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Volumn 43, Issue 2, 2000, Pages 146-155

Structure-based discovery of small molecule inhibitors targeted to protein tyrosine phosphatase 1B

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN TYROSINE PHOSPHATASE INHIBITOR;

EID: 0034719423     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm990329z     Document Type: Article
Times cited : (100)

References (64)
  • 1
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The Yin and Yang of protein phosphorylation and signaling
    • Hunter, T. Protein Kinases and Phosphatases: the Yin and Yang of Protein Phosphorylation and Signaling. Cell 1995, 80, 225-236.
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 2
    • 0030297552 scopus 로고    scopus 로고
    • From form to function: Signaling by protein tyrosine phosphatases
    • Tonks, N. K.; Neel, B. G. From Form to Function: Signaling by Protein Tyrosine Phosphatases. Cell 1996, 87, 365-368.
    • (1996) Cell , vol.87 , pp. 365-368
    • Tonks, N.K.1    Neel, B.G.2
  • 3
    • 0031893253 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatases: Biological function, structural characteristics, and mechanism of catalysis
    • Zhang, Z.-Y. Protein-Tyrosine Phosphatases: Biological Function, Structural Characteristics, and Mechanism of Catalysis. CRC Crit. Rev. Biochem. Mol. Biol. 1998, 33, 1-52.
    • (1998) Crc Crit. Rev. Biochem. Mol. Biol. , vol.33 , pp. 1-52
    • Zhang, Z.-Y.1
  • 5
    • 0029130199 scopus 로고
    • Osmotic loading of neutralizing antibodies demonstrates a role for protein-tyrosine phosphatase IB in negative regulation of the insulin action pathway
    • Ahmad, F.; Li, P.-M.; Meyerovitch, J.; Goldstein, B. J. Osmotic Loading of Neutralizing Antibodies Demonstrates a Role for Protein-Tyrosine Phosphatase IB in Negative Regulation of the Insulin Action Pathway. J. Biol. Chem. 1995, 270, 20503-20508.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20503-20508
    • Ahmad, F.1    Li, P.-M.2    Meyerovitch, J.3    Goldstein, B.J.4
  • 6
    • 0029810614 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase IB is a negative regulator of insulin- and insulin-like growth factor I-stimulated signaling
    • Kenner, K. A.; Anyanwu, E.; Olefsky, J. M.; Kusari, J. Protein-Tyrosine Phosphatase IB Is a Negative Regulator of Insulin- and Insulin-like Growth Factor I-Stimulated Signaling. J. Biol. Chem. 1996, 271, 19810-19816.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19810-19816
    • Kenner, K.A.1    Anyanwu, E.2    Olefsky, J.M.3    Kusari, J.4
  • 7
    • 15844365943 scopus 로고    scopus 로고
    • A peptide-based protein-tyrosine phosphatase inhibitor specifically enhances insulin receptor function in intact cells
    • Kole, H. K.; Garant, M. J.; Kole, S.; Bernier, M. A Peptide-Based Protein-Tyrosine Phosphatase Inhibitor Specifically Enhances Insulin Receptor Function in Intact Cells. J. Biol. Chem. 1996, 271, 14302-14307.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14302-14307
    • Kole, H.K.1    Garant, M.J.2    Kole, S.3    Bernier, M.4
  • 8
    • 0031036223 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase IB complexes with the insulin receptor in vivo and is tyrosine-phosphorylated in the presence of insulin
    • Bandyopadhyay, D.; Kusari, A.; Kenner, K. A.; Liu, F.; Chernoff, J.; Gustafson, T. A.; Kusari, J. Protein-Tyrosine Phosphatase IB Complexes with the Insulin Receptor in vivo and Is Tyrosine-Phosphorylated in the Presence of Insulin. J. Biol. Chem. 1997, 272, 1639-1645.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1639-1645
    • Bandyopadhyay, D.1    Kusari, A.2    Kenner, K.A.3    Liu, F.4    Chernoff, J.5    Gustafson, T.A.6    Kusari, J.7
  • 9
    • 0030961536 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatases PTP1B and Syp are modulators of insulin-stimulated translocation of GLUT4 in transfected rat adipose cells
    • Chen, H.; Wertheimer, S. J.; Lin, C. H.; Amrein, K. E.; Burn, P.; Quon, M. J. Protein-Tyrosine Phosphatases PTP1B and Syp Are Modulators of Insulin-Stimulated Translocation of GLUT4 in Transfected Rat Adipose Cells. J. Biol. Chem. 1997, 272, 8026-8031.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8026-8031
    • Chen, H.1    Wertheimer, S.J.2    Lin, C.H.3    Amrein, K.E.4    Burn, P.5    Quon, M.J.6
  • 10
    • 0028281921 scopus 로고
    • Skeletal muscle protein tyrosine phosphatase activity and tyrosine phosphatase IB protein content are associated with insulin action and resistance
    • Kusari, J.; Kenner, K. A.; Suh, K.-I.; Hill, D. E.; Henry, R. R. Skeletal Muscle Protein Tyrosine Phosphatase Activity and Tyrosine Phosphatase IB Protein Content Are Associated with Insulin Action and Resistance. J. Clin. Invest. 1994, 93, 1156-1162.
    • (1994) J. Clin. Invest. , vol.93 , pp. 1156-1162
    • Kusari, J.1    Kenner, K.A.2    Suh, K.-I.3    Hill, D.E.4    Henry, R.R.5
  • 11
    • 0030840724 scopus 로고    scopus 로고
    • Alterations in skeletal muscle protein-tyrosine phosphatase activity and expression in insulin-resistant human obesity and diabetes
    • Ahmad, F.; Azevedo, J. L.; Cortright, R.; Dohm, G. L.; Goldstein, B. J. Alterations in Skeletal Muscle Protein-Tyrosine Phosphatase Activity and Expression in Insulin-Resistant Human Obesity and Diabetes. J. Clin. Invest. 1997, 700, 449-458.
    • (1997) J. Clin. Invest. , vol.700 , pp. 449-458
    • Ahmad, F.1    Azevedo, J.L.2    Cortright, R.3    Dohm, G.L.4    Goldstein, B.J.5
  • 12
    • 0030821972 scopus 로고    scopus 로고
    • Improved sensitivity to insulin in obese subjects following weight loss is accompanied by reduced protein-tyrosine phosphatases in adipose tissue
    • Ahmad, F.; Considine, R. V.; Bauer, T. L.; Ohannesian, J. P.; Marco. C. C.; Goldstein, B. J. Improved Sensitivity to Insulin in Obese Subjects following Weight Loss Is Accompanied by Reduced Protein-Tyrosine Phosphatases in Adipose Tissue. Metabolism 1997, 46, 1140-1145.
    • (1997) Metabolism , vol.46 , pp. 1140-1145
    • Ahmad, F.1    Considine, R.V.2    Bauer, T.L.3    Ohannesian, J.P.4    Marco, C.C.5    Goldstein, B.J.6
  • 16
    • 0027522358 scopus 로고
    • Structure-based discovery of inhibitors of Thymidylate synthase
    • Shoichet, B. K.; Stroud, R. M.; Santi, D. V.; Kuntz, I. D.; Perry, K. M. Structure-Based Discovery of Inhibitors of Thymidylate Synthase. Science 1993, 259, 1445-1450.
    • (1993) Science , vol.259 , pp. 1445-1450
    • Shoichet, B.K.1    Stroud, R.M.2    Santi, D.V.3    Kuntz, I.D.4    Perry, K.M.5
  • 17
    • 0030964552 scopus 로고    scopus 로고
    • Specificity in structure-based drug design: Identification of a novel, selective inhibitor of pneumocystis carinii dihydrofolate reductase
    • Gschwend, D. A.; Sirawaraporn, W.; Santi, D. V.; Kuntz, I. D. Specificity in Structure-Based Drug Design: Identification of a Novel, Selective Inhibitor of Pneumocystis Carinii Dihydrofolate Reductase. Proteins: Struct., Funct., Genet. 1997, 29, 59-67.
    • (1997) Proteins: Struct., Funct., Genet. , vol.29 , pp. 59-67
    • Gschwend, D.A.1    Sirawaraporn, W.2    Santi, D.V.3    Kuntz, I.D.4
  • 20
    • 0030954877 scopus 로고    scopus 로고
    • Structure-based discovery of ligands targeted to the RNA double helix
    • Chen, Q.; Shafer, R. H.; Kuntz, I. D. Structure-Based Discovery of Ligands Targeted to the RNA Double Helix. Biochemistry 1997, 36, 11402-11407.
    • (1997) Biochemistry , vol.36 , pp. 11402-11407
    • Chen, Q.1    Shafer, R.H.2    Kuntz, I.D.3
  • 21
    • 12644256642 scopus 로고    scopus 로고
    • A computer screening approach to immunoglobulin superfamily structures and interactions: Discovery of small nonpeptidic CD4 inhibitors as novel immunotherapeutics
    • Li, S.; Gao, J.; Satoh, T.; Friedman, T. M.; Edling, A. E.; Koch, U.; Choksi, S.; Han, X.; Korngold, R.; Huang, Z. A Computer Screening Approach to Immunoglobulin Superfamily Structures and Interactions: Discovery of Small Nonpeptidic CD4 Inhibitors as Novel Immunotherapeutics. Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 73-78.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 73-78
    • Li, S.1    Gao, J.2    Satoh, T.3    Friedman, T.M.4    Edling, A.E.5    Koch, U.6    Choksi, S.7    Han, X.8    Korngold, R.9    Huang, Z.10
  • 22
    • 0032189553 scopus 로고    scopus 로고
    • CD4 dimerization and oligomerization: Implications for T-cell function and structure-based drug design
    • Li, S.; Satoh, T.; Korngold, R.; Huang, Z. CD4 Dimerization and Oligomerization: Implications for T-cell Function and Structure-Based Drug Design. Immunol. Today 1998, 19, 455-462.
    • (1998) Immunol. Today , vol.19 , pp. 455-462
    • Li, S.1    Satoh, T.2    Korngold, R.3    Huang, Z.4
  • 23
    • 0029066496 scopus 로고
    • Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase IB
    • Jia, Z.; Barford, D.; Flint, A. J.; Tonks, N. K. Structural Basis for Phosphotyrosine Peptide Recognition by Protein Tyrosine Phosphatase IB. Science 1995, 268, 1754-1758.
    • (1995) Science , vol.268 , pp. 1754-1758
    • Jia, Z.1    Barford, D.2    Flint, A.J.3    Tonks, N.K.4
  • 24
    • 0031457541 scopus 로고    scopus 로고
    • Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase IB: A paradigm for inhibitor design. Proc
    • Puius, Y. A.; Zhao, Y.; Sullivan, M.; Lawrence, D. S.; Almo, S. C.; Zhang, Z.-Y. Identification of a Second Aryl Phosphate-Binding Site in Protein-Tyrosine Phosphatase IB: A Paradigm for Inhibitor Design. Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 13420-13425.
    • (1997) Natl. Acad. Sci. U.S.A. , vol.94 , pp. 13420-13425
    • Puius, Y.A.1    Zhao, Y.2    Sullivan, M.3    Lawrence, D.S.4    Almo, S.C.5    Zhang, Z.-Y.6
  • 26
    • 0026730489 scopus 로고
    • Structure-based strategies for drug design and discovery
    • Kuntz, I. D. Structure-Based Strategies for Drug Design and Discovery. Science 1992, 257, 1078-1082.
    • (1992) Science , vol.257 , pp. 1078-1082
    • Kuntz, I.D.1
  • 27
    • 0028176050 scopus 로고
    • Dissecting the catalytic mechanism of protein-tyrosine phosphatases
    • Zhang, Z.-Y.; Wang, Y.; Dixon, J. E. Dissecting the Catalytic Mechanism of Protein-Tyrosine Phosphatases. Proc. Natl. Acad. Sci. U.S.A. 1994, 91, 1624-1627.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 1624-1627
    • Zhang, Z.-Y.1    Wang, Y.2    Dixon, J.E.3
  • 28
    • 0028231388 scopus 로고
    • Crystal structure of human protein tyrosine phosphatase 1B
    • Barford, D.; Flint, A. J.; Tonks, N. K. Crystal Structure of Human Protein Tyrosine Phosphatase 1B. Science 1994, 263, 1397-1404.
    • (1994) Science , vol.263 , pp. 1397-1404
    • Barford, D.1    Flint, A.J.2    Tonks, N.K.3
  • 29
    • 0028122711 scopus 로고
    • Crystal structure of yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate
    • Stuckey, J. A.; Schubert, H. L.; Fauman, E.; Zhang, Z.-Y.; Dixon, J. E.; Saper, M. A. Crystal Structure of Yersinia Protein Tyrosine Phosphatase at 2.5 A and the Complex with Tungstate. Nature 1994, 370, 571-575.
    • (1994) Nature , vol.370 , pp. 571-575
    • Stuckey, J.A.1    Schubert, H.L.2    Fauman, E.3    Zhang, Z.-Y.4    Dixon, J.E.5    Saper, M.A.6
  • 30
    • 0029759927 scopus 로고    scopus 로고
    • Structural basis for inhibition of receptor protein-tyrosine phosphatase-alpha by dimerization
    • Bilwes, A. M.; den Hertog, J.; Hunter, T.; Noel, J. P. Structural Basis for Inhibition of Receptor Protein-Tyrosine Phosphatase-Alpha by Dimerization. Nature 1996, 382, 555-559.
    • (1996) Nature , vol.382 , pp. 555-559
    • Bilwes, A.M.1    Den Hertog, J.2    Hunter, T.3    Noel, J.P.4
  • 31
    • 0030735366 scopus 로고    scopus 로고
    • The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu
    • Hoffmann, K. M. V.; Tonks, N. K.; Barford, D. The Crystal Structure of Domain 1 of Receptor Protein-Tyrosine Phosphatase mu. J. Biol. Chem. 1997, 275, 27505-27508.
    • (1997) J. Biol. Chem. , vol.275 , pp. 27505-27508
    • Hoffmann, K.M.V.1    Tonks, N.K.2    Barford, D.3
  • 32
    • 0032548830 scopus 로고    scopus 로고
    • Crystal structure of the tyrosine phosphatase SHP-2
    • Hof, P.; Pluskey, S.; Dhe-Paganon, S.; Eck, M. J.; Shoelson, S. E. Crystal Structure of the Tyrosine Phosphatase SHP-2. Cell 1998, 92, 441-450.
    • (1998) Cell , vol.92 , pp. 441-450
    • Hof, P.1    Pluskey, S.2    Dhe-Paganon, S.3    Eck, M.J.4    Shoelson, S.E.5
  • 34
    • 0029975476 scopus 로고    scopus 로고
    • Crystal structure of the dual specificity protein phosphatase VHR
    • Yuvaniyama, J.; Denu, J. M.; Dixon, J. E.; Saper, M. A. Crystal Structure of the Dual Specificity Protein Phosphatase VHR. Science 1996, 272, 1328-1331.
    • (1996) Science , vol.272 , pp. 1328-1331
    • Yuvaniyama, J.1    Denu, J.M.2    Dixon, J.E.3    Saper, M.A.4
  • 35
    • 0028070371 scopus 로고
    • A synthetic tris-sulfotyrosyl dodecapeptide analogue of the insulin receptor 1146-kinase domain inhibits Tyrosine de-phosphorylation of the insulin receptor in situ
    • Liotta, A. S.; Kole, H. K.; Fales, H. M.; Roth, J.; Bernier, M. A Synthetic Tris-Sulfotyrosyl Dodecapeptide Analogue of the Insulin Receptor 1146-Kinase Domain Inhibits Tyrosine De-phosphorylation of the Insulin Receptor in situ. J. Biol. Chem. 1994, 269, 22996-23001.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22996-23001
    • Liotta, A.S.1    Kole, H.K.2    Fales, H.M.3    Roth, J.4    Bernier, M.5
  • 36
    • 0032526549 scopus 로고    scopus 로고
    • Inhibition of protein tyrosine phosphatases PTP1B and CD45 by sulfotyrosyl peptides
    • Desmarais, S.; Jia, Z.; Ramachandran, C. Inhibition of Protein Tyrosine Phosphatases PTP1B and CD45 by Sulfotyrosyl Peptides. Arch. Biochem. Biophys. 1998, 354, 225-231.
    • (1998) Arch. Biochem. Biophys. , vol.354 , pp. 225-231
    • Desmarais, S.1    Jia, Z.2    Ramachandran, C.3
  • 37
    • 0032524855 scopus 로고    scopus 로고
    • Suramin is an active site-directed, reversible, and tight-binding inhibitor of Protein-Tyrosine phosphatases
    • Zhang, Y.-L.; Keng, Y.-F.; Zhao, Y.; Wu, L.; Zhang, Z.-Y. Suramin Is an Active Site-Directed, Reversible, and Tight-Binding Inhibitor of Protein-Tyrosine Phosphatases. J. Biol. Chem. 1998, 273, 12281-12287.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12281-12287
    • Zhang, Y.-L.1    Keng, Y.-F.2    Zhao, Y.3    Wu, L.4    Zhang, Z.-Y.5
  • 38
    • 0028882428 scopus 로고
    • Phosphonate inhibitors of Protein-Tyrosine and Serine/Threonine phosphatases
    • Kole, H. K.; Smyth, M. S.; Russ, P. L.; Burke, T. R., Jr. Phosphonate Inhibitors of Protein-Tyrosine and Serine/Threonine Phosphatases. Biochem. J. 1995, 311, 1025-1031.
    • (1995) Biochem. J. , vol.311 , pp. 1025-1031
    • Kole, H.K.1    Smyth, M.S.2    Russ, P.L.3    Burke T.R., Jr.4
  • 39
    • 0030467887 scopus 로고    scopus 로고
    • Small molecule interactions with Protein-Tyrosine Phosphatase PTP1b and their use in inhibitor design
    • Burke, T. R., Jr.; Ye, B.; Yan, X.; Wang, S.; Jia, Z.; Chen, L.; Zhang, Z.-Y.; Barford, D. Small Molecule Interactions with Protein-Tyrosine Phosphatase PTP1B and Their Use in Inhibitor Design. Biochemistry 1996, 35, 15989-15996.
    • (1996) Biochemistry , vol.35 , pp. 15989-15996
    • Burke, T.R.J.1    Ye, B.2    Yan, X.3    Wang, S.4    Jia, Z.5    Chen, L.6    Zhang, Z.-Y.7    Barford, D.8
  • 40
    • 0032500638 scopus 로고    scopus 로고
    • Molecular basis for substrate specificity of Protein-tyrosine Phosphatase 1B
    • Sarmiento, M.; Zhao, Z.; Gordon, S. J.; Zhang, Z-.Y. Molecular Basis for Substrate Specificity of Protein-tyrosine Phosphatase 1B. J. Biol. Chem. 1998, 273, 26368-26374.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26368-26374
    • Sarmiento, M.1    Zhao, Z.2    Gordon, S.J.3    Zhang, Z.-.Y.4
  • 41
    • 0027215589 scopus 로고
    • A continuous spectrophotometric and fluorimetric assay for protein tyrosine phosphatase using Phosphotyrosine-containing peptides
    • Zhang, Z.-Y.; Maclean, D.; Thieme-Sefler, A. M.; Roeske, R.; Dixon, J. E. A Continuous Spectrophotometric and Fluorimetric Assay for Protein Tyrosine Phosphatase Using Phosphotyrosine-Containing Peptides. Anal. Biochem. 1993, 211, 7-15.
    • (1993) Anal. Biochem. , vol.211 , pp. 7-15
    • Zhang, Z.-Y.1    Maclean, D.2    Thieme-Sefler, A.M.3    Roeske, R.4    Dixon, J.E.5
  • 44
    • 0028298024 scopus 로고
    • Protein Tyrosine Phosphatase substrate specificity: Size and phosphotyrosine positioning requirements in peptide substrates
    • Zhang, Z.-Y.; Maclean, D.; McNamara, D. J.; Dobrusin, E. M.; Sawyer, T. K.; Dixon, J. E. Protein Tyrosine Phosphatase Substrate Specificity: Size and Phosphotyrosine Positioning Requirements in Peptide Substrates. Biochemistry 1994, 33, 2285-2290.
    • (1994) Biochemistry , vol.33 , pp. 2285-2290
    • Zhang, Z.-Y.1    Maclean, D.2    McNamara, D.J.3    Dobrusin, E.M.4    Sawyer, T.K.5    Dixon, J.E.6
  • 46
    • 0027231381 scopus 로고
    • Preparation of Flouro- and Hydroxy-4-(phosphonomethyl)-D,L-phenylalanine suitably protected for solid-phase synthesis of peptides containing hydrolytically stable analogues of O-phosphotyrosine
    • Burke, T. R., Jr.; Smyth, M.; Nomizu, M.; Otaka, A.; Roller, P. P. Preparation of Flouro- and Hydroxy-4-(phosphonomethyl)-D,L-phenylalanine Suitably Protected for Solid-Phase Synthesis of Peptides Containing Hydrolytically Stable Analogues of O-Phosphotyrosine J. Org Chem. 1993, 58, 1336-1340.
    • (1993) J. Org Chem. , vol.58 , pp. 1336-1340
    • Burke T.R., Jr.1    Smyth, M.2    Nomizu, M.3    Otaka, A.4    Roller, P.P.5
  • 48
    • 0028785789 scopus 로고
    • Why is Phosphonodifluoromethyl Phenylalanine a more potent inhibitory moiety than Phosphonomethyl Phenylalanine toward Protein Tyrosine Phosphatases?
    • Chen, L.; Wu, L.; Otaka, A.; Smyth, M. S.; Roller, P. P.; Burke, T. R., Jr.; den Hertog, J.; Zhang, Z.-Y. Why Is Phosphonodifluoromethyl Phenylalanine a More Potent Inhibitory Moiety than Phosphonomethyl Phenylalanine toward Protein Tyrosine Phosphatases? Biochem. Biophys. Res. Commun. 1995, 216, 976-984.
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 976-984
    • Chen, L.1    Wu, L.2    Otaka, A.3    Smyth, M.S.4    Roller, P.P.5    Burke T.R., Jr.6    Den Hertog, J.7    Zhang, Z.-Y.8
  • 49
    • 0028990357 scopus 로고
    • Protein-Tyrosine Phosphatase inhibition by a peptide containing the Phosphotyrosyl Mimetic, L-O-Malonyltyrosine
    • Kole, H. K.; Akamatsu, M.; Ye, B.; Yan, X.; Barford, D.; Roller, P. P.; Burke, T. R., Jr. Protein-Tyrosine Phosphatase Inhibition by a Peptide Containing the Phosphotyrosyl Mimetic, L-O-Malonyltyrosine. Biochem. Biophys. Res. Commun. 1995, 209, 817-822.
    • (1995) Biochem. Biophys. Res. Commun. , vol.209 , pp. 817-822
    • Kole, H.K.1    Akamatsu, M.2    Ye, B.3    Yan, X.4    Barford, D.5    Roller, P.P.6    Burke T.R., Jr.7
  • 50
    • 0032544162 scopus 로고    scopus 로고
    • Potent inhibition of Protein-Tyrosine Phosphatase-1B using the Phosphotyrosyl Mimetic Fluoro-O-Malonyl Tyrosine (FOMT)
    • Roller, P. P.; Wu, L.; Zhang, Z.-Y.; Burke, T. R., Jr. Potent Inhibition of Protein-Tyrosine Phosphatase-1B Using the Phosphotyrosyl Mimetic Fluoro-O-Malonyl Tyrosine (FOMT). Bioorg. Med. Chem. Lett. 1998, 8, 2149-2150.
    • (1998) Bioorg. Med. Chem. Lett. , vol.8 , pp. 2149-2150
    • Roller, P.P.1    Wu, L.2    Zhang, Z.-Y.3    Burke T.R., Jr.4
  • 51
    • 0028815228 scopus 로고
    • Radio frequency tag encoded combinatorial library method for the discovery of Tripeptide-substituted cinnamic acid inhibitors of the Protein Tyrosine Phosphatase PTP1B
    • Moran, E. J.; Sarshar, S.; Cargill, J. F.; Shahbaz, M. M.; Lio, A.; Mjalli, A. M. M.; Armstrong, R. W. Radio Frequency Tag Encoded Combinatorial Library Method for the Discovery of Tripeptide-Substituted Cinnamic Acid Inhibitors of the Protein Tyrosine Phosphatase PTP1B J. Am. Chem. Soc. 1995, 117, 10787-10788.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 10787-10788
    • Moran, E.J.1    Sarshar, S.2    Cargill, J.F.3    Shahbaz, M.M.4    Lio, A.5    Mjalli, A.M.M.6    Armstrong, R.W.7
  • 52
    • 0032552183 scopus 로고    scopus 로고
    • Enantioselective synthesis of Non-phosphorous-containing Phosphotyrosyl Mimetics and their use in the preparation of Tyrosine Phosphatase inhibitory peptides
    • Burke, T. R., Jr.; Yao, Z.-J.; Zhao, H.; Milne, G. W. A.; Wu, L.; Zhang, Z.-Y.; Voigt, J. H. Enantioselective Synthesis of Non-phosphorous-Containing Phosphotyrosyl Mimetics and Their Use in the Preparation of Tyrosine Phosphatase Inhibitory Peptides. Tetrahedron 1998, 54, 9981-9994.
    • (1998) Tetrahedron , vol.54 , pp. 9981-9994
    • Burke T.R., Jr.1    Yao, Z.-J.2    Zhao, H.3    Milne, G.W.A.4    Wu, L.5    Zhang, Z.-Y.6    Voigt, J.H.7
  • 53
    • 0000520794 scopus 로고
    • 1,3,4-Oxadiazoles. III Mannich Bases derived from 5-(O-Hydroxyphenyl)-1,3,4-Oxadiazole-2-Thione
    • Ram, V. J.; Pandey, H. N. 1,3,4-Oxadiazoles. III Mannich Bases Derived from 5-(O-Hydroxyphenyl)-1,3,4-Oxadiazole-2-Thione J. Indian Chem. Soc. 1974, 51, 634-635.
    • (1974) J. Indian Chem. Soc. , vol.51 , pp. 634-635
    • Ram, V.J.1    Pandey, H.N.2
  • 54
    • 0030120054 scopus 로고    scopus 로고
    • Orientational sampling and rigid-body minimization in molecular docking revisited: On-the-fly optimization and degeneracy removal
    • Gschwend, D. A.; Kuntz, I. D. Orientational Sampling and Rigid-Body Minimization in Molecular Docking Revisited: On-the-Fly Optimization and Degeneracy Removal. J. Comput.-Aided. Mol. Des. 1996, 10, 123-132.
    • (1996) J. Comput.-Aided. Mol. Des. , vol.10 , pp. 123-132
    • Gschwend, D.A.1    Kuntz, I.D.2
  • 57
    • 84986432941 scopus 로고
    • Automated docking with grid-based energy evaluation
    • Meng, E. C.; Shoichet, B. K.; Kuntz, I. D. Automated Docking with Grid-Based Energy Evaluation. J. Comput. Chem. 1992, 13, 505-524.
    • (1992) J. Comput. Chem. , vol.13 , pp. 505-524
    • Meng, E.C.1    Shoichet, B.K.2    Kuntz, I.D.3
  • 58
    • 0032144872 scopus 로고    scopus 로고
    • Low-affinity binding determined by titration calorimetry using a high-affinity coupling ligand: A Thermodynamic study of ligand binding to Protein Tyrosine Phosphatase 1B
    • Zhang, Y.-L.; Zhang, Z.-Y. Low-Affinity Binding Determined by Titration Calorimetry Using a High-Affinity Coupling Ligand: a Thermodynamic Study of Ligand Binding to Protein Tyrosine Phosphatase 1B. Anal. Biochem. 1998, 261, 139-148.
    • (1998) Anal. Biochem. , vol.261 , pp. 139-148
    • Zhang, Y.-L.1    Zhang, Z.-Y.2
  • 59
    • 0025977037 scopus 로고
    • Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion proteins with Glutathione S-Transferase
    • Guan, K. L.; Dixon, J. E. Eukaryotic Proteins Expressed in Escherichia coli: An Improved Thrombin Cleavage and Purification Procedure of Fusion Proteins with Glutathione S-Transferase. Anal. Biochem. 1991, 192, 262-267.
    • (1991) Anal. Biochem. , vol.192 , pp. 262-267
    • Guan, K.L.1    Dixon, J.E.2
  • 60
    • 0026038524 scopus 로고
    • Cloning, bacterial expression, purification, and characterization of the cytoplasmic domain of rat LAR, A receptorlike Protein Tyrosine Phosphatase
    • Pot, D. A.; Woodford, T. A.; Remboutsika, E.; Haun, R. S.; Dixon, J. E. Cloning, Bacterial Expression, Purification, and Characterization of the Cytoplasmic Domain of Rat LAR, a ReceptorLike Protein Tyrosine Phosphatase. J. Biol. Chem. 1991, 266, 19688-19696.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19688-19696
    • Pot, D.A.1    Woodford, T.A.2    Remboutsika, E.3    Haun, R.S.4    Dixon, J.E.5
  • 61
    • 0028858055 scopus 로고
    • Transition state and rate-limiting step of the reaction catalyzed by the human dual-specificity Phosphatase, VHR
    • Zhang, Z.-Y.; Wu, L.; Chen, L Transition State and Rate-Limiting Step of the Reaction Catalyzed by the Human Dual-Specificity Phosphatase, VHR. Biochemistry 1995, 34, 16088-16096.
    • (1995) Biochemistry , vol.34 , pp. 16088-16096
    • Zhang, Z.-Y.1    Wu, L.2    Chen, L.3
  • 62
    • 0029015718 scopus 로고
    • Kinetic and mechanistic characterization of a mammalian Protein-Tyrosine Phosphatase, PTP1
    • Zhang, Z.-Y. Kinetic and Mechanistic Characterization of a Mammalian Protein-Tyrosine Phosphatase, PTP1. J. Biol. Chem. 1995, 270, 11199-11204.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11199-11204
    • Zhang, Z.-Y.1
  • 63
    • 0029739468 scopus 로고    scopus 로고
    • VHR and PTP1 Protein Phosphatases exhibit remarkably different active site specificities toward low molecular weight nonpeptidic substrates
    • Chen, L.; Montserat, J.; Lawrence, D. S.; Zhang, Z. Y. VHR and PTP1 Protein Phosphatases Exhibit Remarkably Different Active Site Specificities toward Low Molecular Weight Nonpeptidic Substrates. Biochemistry 1996, 35, 9349-9354.
    • (1996) Biochemistry , vol.35 , pp. 9349-9354
    • Chen, L.1    Montserat, J.2    Lawrence, D.S.3    Zhang, Z.Y.4
  • 64
    • 50549159930 scopus 로고
    • The kinetics of enzyme-catalyzed reactions with two or more substrates or products
    • Cleland, W. W. The Kinetics of Enzyme-Catalyzed Reactions with Two or More Substrates or Products. Biochim. Biophys. Acta 1963, 67, 104-137.
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 104-137
    • Cleland, W.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.