| Literature DB >> 1733852 |
A Y Sakaguchi1, V L Sylvia, L Martinez, E A Smith, E S Han, P A Lalley, T B Shows, G G Choudhury.
Abstract
Phosphorylation of proteins on tyrosine is crucially involved in signal transduction and mitogenesis and is regulated by both kinases and phosphatases. Recently, a number of soluble and transmembrane receptor-linked protein tyrosine phosphatases (PTPase) have been characterized. Among these is a 48.4-kDa PTPase encoded by a cDNA isolated from a T-lymphocyte library by low-stringency screening with probes derived from placental PTPase 1B. A human T-cell PTPase (PTPT) cDNA and somatic cell hybrids were used to assign a PTPT gene to conserved syntentic groups on human chromosome 18 and on mouse chromosome 18. Two unlinked sequences, one on human chromosome 1, were also detected.Entities:
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Year: 1992 PMID: 1733852 DOI: 10.1016/0888-7543(92)90418-r
Source DB: PubMed Journal: Genomics ISSN: 0888-7543 Impact factor: 5.736