Crossref
journal-article
Elsevier BV
Cell (78)
References
59
Referenced
830
10.1242/dev.122.4.1137
/ Development / The SH2-containing tyrosine phosphatase corkscrew is required during signaling by sevenless, Ras1 and Raf by Allard (1996)10.1074/jbc.271.35.21353
/ J. Biol. Chem. / Insulin signaling in mice expressing reduced levels of Syp by Arrandale (1996)10.1002/j.1460-2075.1992.tb05426.x
/ EMBO J. / Phosphatidylinositol 3′-kinase is activated by association with IRS-1 during insulin stimulation by Backer (1992)10.1006/jmbi.1996.0338
/ J. Mol. Biol. / Thermodynamic and structural compensation in “size-switch” core repacking variants of bacteriophage T4 lysozyme by Baldwin (1996)10.1126/science.8128219
/ Science / Crystal structure of human protein tyrosine phosphatase 1B by Barford (1994)10.1128/MCB.16.3.1189
/ Mol. Cell Biol. / Multiple requirements for SHPTP2 in epidermal growth factor-mediated cell cycle progression by Bennett (1996)10.1038/382555a0
/ Nature / Structural basis for inhibition of receptor protein-tyrosine phosphatase-α by dimerization by Bilwes (1996){'year': '1992', 'series-title': 'X-PLOR Version 3.1', 'author': 'Brunger', 'key': '10.1016/S0092-8674(00)80938-1_BIB8'}
/ X-PLOR Version 3.1 by Brunger (1992)10.1016/S0021-9258(18)98375-4
/ J. Biol. Chem. / Phosphoinositide 3-kinase is activated by phosphopeptides that bind to the SH2 domains of the 85 kDa subunit by Carpenter (1993)10.1107/S0021889891007240
/ J. Appl. Cryst. / Ribbons 2.0 by Carson (1991)10.1016/0092-8674(95)90406-9
/ Cell / Modular binding domains in signal transduction proteins by Cohen (1995){'key': '10.1016/S0092-8674(00)80938-1_BIB12', 'first-page': '760', 'article-title': 'The CCP4 suite', 'volume': 'D50', 'author': 'Collaborative Computational Project 4', 'year': '1994', 'journal-title': 'Acta Cryst.'}
/ Acta Cryst. / The CCP4 suite by Collaborative Computational Project 4 (1994)- Cowtan, K. (1994). “DM”: an automated procedure for phase improvement by density modification. Joint CCP4 and ESF-EACBM Newsletter on Protein Cryst. 31, 34–38.
10.1016/S0021-9258(17)37504-X
/ J. Biol. Chem. / Characterization of the protein tyrosine phosphatase SH-PTP2. Study of phosphopeptide substrates and possible regulatory role of the SH2 domains by Dechert (1994)10.1038/379277a0
/ Nature / Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2 by Eck (1996)10.1126/science.1553543
/ Science / Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect by Eriksson (1992)10.1126/science.8096088
/ Science / SH2 containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases by Feng (1993)10.1128/MCB.16.12.6887
/ Mol. Cell. Biol. / A novel membrane glycoprotein, SHPS-1, that binds the SH2-domain-containing protein tyrosine phosphatase SHP-2 in response to mitogens and cell adhesion by Fujioka (1996)10.1074/jbc.272.44.27505
/ J. Biol. Chem. / The crystal structure of domain 1 of receptor protein-tyrosine phosphatase μ by Hoffmann (1997)10.1021/bi00093a002
/ Biochemistry / Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2 by Jackson (1993)10.1021/bi00093a001
/ Biochemistry / Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2 by Jackson (1993)10.1074/jbc.272.40.24868
/ J. Biol. Chem. / 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 by Jackson (1997)10.1126/science.7540771
/ Science / Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B by Jia (1995)- Jones, T.A., Bergdoll, M., and Kjeldgaard, M. (1989). Crystallographic Computing and Modeling Methods in Molecular Design. C. Bugg and S. Ealick, eds. (New York: Springer).
10.1107/S0021889888007903
/ J. Appl. Cryst. / Evaluation of single crystal diffraction data from a position sensitive detector by Kabsch (1988)10.1038/386181a0
/ Nature / A family of proteins that inhibit signaling through tyrosine kinase receptors by Kharitonenkov (1997)10.1107/S0021889891004399
/ Appl. Cryst. / MOLSCRIPT by Kraulis (1991)10.1016/S0021-9258(19)50220-4
/ J. Biol. Chem. / The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp by Kuhne (1993)10.1146/annurev.biophys.26.1.259
/ Annu. Rev. Biophys. Biomol. Struct. / Modular peptide recognition domains in eukaryotic signaling by Kuriyan (1997){'key': '10.1016/S0092-8674(00)80938-1_BIB30', 'first-page': '129', 'volume': 'D49', 'author': 'Lamzin', 'year': '1993', 'journal-title': 'Acta Cryst.'}
/ Acta Cryst. by Lamzin (1993)10.1016/S0021-9258(20)80562-6
/ J. Biol. Chem. / Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor β by Lechleider (1993)10.1016/S0969-2126(00)00044-7
/ Structure / Crystal structures of peptide complexes of the N-terminal SH2 domain of the Syp tyrosine phosphatase by Lee (1994)- Navaza, J. (1992). Molecular Replacement: Proceedings of the CCP4 Study Weekend. E.J. Dodson, S. Gover, and W. Wolf, eds. (Daresbury, UK: SERC), pp. 87–90.
10.1016/S0955-0674(97)80063-4
/ Curr. Opin. Cell Biol. / Protein tyrosine phosphatases in signal transduction by Neel (1997)10.1002/prot.340110407
/ Proteins Struct. Funct. Genet. / Protein folding and association by Nicholls (1991)10.1128/MCB.18.1.161
/ Mol. Cell. Biol. / Structural determinants of SHP-2 function and specificity in xenopus mesoderm induction by O'Reilly (1998)10.1074/jbc.273.2.729
/ J. Biol. Chem. / Tandem SH2 domains confer high specificity in tyrosine kinase signaling by Ottinger (1998)10.1038/373573a0
/ Nature / Protein modules and signaling networks by Pawson (1995)10.1021/bi00255a030
/ Biochemistry / Intramolecular regulation of protein tyrosine phosphatase SH-PTP1 by Pei (1994)10.1073/pnas.93.3.1141
/ Proc. Natl. Acad. Sci. USA / Differential functions of the two Src homology 2 domains in protein tyrosine phosphatase SH-PTP1 by Pei (1996)10.1016/0092-8674(92)90098-W
/ Cell / corkscrew encodes a putative protein tyrosine phosphatase that functions to transduce the terminal signal from the receptor tyrosine kinase torso by Perkins (1992)10.1074/jbc.270.7.2897
/ J. Biol. Chem. / Potent stimulation of SH-PTP2 phosphatase activity by IRS-1 binding to both of its SH2 domains by Pluskey (1995)10.1074/jbc.272.24.15045
/ J. Biol. Chem. / Regulation of phosphoinositide-specific phospholipase C isozymes by Rhee (1997)10.1002/prot.340030202
/ Proteins / Identification of structural motifs from protein coordinate data by Richards (1988)10.1074/jbc.270.19.11590
/ J. Biol. Chem / Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Ig α/Ig β immunoreceptor tyrosine activation motif binding and autophosphorylation by Rowley (1995)10.1093/emboj/16.9.2352
/ EMBO J. / Abnormal mesoderm patterning in mouse embryos mutant for the SH2 tyrosine phosphatase SHP-2 by Saxton (1997)10.1074/jbc.270.18.10498
/ J. Biol. Chem. / Syk is activated by phosphotyrosine-containing peptides representing the tyrosine-based activation motifs of the high affinity receptor for IgE by Shiue (1995)10.1038/385602a0
/ Nature / Crystal structure of the Src family tyrosine kinase Hck by Sicheri (1997)10.1038/370571a0
/ Nature / Crystal structure of the Yersinia protein tyrosine phosphatase at 2.5 Å and the complex with tungstate by Stuckey (1994)10.1016/S0021-9258(18)41593-1
/ J. Biol. Chem. / Expression, purification and catalytic properties of the SH2 domain-containing protein tyrosine phosphatase, SH-PTP2 by Sugimoto (1993)10.1016/S0021-9258(17)36874-6
/ J. Biol. Chem. / Activation of the SH2-containing protein tyrosine phosphatase, SH-PTP2, by phosphotyrosine-containing peptides derived from IRS-1 by Sugimoto (1994)10.1016/0092-8674(95)90498-0
/ Cell / The SH2-containing protein-tyrosine phosphatase SH-PTP2 is required upstream of MAP kinase for early xenopus development by Tang (1995)10.1016/S1054-3589(08)60578-5
/ Adv. Pharmacol. / Protein tyrosine phosphatases and the control of cellular signaling responses by Tonks (1996)10.1021/bi00212a006
/ Biochemistry / Inhibition of the activity of protein tyrosine phosphatase 1C by its SH2 domains by Townley (1993)- Turk, D. (1996). MAIN 96: an interactive software for density modifications, model structure refinement and analysis. In Proceedings from the 1996 Meeting of the International Union of Crystallography and Macromolecular Modeling Computing School.
10.1126/science.7681217
/ Science / Activation of a phosphotyrosine phosphatase by tyrosine phosphorylation by Vogel (1993)10.1016/S0021-9258(17)31581-8
/ J. Biol. Chem. / Interleukin (IL)-3 and granulocyte/macrophage colony-stimulating factor, but not IL-4, induce tyrosine phosphorylation, activation, and association of SHPTP2 with Grb2 and phosphatidylinositol 3′-kinase by Welham (1994)10.1006/jmbi.1997.1426
/ J. Mol. Biol. / The 2.35 A crystal structure of the inactivated form of chicken src by Williams (1997)10.1038/385595a0
/ Nature / Three-dimensional structure of the tyrosine kinase c-Src by Xu (1997)
Dates
Type | When |
---|---|
Created | 21 years, 4 months ago (April 10, 2004, 1:39 a.m.) |
Deposited | 4 years, 2 months ago (June 15, 2021, 5:48 a.m.) |
Indexed | 8 hours, 56 minutes ago (Aug. 27, 2025, 12:04 p.m.) |
Issued | 27 years, 6 months ago (Feb. 1, 1998) |
Published | 27 years, 6 months ago (Feb. 1, 1998) |
Published Print | 27 years, 6 months ago (Feb. 1, 1998) |
@article{Hof_1998, title={Crystal Structure of the Tyrosine Phosphatase SHP-2}, volume={92}, ISSN={0092-8674}, url={http://dx.doi.org/10.1016/s0092-8674(00)80938-1}, DOI={10.1016/s0092-8674(00)80938-1}, number={4}, journal={Cell}, publisher={Elsevier BV}, author={Hof, Peter and Pluskey, Scott and Dhe-Paganon, Sirano and Eck, Michael J and Shoelson, Steven E}, year={1998}, month=feb, pages={441–450} }