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

Identification, activity and disulfide connectivity of C-di-GMP regulating proteins in Mycobacterium tuberculosis.

PloS one - 30 Nov 2010

Gupta Kajal, Kumar Prasun, Chatterji Dipankar

Abstract excerpt

C-di-GMP, a bacterial second messenger plays a key role in survival and adaptation of bacteria under different environmental conditions. The level of c-di-GMP is regulated by two opposing activities, namely diguanylate cyclase (DGC) and phosphodiesterase (PDE-A) exhibited by GGDEF and EAL domain, respectively in the same protein. Previously, we reported a bifunctional GGDEF-EAL domain protein, MSDGC-1 from...

Read the complete abstract on PubMed

Topics

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

Share to Circular Dichroism
Share to Cyclic GMP
Share to Disulfides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microbial Viability

Share to Mycobacterium smegmatis

Share to Phosphoric Diester Hydrolases

Share to Phosphorus-Oxygen Lyases

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

Source

Open in PubMed Open full text

Identifiers

PMID: 21151497
DOI: 10.1371/journal.pone.0015072
PMCID: PMC2994820

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification, activity and disulfide connectivity of C-di-GMP regulating proteins in Mycobacterium tuberculosis.PMID 21151497Read ↗

Discovery of Novel c-di-GMP-Related Genes in <em>Leptospira interrogans</em>Semantic proximity Read ↗

c-di-GMP Turn-Over in Clostridium difficile Is Controlled by a Plethora of Diguanylate Cyclases and PhosphodiesterasesSemantic proximity Read ↗

Enzymatic synthesis of c-di-GMP using a thermophilic diguanylate cyclase.Semantic proximity Read ↗

Exploring the evolutionary divergence of cyclic di-nucleotide signaling in diverse mycobacterial speciesSemantic proximity Read ↗

Detailed analysis of c-di-GMP mediated regulation of csgD expression in Salmonella typhimurium.Semantic proximity Read ↗

ComFB, a new widespread family of c-di-NMP receptor proteinsSemantic proximity Read ↗

Identification of M. tuberculosis Rv3441c and M. smegmatis MSMEG_1556 and essentiality of M. smegmatis MSMEG_1556.Semantic proximity Read ↗

Specialized and shared functions of diguanylate cyclases and phosphodiesterases in <i>Streptomyces</i> developmentSemantic proximity Read ↗

Structure of a diguanylate cyclase from Thermotoga maritima: insights into activation, feedback inhibition and thermostability.Semantic proximity Read ↗

Comparative analysis of diguanylate cyclase and phosphodiesterase genes in Klebsiella pneumoniae.Semantic proximity Read ↗

Diguanylate cyclase activity of the Mycobacterium leprae T cell antigen ML1419c.Semantic proximity Read ↗

The importance of conserved amino acids in heme-based globin-coupled diguanylate cyclases.Semantic proximity Read ↗

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