(Q27748898)

2

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S Dhe-Paganon

3

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M J Eck

4

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S E Shoelson

Insulin signaling in mice expressing reduced levels of Syp.

5

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language of work or name

English

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publication date

20 February 1998

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published in

Cell

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volume

92

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page(s)

441-50

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issue

4

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cites work

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Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme

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Crystal structure of human protein tyrosine phosphatase 1B

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Multiple requirements for SHPTP2 in epidermal growth factor-mediated cell cycle progression.

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Structural basis for inhibition of receptor protein-tyrosine phosphatase-alpha by dimerization

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Modular binding domains in signal transduction proteins

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Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2

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Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect

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SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases.

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A novel membrane glycoprotein, SHPS-1, that binds the SH2-domain-containing protein tyrosine phosphatase SHP-2 in response to mitogens and cell adhesion

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The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu

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Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: a critical test of the protein engineering method of analysis

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Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2

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Characterization of phosphotyrosine binding motifs in the cytoplasmic domain of platelet/endothelial cell adhesion molecule-1 (PECAM-1) that are required for the cellular association and activation of the protein-tyrosine phosphatase, SHP-2

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A family of proteins that inhibit signalling through tyrosine kinase receptors

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Modular peptide recognition domains in eukaryotic signaling

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Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase

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Tandem SH2 domains confer high specificity in tyrosine kinase signaling

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Protein modules and signalling networks

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Intramolecular regulation of protein tyrosine phosphatase SH-PTP1: a new function for Src homology 2 domains

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Differential functions of the two Src homology 2 domains in protein tyrosine phosphatase SH-PTP1

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corkscrew encodes a putative protein tyrosine phosphatase that functions to transduce the terminal signal from the receptor tyrosine kinase torso

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Potent stimulation of SH-PTP2 phosphatase activity by simultaneous occupancy of both SH2 domains

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Regulation of phosphoinositide-specific phospholipase C isozymes

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Identification of structural motifs from protein coordinate data: secondary structure and first-level supersecondary structure

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Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Ig alpha/Ig beta immunoreceptor tyrosine activation motif binding and autophosphorylation

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Abnormal mesoderm patterning in mouse embryos mutant for the SH2 tyrosine phosphatase Shp-2.

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Syk is activated by phosphotyrosine-containing peptides representing the tyrosine-based activation motifs of the high affinity receptor for IgE.

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Crystal structure of the Src family tyrosine kinase Hck

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Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate

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The SH2-containing protein-tyrosine phosphatase SH-PTP2 is required upstream of MAP kinase for early Xenopus development

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Protein tyrosine phosphatases and the control of cellular signaling responses

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Inhibition of the activity of protein tyrosine phosphate 1C by its SH2 domains.

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7 January 2021

Activation of a phosphotyrosine phosphatase by tyrosine phosphorylation.

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The 2.35 A crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions

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7 January 2021

Three-dimensional structure of the tyrosine kinase c-Src

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7 January 2021

Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector

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