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

Redox-regulated rotational coupling of receptor protein-tyrosine phosphatase alpha dimers.

The Journal of biological chemistry - 18 Apr 2003

van der Wijk Thea, Blanchetot Christophe, Overvoorde John, den Hertog Jeroen

Abstract excerpt

Receptor protein-tyrosine phosphatase alpha (RPTP alpha) constitutively forms dimers in the membrane, and activity studies with forced dimer mutants of RPTP alpha revealed that rotational coupling of the dimer defines its activity. The hemagglutinin (HA) tag of wild type RPTP alpha and of constitutively dimeric, active RPTP alpha-F135C with a disulfide bond in the extracellular domain was not accessible for...

Read the complete abstract on PubMed

Topics

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

Share to Biotinylation
Share to Catalytic Domain
Share to Cysteine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dimerization

Share to Epitopes

Share to Hydrogen Peroxide

Share to Precipitin Tests

Share to Protein Tyrosine Phosphatases

Source

Identifiers

PMID: 12582170
DOI: 10.1074/jbc.M300632200

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 · 12 closest

Redox-regulated rotational coupling of receptor protein-tyrosine phosphatase alpha dimers.PMID 12582170Read ↗

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

Reactive oxygen species and epidermal growth factor are antagonistic cues controlling SHP-2 dimerization.Semantic proximity Read ↗

Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain.Semantic proximity Read ↗

Structure of D-AKAP2:PKA RI complex: insights into AKAP specificity and selectivity.Semantic proximity Read ↗

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

Arachidonic acid induces direct interaction of the p67(phox)-Rac complex with the phagocyte oxidase Nox2, leading to superoxide production.Semantic proximity Read ↗

High-level expression, purification and characterization of a constitutively active thromboxane A2 receptor polymorphic variant.Semantic proximity Read ↗

Catalytically active membrane-distal phosphatase domain of receptor protein-tyrosine phosphatase alpha is required for Src activation.Semantic proximity Read ↗

Identification of p130cas as an in vivo substrate of receptor protein-tyrosine phosphatase alpha.Semantic proximity Read ↗

Oligomerization of the alpha and beta isoforms of the thromboxane A2 receptor: relevance to receptor signaling and endocytosis.Semantic proximity Read ↗

Mechanism of allosteric regulation of transglutaminase 2 by GTP.Semantic proximity Read ↗

Activation of the alpha subunit of Gs in intact cells alters its abundance, rate of degradation, and membrane avidity.Semantic proximity Read ↗

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