title: Receptor-like protein tyrosine phosphatases: alike and yet so different.
abstract: Reversible phosphorylation on tyrosine residues is an extremely rapid and powerful posttranslational modification that is used in signalling pathways for the regulation of cell growth and differentiation. Over the past several years an impressive number of receptor-like protein tyrosine phosphatase (RPTPase) family members have been identified by molecular cloning, and undoubtedly many more will follow. This review provides an overview of the molecular data that are available for the currently identified RPTPases and discusses their possible biological implications.
authors.affiliation: Department of Cell Biology & Histology, Institute of Cellular Signalling, University of Nijmegen, The Netherlands.
authors.forename: R
authors.initials: R
authors.lastname: Schaapveld
authors.forename: B
authors.initials: B
authors.lastname: Wieringa
authors.forename: W
authors.initials: W
authors.lastname: Hendriks
mesh_terms: D000818:Animals; D001369:Axons; D001665:Binding Sites; D015815:Cell Adhesion Molecules / Q000378:metabolism; D003922:Diabetes Mellitus, Type 1 / Q000201:enzymology; D004330:Drosophila / Q000201:enzymology; D006801:Humans; D017493:Leukocyte Common Antigens / Q000378:metabolism; D054562:Protein Tyrosine Phosphatase, Non-Receptor Type 1; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*
chemical_list: D015815:Cell Adhesion Molecules; D017493:Leukocyte Common Antigens; D054562:Protein Tyrosine Phosphatase, Non-Receptor Type 1; D017027:Protein Tyrosine Phosphatases