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Negative Regulation of a Protein Tyrosine Phosphatase by Tyrosine Phosphorylation

Journal of the American Chemical Society, 2006
The low molecular weight protein tyrosine phosphatase (LMW-PTP) is a ubiquitously expressed enzyme with several proposed roles in cell signaling. Previously, two tyrosine phosphorylation modifications of LMW-PTP at sites Tyr-131 and Tyr-132 in response to growth factor stimulation have been mapped and suggested to stimulate LMW-PTP phosphatase activity.
Dirk, Schwarzer +3 more
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Protein Tyrosine Phosphatases

2000
The importance of tyrosine phosphorylation in diverse cellular processes such as cell growth, gene expression, metabolism, differentiation, cytoskeletal dynamics, and cell motility was discovered primarily through studies of the protein tyrosine kinases (PTKs).
Cynthia V. Stauffacher, Harry Charbonneau +1 more
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Protein-tyrosine phosphatases

1998
Abstract The first descriptions of PTPases in cell and tissue extracts provided evidence that they were distinct from other protein phosphatases because of their substrate specificity, neutral pH optimum, resistance to EDT A, and unique inhibition by low concentrations of zinc or vanadate [33].
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Protein tyrosine phosphatases

Seminars in Cell & Developmental Biology, 2015
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Introduction: Protein tyrosine phosphatases

Seminars in Cell Biology, 1993
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Dominant Role of the Protein-Tyrosine Phosphatase CD148 in Regulating Platelet Activation Relative to Protein-Tyrosine Phosphatase-1B

Arteriosclerosis, Thrombosis, and Vascular Biology, 2012
Michel L Tremblay, Yotis Senis, Jun Mori +2 more
exaly

Protein tyrosine phosphatase inhibitors