Results 211 to 220 of about 41,275 (256)

Assays for Protein-Tyrosine Phosphatases

2002
Many 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
openaire   +2 more sources

Drosophila protein tyrosine phosphatases

Seminars in Cell Biology, 1993
Seven 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
openaire   +3 more sources

Protein tyrosine phosphatases

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, Julie J. Wirth, Clifford W. Welsch, Walter J. Esselman   +3 more
openaire   +1 more source

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
openaire   +1 more source

Drug Discovery and Protein Tyrosine Phosphatases

Current Medicinal Chemistry, 2009
Protein 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.
openaire   +5 more sources

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, Zhongsen, Zhang, Weiping, Zheng, Philip A, Cole   +3 more
openaire   +2 more sources

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
openaire   +2 more sources

The role and therapeutic implication of protein tyrosine phosphatases in Alzheimer’s disease

Biomedicine and Pharmacotherapy, 2022
Guang Liang
exaly  

Linoleic acid exerts antidiabetic effects by inhibiting protein tyrosine phosphatases associated with insulin resistance

Journal of Functional Foods, 2021
Dohee Ahn, Sang Jeon Chung
exaly