Journal ArticleDOI
Inhibition of membrane phosphotyrosyl-protein phosphatase activity by vanadate.
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TLDR
Results show that vanadate is a potent and selective inhibitor of phosphotyrosyl-protein phosphatase.About:
This article is published in Biochemical and Biophysical Research Communications.The article was published on 1982-08-16. It has received 675 citations till now. The article focuses on the topics: Vanadate & Dephosphorylation.read more
Citations
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Journal ArticleDOI
Protein tyrosine phosphatases: a diverse family of intracellular and transmembrane enzymes
TL;DR: A hypothesis is proposed explaining how phosphatases might act synergistically with the kinases to elicit a full physiological response, without regard to the state of phosphorylation of the target proteins.
Journal ArticleDOI
Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate
Gregory Huyer,Susana Liu,John F. Kelly,Jason Moffat,Paul Payette,Brian K. Kennedy,George Tsaprailis,Michael J. Gresser,Chidambaram Ramachandran +8 more
TL;DR: The results show that vanadate is a competitive inhibitor for the protein-tyrosine phosphatase PTP1B, with a Ki of 0.38 ± 0.02 μM, and reducing agents such as dithiothreitol that are used in PTP assays to keep the catalytic cysteine reduced and active were found to convert pervanadate rapidly toVanadate.
Journal ArticleDOI
Regulation of NMDA receptors by tyrosine kinases and phosphatases.
Yu Tian Wang,Michael W. Salter +1 more
TL;DR: Evidence is presented that in mammalian central neurons tyrosine phosphorylation regulates the function of the NMDA (N-methyl-D-aspartate) receptor, a subtype of excitatory amino-acid receptor, which may be important in neuronal development, plasticity and toxicity.
Book ChapterDOI
Use of vanadate as protein-phosphotyrosine phosphatase inhibitor.
TL;DR: This chapter discusses the use of vanadate as protein-phosphotyrosine phosphatase inhibitor, which is conveniently separable from the phosphoseryl and phosphothreonyl phosphatases activities inhibited by EDTA and fluoride.
Journal ArticleDOI
Characterization of the major protein-tyrosine-phosphatases of human placenta.
TL;DR: Peptide mapping following digestion with Achromobacter protease I or Staphylococcus aureus V8 protease supported the view that, whereas protein-tyrosine-phosphatase subtypes 1A and 1B are different, their soluble and particulate counterparts are closely related structurally and are distinct from serine/threonine phosphatases 1 and 2A.
References
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Journal ArticleDOI
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article
Cleavage of structural proteins during the assemble of the head of bacterio-phage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
Journal ArticleDOI
Identification of phosphotyrosine as a product of epidermal growth factor-activated protein kinase in A-431 cell membranes.
TL;DR: Epidermal growth factor-enhanced protein kinase activity in plasma membrane preparations of A-431 human epidermoid carcinoma cells was shown to involve the phosphorylation of tyrosine residues, which was detected in both endogenous membrane proteins and in histone when added as an exogenous protein substrate.
Journal ArticleDOI
Insulin stimulates the phosphorylation of the 95,000-dalton subunit of its own receptor
M Kasuga,F A Karlsson,C. R. Kahn +2 more
TL;DR: Phosphorylation was specifically stimulated by insulin in a dose-dependent fashion after 1 and 15 minutes of hormone treatment, whereas human growth hormone was without effect, suggesting this phosphorylation may be a very early event in insulin action.
Journal ArticleDOI
Vanadate is a potent (Na,K)-ATPase inhibitor found in ATP derived from muscle.
TL;DR: A potent (Na,K)-ATPase inhibitor purified from "Sigma Grade* ATP" has been identified as vanadium using electron probe microanalysis and confirmed by microwave-induced emission spectroscopy and electron paramagnetic resonanceSpectroscopy.