Forkhead-associated domain-containing protein Rv0019c and polyketide-associated protein PapA5, from substrates of serine/threonine protein kinase PknB to interacting proteins of Mycobacterium tuberculosis - Wikidata - wikimedia - TriplyDB

Forkhead-associated domain-containing protein Rv0019c and polyketide-associated protein PapA5, from substrates of serine/threonine protein kinase PknB to interacting proteins of Mycobacterium tuberculosis

Forkhead-associated domain-containing protein Rv0019c and polyketide-associated protein PapA5, from substrates of serine/threonine protein kinase PknB to interacting proteins of Mycobacterium tuberculosis

http://www.wikidata.org/entity/Q28487000

about

Identification of Ser/Thr kinase and forkhead associated domains in Mycobacterium ulcerans: characterization of novel association between protein kinase Q and MupFHA Understanding the role of PknJ in Mycobacterium tuberculosis: biochemical characterization and identification of novel substrate pyruvate kinase A Phosphorylation of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein reductase MabA regulates mycolic acid biosynthesis Novel role of phosphorylation-dependent interaction between FtsZ and FipA in mycobacterial cell division Fha interaction with phosphothreonine of TssL activates type VI secretion in Agrobacterium tumefaciens Phosphorylation of Mycobacterium tuberculosis Ser/Thr phosphatase by PknA and PknB HupB, a nucleoid-associated protein of Mycobacterium tuberculosis, is modified by serine/threonine protein kinases in vivo.Mycobacterium tuberculosis Serine/Threonine Protein Kinases.Mycobacterium tuberculosis cyclophilin A uses novel signal sequence for secretion and mimics eukaryotic cyclophilins for interaction with host protein repertoire 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.Unveiling the novel dual specificity protein kinases in Bacillus anthracis: identification of the first prokaryotic dual specificity tyrosine phosphorylation-regulated kinase (DYRK)-like kinase.Diacyltransferase Activity and Chain Length Specificity of Mycobacterium tuberculosis PapA5 in the Synthesis of Alkyl β-Diol Lipids Acyltransferases in bacteria.A chemical proteomics approach to profiling the ATP-binding proteome of Mycobacterium tuberculosis.Disruption of the serine/threonine protein kinase H affects phthiocerol dimycocerosates synthesis in Mycobacterium tuberculosis.A pseudokinase debut at the mycobacterial cell wall.Cytoskeletal proteins of actinobacteria.Virulence factors of the Mycobacterium tuberculosis complex Elimination of intracellularly residing Mycobacterium tuberculosis through targeting of host and bacterial signaling mechanisms.Improved understanding of pathogenesis from protein interactions in Mycobacterium tuberculosis.Role of eukaryotic-like serine/threonine kinases in bacterial cell division and morphogenesis.Mycobacterium tuberculosis universal stress protein Rv2623 interacts with the putative ATP binding cassette (ABC) transporter Rv1747 to regulate mycobacterial growth.Leishmania donovani-specific Ub-related modifier-1: an early endosome-associated ubiquitin-like conjugation in Leishmania donovani.Regulation of homocysteine metabolism by Mycobacterium tuberculosis S-adenosylhomocysteine hydrolase Forkhead-associated proteins genetically linked to the serine/threonine kinase PknB regulate carbon flux towards antibiotic biosynthesis in Streptomyces coelicolor.Ser/Thr protein kinase PrkC-mediated regulation of GroEL is critical for biofilm formation in Bacillus anthracis.Zinc regulates the activity of kinase-phosphatase pair (BasPrkC/BasPrpC) in Bacillus anthracis.Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments

P2860

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P2860

Forkhead-associated domain-containing protein Rv0019c and polyketide-associated protein PapA5, from substrates of serine/threonine protein kinase PknB to interacting proteins of Mycobacterium tuberculosis

http://www.wikidata.org/entity/Q28487000

description

2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

article publié dans la revue scientifique Journal of Biological Chemistry

@fr

artículu científicu espublizáu en 2009

@ast

im Dezember 2009 veröffentlichter wissenschaftlicher Artikel

@de

scientific journal article

@en

vedecký článok (publikovaný 2009/12/11)

@sk

vědecký článek publikovaný v roce 2009

@cs

wetenschappelijk artikel (gepubliceerd op 2009/12/11)

@nl

наукова стаття, опублікована в грудні 2009

@uk

name

Forkhead-associated domain-con ...... of Mycobacterium tuberculosis

@ast

Forkhead-associated domain-con ...... of Mycobacterium tuberculosis

@en

Forkhead-associated domain-con ...... of Mycobacterium tuberculosis

@nl

type

label

Forkhead-associated domain-con ...... of Mycobacterium tuberculosis

@ast

Forkhead-associated domain-con ...... of Mycobacterium tuberculosis

@en

Forkhead-associated domain-con ...... of Mycobacterium tuberculosis

@nl

prefLabel

Forkhead-associated domain-con ...... of Mycobacterium tuberculosis

@ast

Forkhead-associated domain-con ...... of Mycobacterium tuberculosis

@en

Forkhead-associated domain-con ...... of Mycobacterium tuberculosis

@nl

P1433

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P1476

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P2860

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P698

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P932

Q28487000-58C824EA-2EFC-4075-8160-39ECAE860045

P356

JBC.M109.058834

P1433

Journal of Biological Chemistry

P1476

Forkhead-associated domain-con ...... of Mycobacterium tuberculosis

@en

P2093

Andaleeb Sajid

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

Gunjan Arora

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

Meetu Gupta

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

Vibha Tandon

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

Yogendra Singh

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

P2860

Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence

Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation

Structure and function of a new phosphopeptide-binding domain containing the FHA2 of Rad53

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

Structural and functional versatility of the FHA domain in DNA-damage signaling by the tumor suppressor kinase Chk2

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

Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functions

An intramolecular switch regulates phosphoindependent FHA domain interactions in Mycobacterium tuberculosis

Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates

SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins

P304

34723–34734

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

P31

scholarly article

P356

10.1074/JBC.M109.058834

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

P407

P433

50

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

P478

284

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

P577

2009-12-11T00:00:00Z

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

P698

19826007

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P921

Mycobacterium tuberculosis

P932

2787335

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