Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The Mycobacterium tuberculosis Ser/Thr kinase substrate Rv2175c is a DNA-binding protein regulated by phosphorylation.

The Journal of biological chemistry - 17 Jul 2009

Cohen-Gonsaud Martin, Barthe Philippe, Canova Marc J, Stagier-Simon Charlotte, Kremer Laurent, Roumestand Christian, Molle Virginie

Abstract excerpt

Recent efforts have underlined the role of serine/threonine protein kinases in growth, pathogenesis, and cell wall metabolism in Mycobacterium tuberculosis. Although most kinases have been investigated for their physiological roles, little information is available regarding how serine/threonine protein kinase-dependent phosphorylation regulates the activity of kinase substrates. Herein, we focused on M....

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Chromatography, Liquid
Share to Electrophoretic Mobility Shift Assay

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Fluorescence Polarization

Share to Magnetic Resonance Spectroscopy

Share to Mycobacterium tuberculosis

Share to Protein Structure, Secondary

Share to Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 19457863
DOI: 10.1074/jbc.M109.019653
PMCID: PMC2740554

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Mycobacterium tuberculosis Ser/Thr kinase substrate Rv2175c is a DNA-binding protein regulated by phosphorylation.PMID 19457863Read ↗

Mycobacterium tuberculosis supports protein tyrosine phosphorylation.Semantic proximity Read ↗

Forkhead-associated (FHA) domain containing ABC transporter Rv1747 is positively regulated by Ser/Thr phosphorylation in Mycobacterium tuberculosis.Semantic proximity Read ↗

The Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III activity is inhibited by phosphorylation on a single threonine residue.Semantic proximity Read ↗

Serine threonine protein kinases of mycobacterial genus: phylogeny to functionSemantic proximity Read ↗

An atlas of bacterial serine-threonine kinases reveals functional diversity and key distinctions from eukaryotic kinasesSemantic proximity Read ↗

RD-1 encoded EspJ protein gets phosphorylated prior to affect the growth and intracellular survival of mycobacteria.Semantic proximity Read ↗

Two FHA domains on an ABC transporter, Rv1747, mediate its phosphorylation by PknF, a Ser/Thr protein kinase from Mycobacterium tuberculosis.Semantic proximity Read ↗

Bacterial Eukaryotic Type Serine-Threonine Protein Kinases: From Structural Biology to Targeted Anti-Infective Drug DesignSemantic proximity Read ↗

Phosphorylation of CFP10 modulates Mycobacterium tuberculosis virulenceSemantic proximity Read ↗

Phosphorylation of KasB Regulates Virulence and Acid-Fastness in Mycobacterium tuberculosisSemantic proximity Read ↗

Role of post‐translational modifications in the acquisition of drug resistance in <i>Mycobacterium tuberculosis</i>Semantic proximity Read ↗

The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: substrate identification and regulation of cell shape.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.