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Article

H2O2-induced intermolecular disulfide bond formation between receptor protein-tyrosine phosphatases.

The Journal of biological chemistry - 22 Oct 2004

van der Wijk Thea, Overvoorde John, den Hertog Jeroen

Abstract excerpt

Receptor protein-tyrosine phosphatase alpha (RPTPalpha) belongs to the subfamily of receptor-like protein-tyrosine phosphatases that are characterized by two catalytic domains of which only the membrane-proximal one (D1) exhibits appreciable catalytic activity. The C-terminal catalytic domain (D2) regulates RPTPalpha catalytic activity by controlling rotational coupling within RPTPalpha dimers. RPTPalpha-D2...

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PMID: 15294898
DOI: 10.1074/jbc.M407483200

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

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