Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase - Test2 - elhamkhani - TriplyDB

Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase

Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase

http://www.wikidata.org/entity/Q27652901

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Allosteric Activation Mechanism of the Mycobacterium tuberculosis Receptor Ser/Thr Protein Kinase, PknB X-ray structural studies of the entire extracellular region of the serine/threonine kinase PrkC from Staphylococcus aureus A Phosphorylated Pseudokinase Complex Controls Cell Wall Synthesis in Mycobacteria Structural Analysis of Staphylococcus aureus Serine/Threonine Kinase PknB Evidence that phosphorylation of threonine in the GT motif triggers activation of PknA, a eukaryotic-type serine/threonine kinase from Mycobacterium tuberculosis Structural and Genetic Analyses of the Mycobacterium tuberculosis Protein Kinase B Sensor Domain Identify a Potential Ligand-binding Site Understanding the role of PknJ in Mycobacterium tuberculosis: biochemical characterization and identification of novel substrate pyruvate kinase A Structure of CrgA, a cell division structural and regulatory protein from Mycobacterium tuberculosis, in lipid bilayers.Validated LC--MS/MS method for determination of YH-8, a novel PKnB inhibitor, in rat plasma and its application to pharmacokinetic study Protein kinase B (PknB) of Mycobacterium tuberculosis is essential for growth of the pathogen in vitro as well as for survival within the host.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 Serine/threonine protein phosphatase-mediated control of the peptidoglycan cross-linking L,D-transpeptidase pathway in Enterococcus faecium Mycobacterium tuberculosis Serine/Threonine Protein Kinases.Structural assembly of the signaling competent ERK2-RSK1 heterodimeric protein kinase complex.Protein synthesis during cellular quiescence is inhibited by phosphorylation of a translational elongation factor.The external PASTA domain of the essential serine/threonine protein kinase PknB regulates mycobacterial growth Key residues in Mycobacterium tuberculosis protein kinase G play a role in regulating kinase activity and survival in the host.Signaling mechanisms of the Mycobacterium tuberculosis receptor Ser/Thr protein kinases.Eukaryote-like serine/threonine kinases and phosphatases in bacteria.Bacterial cell division regulation by Ser/Thr kinases: a structural perspective Role of eukaryotic-like serine/threonine kinases in bacterial cell division and morphogenesis.The crystal structure of PknI from Mycobacterium tuberculosis shows an inactive, pseudokinase-like conformation.Do Shoot the Messenger: PASTA Kinases as Virulence Determinants and Antibiotic Targets.Growth- and stress-induced PASTA kinase phosphorylation in Enterococcus faecalis.A measured approach: determining the PLCγ1 docking site on Itk using a biochemical ruler.PknB remains an essential and a conserved target for drug development in susceptible and MDR strains of M. Tuberculosis.Forkhead-associated proteins genetically linked to the serine/threonine kinase PknB regulate carbon flux towards antibiotic biosynthesis in Streptomyces coelicolor.New Test System for Serine/Threonine Protein Kinase Inhibitors Screening: E. coli APHVIII/Pk25 design Lauric acid and myristic acid from Allium sativum inhibit the growth of Mycobacterium tuberculosis H37Ra: in silico analysis reveals possible binding to protein kinase B.Autophosphorylation Mechanism of the Ser/Thr Kinase Stk1 From Staphylococcus aureus.Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments

P2860

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P2860

Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase

http://www.wikidata.org/entity/Q27652901

description

2008 nî lūn-bûn

@nan

2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase

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Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase

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Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase

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label

Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase

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Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase

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Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase

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prefLabel

Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase

@ast

Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase

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Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase

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The EMBO Journal

P1476

Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase

@en

P2093

Anthony T Iavarone

http://www.w3.org/2001/XMLSchema#string

Carl Mieczkowski

http://www.w3.org/2001/XMLSchema#string

Tom Alber

http://www.w3.org/2001/XMLSchema#string

P2860

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

Trans-activation of the DNA-damage signalling protein kinase Chk2 by T-loop exchange

A dimeric kinase assembly underlying autophosphorylation in the p21 activated kinases

Activation segment dimerization: a mechanism for kinase autophosphorylation of non-consensus sites

PROCHECK: a program to check the stereochemical quality of protein structures

Crystal structure of a transition state mimic of the catalytic subunit of cAMP-dependent protein kinase

Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases

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

From The Cover: Automated protein crystal structure determination using ELVES

Structural basis for the specific inhibition of protein kinase G, a virulence factor of Mycobacterium tuberculosis.

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3186-97

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scholarly article

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10.1038/EMBOJ.2008.236

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23

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27

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19008858

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Mycobacterium tuberculosis

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2599879

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