메뉴 건너뛰기




Volumn 73, Issue , 2003, Pages 171-220

Mechanistic Studies on Protein Tyrosine Phosphatases

Author keywords

[No Author keywords available]

Indexed keywords


EID: 2542559631     PISSN: 00796603     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0079-6603(03)01006-7     Document Type: Article
Times cited : (101)

References (194)
  • 1
    • 0034614490 scopus 로고    scopus 로고
    • Signaling—2000 and beyond
    • T. Hunter Signaling—2000 and beyond Cell 100 2000 113 127
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 2
    • 0036731485 scopus 로고    scopus 로고
    • STATS: Transcriptional control and biological impact
    • D.E. Levy J.E. Darnell Jr., STATS: Transcriptional control and biological impact Nat. Rev. Mol. Cell Biol. 3 2002 651 662
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 651-662
    • Levy, D.E.1    Darnell, J.E.2
  • 3
    • 0032577051 scopus 로고    scopus 로고
    • The Croonian Lecture 1997. The phosphorylation of proteins on tyrosine: Its role in cell growth and disease
    • T. Hunter The Croonian Lecture 1997. The phosphorylation of proteins on tyrosine: Its role in cell growth and disease Phil. Trans. R. Soc. Lond. B. 353 1998 583 605
    • (1998) Phil. Trans. R. Soc. Lond. B. , vol.353 , pp. 583-605
    • Hunter, T.1
  • 4
    • 0030953448 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases in signal transduction
    • B.G. Neel N.K. Tonks Protein tyrosine phosphatases in signal transduction Curr. Opin. Cell Biol. 9 1997 193 204
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 193-204
    • Neel, B.G.1    Tonks, N.K.2
  • 5
    • 0033994516 scopus 로고    scopus 로고
    • Form, function, and regulation of protein tyrosine phosphatases and their involvement in human diseases
    • L. Li J.E. Dixon Form, function, and regulation of protein tyrosine phosphatases and their involvement in human diseases Semin. Immunol. 12 2000 75 84
    • (2000) Semin. Immunol. , vol.12 , pp. 75-84
    • Li, L.1    Dixon, J.E.2
  • 6
    • 0035415662 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: Prospects for therapeutics
    • Z.-Y. Zhang Protein tyrosine phosphatases: Prospects for therapeutics Curr. Opin. Chem. Biol. 5 2001 416 423
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 416-423
    • Zhang, Z.-Y.1
  • 7
    • 0024287614 scopus 로고
    • Characterization of the major protein-tyrosine phosphatases of human placenta
    • N.K. Tonks C.D. Diltz E.H. Fischer Characterization of the major protein-tyrosine phosphatases of human placenta J. Biol. Chem. 263 1988 6731 6737
    • (1988) J. Biol. Chem. , vol.263 , pp. 6731-6737
    • Tonks, N.K.1    Diltz, C.D.2    Fischer, E.H.3
  • 9
    • 0026584285 scopus 로고
    • The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence
    • J.V. Frangioni P.H. Beahm V. Shifrin C.A. Jost B.G. Neel The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence Cell 68 1992 545 560
    • (1992) Cell , vol.68 , pp. 545-560
    • Frangioni, J.V.1    Beahm, P.H.2    Shifrin, V.3    Jost, C.A.4    Neel, B.G.5
  • 11
    • 0036500994 scopus 로고    scopus 로고
    • Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum
    • F.G. Haj P.J. Verveer A. Squire B.G. Neel P.I. Bastiaens Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum Science 295 2002 1708 1711
    • (2002) Science , vol.295 , pp. 1708-1711
    • Haj, F.G.1    Verveer, P.J.2    Squire, A.3    Neel, B.G.4    Bastiaens, P.I.5
  • 12
    • 0036181649 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: Structure and function, substrate specificity, and inhibitor development
    • Z.-Y. Zhang Protein tyrosine phosphatases: Structure and function, substrate specificity, and inhibitor development Annu. Rev. Pharmacol. Toxicol. 42 2002 209 234
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 209-234
    • Zhang, Z.-Y.1
  • 14
    • 0025865103 scopus 로고
    • A Tyr⧸Ser protein phosphatase encoded by Vaccinia virus
    • K.L. Guan S. Broyles J.E. Dixon A Tyr⧸Ser protein phosphatase encoded by Vaccinia virus Nature 350 1991 359 361
    • (1991) Nature , vol.350 , pp. 359-361
    • Guan, K.L.1    Broyles, S.2    Dixon, J.E.3
  • 15
    • 0029975476 scopus 로고    scopus 로고
    • Crystal structure of the dual specificity protein phosphatase VHR
    • J. Yuvaniyama J.M. Denu J.E. Dixon M.A. Saper Crystal structure of the dual specificity protein phosphatase VHR Science 272 1996 1328 1331
    • (1996) Science , vol.272 , pp. 1328-1331
    • Yuvaniyama, J.1    Denu, J.M.2    Dixon, J.E.3    Saper, M.A.4
  • 16
    • 0033970533 scopus 로고    scopus 로고
    • Dual specificity phosphatases: A gene family for control of MAP kinase function
    • M. Camps A. Nichols S. Arkinstall Dual specificity phosphatases: A gene family for control of MAP kinase function FASEB J. 14 2000 6 16
    • (2000) FASEB J. , vol.14 , pp. 6-16
    • Camps, M.1    Nichols, A.2    Arkinstall, S.3
  • 17
    • 0028970682 scopus 로고
    • Dephosphorylation of Cdk2 Thr160 by the cyclin-dependent kinase-interacting phosphatase KAP in the absence of cyclin
    • R.Y. Poon T. Hunter Dephosphorylation of Cdk2 Thr160 by the cyclin-dependent kinase-interacting phosphatase KAP in the absence of cyclin Science 270 1995 90 93
    • (1995) Science , vol.270 , pp. 90-93
    • Poon, R.Y.1    Hunter, T.2
  • 18
    • 0035545924 scopus 로고    scopus 로고
    • The role of the yeast spindle pole body and the mammalian centrosome in regulating late mitotic events
    • G. Pereira E. Schiebel The role of the yeast spindle pole body and the mammalian centrosome in regulating late mitotic events Curr. Opin. Cell Biol. 13 2001 762 769
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 762-769
    • Pereira, G.1    Schiebel, E.2
  • 19
    • 0035930555 scopus 로고    scopus 로고
    • Regulation of the anaphase-promoting complex by the dual specificity phosphatase human Cdc14a
    • J. Bembenek H. Yu Regulation of the anaphase-promoting complex by the dual specificity phosphatase human Cdc14a J. Biol. Chem. 276 2001 48237 48242
    • (2001) J. Biol. Chem. , vol.276 , pp. 48237-48242
    • Bembenek, J.1    Yu, H.2
  • 20
    • 0034723170 scopus 로고    scopus 로고
    • The human Cdc14 phosphatases interact with and dephosphorylate the tumor suppressor protein p53
    • L. Li M. Ljungman J.E. Dixon The human Cdc14 phosphatases interact with and dephosphorylate the tumor suppressor protein p53 J. Biol. Chem. 275 2000 2410 2414
    • (2000) J. Biol. Chem. , vol.275 , pp. 2410-2414
    • Li, L.1    Ljungman, M.2    Dixon, J.E.3
  • 22
  • 24
    • 0034647510 scopus 로고    scopus 로고
    • Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome
    • Q. Zeng X. Si H. Horstmann Y. Xu W. Hong C.J. Pallen Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome J. Biol. Chem. 275 2000 21444 21452
    • (2000) J. Biol. Chem. , vol.275 , pp. 21444-21452
    • Zeng, Q.1    Si, X.2    Horstmann, H.3    Xu, Y.4    Hong, W.5    Pallen, C.J.6
  • 27
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN⧸MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-triphosphate
    • T. Maehama J.E. Dixon The tumor suppressor, PTEN⧸MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-triphosphate J. Biol. Chem. 273 1998 13375 13378
    • (1998) J. Biol. Chem. , vol.273 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 28
    • 0035605844 scopus 로고    scopus 로고
    • TPIP: A novel phosphoinositide 3-phosphatase
    • S.M. Walker C.P. Downes N.R. Leslie TPIP: A novel phosphoinositide 3-phosphatase Biochem. J. 360 2001 277 283
    • (2001) Biochem. J. , vol.360 , pp. 277-283
    • Walker, S.M.1    Downes, C.P.2    Leslie, N.R.3
  • 29
    • 0035877809 scopus 로고    scopus 로고
    • PTEN 2, a Golgi-associated testis-specific homologue of the PTEN tumor suppressor lipid phosphatase
    • Y. Wu D. Dowbenko M.T. Pisabarro L. Dillard-Telm H. Koeppen L.A. Lasky PTEN 2, a Golgi-associated testis-specific homologue of the PTEN tumor suppressor lipid phosphatase J. Biol. Chem. 276 2001 21745 21753
    • (2001) J. Biol. Chem. , vol.276 , pp. 21745-21753
    • Wu, Y.1    Dowbenko, D.2    Pisabarro, M.T.3    Dillard-Telm, L.4    Koeppen, H.5    Lasky, L.A.6
  • 31
    • 0034244437 scopus 로고    scopus 로고
    • Myotubularin, a protein tyrosine phosphatase mutated in myotubular myopathy, dephosphorylates the lipid second messenger, phosphatidylinositol 3-phosphate
    • G.S. Taylor T. Maehama J.E. Dixon Myotubularin, a protein tyrosine phosphatase mutated in myotubular myopathy, dephosphorylates the lipid second messenger, phosphatidylinositol 3-phosphate Proc. Natl. Acad. Sci. USA 97 2000 8910 8915
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8910-8915
    • Taylor, G.S.1    Maehama, T.2    Dixon, J.E.3
  • 32
    • 0034703432 scopus 로고    scopus 로고
    • Myotubularin, a phosphatase deficient in myotubular myopathy, acts on phosphatidylinositol 3-kinase and phosphatidylinositol 3-phosphate pathway
    • F. Blondeau J. Laporte S. Bodin G. Superti-Furga B. Payrastre J.L. Mandel Myotubularin, a phosphatase deficient in myotubular myopathy, acts on phosphatidylinositol 3-kinase and phosphatidylinositol 3-phosphate pathway Hum. Mol. Genet. 9 2000 2223 2229
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2223-2229
    • Blondeau, F.1    Laporte, J.2    Bodin, S.3    Superti-Furga, G.4    Payrastre, B.5    Mandel, J.L.6
  • 33
    • 0030807902 scopus 로고    scopus 로고
    • An RNA 5′-triphosphatase related to the protein tyrosine phosphatases
    • T. Takagi C.R. Moore F. Diehn S. Buratowski An RNA 5′-triphosphatase related to the protein tyrosine phosphatases Cell 89 1997 867 873
    • (1997) Cell , vol.89 , pp. 867-873
    • Takagi, T.1    Moore, C.R.2    Diehn, F.3    Buratowski, S.4
  • 34
    • 0031820701 scopus 로고    scopus 로고
    • Characterization of a baculovirus encoded RNA 5′-triphosphatase
    • C.H. Gross S. Shuman Characterization of a baculovirus encoded RNA 5′-triphosphatase J. Virol. 72 1998 7057 7063
    • (1998) J. Virol. , vol.72 , pp. 7057-7063
    • Gross, C.H.1    Shuman, S.2
  • 35
    • 0033523023 scopus 로고    scopus 로고
    • Human PIR1 of the protein-tyrosine phosphatase superfamily has RNA 5′-triphosphatase and diphosphatase activities
    • T. Deshpande T. Takagi L. Hao S. Buratowski H. Charbonneau Human PIR1 of the protein-tyrosine phosphatase superfamily has RNA 5′-triphosphatase and diphosphatase activities J. Biol. Chem. 274 1999 16590 16594
    • (1999) J. Biol. Chem. , vol.274 , pp. 16590-16594
    • Deshpande, T.1    Takagi, T.2    Hao, L.3    Buratowski, S.4    Charbonneau, H.5
  • 36
    • 0025938467 scopus 로고
    • The cdc25 protein contains an intrinsic phosphatase activity
    • W.G. Dunphy A. Kumagai The cdc25 protein contains an intrinsic phosphatase activity Cell 67 1991 189 196
    • (1991) Cell , vol.67 , pp. 189-196
    • Dunphy, W.G.1    Kumagai, A.2
  • 37
    • 0026569665 scopus 로고
    • The cdc25 M-phase inducer: An unconventional protein phosphatase
    • J.B.A. Millar P. Russell The cdc25 M-phase inducer: An unconventional protein phosphatase Cell 68 1992 407 410
    • (1992) Cell , vol.68 , pp. 407-410
    • Millar, J.B.A.1    Russell, P.2
  • 41
    • 0036367267 scopus 로고    scopus 로고
    • Low-molecular-weight protein tyrosine phosphatase and human disease: In search of biochemical mechanisms
    • N. Bottini E. Bottini F. Gloria-Bottini T. Mustelin Low-molecular-weight protein tyrosine phosphatase and human disease: In search of biochemical mechanisms Arch. Immunol. Ther. Exp. 50 2002 95 104
    • (2002) Arch. Immunol. Ther. Exp. , vol.50 , pp. 95-104
    • Bottini, N.1    Bottini, E.2    Gloria-Bottini, F.3    Mustelin, T.4
  • 43
    • 0036237740 scopus 로고    scopus 로고
    • Low-molecular-weight protein tyrosine phosphatase is a positive component of the fibroblast growth factor receptor signaling pathway
    • E.K. Park N. Warner K. Mood T. Pawson I.O. Daar Low-molecular-weight protein tyrosine phosphatase is a positive component of the fibroblast growth factor receptor signaling pathway Mol. Cell Biol. 22 2002 3404 3414
    • (2002) Mol. Cell Biol. , vol.22 , pp. 3404-3414
    • Park, E.K.1    Warner, N.2    Mood, K.3    Pawson, T.4    Daar, I.O.5
  • 45
    • 0024995069 scopus 로고
    • Purification and characterization of a low molecular weight acid phosphatase—a major phosphotyrosyl-protein phosphatase from bovine heart
    • Z.-Y. Zhang R.L. Van Etten Purification and characterization of a low molecular weight acid phosphatase—a major phosphotyrosyl-protein phosphatase from bovine heart Arch. Biochem. Biophys. 282 1990 39 49
    • (1990) Arch. Biochem. Biophys. , vol.282 , pp. 39-49
    • Zhang, Z.-Y.1    Van Etten, R.L.2
  • 47
    • 0031893253 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatases: Biological function, structural characteristics, and mechanism of catalysis
    • Z.-Y. Zhang Protein-tyrosine phosphatases: Biological function, structural characteristics, and mechanism of catalysis Crit. Rev. Biochem. Mol. Biol. 33 1998 1 52
    • (1998) Crit. Rev. Biochem. Mol. Biol. , vol.33 , pp. 1-52
    • Zhang, Z.-Y.1
  • 48
    • 0035313868 scopus 로고    scopus 로고
    • Combinatorial control of the specificity of protein tyrosine phosphatases
    • N.K. Tonks B.G. Neel Combinatorial control of the specificity of protein tyrosine phosphatases Curr. Opin. Cell Biol. 13 2001 182 195
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 182-195
    • Tonks, N.K.1    Neel, B.G.2
  • 49
    • 0027197067 scopus 로고
    • Mutations at the murine motheaten locus are within the hematopoietic cell protein tyrosine phosphatase (Hcph) gene
    • L.D. Shultz P.A. Schweitzer T.V. Rajan T. Yi J.N. Ihle R.J. Matthews M.L. Thomas D.R. Beier Mutations at the murine motheaten locus are within the hematopoietic cell protein tyrosine phosphatase ( Hcph ) gene Cell 73 1993 1445 1454
    • (1993) Cell , vol.73 , pp. 1445-1454
    • Shultz, L.D.1    Schweitzer, P.A.2    Rajan, T.V.3    Yi, T.4    Ihle, J.N.5    Matthews, R.J.6    Thomas, M.L.7    Beier, D.R.8
  • 50
    • 0028956353 scopus 로고
    • Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals
    • U. Klingmuller U. Lorenz L.C. Cantley B.G. Neel H.F. Lodish Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals Cell 80 1995 729 738
    • (1995) Cell , vol.80 , pp. 729-738
    • Klingmuller, U.1    Lorenz, U.2    Cantley, L.C.3    Neel, B.G.4    Lodish, H.F.5
  • 55
    • 0024416009 scopus 로고
    • Evidence that the leukocyte-common antigen is required for antigen-induced T lymphocyte proliferation
    • J.T. Pingel M.L. Thomas Evidence that the leukocyte-common antigen is required for antigen-induced T lymphocyte proliferation Cell 58 1989 1055 1065
    • (1989) Cell , vol.58 , pp. 1055-1065
    • Pingel, J.T.1    Thomas, M.L.2
  • 56
    • 0026630991 scopus 로고
    • Corkscrew encodes a putative protein tyrosine phosphatase that functions to transduce the terminal signal from the receptor tyrosine kinase torso
    • L.A. Perkins I. Larsen N. Perrimon Corkscrew encodes a putative protein tyrosine phosphatase that functions to transduce the terminal signal from the receptor tyrosine kinase torso Cell 70 1992 225 236
    • (1992) Cell , vol.70 , pp. 225-236
    • Perkins, L.A.1    Larsen, I.2    Perrimon, N.3
  • 57
    • 0028124504 scopus 로고
    • Role of SH-PTP2, a protein-tyrosine phosphatase with src homology 2 domains, in insulin-stimulated Ras activation
    • T. Noguchi T. Matozaki K. Horita Y. Fujioka M. Kasuga Role of SH-PTP2, a protein-tyrosine phosphatase with src homology 2 domains, in insulin-stimulated Ras activation Mol. Cell Biol. 14 1994 6674 6682
    • (1994) Mol. Cell Biol. , vol.14 , pp. 6674-6682
    • Noguchi, T.1    Matozaki, T.2    Horita, K.3    Fujioka, Y.4    Kasuga, M.5
  • 58
    • 0028122711 scopus 로고
    • Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 Å and the complex with tungstate
    • J.A. Stuckey H.L. Schubert E. Fauman Z.-Y. Zhang J.E. Dixon M.A. Saper Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 Å and the complex with tungstate Nature 370 1994 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
  • 59
    • 0028231388 scopus 로고
    • Crystal structure of human protein tyrosine phosphatase 1B
    • D. Barford A.J. Flint N.K. Tonks Crystal structure of human protein tyrosine phosphatase 1B Science 263 1994 1397 1404
    • (1994) Science , vol.263 , pp. 1397-1404
    • Barford, D.1    Flint, A.J.2    Tonks, N.K.3
  • 60
    • 0035265679 scopus 로고    scopus 로고
    • Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2
    • H. Song N. Hanlon N.R. Brown M.E. Noble L.N. Johnson D. Barford Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2 Mol. Cell 7 2001 615 626
    • (2001) Mol. Cell , vol.7 , pp. 615-626
    • Song, H.1    Hanlon, N.2    Brown, N.R.3    Noble, M.E.4    Johnson, L.N.5    Barford, D.6
  • 61
    • 0033615538 scopus 로고    scopus 로고
    • Crystal structure of the PTEN tumor suppressor: Implications for its phosphoinositide phosphatase activity and membrane association
    • J.O. Lee H. Yang M.M. Georgescu A. Di Cristofano T. Maehama Y. Shi J.E. Dixon P. Pandolfi N.P. Pavletich Crystal structure of the PTEN tumor suppressor: Implications for its phosphoinositide phosphatase activity and membrane association Cell 99 1999 323 334
    • (1999) Cell , vol.99 , pp. 323-334
    • Lee, J.O.1    Yang, H.2    Georgescu, M.M.3    Di Cristofano, A.4    Maehama, T.5    Shi, Y.6    Dixon, J.E.7    Pandolfi, P.8    Pavletich, N.P.9
  • 62
    • 0035873620 scopus 로고    scopus 로고
    • Structure and mechanism of the RNA triphosphatase component of mammalian mRNA capping enzyme
    • A. Changela C.K. Ho A. Martins S. Shuman A. Mondragon Structure and mechanism of the RNA triphosphatase component of mammalian mRNA capping enzyme EMBO J. 20 2001 2575 2586
    • (2001) EMBO J. , vol.20 , pp. 2575-2586
    • Changela, A.1    Ho, C.K.2    Martins, A.3    Shuman, S.4    Mondragon, A.5
  • 63
    • 0028016349 scopus 로고
    • Crystal structure of bovine heart phosphotyrosyl phosphatase at 2.2-Å resolution
    • M. Zhang R.L. Van Etten C.V. Stauffacher Crystal structure of bovine heart phosphotyrosyl phosphatase at 2.2-Å resolution Biochemistry 33 1994 11097 11105
    • (1994) Biochemistry , vol.33 , pp. 11097-11105
    • Zhang, M.1    Van Etten, R.L.2    Stauffacher, C.V.3
  • 64
    • 0025945823 scopus 로고
    • Evidence for protein-tyrosine phosphatase catalysis proceeding via a cysteine-phosphate intermediate
    • K.L. Guan J.E. Dixon Evidence for protein-tyrosine phosphatase catalysis proceeding via a cysteine-phosphate intermediate J. Biol. Chem. 266 1991 17026 17030
    • (1991) J. Biol. Chem. , vol.266 , pp. 17026-17030
    • Guan, K.L.1    Dixon, J.E.2
  • 65
    • 0029066496 scopus 로고
    • Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B
    • Z. Jia D. Barford A.J. Flint N.K. Tonks Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B Science 268 1995 1754 1758
    • (1995) Science , vol.268 , pp. 1754-1758
    • Jia, Z.1    Barford, D.2    Flint, A.J.3    Tonks, N.K.4
  • 66
    • 0028176050 scopus 로고
    • Dissecting the catalytic mechanism of protein tyrosine phosphatases
    • Z.-Y. Zhang Y. Wang J.E. Dixon Dissecting the catalytic mechanism of protein tyrosine phosphatases Proc. Natl. Acad. Sci. USA 91 1994 1624 1627
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1624-1627
    • Zhang, Z.-Y.1    Wang, Y.2    Dixon, J.E.3
  • 67
    • 0032500638 scopus 로고    scopus 로고
    • Molecular basis of substrate specificity of protein tyrosine phosphatase 1B
    • M. Sarmiento Y. Zhao S.J. Gordon Z.-Y. Zhang Molecular basis of substrate specificity of protein tyrosine phosphatase 1B J. Biol. Chem. 273 1998 26368 26374
    • (1998) J. Biol. Chem. , vol.273 , pp. 26368-26374
    • Sarmiento, M.1    Zhao, Y.2    Gordon, S.J.3    Zhang, Z.-Y.4
  • 69
    • 0030028068 scopus 로고    scopus 로고
    • The active-site specificity of the Yersinia protein-tyrosine phosphatase
    • D. Dunn L. Chen D.S. Lawrence Z.-Y. Zhang The active-site specificity of the Yersinia protein-tyrosine phosphatase J. Biol. Chem. 271 1996 168 173
    • (1996) J. Biol. Chem. , vol.271 , pp. 168-173
    • Dunn, D.1    Chen, L.2    Lawrence, D.S.3    Zhang, Z.-Y.4
  • 70
    • 0032910476 scopus 로고    scopus 로고
    • Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation
    • A.E. Stewart S. Dowd S.M. Keyse N.Q. McDonald Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation Nat. Struct. Biol. 6 1999 174 181
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 174-181
    • Stewart, A.E.1    Dowd, S.2    Keyse, S.M.3    McDonald, N.Q.4
  • 71
    • 0018881742 scopus 로고
    • Enzyme-catalyzed phosphoryl transfer reactions
    • J.R. Knowles Enzyme-catalyzed phosphoryl transfer reactions Annu. Rev. Biochem. 49 1980 877 919
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 877-919
    • Knowles, J.R.1
  • 72
    • 0025777694 scopus 로고
    • Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis
    • E.E. Kim H.W. Wyckoff Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis J. Mol. Biol. 218 1991 449 464
    • (1991) J. Mol. Biol. , vol.218 , pp. 449-464
    • Kim, E.E.1    Wyckoff, H.W.2
  • 73
    • 0026773209 scopus 로고
    • Structure and mechanism of alkaline phosphatase
    • J.E. Coleman Structure and mechanism of alkaline phosphatase Annu. Rev. Biophys. Biomol. Struct. 21 1992 441 483
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 441-483
    • Coleman, J.E.1
  • 74
    • 0020331699 scopus 로고
    • Human prostatic acid phosphatase: A histidine phosphatase
    • R.L. Van Etten Human prostatic acid phosphatase: A histidine phosphatase Ann. N.Y. Acad. Sci. 390 1982 27 51
    • (1982) Ann. N.Y. Acad. Sci. , vol.390 , pp. 27-51
    • Van Etten, R.L.1
  • 75
    • 0015748815 scopus 로고
    • A borohydride reduction method for characterization of the acyl phosphate linkage in proteins and its application to sarcoplasmic reticulum adenosine triphosphatase
    • C. Degani P.D. Boyer A borohydride reduction method for characterization of the acyl phosphate linkage in proteins and its application to sarcoplasmic reticulum adenosine triphosphatase J. Biol. Chem. 248 1973 8222 8226
    • (1973) J. Biol. Chem. , vol.248 , pp. 8222-8226
    • Degani, C.1    Boyer, P.D.2
  • 76
    • 0033378614 scopus 로고    scopus 로고
    • Structural studies of reversible protein phosphorylation and protein phosphatases
    • D. Barford Structural studies of reversible protein phosphorylation and protein phosphatases Biochem. Soc. Trans. 27 1999 751 766
    • (1999) Biochem. Soc. Trans. , vol.27 , pp. 751-766
    • Barford, D.1
  • 77
    • 0028155865 scopus 로고
    • Protein tyrosine phosphatases: Mechanism of catalysis and substrate specificity
    • Z.-Y. Zhang J.E. Dixon Protein tyrosine phosphatases: Mechanism of catalysis and substrate specificity Adv. Enzymol. 68 1994 1 36
    • (1994) Adv. Enzymol. , vol.68 , pp. 1-36
    • Zhang, Z.-Y.1    Dixon, J.E.2
  • 78
    • 85176160163 scopus 로고
    • Z.-Y. Zhang Mechanistic and kinetic studies of the bovine heart low molecular weight phosphotyrosyl protein phosphatase 1990 Purdue University West Lafayette, IN Ph.D. Thesis
    • (1990)
    • Zhang, Z.-Y.1
  • 79
    • 0026528237 scopus 로고
    • Cloning, expression, and catalytic mechanism of a low molecular weight phosphotyrosyl protein phosphatase from bovine heart
    • Y.-Y.P. Wo M.-M. Zhou P. Stevis J.P. Davis Z.-Y. Zhang R.L. Van Etten Cloning, expression, and catalytic mechanism of a low molecular weight phosphotyrosyl protein phosphatase from bovine heart Biochemistry 31 1992 1712 1721
    • (1992) Biochemistry , vol.31 , pp. 1712-1721
    • Wo, Y.-Y.P.1    Zhou, M.-M.2    Stevis, P.3    Davis, J.P.4    Zhang, Z.-Y.5    Van Etten, R.L.6
  • 80
    • 0000630849 scopus 로고
    • Isolation and structural elucidation of a novel phosphocysteine intermediate in the LAR protein tyrosine phosphatase enzymatic pathway
    • H. Cho R. Krishnaraj E. Kitas W. Bannwarth C.T. Walsh K.S. Anderson Isolation and structural elucidation of a novel phosphocysteine intermediate in the LAR protein tyrosine phosphatase enzymatic pathway J. Am. Chem. Soc. 114 1992 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
  • 81
    • 0028171416 scopus 로고
    • The catalytic role of Cys124 in the dual specificity phosphatase VHR
    • G. Zhou J.M. Denu L. Wu J.E. Dixon The catalytic role of Cys124 in the dual specificity phosphatase VHR J. Biol. Chem. 269 1994 28084 28090
    • (1994) J. Biol. Chem. , vol.269 , pp. 28084-28090
    • Zhou, G.1    Denu, J.M.2    Wu, L.3    Dixon, J.E.4
  • 82
    • 0034634475 scopus 로고    scopus 로고
    • Mechanism of phosphoanhydride cleavage by baculovirus phosphatase
    • A. Martins S. Shuman Mechanism of phosphoanhydride cleavage by baculovirus phosphatase J. Biol. Chem. 275 2000 35070 35076
    • (2000) J. Biol. Chem. , vol.275 , pp. 35070-35076
    • Martins, A.1    Shuman, S.2
  • 83
    • 0035943595 scopus 로고    scopus 로고
    • The mechanism of dephosphorylation of extracellular signal-regulated kinase 2 by mitogen-activated protein kinase phosphatase 3
    • Y Zhao Z.-Y. Zhang The mechanism of dephosphorylation of extracellular signal-regulated kinase 2 by mitogen-activated protein kinase phosphatase 3 J. Biol. Chem. 276 2001 32382 32391
    • (2001) J. Biol. Chem. , vol.276 , pp. 32382-32391
    • Zhao, Y1    Zhang, Z.-Y.2
  • 84
    • 0029917244 scopus 로고    scopus 로고
    • Visualization of intermediate and transition-state structures in protein-tyrosine phosphatase catalysis
    • J.M. Denu D.L. Lohse J. Vijayalakshmi M.A. Saper J.E. Dixon Visualization of intermediate and transition-state structures in protein-tyrosine phosphatase catalysis Proc. Natl. Acad. Sci. USA 93 1996 2493 2498
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2493-2498
    • Denu, J.M.1    Lohse, D.L.2    Vijayalakshmi, J.3    Saper, M.A.4    Dixon, J.E.5
  • 86
    • 2642679682 scopus 로고
    • Thiophosphates as possible intermediates in phosphate transfer
    • E.O'F. Walsh Thiophosphates as possible intermediates in phosphate transfer Nature 169 1952 546
    • (1952) Nature , vol.169 , pp. 546
    • Walsh, E.O'F.1
  • 87
    • 1842323661 scopus 로고
    • Phosphate esters
    • T.C. Bruice S.J. Benkovic Phosphate esters “Bioorganic Mechanisms” Vol. II 1966 Benjamin New York 1 103
    • (1966) , pp. 1-103
    • Bruice, T.C.1    Benkovic, S.J.2
  • 88
    • 0025976707 scopus 로고
    • Pre-steady-state and steady-state kinetic analysis of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart
    • Z.-Y. Zhang R.L. Van Etten Pre-steady-state and steady-state kinetic analysis of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart J. Biol. Chem. 266 1991 1516 1525
    • (1991) J. Biol. Chem. , vol.266 , pp. 1516-1525
    • Zhang, Z.-Y.1    Van Etten, R.L.2
  • 89
    • 0028239771 scopus 로고
    • The nature of the rate-determining steps of the Yersinia protein tyrosine phosphatase-catalyzed reactions
    • Z.-Y. Zhang W.P. Malachowski R.L. Van Etten J.E. Dixon The nature of the rate-determining steps of the Yersinia protein tyrosine phosphatase-catalyzed reactions J. Biol. Chem. 269 1994 8140 8145
    • (1994) J. Biol. Chem. , vol.269 , pp. 8140-8145
    • Zhang, Z.-Y.1    Malachowski, W.P.2    Van Etten, R.L.3    Dixon, J.E.4
  • 90
    • 0029015718 scopus 로고
    • Kinetic and mechanistic characterization of a mammalian protein tyrosine phosphatase, PTP1
    • Z.-Y. Zhang Kinetic and mechanistic characterization of a mammalian protein tyrosine phosphatase, PTP1 J. Biol. Chem. 270 1995 11199 11204
    • (1995) J. Biol. Chem. , vol.270 , pp. 11199-11204
    • Zhang, Z.-Y.1
  • 91
    • 0018727622 scopus 로고
    • Product inhibition and abortive complex formation
    • F.B. Rudolph Product inhibition and abortive complex formation Methods Enzymol. 63 1979 411 436
    • (1979) Methods Enzymol. , vol.63 , pp. 411-436
    • Rudolph, F.B.1
  • 92
    • 0026063177 scopus 로고
    • Leaving group dependence and proton inventory studies of the phosphorylation of a cytoplasmic phosphotyrosyl protein phosphatase from bovine heart
    • Z.-Y. Zhang R.L. Van Etten Leaving group dependence and proton inventory studies of the phosphorylation of a cytoplasmic phosphotyrosyl protein phosphatase from bovine heart Biochemistry 30 1991 8954 8959
    • (1991) Biochemistry , vol.30 , pp. 8954-8959
    • Zhang, Z.-Y.1    Van Etten, R.L.2
  • 93
    • 0027215589 scopus 로고
    • A continuous spectrophotometric and fluorimetric assay for protein tyrosine phosphatase using phosphotyrosine containing peptides
    • Z.-Y. Zhang A.M. Thieme-Sefler D. Maclean R. Roeske J.E. Dixon A continuous spectrophotometric and fluorimetric assay for protein tyrosine phosphatase using phosphotyrosine containing peptides Anal. Biochem. 211 1993 7 15
    • (1993) Anal. Biochem. , vol.211 , pp. 7-15
    • Zhang, Z.-Y.1    Thieme-Sefler, A.M.2    Maclean, D.3    Roeske, R.4    Dixon, J.E.5
  • 95
    • 0028298024 scopus 로고
    • Protein tyrosine phosphatase substrate specificity: The minimum size of the peptide and the positioning of the phosphotyrosine
    • Z.-Y. Zhang D. Maclean D.J. McNamara T.K. Sawyer J.E. Dixon Protein tyrosine phosphatase substrate specificity: The minimum size of the peptide and the positioning of the phosphotyrosine Biochemistry 33 1994 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
  • 97
    • 0027383705 scopus 로고
    • Active site labeling of the Yersinia protein tyrosine phosphatase: The determination of the pKa of the active site cysteine and the function of the conserved histidine 402
    • a of the active site cysteine and the function of the conserved histidine 402 Biochemistry 32 1993 9340 9345
    • (1993) Biochemistry , vol.32 , pp. 9340-9345
    • Zhang, Z.-Y.1    Dixon, J.E.2
  • 99
    • 0029584325 scopus 로고
    • Catalytic function of the conserved hydroxyl group in the protein-tyrosine phosphatase signature motif
    • Z.-Y. Zhang B.A. Palfey L. Wu Y. Zhao Catalytic function of the conserved hydroxyl group in the protein-tyrosine phosphatase signature motif Biochemistry 34 1995 16389 16396
    • (1995) Biochemistry , vol.34 , pp. 16389-16396
    • Zhang, Z.-Y.1    Palfey, B.A.2    Wu, L.3    Zhao, Y.4
  • 100
    • 0028871944 scopus 로고
    • Nature of the transition state of the protein-tyrosine phosphatase-catalyzed reaction
    • A.C. Hengge G. Sowa L. Wu Z.-Y. Zhang Nature of the transition state of the protein-tyrosine phosphatase-catalyzed reaction Biochemistry 34 1995 13982 13987
    • (1995) Biochemistry , vol.34 , pp. 13982-13987
    • Hengge, A.C.1    Sowa, G.2    Wu, L.3    Zhang, Z.-Y.4
  • 101
    • 0031024565 scopus 로고    scopus 로고
    • The single sulfur to oxygen substitution in the active site nucleophile of the Yersinia protein-tyrosine phosphatase leads to substantial structural and functional perturbations
    • Z.-Y. Zhang L. Wu The single sulfur to oxygen substitution in the active site nucleophile of the Yersinia protein-tyrosine phosphatase leads to substantial structural and functional perturbations Biochemistry 36 1997 1362 1369
    • (1997) Biochemistry , vol.36 , pp. 1362-1369
    • Zhang, Z.-Y.1    Wu, L.2
  • 103
    • 0032489458 scopus 로고    scopus 로고
    • Altering the nucleophile specificity of a protein-tyrosine phosphatase-catalyzed reaction: Probing the function of the invariant glutamine residues
    • Y. Zhao L. Wu S.J. Noh K.-L. Guan Z.-Y. Zhang Altering the nucleophile specificity of a protein-tyrosine phosphatase-catalyzed reaction: Probing the function of the invariant glutamine residues J. Biol. Chem. 273 1998 5484 5492
    • (1998) J. Biol. Chem. , vol.273 , pp. 5484-5492
    • Zhao, Y.1    Wu, L.2    Noh, S.J.3    Guan, K.-L.4    Zhang, Z.-Y.5
  • 104
    • 0032480809 scopus 로고    scopus 로고
    • Conformational and dynamic changes of Yersinia protein tyrosine phosphatase induced by ligand binding and active site mutation and revealed by H⧸D exchange and electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry
    • F. Wang W. Li M.R. Emmett C.L. Hendrickson A.G. Marshall Y.-L. Zhang L. Wu Z.-Y. Zhang Conformational and dynamic changes of Yersinia protein tyrosine phosphatase induced by ligand binding and active site mutation and revealed by H⧸D exchange and electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry Biochemistry 37 1998 15289 15299
    • (1998) Biochemistry , vol.37 , pp. 15289-15299
    • Wang, F.1    Li, W.2    Emmett, M.R.3    Hendrickson, C.L.4    Marshall, A.G.5    Zhang, Y.-L.6    Wu, L.7    Zhang, Z.-Y.8
  • 105
    • 0033083853 scopus 로고    scopus 로고
    • Probing the function of the invariant tryptophan in the flexible loop of the Yersinia protein-tyrosine phosphatase
    • Y.-F. Keng L. Wu Z.-Y. Zhang Probing the function of the invariant tryptophan in the flexible loop of the Yersinia protein-tyrosine phosphatase Eur. J. Biochem. 259 1999 809 814
    • (1999) Eur. J. Biochem. , vol.259 , pp. 809-814
    • Keng, Y.-F.1    Wu, L.2    Zhang, Z.-Y.3
  • 106
    • 0033554393 scopus 로고    scopus 로고
    • Impaired transition state complementarity in the hydrolysis of O-arylphosphorothioates by protein-tyrosine phosphatases
    • Y.-L. Zhang F. Hollfelder S.J. Gordon L. Chen Y.-F. Keng L. Wu D. Herschlag Z.-Y. Zhang Impaired transition state complementarity in the hydrolysis of O -arylphosphorothioates by protein-tyrosine phosphatases Biochemistry 38 1999 12111 12123
    • (1999) Biochemistry , vol.38 , pp. 12111-12123
    • Zhang, Y.-L.1    Hollfelder, F.2    Gordon, S.J.3    Chen, L.4    Keng, Y.-F.5    Wu, L.6    Herschlag, D.7    Zhang, Z.-Y.8
  • 107
    • 0032731882 scopus 로고    scopus 로고
    • Does positive charge at the active site of a phosphatase cause a change in mechanism? The effect of the conserved arginine on the transition state for enzymatic phosphoryl transfer in the protein-tyrosine phosphatase from Yersinia
    • R.H. Hoff L. Wu B. Zhou Z.-Y. Zhang A.C. Hengge Does positive charge at the active site of a phosphatase cause a change in mechanism? The effect of the conserved arginine on the transition state for enzymatic phosphoryl transfer in the protein-tyrosine phosphatase from Yersinia J. Am. Chem. Soc. 121 1999 9514 9521
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9514-9521
    • Hoff, R.H.1    Wu, L.2    Zhou, B.3    Zhang, Z.-Y.4    Hengge, A.C.5
  • 108
    • 0034635121 scopus 로고    scopus 로고
    • The effects on general acid catalysis from mutations of the invariant tryptophan and arginine residues in the protein-tyrosine phosphatase from Yersinia
    • R.H. Hoff A.C. Hengge L. Wu Y.-F. Keng Z.-Y. Zhang The effects on general acid catalysis from mutations of the invariant tryptophan and arginine residues in the protein-tyrosine phosphatase from Yersinia Biochemistry 39 2000 46 54
    • (2000) Biochemistry , vol.39 , pp. 46-54
    • Hoff, R.H.1    Hengge, A.C.2    Wu, L.3    Keng, Y.-F.4    Zhang, Z.-Y.5
  • 109
    • 0037035541 scopus 로고    scopus 로고
    • Is PTPase-vanadate a true transition state analog?
    • H. Deng R. Callender Z. Huang Z.-Y. Zhang Is PTPase-vanadate a true transition state analog? Biochemistry 41 2002 5865 5872
    • (2002) Biochemistry , vol.41 , pp. 5865-5872
    • Deng, H.1    Callender, R.2    Huang, Z.3    Zhang, Z.-Y.4
  • 110
    • 0029005759 scopus 로고
    • Are protein-tyrosine phosphatases specific for phosphotyrosine?
    • Z.-Y. Zhang Are protein-tyrosine phosphatases specific for phosphotyrosine? J. Biol. Chem. 270 1995 16052 16055
    • (1995) J. Biol. Chem. , vol.270 , pp. 16052-16055
    • Zhang, Z.-Y.1
  • 111
    • 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
    • D.L. Lohse J.M. Denu N. Santoro J.E. Dixon Roles of aspartic acid-181 and serine-222 in intermediate formation and hydrolysis of the mammalian protein-tyrosine-phosphatase PTP1 Biochemistry 36 1997 4568 4575
    • (1997) Biochemistry , vol.36 , pp. 4568-4575
    • Lohse, D.L.1    Denu, J.M.2    Santoro, N.3    Dixon, J.E.4
  • 112
    • 0034602144 scopus 로고    scopus 로고
    • Thermodynamic study of ligand binding to protein-tyrosine phosphatase 1B and its substrate-trapping mutants
    • Y.-L. Zhang Z.-J. Yao M. Sarmiento L. Wu T.R. Burke Jr. Z.-Y. Zhang Thermodynamic study of ligand binding to protein-tyrosine phosphatase 1B and its substrate-trapping mutants J. Biol. Chem. 275 2000 34205 34212
    • (2000) J. Biol. Chem. , vol.275 , pp. 34205-34212
    • Zhang, Y.-L.1    Yao, Z.-J.2    Sarmiento, M.3    Wu, L.4    Burke, T.R.5    Zhang, Z.-Y.6
  • 113
    • 0037177212 scopus 로고    scopus 로고
    • Design and characterization of an improved protein tyrosine phosphatase substrate-trapping mutant
    • L. Xie Y.-L. Zhang Z.-Y. Zhang Design and characterization of an improved protein tyrosine phosphatase substrate-trapping mutant Biochemistry 41 2002 4032 4039
    • (2002) Biochemistry , vol.41 , pp. 4032-4039
    • Xie, L.1    Zhang, Y.-L.2    Zhang, Z.-Y.3
  • 114
    • 0037174872 scopus 로고    scopus 로고
    • Probing the molecular basis for potent and selective PTP1B inhibition
    • X.-L. Guo K. Shen F. Wang D.S. Lawrence Z.-Y. Zhang Probing the molecular basis for potent and selective PTP1B inhibition J. Biol. Chem. 277 2002 41014 41022
    • (2002) J. Biol. Chem. , vol.277 , pp. 41014-41022
    • Guo, X.-L.1    Shen, K.2    Wang, F.3    Lawrence, D.S.4    Zhang, Z.-Y.5
  • 115
    • 0030956238 scopus 로고    scopus 로고
    • Comparative kinetic analysis and substrate specificity of the tandem catalytic domains of the receptor-like protein-tyrosine phosphatase α
    • L. Wu A. Buist J. den Hertog Z.-Y. Zhang Comparative kinetic analysis and substrate specificity of the tandem catalytic domains of the receptor-like protein-tyrosine phosphatase α J. Biol. Chem. 272 1997 6994 7002
    • (1997) J. Biol. Chem. , vol.272 , pp. 6994-7002
    • Wu, L.1    Buist, A.2    den Hertog, J.3    Zhang, Z.-Y.4
  • 116
    • 0033579927 scopus 로고    scopus 로고
    • Restoration of potent protein-tyrosine phosphatase activity into the membrane-distal domain of receptor protein-tyrosine phosphatase α
    • A. Buist Y.-L. Zhang Y.-F. Keng L. Wu Z.-Y. Zhang J. den Hertog Restoration of potent protein-tyrosine phosphatase activity into the membrane-distal domain of receptor protein-tyrosine phosphatase α Biochemistry 38 1999 914 922
    • (1999) Biochemistry , vol.38 , pp. 914-922
    • Buist, A.1    Zhang, Y.-L.2    Keng, Y.-F.3    Wu, L.4    Zhang, Z.-Y.5    den Hertog, J.6
  • 117
    • 0029043627 scopus 로고
    • A catalytic mechanism for the dual-specific phosphatases
    • J.M. Denu J.E. Dixon A catalytic mechanism for the dual-specific phosphatases Proc. Natl. Acad. Sci. USA 92 1995 5910 5914
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5910-5914
    • Denu, J.M.1    Dixon, J.E.2
  • 118
    • 0028903589 scopus 로고
    • The catalytic role of aspartic acid-92 in a human dual-specific protein-tyrosine-phosphatase
    • J.M. Denu G. Zhou Y. Guo J.E. Dixon The catalytic role of aspartic acid-92 in a human dual-specific protein-tyrosine-phosphatase Biochemistry 34 1995 3396 3403
    • (1995) Biochemistry , vol.34 , pp. 3396-3403
    • Denu, J.M.1    Zhou, G.2    Guo, Y.3    Dixon, J.E.4
  • 119
    • 0028858055 scopus 로고
    • Transition state and rate-limiting step of the reaction catalyzed by the human dual specificity phosphatase, VHR
    • Z.-Y. Zhang L. Wu L. Chen Transition state and rate-limiting step of the reaction catalyzed by the human dual specificity phosphatase, VHR Biochemistry 34 1995 16088 16096
    • (1995) Biochemistry , vol.34 , pp. 16088-16096
    • Zhang, Z.-Y.1    Wu, L.2    Chen, L.3
  • 120
    • 0029994512 scopus 로고    scopus 로고
    • Transition-state structures for the native dual-specific phosphatase VHR and D92N and S131A mutants. Contributions to the driving force for catalysis
    • A.C. Hengge J.M. Denu J.E. Dixon Transition-state structures for the native dual-specific phosphatase VHR and D92N and S131A mutants. Contributions to the driving force for catalysis Biochemistry 35 1996 7084 7092
    • (1996) Biochemistry , vol.35 , pp. 7084-7092
    • Hengge, A.C.1    Denu, J.M.2    Dixon, J.E.3
  • 122
    • 0029868796 scopus 로고    scopus 로고
    • Probing the function of Asp128 in the low molecular weight protein-tyrosine phosphatase catalyzed reaction. A pre-steady-state and steady-state kinetic investigation
    • L. Wu Z.-Y. Zhang Probing the function of Asp128 in the low molecular weight protein-tyrosine phosphatase catalyzed reaction. A pre-steady-state and steady-state kinetic investigation Biochemistry 35 1996 5426 5434
    • (1996) Biochemistry , vol.35 , pp. 5426-5434
    • Wu, L.1    Zhang, Z.-Y.2
  • 123
    • 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
    • Y. Zhao Z.-Y. Zhang Reactivity of alcohols toward the phosphoenzyme intermediate in the protein-tyrosine phosphatase-catalyzed reaction: Probing the transition state of the dephosphorylation step Biochemistry 35 1996 11797 11804
    • (1996) Biochemistry , vol.35 , pp. 11797-11804
    • Zhao, Y.1    Zhang, Z.-Y.2
  • 124
    • 0030804063 scopus 로고    scopus 로고
    • Examination of the transition state of the low molecular mass small tyrosine phosphatase 1. Comparisons with other protein phosphatases
    • A.C. Hengge Y. Zhao L. Wu Z.-Y. Zhang Examination of the transition state of the low molecular mass small tyrosine phosphatase 1. Comparisons with other protein phosphatases Biochemistry 36 1997 7928 7936
    • (1997) Biochemistry , vol.36 , pp. 7928-7936
    • Hengge, A.C.1    Zhao, Y.2    Wu, L.3    Zhang, Z.-Y.4
  • 125
    • 0025277449 scopus 로고
    • Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR
    • M. Streuli N.X. Krueger T. Thai M. Tang H. Saito Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR EMBO J. 9 1990 2399 2407
    • (1990) EMBO J. , vol.9 , pp. 2399-2407
    • Streuli, M.1    Krueger, N.X.2    Thai, T.3    Tang, M.4    Saito, H.5
  • 126
    • 0025024995 scopus 로고
    • Protein tyrosine phosphatase activity of an essential virulence determinant in Yersinia
    • K.L. Guan J.E. Dixon Protein tyrosine phosphatase activity of an essential virulence determinant in Yersinia Science 249 1990 553 556
    • (1990) Science , vol.249 , pp. 553-556
    • Guan, K.L.1    Dixon, J.E.2
  • 128
    • 0027314525 scopus 로고
    • The role of Cys12, Cys17 and Arg18 in the catalytic mechanism of low-Mr cytosolic phosphotyrosine protein phosphatase
    • P. Cirri P. Chiarugi G. Camici G. Manao G. Raugei G. Cappugi G. Ramponi The role of Cys12, Cys17 and Arg18 in the catalytic mechanism of low-Mr cytosolic phosphotyrosine protein phosphatase Eur. J. Biochem. 214 1993 647 657
    • (1993) Eur. J. Biochem. , vol.214 , pp. 647-657
    • Cirri, P.1    Chiarugi, P.2    Camici, G.3    Manao, G.4    Raugei, G.5    Cappugi, G.6    Ramponi, G.7
  • 129
    • 0026038524 scopus 로고
    • Cloning, bacterial expression, purification, and characterization of the cytoplasmic domain of rat LAR, a receptor-like protein tyrosine phosphatase
    • D.A. Pot T.A. Woodford E. Remboutsika R.S. Haun J.E. Dixon Cloning, bacterial expression, purification, and characterization of the cytoplasmic domain of rat LAR, a receptor-like protein tyrosine phosphatase J. Biol. Chem. 266 1991 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
  • 130
    • 0028030520 scopus 로고
    • The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase
    • X.D. Su N. Taddei M. Stefani G. Ramponi P. Nordlund The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase Nature 370 1994 575 578
    • (1994) Nature , vol.370 , pp. 575-578
    • Su, X.D.1    Taddei, N.2    Stefani, M.3    Ramponi, G.4    Nordlund, P.5
  • 131
    • 0027358722 scopus 로고
    • MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo
    • H. Sun C.H. Charles L.F. Lau N.K. Tonks MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo Cell 75 1993 487 493
    • (1993) Cell , vol.75 , pp. 487-493
    • Sun, H.1    Charles, C.H.2    Lau, L.F.3    Tonks, N.K.4
  • 132
    • 0030913232 scopus 로고    scopus 로고
    • Identification of p130Cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions
    • D.S. Black J.B. Bliska Identification of p130Cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions EMBO J. 16 1997 2730 2744
    • (1997) EMBO J. , vol.16 , pp. 2730-2744
    • Black, D.S.1    Bliska, J.B.2
  • 133
    • 0031457541 scopus 로고    scopus 로고
    • Identification of a second ary1 phosphate-binding site in protein-tyrosine phosphatase 1B: A paradigm for inhibitor design
    • Y.A. Puius Y. Zhao M. Sullivan D.S. Lawrence S.C. Almo Z.-Y. Zhang Identification of a second ary1 phosphate-binding site in protein-tyrosine phosphatase 1B: A paradigm for inhibitor design Proc. Natl. Acad. Sci. USA 94 1997 13420 13425
    • (1997) Proc. Natl. Acad. Sci. USA , 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
  • 134
    • 0029091493 scopus 로고
    • A ligand-induced conformational change in the Yersinia protein tyrosine phosphatase
    • H.L. Schubert E.B. Fauman J.A. Stuckey J.E. Dixon M.A. Saper A ligand-induced conformational change in the Yersinia protein tyrosine phosphatase Protein Sci. 4 1995 1904 1913
    • (1995) Protein Sci. , vol.4 , pp. 1904-1913
    • Schubert, H.L.1    Fauman, E.B.2    Stuckey, J.A.3    Dixon, J.E.4    Saper, M.A.5
  • 135
    • 0032524855 scopus 로고    scopus 로고
    • Suramin is an active site-directed, reversible, and tight-binding inhibitor of protein-tyrosine phosphatases
    • Y.-L. Zhang Y.-F. Keng Y. Zhao L. Wu Z.-Y. Zhang Suramin is an active site-directed, reversible, and tight-binding inhibitor of protein-tyrosine phosphatases J. Biol. Chem. 273 1998 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
  • 136
    • 0034926053 scopus 로고    scopus 로고
    • The structure of apo protein-tyrosine phosphatase 1B C215S mutant: More than just an S → O change
    • G. Scapin S. Patel V. Patel B. Kennedy E. Asante-Appiah The structure of apo protein-tyrosine phosphatase 1B C215S mutant: More than just an S → O change Protein Sci. 10 2001 1596 1605
    • (2001) Protein Sci. , vol.10 , pp. 1596-1605
    • Scapin, G.1    Patel, S.2    Patel, V.3    Kennedy, B.4    Asante-Appiah, E.5
  • 137
    • 0026779225 scopus 로고
    • Mutational analysis of CD45, a leukocyte-specific protein tyrosine phosphatase
    • P. Johnson H.L. Ostergaard C. Wasden I.S. Trowbridge Mutational analysis of CD45, a leukocyte-specific protein tyrosine phosphatase J. Biol. Chem. 267 1992 8035 8041
    • (1992) J. Biol. Chem. , vol.267 , pp. 8035-8041
    • Johnson, P.1    Ostergaard, H.L.2    Wasden, C.3    Trowbridge, I.S.4
  • 138
    • 0031055324 scopus 로고    scopus 로고
    • Development of “substrate- trapping” mutants to identify physiological substrates of protein tyrosine phosphatases
    • A.J. Flint T. Taganis D. Barford N.K. Tonks Development of “substrate- trapping” mutants to identify physiological substrates of protein tyrosine phosphatases Proc. Natl. Acad. Sci. USA 94 1997 1680 1685
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1680-1685
    • Flint, A.J.1    Taganis, T.2    Barford, D.3    Tonks, N.K.4
  • 139
    • 0042432661 scopus 로고
    • Biochemical importance of the binding of phosphate by arginyl groups. Model compounds containing methylguanidinium ion
    • F.A. Cotton E.E. Hazen Jr. V.W. Day S. Larsen J.G. Norman Jr. S.T.K. Wong K.H. Johnson Biochemical importance of the binding of phosphate by arginyl groups. Model compounds containing methylguanidinium ion J. Am. Chem. Soc. 95 1973 2367 2369
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 2367-2369
    • Cotton, F.A.1    Hazen, E.E.2    Day, V.W.3    Larsen, S.4    Norman, J.G.5    Wong, S.T.K.6    Johnson, K.H.7
  • 140
    • 0028172937 scopus 로고
    • Asp129 of low molecular weight protein tyrosine phosphatase is involved in leaving group protonation
    • Z. Zhang E. Harms R.L. Van Etten Asp129 of low molecular weight protein tyrosine phosphatase is involved in leaving group protonation J. Biol. Chem. 269 1994 25947 25950
    • (1994) J. Biol. Chem. , vol.269 , pp. 25947-25950
    • Zhang, Z.1    Harms, E.2    Van Etten, R.L.3
  • 141
    • 0028018098 scopus 로고
    • Aspartic-129 is an essential residue in the catalytic mechanism of the low M(r) phosphotyrosine protein phosphatase
    • N. Taddei P. Chiarugi P. Cirri T. Fiaschi M. Stefani G. Camici G. Raugei G. Ramponi Aspartic-129 is an essential residue in the catalytic mechanism of the low M(r) phosphotyrosine protein phosphatase FEBS Lett. 350 1994 328 332
    • (1994) FEBS Lett. , vol.350 , pp. 328-332
    • Taddei, N.1    Chiarugi, P.2    Cirri, P.3    Fiaschi, T.4    Stefani, M.5    Camici, G.6    Raugei, G.7    Ramponi, G.8
  • 142
    • 0032562586 scopus 로고    scopus 로고
    • Visualization of the cysteinyl-phosphate intermediate of a protein-tyrosine phosphatase by x-ray crystallography
    • A.D. Pannifer A.J. Flint N.K. Tonks D. Barford Visualization of the cysteinyl-phosphate intermediate of a protein-tyrosine phosphatase by x-ray crystallography J. Biol. Chem. 273 1998 10454 10462
    • (1998) J. Biol. Chem. , vol.273 , pp. 10454-10462
    • Pannifer, A.D.1    Flint, A.J.2    Tonks, N.K.3    Barford, D.4
  • 143
    • 0031021981 scopus 로고    scopus 로고
    • Crystal structure of bovine low molecular weight phosphotyrosyl phosphatase complexed with the transition state analog vanadate
    • M. Zhang M. Zhou R.L. Van Etten C.V. Stauffacher Crystal structure of bovine low molecular weight phosphotyrosyl phosphatase complexed with the transition state analog vanadate Biochemistry 36 1997 15 23
    • (1997) Biochemistry , vol.36 , pp. 15-23
    • Zhang, M.1    Zhou, M.2    Van Etten, R.L.3    Stauffacher, C.V.4
  • 146
    • 0029780526 scopus 로고    scopus 로고
    • The X-ray crystal structures of Yersinia tyrosine phosphatase with bound tungstate and nitrate
    • E.B. Fauman C. Yuvaniyama H.L. Schubert J.A. Stuckey M.A. Saper The X-ray crystal structures of Yersinia tyrosine phosphatase with bound tungstate and nitrate J. Biol. Chem. 271 1996 18780 18788
    • (1996) J. Biol. Chem. , vol.271 , pp. 18780-18788
    • Fauman, E.B.1    Yuvaniyama, C.2    Schubert, H.L.3    Stuckey, J.A.4    Saper, M.A.5
  • 147
    • 0026471741 scopus 로고
    • The Yersinia tyrosine phosphatase: Specificity of a bacterial virulence determinant for phosphoproteins in the J774A.1 macrophage
    • J.B. Bliska J.C. Clemens J.E. Dixon S. Falkow The Yersinia tyrosine phosphatase: Specificity of a bacterial virulence determinant for phosphoproteins in the J774A.1 macrophage J. Exp. Med. 176 1992 1625 1630
    • (1992) J. Exp. Med. , vol.176 , pp. 1625-1630
    • Bliska, J.B.1    Clemens, J.C.2    Dixon, J.E.3    Falkow, S.4
  • 149
    • 0029826289 scopus 로고    scopus 로고
    • Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST
    • A.J. Garton A.J. Flint N.K. Tonks Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST Mol. Cell Biol. 16 1996 6408 6418
    • (1996) Mol. Cell Biol. , vol.16 , pp. 6408-6418
    • Garton, A.J.1    Flint, A.J.2    Tonks, N.K.3
  • 150
    • 0029856493 scopus 로고    scopus 로고
    • Direct binding of the proline-rich region of protein tyrosine phosphatase 1B to the Src homology 3 domain of p130(Cas)
    • F. Liu D.E. Hill J. Chernoff Direct binding of the proline-rich region of protein tyrosine phosphatase 1B to the Src homology 3 domain of p130(Cas) J. Biol. Chem. 271 1996 31290 31295
    • (1996) J. Biol. Chem. , vol.271 , pp. 31290-31295
    • Liu, F.1    Hill, D.E.2    Chernoff, J.3
  • 151
    • 0034616884 scopus 로고    scopus 로고
    • Identification of p130cas as an in vivo substrate of receptor protein-tyrosine phosphatase alpha
    • A. Buist C. Blanchetot L.G. Tertoolen J. den Hertog Identification of p130cas as an in vivo substrate of receptor protein-tyrosine phosphatase alpha J. Biol. Chem. 275 2000 20754 20761
    • (2000) J. Biol. Chem. , vol.275 , pp. 20754-20761
    • Buist, A.1    Blanchetot, C.2    Tertoolen, L.G.3    den Hertog, J.4
  • 152
    • 0033055089 scopus 로고    scopus 로고
    • Transmembrane tyrosine phosphatase LAR induces apoptosis by dephosphorylating and destabilizing p130Cas
    • L.-P. Weng X. Wang Q. Yu Transmembrane tyrosine phosphatase LAR induces apoptosis by dephosphorylating and destabilizing p130Cas Genes Cells 4 1999 185 196
    • (1999) Genes Cells , vol.4 , pp. 185-196
    • Weng, L.-P.1    Wang, X.2    Yu, Q.3
  • 153
    • 0035805502 scopus 로고    scopus 로고
    • Inhibition of cell growth and spreading by stomach cancer-associated protein-tyrosine phosphatase-1 (SAP-1) through dephosphorylation of p130
    • T. Noguchi M. Tsuda H. Takeda T. Takada K. Inagaki T. Yamao K. Fukunaga T. Matozaki M. Kasuga Inhibition of cell growth and spreading by stomach cancer-associated protein-tyrosine phosphatase-1 (SAP-1) through dephosphorylation of p130 cas. J. Biol. Chem. 276 2001 15216 15224
    • (2001) cas. J. Biol. Chem. , vol.276 , pp. 15216-15224
    • Noguchi, T.1    Tsuda, M.2    Takeda, H.3    Takada, T.4    Inagaki, K.5    Yamao, T.6    Fukunaga, K.7    Matozaki, T.8    Kasuga, M.9
  • 155
    • 0032738102 scopus 로고    scopus 로고
    • Crystal structure of the catalytic subunit of Cdc25B required for G2⧸M phase transition of the cell cycle
    • R.A. Reynolds A.W. Yem C.L. Wolfe M.R. Deibel Jr. C.G. Chidester K.D. Watenpaugh Crystal structure of the catalytic subunit of Cdc25B required for G2⧸M phase transition of the cell cycle J. Mol. Biol. 293 1999 559 568
    • (1999) J. Mol. Biol. , vol.293 , pp. 559-568
    • Reynolds, R.A.1    Yem, A.W.2    Wolfe, C.L.3    Deibel, M.R.4    Chidester, C.G.5    Watenpaugh, K.D.6
  • 156
    • 0034609567 scopus 로고    scopus 로고
    • Dual-specific Cdc25B phosphatase: In search of the catalytic acid
    • W. Chen M. Wilborn J. Rudolph Dual-specific Cdc25B phosphatase: In search of the catalytic acid Biochemistry 39 2000 10781 10789
    • (2000) Biochemistry , vol.39 , pp. 10781-10789
    • Chen, W.1    Wilborn, M.2    Rudolph, J.3
  • 157
    • 73849170189 scopus 로고
    • Mechanism of phosphate ester cleavage
    • W.P. Jencks Mechanism of phosphate ester cleavage Brookhaven Symp. Biol. 15 1962 135 153
    • (1962) Brookhaven Symp. Biol. , vol.15 , pp. 135-153
    • Jencks, W.P.1
  • 158
    • 0001981310 scopus 로고
    • The mechanism of phosphoryl transfer
    • S.J. Benkovic K.J. Schray The mechanism of phosphoryl transfer R.D. Gandour R.L. Schowen “Transition States of Biochemical Processes” 1978 Plenum Press New York 493 527
    • (1978) , pp. 493-527
    • Benkovic, S.J.1    Schray, K.J.2
  • 159
    • 0001323093 scopus 로고
    • Monomeric metaphosphates
    • F.H. Westheimer Monomeric metaphosphates Chem. Rev. 81 1981 313 326
    • (1981) Chem. Rev. , vol.81 , pp. 313-326
    • Westheimer, F.H.1
  • 160
    • 0004731351 scopus 로고
    • Acyl group transfer-phosphoryl transfer
    • P.M. Cullis Acyl group transfer-phosphoryl transfer M.L. Page A. Williams “Enzyme Mechanisms” 1987 The Royal Society of Chemistry London 179 220
    • (1987) , pp. 179-220
    • Cullis, P.M.1
  • 161
    • 0024569057 scopus 로고
    • Chiral phosphorothioates: Stereochemical analysis of enzymatic substitution at phosphorus
    • P.A. Frey Chiral phosphorothioates: Stereochemical analysis of enzymatic substitution at phosphorus Adv. Enzymol. 62 1989 119 201
    • (1989) Adv. Enzymol. , vol.62 , pp. 119-201
    • Frey, P.A.1
  • 162
    • 23044505158 scopus 로고
    • Mechanism and catalysis of nucleophilic substitution in phosphate esters
    • G.R.J. Thatcher R. Kluger Mechanism and catalysis of nucleophilic substitution in phosphate esters Adv. Phys. Org. Chem. 25 1989 99 265
    • (1989) Adv. Phys. Org. Chem. , vol.25 , pp. 99-265
    • Thatcher, G.R.J.1    Kluger, R.2
  • 163
    • 0029620544 scopus 로고
    • Mechanisms of phosphoryl and acyl transfer
    • W.W. Cleland A.C. Hengge Mechanisms of phosphoryl and acyl transfer FASEB J. 9 1995 1585 1594
    • (1995) FASEB J. , vol.9 , pp. 1585-1594
    • Cleland, W.W.1    Hengge, A.C.2
  • 164
    • 0000174890 scopus 로고    scopus 로고
    • Transfer of the phosphoryl group
    • A.C. Hengge Transfer of the phosphoryl group M. Sinnott “Comprehensive Biological Catalysis: A Mecahnistic Reference” Vol. 1 1998 Academic Press San Diego, CA 517 542
    • (1998) , pp. 517-542
    • Hengge, A.C.1
  • 165
    • 33947333789 scopus 로고
    • The reactivity of phosphate esters. Monoester hydrolysis
    • A.J. Kirby A.G. Varvoglis The reactivity of phosphate esters. Monoester hydrolysis J. Am. Chem. Soc. 89 1967 415 423
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 415-423
    • Kirby, A.J.1    Varvoglis, A.G.2
  • 166
    • 85176187928 scopus 로고
    • A.J. Kirby S.G. Warren “The Organic Chemistry of Phosphorus,” 1967 Elsevier Publishing Company Amsterdam 274 364
    • (1967) , pp. 274-364
    • Kirby, A.J.1    Warren, S.G.2
  • 167
    • 0001158302 scopus 로고
    • Transition-state structures for phosphoryl-transfer reactions of p-nitrophenyl phosphate
    • A.C. Hengge W.A. Edens H. Elsing Transition-state structures for phosphoryl-transfer reactions of p -nitrophenyl phosphate J. Am. Chem. Soc. 116 1994 5045 5049
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 5045-5049
    • Hengge, A.C.1    Edens, W.A.2    Elsing, H.3
  • 168
    • 0000047385 scopus 로고
    • Kinetic isotope effects in the reactions of aryl-18O-2,4-dinitrophenyl dibenzyl phosphate and aryl-18O-2,4-dinitrophenyl phosphate. Evidence for monomeric metaphosphate
    • 18O-2,4-dinitrophenyl phosphate. Evidence for monomeric metaphosphate J. Am. Chem. Soc. 99 1977 2264 2267
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 2264-2267
    • Gorenstein, D.G.1    Lee, Y.-G.2    Kar, D.3
  • 169
  • 170
    • 0011904301 scopus 로고
    • Electrophilic catalysis. The hydrolysis of phosphoramidate
    • W.P. Jencks M. Gilchrist Electrophilic catalysis. The hydrolysis of phosphoramidate J. Am. Chem. Soc. 86 1964 1410 1417
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 1410-1417
    • Jencks, W.P.1    Gilchrist, M.2
  • 171
    • 0001631145 scopus 로고
    • Reactions of nucleophilic reagents with phosphoramidate
    • W.P. Jencks M. Gilchrist Reactions of nucleophilic reagents with phosphoramidate J. Am. Chem. Soc. 87 1965 3199 3209
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 3199-3209
    • Jencks, W.P.1    Gilchrist, M.2
  • 172
    • 0000443933 scopus 로고
    • The reactivity of nucleophilic reagents toward the p-nitrophenyl phosphate dianion
    • A.J. Kirby W.P. Jencks The reactivity of nucleophilic reagents toward the p -nitrophenyl phosphate dianion J. Am. Chem. Soc. 87 1965 3209 3216
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 3209-3216
    • Kirby, A.J.1    Jencks, W.P.2
  • 173
    • 12444255826 scopus 로고
    • Evidence that metaphosphate monoanion is not an intermediate in solvolysis reactions in aqueous solution
    • D. Herschlag W.P. Jencks Evidence that metaphosphate monoanion is not an intermediate in solvolysis reactions in aqueous solution J. Am. Chem. Soc. 111 1989 7579 7586
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 7579-7586
    • Herschlag, D.1    Jencks, W.P.2
  • 174
    • 0029410712 scopus 로고
    • Mapping the transition state for ATP hydrolysis: Implications for enzymatic catalysis
    • S.J. Admiraal D. Herschlag Mapping the transition state for ATP hydrolysis: Implications for enzymatic catalysis Chem. Biol. 2 1995 729 739
    • (1995) Chem. Biol. , vol.2 , pp. 729-739
    • Admiraal, S.J.1    Herschlag, D.2
  • 175
    • 0001623849 scopus 로고
    • Evidence for a single transition state in the transfer of the phosphoryl group (-PO32−) to nitrogen nucleophiles from pyridino-N-phosphonates
    • 2−) to nitrogen nucleophiles from pyridino-N-phosphonates J. Am. Chem. Soc. 106 1984 7591 7596
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 7591-7596
    • Bourne, N.1    Williams, A.2
  • 176
    • 0001711438 scopus 로고
    • Reactions of pyridines and primary amines with N-phosphorylated pyridines
    • M.T. Skoog W.P. Jencks Reactions of pyridines and primary amines with N-phosphorylated pyridines J. Am. Chem. Soc. 106 1984 7597 7606
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 7597-7606
    • Skoog, M.T.1    Jencks, W.P.2
  • 178
    • 0001570578 scopus 로고
    • Pyrophosphate formation from acetyl phosphate and orthophosphate anions in concentrated aqueous salt solutions does not provide evidence for a metaphosphate intermediate
    • D. Herschlag W.P. Jencks Pyrophosphate formation from acetyl phosphate and orthophosphate anions in concentrated aqueous salt solutions does not provide evidence for a metaphosphate intermediate J. Am. Chem. Soc. 108 1986 7938 7946
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 7938-7946
    • Herschlag, D.1    Jencks, W.P.2
  • 179
    • 0023099216 scopus 로고
    • Why nature chose phosphates
    • F.H. Westheimer Why nature chose phosphates Science 235 1987 1173 1178
    • (1987) Science , vol.235 , pp. 1173-1178
    • Westheimer, F.H.1
  • 180
    • 0001204721 scopus 로고
    • Acid and base catalysis in a non-enzymic transfer reaction: A possible model
    • E.B. Herr Jr. D.E. Koshland Jr. Acid and base catalysis in a non-enzymic transfer reaction: A possible model Biochim. Biophys. Acta. 25 1957 219 220
    • (1957) Biochim. Biophys. Acta. , vol.25 , pp. 219-220
    • Herr, E.B.1    Koshland, D.E.2
  • 181
    • 6844227333 scopus 로고
    • Reactivity of thiophosphates. II. Hydrolysis of S-n-butylphosphorothioate and S-(2-aminoethyl) phosphorothioate
    • D.C. Dittmer O.B. Ramsay R.E. Spalding Reactivity of thiophosphates. II. Hydrolysis of S-n-butylphosphorothioate and S-(2-aminoethyl) phosphorothioate J. Org. Chem. 28 1963 1273 1278
    • (1963) J. Org. Chem. , vol.28 , pp. 1273-1278
    • Dittmer, D.C.1    Ramsay, O.B.2    Spalding, R.E.3
  • 182
    • 0014196416 scopus 로고
    • The hydrolysis of S-aryl phosphorothioates
    • S. Milstien T.H. Fife The hydrolysis of S-aryl phosphorothioates J. Am. Chem. Soc. 89 1967 5820 5826
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 5820-5826
    • Milstien, S.1    Fife, T.H.2
  • 183
    • 0020477044 scopus 로고
    • Pyruvate kinase: Is the mechanism of phospho transfer associative or dissociative?
    • A. Hasset W. Blättler J.R. Knowles Pyruvate kinase: Is the mechanism of phospho transfer associative or dissociative? Biochemistry 21 1982 6335 6340
    • (1982) Biochemistry , vol.21 , pp. 6335-6340
    • Hasset, A.1    Blättler, W.2    Knowles, J.R.3
  • 184
    • 0023172934 scopus 로고
    • NMR studies of the mechanism of enzyme action
    • A.S. Mildvan D.C. Fry NMR studies of the mechanism of enzyme action Adv. Enzymol. 59 1987 241 313
    • (1987) Adv. Enzymol. , vol.59 , pp. 241-313
    • Mildvan, A.S.1    Fry, D.C.2
  • 185
    • 33845559886 scopus 로고
    • Heavy-atom isotope effects on the alkaline hydrolysis and hydrazinolysis of methyl benzoate
    • M.H. O'Leary J.F. Marlier Heavy-atom isotope effects on the alkaline hydrolysis and hydrazinolysis of methyl benzoate J. Am. Chem. Soc. 101 1979 3300 3306
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 3300-3306
    • O'Leary, M.H.1    Marlier, J.F.2
  • 186
    • 0025833708 scopus 로고
    • Transition-state structures for enzymatic and alkaline phosphotriester hydrolysis
    • S.R. Caldwell F.M. Raushel P.M. Weiss W.W. Cleland Transition-state structures for enzymatic and alkaline phosphotriester hydrolysis Biochemistry 30 1991 7444 7450
    • (1991) Biochemistry , vol.30 , pp. 7444-7450
    • Caldwell, S.R.1    Raushel, F.M.2    Weiss, P.M.3    Cleland, W.W.4
  • 187
    • 0001611523 scopus 로고
    • Direct measurement of transition-state bond cleavage in hydrolysis of phosphate esters of p-nitrophenol
    • A.C. Hengge W.W. Cleland Direct measurement of transition-state bond cleavage in hydrolysis of phosphate esters of p -nitrophenol J. Am. Chem. Soc. 112 1990 7421 7422
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 7421-7422
    • Hengge, A.C.1    Cleland, W.W.2
  • 188
    • 33947322034 scopus 로고
    • Nonlinear structure-reactivity correlations. The reactivity of nucleophilic reagents towards esters
    • W.P. Jencks M. Gilchrist Nonlinear structure-reactivity correlations. The reactivity of nucleophilic reagents towards esters J. Am. Chem. Soc. 90 1968 2622 2637
    • (1968) J. Am. Chem. Soc. , vol.90 , pp. 2622-2637
    • Jencks, W.P.1    Gilchrist, M.2
  • 189
    • 33845921520 scopus 로고
    • The reactivity of phosphate esters. Multiple structure-reactivity correlations for the reactions of triesters with nucleophiles
    • S.A. Khan A.J. Kirby The reactivity of phosphate esters. Multiple structure-reactivity correlations for the reactions of triesters with nucleophiles J. Chem. Soc. B. 1970 1172 1182
    • (1970) J. Chem. Soc. B. , pp. 1172-1182
    • Khan, S.A.1    Kirby, A.J.2
  • 190
    • 0037129951 scopus 로고    scopus 로고
    • A kinetic approach for the study of phosphatase-catalyzed regulation of kinase activity
    • Z.-X. Wang B. Zhou Q.M. Wang Z.-Y. Zhang A kinetic approach for the study of phosphatase-catalyzed regulation of kinase activity Biochemistry 41 2002 7849 7857
    • (2002) Biochemistry , vol.41 , pp. 7849-7857
    • Wang, Z.-X.1    Zhou, B.2    Wang, Q.M.3    Zhang, Z.-Y.4
  • 191
    • 0037200054 scopus 로고    scopus 로고
    • The specificity of extracellular signal-regulated kinase 2 dephosphorylation by protein phosphatases
    • B. Zhou Z.-X. Wang Y. Zhao D.L. Brautigan Z.-Y. Zhang The specificity of extracellular signal-regulated kinase 2 dephosphorylation by protein phosphatases J. Biol. Chem. 277 2002 31818 31825
    • (2002) J. Biol. Chem. , vol.277 , pp. 31818-31825
    • Zhou, B.1    Wang, Z.-X.2    Zhao, Y.3    Brautigan, D.L.4    Zhang, Z.-Y.5
  • 192
    • 0033544855 scopus 로고    scopus 로고
    • Mechanism of mitogen-activated protein kinase phosphatase-3 activation by ERK2
    • B. Zhou Z.-Y. Zhang Mechanism of mitogen-activated protein kinase phosphatase-3 activation by ERK2 J. Biol. Chem. 274 1999 35526 35534
    • (1999) J. Biol. Chem. , vol.274 , pp. 35526-35534
    • Zhou, B.1    Zhang, Z.-Y.2
  • 193
    • 0035794213 scopus 로고    scopus 로고
    • Multiple regions of MAP kinase phosphatase 3 are involved in its recognition and activation by ERK2
    • B. Zhou L. Wu K. Shen J. Zhang D.S. Lawrence Z.-X. Zhang Multiple regions of MAP kinase phosphatase 3 are involved in its recognition and activation by ERK2 J. Biol. Chem. 276 2001 6506 6515
    • (2001) J. Biol. Chem. , vol.276 , pp. 6506-6515
    • Zhou, B.1    Wu, L.2    Shen, K.3    Zhang, J.4    Lawrence, D.S.5    Zhang, Z.-X.6
  • 194
    • 0033597122 scopus 로고    scopus 로고
    • Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP)
    • M. Saxena S. Williams J. Brockdorff J. Gilman T. Mustelin Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP) J. Biol. Chem. 274 1999 11693 11700
    • (1999) J. Biol. Chem. , vol.274 , pp. 11693-11700
    • Saxena, M.1    Williams, S.2    Brockdorff, J.3    Gilman, J.4    Mustelin, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.