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Protein tyrosine phosphatases in signaling
Current Opinion in Cell Biology, 1996During the past few years, molecular cloning has established the existence of a structurally diverse family of intracellular and transmembrane protein tyrosine phosphatases (PTPases). The importance of PTPases in signaling is best understood in three model systems: the mammalian transmembrane CD45 PTPase, the Drosophila Src homology (SH)2 domain ...
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Assays for Protein-Tyrosine Phosphatases
2002Many studies have implicated protein-tyrosine phosphatases (PTPases) as important regulators of cellular functions and as potential drug targets. This has led to an increased interest in the development of precise assays for detailed mechanistic studies of PTPases, rapid assays for high-throughput PTPase inhibitor screening, and more biologically ...
Daniel F, McCain, Zhong-Yin, Zhang
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Drosophila protein tyrosine phosphatases
Seminars in Cell Biology, 1993Seven protein tyrosine phosphatase (PTPase) genes have been identified in the fruit-fly Drosophila melanogaster. Four of these genes encode receptor-linked PTPases (R-PTPs) that are expressed on central nervous system axons in the embryo. Each axonal R-PTP has an extracellular domain that is homologous to vertebrate adhesion molecules and to identified
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Drug Discovery and Protein Tyrosine Phosphatases
Current Medicinal Chemistry, 2009Protein tyrosine phosphatases (PTPs) play a critical role in physiological signaling pathways by controlling the level of tyrosine phosphorylation. The past decade has seen a vast increase in both academic and industrial interest in PTPs and their relevance as potential therapeutic targets, with several PTP inhibitors recently entering clinical trials.
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1996
Protein tyrosine phosphorylation and dephosphorylation are believed to be key regulatory mechanisms in the control of signal transduction, cell proliferation, differentiation, and neoplastic transformation [1–4]. The net cellular level of tyrosine phosphorylation is maintained dynamically by the opposing actions of protein tyrosine kinases (PTKs) and ...
Yi-Fan Zhai +3 more
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Protein tyrosine phosphorylation and dephosphorylation are believed to be key regulatory mechanisms in the control of signal transduction, cell proliferation, differentiation, and neoplastic transformation [1–4]. The net cellular level of tyrosine phosphorylation is maintained dynamically by the opposing actions of protein tyrosine kinases (PTKs) and ...
Yi-Fan Zhai +3 more
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Negative Regulation of a Protein Tyrosine Phosphatase by Tyrosine Phosphorylation
Journal of the American Chemical Society, 2006The 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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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 +1 more
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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 +1 more
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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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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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