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

Genome-wide survey of prokaryotic O-protein phosphatases.

Journal of molecular biology - 23 Sept 2005

Bhaduri Anirban, Sowdhamini R

Abstract excerpt

Complex and diverse signal transduction circuits are responsible for the efficient functioning of cellular network. Protein kinases and O-protein phosphatases are primarily responsible for propagating such stimuli within a eukaryotic cell. However, there is limited understanding of O-protein phosphatases in the prokaryotic genomes. The availability of complete genome sequence information for several prokaryotes...

Read the complete abstract on PubMed

Topics

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

Share to Eukaryotic Cells
Share to Genome
Share to Phosphoprotein Phosphatases

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

Share to Archaea

Share to Bacteria

Share to Prokaryotic Cells

Share to Protein Conformation

Share to Sequence Homology, Amino Acid

Source

Identifiers

PMID: 16095610
DOI: 10.1016/j.jmb.2005.07.004

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

Genome-wide survey of prokaryotic O-protein phosphatases.PMID 16095610Read ↗

A brief introduction to the protein phosphatase families.Semantic proximity Read ↗

The histidine phosphatase superfamily: structure and functionSemantic proximity Read ↗

A comprehensive analysis of protein phosphatases in rice and ArabidopsisSemantic proximity Read ↗

The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domainsSemantic proximity Read ↗

A polyphosphate kinase (PPK2) widely conserved in bacteriaSemantic proximity Read ↗

Tracing the origin and evolution of pseudokinases across the tree of lifeSemantic proximity Read ↗

In vitro characterization and identification of potential substrates of a low molecular weight protein tyrosine phosphatase in Streptococcus pneumoniae.Semantic proximity Read ↗

Conserved residues in membrane-bound acid pyrophosphatase from Sulfolobus tokodaii, a thermoacidophilic archaeon.Semantic proximity Read ↗

Structural analysis of the PP2C phosphatase tPphA from Thermosynechococcus elongatus: a flexible flap subdomain controls access to the catalytic site.Semantic proximity Read ↗

Identification and Biochemical Characterization of a Eukaryotic-type Serine/Threonine Kinase and its Cognate Phosphatase in Streptococcus pyogenes: Their Biological Functions and Substrate IdentificationSemantic proximity Read ↗

An Asymmetrically Balanced Organization of Kinases versus Phosphatases across Eukaryotes Determines Their Distinct Impacts.Semantic proximity Read ↗

Polyphosphate Kinase 2 (PPK2) Enzymes: Structure, Function, and Roles in Bacterial Physiology and VirulenceSemantic proximity Read ↗

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