Literature DB >> 14731595

Protein tyrosine phosphatases: from structure to function.

S M Brady-Kalnay1, N K Tonks.   

Abstract

In the past few years, a diverse family of receptor-like and nontransmembrane protein tyrosine phosphatases (PTPases) have been identified and characterized at the level of primary structure. Progress is now being made towards defining physiological processes in which the activity of PTPases is important. One thing seems clear: the PTPases cannot be regarded simply as antagonists of the protein tyrosine kinases (PTKs)--rather, they have the potential to act both positively and negatively in mediating cellular signalling responses.

Year:  1994        PMID: 14731595     DOI: 10.1016/0962-8924(94)90172-4

Source DB:  PubMed          Journal:  Trends Cell Biol        ISSN: 0962-8924            Impact factor:   20.808


  3 in total

1.  Increase in receptor-like protein tyrosine phosphatase activity and expression level on density-dependent growth arrest of endothelial cells.

Authors:  F Gaits; R Y Li; A Ragab; J M Ragab-Thomas; H Chap
Journal:  Biochem J       Date:  1995-10-01       Impact factor: 3.857

2.  G protein beta gamma subunits stimulate phosphorylation of Shc adapter protein.

Authors:  K Touhara; B E Hawes; T van Biesen; R J Lefkowitz
Journal:  Proc Natl Acad Sci U S A       Date:  1995-09-26       Impact factor: 11.205

3.  PTPmu regulates N-cadherin-dependent neurite outgrowth.

Authors:  S M Burden-Gulley; S M Brady-Kalnay
Journal:  J Cell Biol       Date:  1999-03-22       Impact factor: 10.539

  3 in total

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