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1002 Protein Phosphatases?

Annual Review of Cell Biology, 1992
phosphatases, tyrosine phosphorylation, signal transduction, dephosphorylatio n.
H, Charbonneau, N K, Tonks
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Protein tyrosine phosphatases

Frontiers in Bioscience, 2002
The molecular mechanisms of signal transduction have been at the focus of increasingly intense scientific research. As a result, our understanding of protein tyrosine kinase-mediated signaling has advanced at an unprecedented pace during the past decade.
T, Mustelin   +7 more
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PLANT PROTEIN PHOSPHATASES

Annual Review of Plant Physiology and Plant Molecular Biology, 1996
▪ Abstract  Posttranslational modification of proteins by phosphorylation is a universal mechanism for regulating diverse biological functions. Recognition that many cellular proteins are reversibly phosphorylated in response to external stimuli or intracellular signals has generated an ongoing interest in identifying and characterizing plant protein ...
Robert D., Smith, John C., Walker
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Protein phosphatases

Current Opinion in Structural Biology, 1995
Protein phosphatases are signal transducing enzymes that dephosphorylate cellular phosphoproteins. The recently determined crystal structures of protein tyrosine and serine/threonine phosphatases reveal that these proteins adopt distinct structures and catalyze dephosphorylation reactions by means of different enzymatic mechanisms.
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Protein Phosphatases

Science's STKE, 2005
This Teaching Resource provides lecture notes and slides for a class covering the structure and function of protein phosphatases and is part of the course "Cell Signaling Systems: A Course for Graduate Students." The lecture begins with a discussion of the importance of phosphatases in physiology, recognized by the award of a Nobel Prize in 1992, and ...
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Phosphotyrosyl-Protein Phosphatases

1983
Extensive genetic evidence indicates that the protein product of a single gene of RNA tumor viruses is responsible for the transformation of virus-infected cells to the malignant state (Hanafusa 1977; Duesberg and Bister 1981; Bishop and Varmus 1982; Linial and Blair 1982; Varmus 1982).
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Protein serine/threonine phosphatases

Current Opinion in Biotechnology, 1996
In the past year, the three-dimensional structures of two serine/threonine phosphatases, protein phosphatase-1 and protein phosphatase-2b (calcineurin), have been determined. The new information puts previous sequence comparisons and mutagenesis studies into a detailed structural perspective.
J E, Villafranca   +2 more
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Protozoan protein tyrosine phosphatases

International Journal for Parasitology, 2008
The aim of this review is to provide a synthesis of the published experimental data on protein tyrosine phosphatases from parasitic protozoa, in silico analysis based on the availability of completed genomes and to place available data for individual phosphatases from different unicellular parasites into the comparative and evolutionary context.
Alexandra V, Andreeva   +1 more
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Protein phosphatase 2Bw and protein phosphatase Z are Saccharomyces cerevisiae enzymes

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1991
cDNAs encoding three protein phosphatases, termed PP2Bw (Da Cruz e Silva, E.F. and Cohen, P.T.W. (1989) Biochim. Biophys. Acta 1009, 293-296), PPZ1 and PPZ2 that have been isolated from a Clontech 'rabbit brain' library are shown to be Saccharomyces cerevisiae clones.
Silva, E.F. Da Cruz e   +4 more
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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
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