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

Enzyme activity of phosphatase of regenerating liver is controlled by the redox environment and its C-terminal residues.

Biochemistry - 26 May 2009

Skinner Andria L, Vartia Anthony A, Williams Todd D, Laurence Jennifer S

Abstract excerpt

Phosphatase of regenerating liver-1 (PRL-1) belongs to a unique subfamily of protein tyrosine phosphatases (PTPases) associated with oncogenic and metastatic phenotypes. While considerable evidence supports a role for PRL-1 in promoting proliferation, the biological regulators and effectors of PRL-1 activity remain unknown. PRL-1 activity is inhibited by disulfide bond formation at the active site in vitro,...

Read the complete abstract on PubMed

Topics

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

Share to Cell Cycle Proteins
Share to Magnetic Resonance Spectroscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Conformation

Share to Oxidation-Reduction

Share to Oxygen

Share to Phosphoric Monoester Hydrolases

Share to Protein Tyrosine Phosphatases

Share to Spectrometry, Mass, Electrospray Ionization

Source

Open in PubMed Open full text

Identifiers

PMID: 19341304
DOI: 10.1021/bi900241k
PMCID: PMC2759777

Genes

PRL

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 11 closest

Enzyme activity of phosphatase of regenerating liver is controlled by the redox environment and its C-terminal residues.PMID 19341304Read ↗

Phosphatase of regenerating liver: a novel target for cancer therapySemantic proximity Read ↗

Thioredoxin-related protein 32 (TRP32) specifically reduces oxidized phosphatase of regenerating liver (PRL).Semantic proximity Read ↗

Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phosphatase in response to platelet-derived growth factor receptor stimulation.Semantic proximity Read ↗

Downregulation of p53 by phosphatase of regenerating liver 3 is mediated by MDM2 and PIRH2.Semantic proximity Read ↗

The metastasis-promoting phosphatase PRL-3 shows activity toward phosphoinositides.Semantic proximity Read ↗

Pathological Oxidation of PTPN12 Underlies ABL1 Phosphorylation in HLRCCSemantic proximity Read ↗

PRL3 pseudophosphatase activity is necessary and sufficient to promote metastatic growth.Semantic proximity Read ↗

Identification of redox-active cell-surface proteins by mechanism-based kinetic trapping.Semantic proximity Read ↗

H2O2-induced intermolecular disulfide bond formation between receptor protein-tyrosine phosphatases.Semantic proximity Read ↗

(77)Se enrichment of proteins expands the biological NMR toolbox.Semantic proximity Read ↗

Active site serine promotes stabilization of the reactive glutathione thiolate in rat glutathione transferase T2-2. Evidence against proposed sulfatase activity of the corresponding human enzyme.Semantic proximity Read ↗

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