine/threonine protein kinases

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Proceedings of the National Academy of Sciences of the United States of America

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Extensive phosphorylation with ...... rine/threonine protein kinases

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Choong-Min Kang

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Daniel Schwartz

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Guy Bemis

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Hanno Steen

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Michael F Chou

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Selasi Dankwa

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P2860

A probability-based approach for high-throughput protein phosphorylation analysis and site localization

The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition.

Sequence logos: a new way to display consensus sequences

The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms

Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis

An intramolecular switch regulates phosphoindependent FHA domain interactions in Mycobacterium tuberculosis

WebLogo: A Sequence Logo Generator

Mycobacterium tuberculosis serine/threonine kinases PknB, PknD, PknE, and PknF phosphorylate multiple FHA domains

The serine/threonine kinase PknB of Mycobacterium tuberculosis phosphorylates PBPA, a penicillin-binding protein required for cell division

Proteomic identification of M. tuberculosis protein kinase substrates: PknB recruits GarA, a FHA domain-containing protein, through activation loop-mediated interactions

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George M. Church

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