메뉴 건너뛰기




Volumn 77, Issue 1, 1999, Pages 505-515

Molecular dynamics simulations of protein-tyrosine phosphatase 1B. I. Ligand-induced changes in the protein motions

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; PROTEIN TYROSINE PHOSPHATASE;

EID: 0032976539     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)76907-9     Document Type: Article
Times cited : (40)

References (69)
  • 2
    • 0029893417 scopus 로고    scopus 로고
    • A common amino acid polymorphism in insulin receptor substrate-1 causes impaired insulin signaling
    • Almind, K., G. Inoue, O. Pedersen, and C. R. Kahn. 1996. A common amino acid polymorphism in insulin receptor substrate-1 causes impaired insulin signaling. J. Clin. Invest. 97:2569-2575.
    • (1996) J. Clin. Invest. , vol.97 , pp. 2569-2575
    • Almind, K.1    Inoue, G.2    Pedersen, O.3    Kahn, C.R.4
  • 4
    • 0028305457 scopus 로고
    • Prediction of pH-dependent properties of proteins
    • Antosiewicz, J., J. A. McCammon, and M. K. Gilson. 1994. Prediction of pH-dependent properties of proteins. J. Mol. Biol. 238:415-436.
    • (1994) J. Mol. Biol. , vol.238 , pp. 415-436
    • Antosiewicz, J.1    McCammon, J.A.2    Gilson, M.K.3
  • 7
    • 0028231388 scopus 로고
    • Crystal structure of human protein tyrosine phosphatase 1B
    • Barford, D., A. J. Flint, and N. K. Tonks. 1994. Crystal structure of human protein tyrosine phosphatase 1B. Science. 263:1397-1404.
    • (1994) Science , vol.263 , pp. 1397-1404
    • Barford, D.1    Flint, A.J.2    Tonks, N.K.3
  • 10
    • 0027164289 scopus 로고
    • Designed replacement of an internal hydration water molecule in BPTI: Structural and functional implications of a glycine-to-serine mutation
    • Berndt, K. D., J. Beunink, W. Schröder, and K. Wüthrich. 1993. Designed replacement of an internal hydration water molecule in BPTI: structural and functional implications of a glycine-to-serine mutation. Biochemistry. 32:4564-4570.
    • (1993) Biochemistry , vol.32 , pp. 4564-4570
    • Berndt, K.D.1    Beunink, J.2    Schröder, W.3    Wüthrich, K.4
  • 13
    • 0000630849 scopus 로고
    • Isolation and structural elucidation of a novel phosphocysteine intermediate in the LAR protein tyrosine phosphatase enzymatic pathway
    • Cho, H., R. Krishnaraj, E. Kitas, W. Bannwarth, C. T. Walsh, and K. S. Anderson. 1992. Isolation and structural elucidation of a novel phosphocysteine intermediate in the LAR protein tyrosine phosphatase enzymatic pathway. J. Am. Chem. Soc. 114:7296-7298.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 7296-7298
    • Cho, H.1    Krishnaraj, R.2    Kitas, E.3    Bannwarth, W.4    Walsh, C.T.5    Anderson, K.S.6
  • 14
    • 0026124585 scopus 로고
    • Electrostatics and diffusion of molecules in solution: Simulations with the University of Houston Brownian dynamics program
    • Davis, M. E., J. D. Madura, B. A. Luty, and J. A. McCammon. 1991. Electrostatics and diffusion of molecules in solution: simulations with the University of Houston Brownian dynamics program. Comp. Phys. Comm. 62:187-197.
    • (1991) Comp. Phys. Comm. , vol.62 , pp. 187-197
    • Davis, M.E.1    Madura, J.D.2    Luty, B.A.3    McCammon, J.A.4
  • 15
    • 33748593093 scopus 로고    scopus 로고
    • Improving the continuum dielectric approach to calculating pKas of ionizable groups in proteins
    • Demchuk, E., and R. C. Wade. 1996. Improving the continuum dielectric approach to calculating pKas of ionizable groups in proteins. J. Phys. Chem. 100:17373-17387.
    • (1996) J. Phys. Chem. , vol.100 , pp. 17373-17387
    • Demchuk, E.1    Wade, R.C.2
  • 16
    • 0028049327 scopus 로고
    • Dynamics of a flexible loop in dihydrofolate reductase from Escherichia coli and its implication for catalysis
    • Falzone, C. J., P. E. Wright, and S. J. Benkovic. 1994. Dynamics of a flexible loop in dihydrofolate reductase from Escherichia coli and its implication for catalysis. Biochemistry. 33:439-442.
    • (1994) Biochemistry , vol.33 , pp. 439-442
    • Falzone, C.J.1    Wright, P.E.2    Benkovic, S.J.3
  • 17
    • 0030296632 scopus 로고    scopus 로고
    • Structure an function of the protein tyrosine phosphatases
    • Fauman, E. B., and M. A. Saper. 1996. Structure an function of the protein tyrosine phosphatases. Trends Biochem. Sci. 21:413-417.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 413-417
    • Fauman, E.B.1    Saper, M.A.2
  • 18
  • 19
    • 0027477251 scopus 로고
    • Multiple-site titration and molecular modeling: Two rapid methods for computing energies and forces for ionizable groups in proteins
    • Gilson, M. K. 1993. Multiple-site titration and molecular modeling: two rapid methods for computing energies and forces for ionizable groups in proteins. Proteins Struct. Fund. Genet. 15:266-282.
    • (1993) Proteins Struct. Fund. Genet. , vol.15 , pp. 266-282
    • Gilson, M.K.1
  • 20
    • 0025945823 scopus 로고
    • Evidence for protein-tyrosine-phosphatase catalysis proceeding via a cysteine-phosphate intermediate
    • Guan, K. L., and J. E. Dixon. 1991. Evidence for protein-tyrosine-phosphatase catalysis proceeding via a cysteine-phosphate intermediate. J. Biol. Chem. 266:17026-17030.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17026-17030
    • Guan, K.L.1    Dixon, J.E.2
  • 21
    • 0031575408 scopus 로고    scopus 로고
    • Energetics of nucleophile activation in a protein tyrosine phosphatase
    • Hansson, T., P. Nordlund, and J. Åqvist. 1997. Energetics of nucleophile activation in a protein tyrosine phosphatase. J. Mol. Biol. 265:118-127.
    • (1997) J. Mol. Biol. , vol.265 , pp. 118-127
    • Hansson, T.1    Nordlund, P.2    Åqvist, J.3
  • 22
    • 0022965255 scopus 로고
    • Stabilization of A repressor against thermal denaturation by site-directed Gly → Ala changes in α-helix 3
    • Hecht, M. H., J. M. Sturtevant, and R. T. Sauer. 1986. Stabilization of A repressor against thermal denaturation by site-directed Gly → Ala changes in α-helix 3. Proteins Struct. Fund. Genet. 1:43-46.
    • (1986) Proteins Struct. Fund. Genet. , vol.1 , pp. 43-46
    • Hecht, M.H.1    Sturtevant, J.M.2    Sauer, R.T.3
  • 23
    • 0026611519 scopus 로고
    • 188 → Glu mutation in South Africans of Indian descent: Evidence suggesting common origins and an increased frequency
    • 188 → Glu mutation in South Africans of Indian descent: evidence suggesting common origins and an increased frequency. J. Med. Gen. 29:119-122.
    • (1992) J. Med. Gen. , vol.29 , pp. 119-122
    • Henderson, H.E.1    Hassan, F.2    Berger, G.M.B.3    Hayden, M.R.4
  • 24
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig, B., and A. Nicholls. 1995. Classical electrostatics in biology and chemistry. Science. 268:1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 25
    • 0026076090 scopus 로고
    • Collective motions in proteins: A covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations
    • Ichiye, T., and M. Karplus. 1991. Collective motions in proteins: a covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations. Proteins Struct. Funct. Genet. 11:205-217.
    • (1991) Proteins Struct. Funct. Genet. , vol.11 , pp. 205-217
    • Ichiye, T.1    Karplus, M.2
  • 26
    • 0028576992 scopus 로고
    • Regulation of scallop myosin by the regulatory light chain depends on a single glycine residue
    • Jancso, A., and A. G. Szent-Györgyi. 1994. Regulation of scallop myosin by the regulatory light chain depends on a single glycine residue. Proc. Natl. Acad. Sci. USA. 91:8762-8766.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8762-8766
    • Jancso, A.1    Szent-Györgyi, A.G.2
  • 27
    • 0029066496 scopus 로고
    • Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B
    • Jia, Z., D. Barford, A. J. Flint, and N. K. Tonks. 1995. Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B. Science. 268:1754-1758.
    • (1995) Science , vol.268 , pp. 1754-1758
    • Jia, Z.1    Barford, D.2    Flint, A.J.3    Tonks, N.K.4
  • 28
  • 29
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and C. Sander. 1983. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 30
    • 0027196872 scopus 로고
    • Movable lobes and flexible loops in proteins
    • Kempner, E. S. 1993. Movable lobes and flexible loops in proteins. FEBS Lett. 326:4-10.
    • (1993) FEBS Lett. , vol.326 , pp. 4-10
    • Kempner, E.S.1
  • 31
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • Koshland, D. E., Jr. 1958. Application of a theory of enzyme specificity to protein synthesis. Proc. Natl. Acad. Sci. USA. 44:98-106.
    • (1958) Proc. Natl. Acad. Sci. USA , vol.44 , pp. 98-106
    • Koshland D.E., Jr.1
  • 32
    • 0025146562 scopus 로고
    • Structural diversity and evolution of human receptor-like protein tyrosine phosphatases
    • Krueger, N. X., M. Streuli, and H. Saito. 1990. Structural diversity and evolution of human receptor-like protein tyrosine phosphatases. EMBO J. 9:3241-3252.
    • (1990) EMBO J. , vol.9 , pp. 3241-3252
    • Krueger, N.X.1    Streuli, M.2    Saito, H.3
  • 33
    • 0019873836 scopus 로고
    • Effect of cysteine-25 on the ionization of histidine-159 in papain as determined by proton nuclear magnetic resonance spectroscopy. Evidence for a His-Cys-25 ion pair and its possible role in catalysis
    • Lewis, S. D., F. A. Johnson, and J. A. Shafer. 1981. Effect of cysteine-25 on the ionization of histidine-159 in papain as Determined by proton nuclear magnetic resonance spectroscopy. Evidence for a His-Cys-25 ion pair and its possible role in catalysis. Biochemistry. 20:48-51.
    • (1981) Biochemistry , vol.20 , pp. 48-51
    • Lewis, S.D.1    Johnson, F.A.2    Shafer, J.A.3
  • 34
    • 0030887994 scopus 로고    scopus 로고
    • Roles of aspartic acid-181 and serine-222 in intermediate formation and hydrolysis of the mammalian protein-tyrosine-phosphatase PTP1
    • Lohse, D. L., J. M. Denu, M. Santoro, and J. E. Dixon. 1997. Roles of aspartic acid-181 and serine-222 in intermediate formation and hydrolysis of the mammalian protein-tyrosine-phosphatase PTP1. Biochemistry. 36:4568-4575.
    • (1997) Biochemistry , vol.36 , pp. 4568-4575
    • Lohse, D.L.1    Denu, J.M.2    Santoro, M.3    Dixon, J.E.4
  • 36
    • 0026588875 scopus 로고
    • Pathological changes in the brain of a patient with familial Alzheimer's disease having a missense mutation at codon 717 in the amyloid precursor protein gene
    • Mann, D. M. A., D. Jones, J. S. Snowden, D. Neary, and J. Hardy. 1992. Pathological changes in the brain of a patient with familial Alzheimer's disease having a missense mutation at codon 717 in the amyloid precursor protein gene. Neurosci. Lett. 137:225-228.
    • (1992) Neurosci. Lett. , vol.137 , pp. 225-228
    • Mann, D.M.A.1    Jones, D.2    Snowden, J.S.3    Neary, D.4    Hardy, J.5
  • 37
    • 0023643422 scopus 로고
    • Genetic and structural analysis of the protein stability problem
    • Matthews, B. W. 1987. Genetic and structural analysis of the protein stability problem. Biochemistry. 26:6885-6888.
    • (1987) Biochemistry , vol.26 , pp. 6885-6888
    • Matthews, B.W.1
  • 38
    • 0028009549 scopus 로고
    • Protein tyrosine phosphatases of extracellular and intracellular domains
    • Mourey, R. J., and J. E. Dixon. 1994. Protein tyrosine phosphatases of extracellular and intracellular domains. Curr. Opin. Genet. Dev. 4:31-39.
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 31-39
    • Mourey, R.J.1    Dixon, J.E.2
  • 39
    • 0032562586 scopus 로고    scopus 로고
    • Visualization of the cysteinyl-phosphate intermediate of a protein-tyrosine phosphatase by x-ray crystallography
    • Pannifer, A. D. B., A. J. Flint, N. K. Tonks, and D. Barford. 1998. Visualization of the cysteinyl-phosphate intermediate of a protein-tyrosine phosphatase by x-ray crystallography. J. Biol. Chem. 273: 10454-10462.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10454-10462
    • Pannifer, A.D.B.1    Flint, A.J.2    Tonks, N.K.3    Barford, D.4
  • 40
    • 0025160881 scopus 로고
    • Refined structure of dienelactone hydrolase at 1.8 Å
    • Pathak, D., and D. J. Ollis. 1990. Refined structure of dienelactone hydrolase at 1.8 Å. J. Mol. Biol. 214:497-525.
    • (1990) J. Mol. Biol. , vol.214 , pp. 497-525
    • Pathak, D.1    Ollis, D.J.2
  • 41
    • 0029926518 scopus 로고    scopus 로고
    • Dynamics of proteins in different solvent systems: Analysis of essential motion in lipases
    • Peters, G. H., D. M. F. van Aalten, O. Edholm, S. Toxvaerd, and R. Bywater. 1996. Dynamics of proteins in different solvent systems: analysis of essential motion in lipases. Biophys. J. 71:2245-2255.
    • (1996) Biophys. J. , vol.71 , pp. 2245-2255
    • Peters, G.H.1    Van Aalten, D.M.F.2    Edholm, O.3    Toxvaerd, S.4    Bywater, R.5
  • 42
    • 0001024343 scopus 로고    scopus 로고
    • Essential motions in enzyme binding sites and bound inhibitors: The effect of inhibitors of different chain length
    • Peters, G. H., D. M. F. van Aalten, A. Svendsen, and R. Bywater. 1997. Essential motions in enzyme binding sites and bound inhibitors: the effect of inhibitors of different chain length. Protein Eng. 10:148-156.
    • (1997) Protein Eng. , vol.10 , pp. 148-156
    • Peters, G.H.1    Van Aalten, D.M.F.2    Svendsen, A.3    Bywater, R.4
  • 43
    • 0028854555 scopus 로고
    • Identifying the mechanism of protein loop closure: A molecular dynamics simulation of the Bacillus stearothermophilus LDH loop in solution
    • Philippopoulos, M., Y. Xiang, and C. Lim. 1995. Identifying the mechanism of protein loop closure: a molecular dynamics simulation of the Bacillus stearothermophilus LDH loop in solution. Protein Eng. 8:565-573.
    • (1995) Protein Eng. , vol.8 , pp. 565-573
    • Philippopoulos, M.1    Xiang, Y.2    Lim, C.3
  • 44
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J. P., G. Ciccotti, and H. J. C. Berendsen. 1977. Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J. Comp. Physiol. 23: 327-341.
    • (1977) J. Comp. Physiol. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 45
    • 0030908397 scopus 로고    scopus 로고
    • a calculations along a bacteriorhodopsin molecular dynamics trajectory
    • a calculations along a bacteriorhodopsin molecular dynamics trajectory. Biophys. Chem. 65:189-204.
    • (1997) Biophys. Chem. , vol.65 , pp. 189-204
    • Sandberg, L.1    Edholm, O.2
  • 46
    • 0027970874 scopus 로고
    • Protein-tyrosine phosphatases
    • Stone, R. L., and J. E. Dixon. 1994. Protein-tyrosine phosphatases. J. Biol. Chem. 269:31323-31326.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31323-31326
    • Stone, R.L.1    Dixon, J.E.2
  • 47
    • 0028122711 scopus 로고
    • Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 Å and the complex with tungstate
    • Stuckey, J. A., H. L. Schubert, E. B. Fauman, Z.-Y. Zhang, J. E. Dixon, and M. A. Saper. 1994. Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 Å and the complex with tungstate. Nature. 370:571-574.
    • (1994) Nature , vol.370 , pp. 571-574
    • Stuckey, J.A.1    Schubert, H.L.2    Fauman, E.B.3    Zhang, Z.-Y.4    Dixon, J.E.5    Saper, M.A.6
  • 49
    • 0029075795 scopus 로고
    • The essential dynamics of thermolysin-conformation of hinge-bending motion and comparison of simulations in vacuum and water
    • van Aalten, D. M. F., A. Amadei, A. B. M. Linssen, V. G. H. Eijsink, and G. Vriend. 1995. The essential dynamics of thermolysin-conformation of hinge-bending motion and comparison of simulations in vacuum and water. Proteins Struct. Funct. Genet. 22:45-54.
    • (1995) Proteins Struct. Funct. Genet. , vol.22 , pp. 45-54
    • Van Aalten, D.M.F.1    Amadei, A.2    Linssen, A.B.M.3    Eijsink, V.G.H.4    Vriend, G.5
  • 50
    • 0031019423 scopus 로고    scopus 로고
    • Engineering protein mechanics: Inhibition of concerted motions of the cellular retinol binding protein by site-directed mutagenesis
    • van Aalten, D. M. F., P. C. Jones, M. De Sousa, and J. B. C. Findlay. 1997. Engineering protein mechanics: inhibition of concerted motions of the cellular retinol binding protein by site-directed mutagenesis. Protein Eng. 10:31-37.
    • (1997) Protein Eng. , vol.10 , pp. 31-37
    • Van Aalten, D.M.F.1    Jones, P.C.2    De Sousa, M.3    Findlay, J.B.C.4
  • 52
    • 0025162702 scopus 로고
    • A Pro to Gly mutation in the hinge of the arabmose-binding protein enhances binding and alters specificity
    • Vermersch, P. S., J. J. G. Tesmer, D. D. Lemon, and F. A. Quiocho. 1990. A Pro to Gly mutation in the hinge of the arabmose-binding protein enhances binding and alters specificity. J. Biol. Chem. 265: 16592-16603.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16592-16603
    • Vermersch, P.S.1    Tesmer, J.J.G.2    Lemon, D.D.3    Quiocho, F.A.4
  • 53
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend, G. 1990. WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8:52-56.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 55
    • 0027446430 scopus 로고
    • Gating of the active site of triose phosphate isomerase: Brownian dynamics simulations of flexible peptide loops in the enzyme
    • Wade, R. C., M. E. Davis, B. A. Luty, J. D. Madura, and J. A. McCammon. 1993. Gating of the active site of triose phosphate isomerase: Brownian dynamics simulations of flexible peptide loops in the enzyme. Biophys. J. 64:9-15.
    • (1993) Biophys. J. , vol.64 , pp. 9-15
    • Wade, R.C.1    Davis, M.E.2    Luty, B.A.3    Madura, J.D.4    McCammon, J.A.5
  • 57
    • 0027183416 scopus 로고
    • Protein tyrosine phosphatases
    • Walton, K. M., and J. E. Dixon. 1993. Protein tyrosine phosphatases. Annu. Rev. Biochem. 62:101-120.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 101-120
    • Walton, K.M.1    Dixon, J.E.2
  • 59
    • 0021476470 scopus 로고
    • Calculations of electrostatic interactions in biological systems and in solutions
    • Warshel, A., and S. T. Russel. 1984. Calculations of electrostatic interactions in biological systems and in solutions. Q. Rev. Biophys. 17: 283-422.
    • (1984) Q. Rev. Biophys. , vol.17 , pp. 283-422
    • Warshel, A.1    Russel, S.T.2
  • 60
    • 0021107943 scopus 로고
    • Site-directed mutagenesis as a probe of enzyme structure and catalysis: Tyrosyl-tRNA synthetase cysteine-35 to glycine-35 mutation
    • Wilkinson, A. J., A. R. Fersht, D. M. Blow, and G. Winter. 1983. Site-directed mutagenesis as a probe of enzyme structure and catalysis: tyrosyl-tRNA synthetase cysteine-35 to glycine-35 mutation. Biochemistry. 22:3581-3586.
    • (1983) Biochemistry , vol.22 , pp. 3581-3586
    • Wilkinson, A.J.1    Fersht, A.R.2    Blow, D.M.3    Winter, G.4
  • 61
    • 0029000872 scopus 로고
    • Dynamics of the flexible loop of triosephosphate isomerase: The loop motion is not ligand gated
    • Williams, J. C., and A. E. McDermott. 1995. Dynamics of the flexible loop of triosephosphate isomerase: the loop motion is not ligand gated. Biochemistry. 34:8309-8319.
    • (1995) Biochemistry , vol.34 , pp. 8309-8319
    • Williams, J.C.1    McDermott, A.E.2
  • 62
    • 0026528237 scopus 로고
    • Cloning, expression, and catalytic mechanism of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart
    • Wo, Y.-Y., M.-M. Zhou, P. Stevis, J. P. Davis, Z.-Y. Zhang, and R. L. Van Etten. 1992. Cloning, expression, and catalytic mechanism of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart. Biochemistry. 31:1712-1721.
    • (1992) Biochemistry , vol.31 , pp. 1712-1721
    • Wo, Y.-Y.1    Zhou, M.-M.2    Stevis, P.3    Davis, J.P.4    Zhang, Z.-Y.5    Van Etten, R.L.6
  • 64
    • 0029975476 scopus 로고    scopus 로고
    • Crystal-structure of the dual-specificity protein phosphatase vhr
    • Yuvaniyama, J., J. M. Denu, J. E. Dixon, and M. A. Saper. 1996. Crystal-structure of the dual-specificity protein phosphatase vhr. Science. 272: 1328-1333.
    • (1996) Science , vol.272 , pp. 1328-1333
    • Yuvaniyama, J.1    Denu, J.M.2    Dixon, J.E.3    Saper, M.A.4
  • 66
    • 0028298024 scopus 로고
    • Protein tyrosine phosphatase substrate specificity: Size and phosphotyrosine positioning requirements in peptide substrates
    • Zhang, Z.-Y., D. Maclean, D. J. McNamara, T. K. Sawyer, and J. E. Dixon. 1994b. Protein tyrosine phosphatase substrate specificity: size and phosphotyrosine positioning requirements in peptide substrates. Biochemistry. 33:2285-2290.
    • (1994) Biochemistry , vol.33 , pp. 2285-2290
    • Zhang, Z.-Y.1    Maclean, D.2    McNamara, D.J.3    Sawyer, T.K.4    Dixon, J.E.5
  • 67
    • 0029584325 scopus 로고
    • Catalytic function of the conserved hydroxyl group in the protein tyrosine phosphatase signature motif
    • Zhang, Z.-Y., B. A. Palfey, L. Wu, and Y. Zhao. 1995. Catalytic function of the conserved hydroxyl group in the protein tyrosine phosphatase signature motif. Biochemistry. 34:16389-16396.
    • (1995) Biochemistry , vol.34 , pp. 16389-16396
    • Zhang, Z.-Y.1    Palfey, B.A.2    Wu, L.3    Zhao, Y.4
  • 68
    • 0028176050 scopus 로고
    • Dissecting the catalytic mechanism of protein-tyrosine phosphatases
    • Zhang, Z.-Y., Y. Wang, and J. E. Dixon. 1994a. Dissecting the catalytic mechanism of protein-tyrosine phosphatases. Proc. Natl. Acad. Sci. USA. 91:1624-1627.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1624-1627
    • Zhang, Z.-Y.1    Wang, Y.2    Dixon, J.E.3
  • 69
    • 0029786801 scopus 로고    scopus 로고
    • Reactivity of alcohols toward the phosphoenzyme intermediate in the protein-tyrosine phosphatase-catalyzed reaction: Probing the transition state of the dephosphorylation step
    • Zhao, Y., and Z.-Y. Zhang. 1996. Reactivity of alcohols toward the phosphoenzyme intermediate in the protein-tyrosine phosphatase-catalyzed reaction: probing the transition state of the dephosphorylation step. Biochemistry. 35:11797-11804.
    • (1996) Biochemistry , vol.35 , pp. 11797-11804
    • Zhao, Y.1    Zhang, Z.-Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.