메뉴 건너뛰기




Volumn 2, Issue 12, 1995, Pages 1131-1137

Protein tyrosine phosphatases take off

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN KINASE; PROTEIN TYROSINE PHOSPHATASE;

EID: 0028880718     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb1295-1043     Document Type: Article
Times cited : (184)

References (69)
  • 1
    • 0027310848 scopus 로고
    • The effects of phosphorylationon the structure and function of proteins. A
    • Johnson, L.N. & Barford, D. The effects of phosphorylation on the structure and function of proteins. A Rev. Biophys. biomolec. Struct. 22, 199-232 (1993).
    • (1993) Rev. Biophys. Biomolec. Struct , vol.22 , pp. 199-232
    • Johnson, L.N.1    Barford, D.2
  • 3
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases. A
    • Cohen, P. The structure and regulation of protein phosphatases. A Rev. Biochem. 58, 453-508 (1989).
    • (1989) Rev. Biochem , vol.58 , pp. 453-508
    • Cohen, P.1
  • 4
    • 0001574833 scopus 로고
    • Nomenclature and chromosomal localization of human protein serine/threonine phosphatase genes
    • Cohen, P. Nomenclature and chromosomal localization of human protein serine/threonine phosphatase genes. Adv. prot. Phosphatases 8, 371-376 (1994).
    • (1994) Adv. Prot. Phosphatases , vol.8 , pp. 371-376
    • Cohen, P.1
  • 5
    • 0027721423 scopus 로고
    • Protein tyrosine phosphatases. Semin
    • Tonks N.K. Protein tyrosine phosphatases. Semin. Cell Biol. 4, 373-453 (1993).
    • (1993) Cell Biol , vol.4 , pp. 373-453
    • Tonks, N.K.1
  • 6
    • 0027183416 scopus 로고
    • Protein tyrosine phosphatases. A
    • Walton, K.M. & Dixon, J.E, Protein tyrosine phosphatases. A Rev. Biochem. 62, 101-120 (1993).
    • (1993) Rev. Biochem , vol.62 , pp. 101-120
    • Walton, K.M.1    Dixon, J.E.2
  • 7
  • 8
    • 0025945823 scopus 로고
    • Evidence of protein tyrosine catalysis proceeding via a cysteine-phosphate intermediate./biol
    • Guan, K.L. & Dixon, J.E. Evidence of protein tyrosine catalysis proceeding via a cysteine-phosphate intermediate./biol. Chem. 266, 17026-17030 (1991).
    • (1991) Chem , vol.266 , pp. 17026-17030
    • Guan, K.L.1    Dixon, J.E.2
  • 9
    • 0026038524 scopus 로고
    • Cloning, bacterial expression, purification, and characterization of the cytoplasmic domain of rat LAR, a receptor-like protein tyrosine phosphatese
    • Pot, D.A., Woodford, T.A., Remboutsika, E., Haun, R.S. & Dixon, J.E. Cloning, bacterial expression, purification, and characterization of the cytoplasmic domain of rat LAR, a receptor-like protein tyrosine phosphatese.J. biol. Chem. 266, 19688-19696 (1991).
    • (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
  • 10
    • 0028346560 scopus 로고
    • CD45: An emerging role as a protein tyrosine phosphatase required for lymphocyte activation and development. A
    • Trowbridge, I.S. & Thomas, M.L. CD45: An emerging role as a protein tyrosine phosphatase required for lymphocyte activation and development. A. Rev. Immunol. 12, 85-116 (1994).
    • (1994) Rev. Immunol , vol.12 , pp. 85-116
    • Trowbridge, I.S.1    Thomas, M.L.2
  • 11
    • 0026705734 scopus 로고
    • Cell transformation and activation of pp60c'src by overexpression of a protein tyrosine phosphatase
    • Zheng, X.M., Wang, Y. & Pallen, CJ. Cell transformation and activation of pp60c'src by overexpression of a protein tyrosine phosphatase. Nature 359, 336-339 (1992).
    • (1992) Nature , vol.359 , pp. 336-339
    • Zheng, X.M.1    Wang, Y.2    Pallen, C.J.3
  • 12
    • 0027329003 scopus 로고
    • Receptor protein tyrosine phosphatase a acyivates pp60c'src and is involved in neuronal differentiaition
    • den Hertog, J. etal. Receptor protein tyrosine phosphatase a acyivates pp60c'src and is involved in neuronal differentiaition. EMBO J. 12, 3789-3798 (1993).
    • (1993) EMBO J , vol.12 , pp. 3789-3798
    • Hertog, D.1    Etal, J.2
  • 13
    • 0027296921 scopus 로고
    • Homophtiic binding of PTPm, a receptor-type protein tyrosine phosphatase, can mediate cellcell aggregation
    • Brady-Kalnay, S.M., Flint, A.J. & Tonks, N.K. Homophtiic binding of PTPm, a receptor-type protein tyrosine phosphatase, can mediate cellcell aggregation. J. cell. Biol. 122, 961-972 (1993).
    • (1993) J. Cell. Biol , vol.122 , pp. 961-972
    • Brady-Kalnay, S.M.1    Flint, A.J.2    Tonks, N.K.3
  • 15
    • 0029149746 scopus 로고
    • Receptor protein tyrosine phosphatase PTPm associates with cadherins and catenins in vitro
    • Brady-Kalnay, S.M., Rimm, D.L. & Tonks, N.K, Receptor protein tyrosine phosphatase PTPm associates with cadherins and catenins in vitro. J. Cell Biol. 130, 977-986 (1995).
    • (1995) J. Cell Biol , vol.130 , pp. 977-986
    • Brady-Kalnay, S.M.1    Rimm, D.L.2    Tonks, N.K.3
  • 16
    • 0029096048 scopus 로고
    • The carbonic anhydrase domain of receptor tyrosine phosphatase b is a functional ligand for the axonal cell recognition molecule contactin
    • Peles, E. ef al. The carbonic anhydrase domain of receptor tyrosine phosphatase b is a functional ligand for the axonal cell recognition molecule contactin. Cell 82, 251-260 (1995).
    • (1995) Cell , vol.82 , pp. 251-260
    • Peles, E.E.A.1
  • 17
    • 0028235153 scopus 로고
    • Receptor tyrosine phosphatase b is expressed in the form of proteoglycan and binds to the extracellular matrix protein Tenascin.7. biol
    • Barnea, G. et al. Receptor tyrosine phosphatase b is expressed in the form of proteoglycan and binds to the extracellular matrix protein Tenascin.7. biol. Chem. 269, 14349-14352 (1994).
    • (1994) Chem , vol.269 , pp. 14349-14352
    • Barnea, G.1
  • 19
    • 0027296521 scopus 로고
    • Normal B lymphocyte but impaired T cell maturation in CD45-exon protein tyrosine phosphatase-deficient mice
    • Kishihara, K. et al. Normal B lymphocyte but impaired T cell maturation in CD45-exon protein tyrosine phosphatase-deficient mice. Cell 74, 143-156 (1993).
    • (1993) Cell , vol.74 , pp. 143-156
    • Kishihara, K.1
  • 20
    • 0027757991 scopus 로고
    • Structure and function of SH2-domain containing tyrosine phosphatase
    • Neel, B.G. Structure and function of SH2-domain containing tyrosine phosphatase. Cell Biol. 4, 419-432 (1993).
    • (1993) Cell Biol , vol.4 , pp. 419-432
    • Neel, B.G.1
  • 21
    • 0028956353 scopus 로고
    • Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals
    • Klingmuller, U., Lorenz, U., Cantley, L.C., Neel, B.G. & Lodish, H.F. Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals. Cell 80, 729-738(1995).
    • (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
  • 22
    • 0028932411 scopus 로고
    • Recruitment & activation of PTP1C in negative regulation of antigen receptor signalling by FCgRIIB 1
    • D'Ambrosîo, D., et al. (1995) Recruitment & activation of PTP1C in negative regulation of antigen receptor signalling by FCgRIIB 1. Science 268, 293-297 (1995).
    • (1995) Science , vol.268 , pp. 293-297
    • D'ambrosîo, D.1
  • 23
    • 0028123457 scopus 로고
    • A new function for a phosphotyrosine phosphatase: Linking GRB2-So$ to a receptor tyrosine kinase. Molec. cell
    • Li, W. ef al. A new function for a phosphotyrosine phosphatase: linking GRB2-So$ to a receptor tyrosine kinase. Molec. cell. Biol. 14, 509-517 (1994).
    • (1994) Biol , vol.14 , pp. 509-517
    • Li, W.E.A.1
  • 25
    • 0028149381 scopus 로고
    • The coordinated action of protein tyrosine phosphatases and kinases in cell signalling
    • Sun, H., & Tonks, N.K. The coordinated action of protein tyrosine phosphatases and kinases in cell signalling. Trends biochem Sci. 19, 480-485(1994).
    • (1994) Trends Biochem Sci , vol.19 , pp. 480-485
    • Sun, H.1    Tonks, N.K.2
  • 26
    • 0027314989 scopus 로고
    • Negative growth control by a novel Mr phosphotyrosine protein phosphatase in normal and transformed ceils
    • Ruggiero, M. ef al. Negative growth control by a novel Mr phosphotyrosine protein phosphatase in normal and transformed ceils. FEBS Lett. 326, 294-298 (1993).
    • (1993) FEBS Lett , vol.326 , pp. 294-298
    • Ruggiero, M.E.A.1
  • 27
    • 0028231388 scopus 로고
    • The crystal structure of human protein tyrosine phosphatase 1B
    • Barford, D., Flint, A.J., Tonks, N.K. The crystal structure of human protein tyrosine phosphatase 1B. Science 263 1397-1404 (1994).
    • (1994) Science , vol.263 , pp. 1397-1404
    • Barford, D.1    Flint, A.J.2    Tonks, N.K.3
  • 28
    • 0029066496 scopus 로고
    • Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B
    • Jia, Z., Barford, D., Flint, AJ. & Tonks, N.K. Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B. Science 268, 1754-1758 (1995).
    • (1995) Science , vol.268 , pp. 1754-1758
    • Jia, Z.1    Barford, D.2    Flint, A.J.3    Tonks, N.K.4
  • 29
    • 0028122711 scopus 로고
    • Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 and the complex with tungstate
    • Stuckley, J.A. et al. Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 and the complex with tungstate. Nature 370, 571(1994).
    • (1994) Nature , vol.571 , pp. 370
    • Stuckley, J.A.1
  • 30
    • 0029091493 scopus 로고
    • Ligand-induced conformational change in the Yersinia protein tyrosine phosphatase. Prot
    • Schubert, H.L., Fauman, E.B., Stuckey, J.A., Dixon, J.E. & Saper, M.A. A ligand-induced conformational change in the Yersinia protein tyrosine phosphatase. Prot. Sci. 4, 1904-11105 (1995).
    • (1995) Sci , vol.4 , pp. 1904-11105
    • Schubert, H.L.1    Fauman, E.B.2    Stuckey, J.A.3    Dixon, J.E.4    Saper, M.5
  • 31
    • 0028030520 scopus 로고
    • The crystal structure of a low-molecular weight phosphotyrosine protein phosphatase
    • Su, X.-D., Taddei, N., Stéfani, M., Ramponi, G. & Nordlund, P. The crystal structure of a low-molecular weight phosphotyrosine protein phosphatase. Nature 370, 575-578 (1994).
    • (1994) Nature , vol.370 , pp. 575-578
    • Su, X.-D.1    Taddei, N.2    Stéfani, M.3    Ramponi, G.4    Nordlund, P.5
  • 32
    • 0028016349 scopus 로고
    • Crystal structure of bovine heart phosphotyrosyl phosphatase at 2.2 resolution
    • Zhang, M., Van Etten, R.L. & Stauffacher, C.V. Crystal structure of bovine heart phosphotyrosyl phosphatase at 2.2 resolution. Biochemistry 33, 11097-11105 (1994).
    • (1994) Biochemistry , vol.33 , pp. 11097-11105
    • Zhang, M.1    Van Etten, R.L.2    Stauffacher, C.V.3
  • 33
    • 0028176050 scopus 로고
    • Dissecting the catalytic mechanism of protein tyrosine phosphatases
    • Zhang, Z.-Y, Wang, Y, Dixon, J.E. Dissecting the catalytic mechanism of protein tyrosine phosphatases. Proc. natn. Acad. Sci. U.S.A. 91, 1624-1628 (1994).
    • (1994) Proc. Natn. Acad. Sci. U.S.A. , vol.91 , pp. 1624-1628
    • Zhang, Z.-Y.1    Wang, Y.2    Dixon, J.E.3
  • 34
    • 0028903589 scopus 로고
    • The catalytic role of Aspartate-92 in a Human Dual-Specific Protein-Tyrosine-Phosphatase
    • Denu, J.M., Zhou, G., Guo, Y. & Dixon, J.E. The catalytic role of Aspartate-92 in a Human Dual-Specific Protein-Tyrosine-Phosphatase. Biochemistry 34, 3396-3403 (1995).
    • (1995) Biochemistry , vol.34 , pp. 3396-3403
    • Denu, J.M.1    Zhou, G.2    Guo, Y.3    Dixon, J.E.4
  • 35
    • 0028670682 scopus 로고
    • The Cys(X)sArg catalytic motif in phosphoester hydrolysis
    • Zhang, Z.Y. et al. (1994c) The Cys(X)sArg catalytic motif in phosphoester hydrolysis. Biochemistry 33, 15266-15270 (1994).
    • (1994) Biochemistry , vol.33 , pp. 15266-15270
    • Zhang, Z.Y.1
  • 36
    • 0026698924 scopus 로고
    • Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides
    • Waksman, G. Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides. Nature 358, 646-653 (1992).
    • (1992) Nature , vol.358 , pp. 646-653
    • Waksman, G.1
  • 37
    • 0027409064 scopus 로고
    • Binding of a high affinity phosphotyrosyl peptide to the src SH2 domain; Crystal structures of the complexed and peptide-free forms
    • Waksman, G-, Shoelson, S.E., Pant, N., Cowburn, D. & Kuriyan, J. Binding of a high affinity phosphotyrosyl peptide to the src SH2 domain; Crystal structures of the complexed and peptide-free forms. Ceil 72, 779-790 (1992).
    • (1992) Ceil , vol.72 , pp. 779-790
    • Waksman, G.1    Shoelson, S.E.2    Pant, N.3    Cowburn, D.4    Kuriyan, J.5
  • 38
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the human insulin receptor
    • Hubbard, S.R., Weî, L, Ellis, L. & Hendrickson, W.A. Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 372, 746-754 (1994).
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Weî, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 39
    • 0029005759 scopus 로고
    • Are protein tyrosine phosphatases specific for phosphotyrosine
    • Zhang, Z.-Y. Are protein tyrosine phosphatases specific for phosphotyrosine? J. biol. Chem. 270, 16052-16059 (1995).
    • (1995) J. Biol. Chem , vol.270 , pp. 16052-16059
    • Zhang, Z.-Y.1
  • 40
    • 0024287614 scopus 로고
    • Characterization of the major protein tyrosine phosphatases of human placenta
    • Tonks, N.K., Diltz, C.D. & Fischer, E.H. Characterization of the major protein tyrosine phosphatases of human placenta. J. biol. Chem. 263, 6731-6737 (1988).
    • (1988) J. Biol. Chem , vol.263 , pp. 6731-6737
    • Tonks, N.K.1    Diltz, C.D.2    Fischer, E.H.3
  • 41
    • 0027174567 scopus 로고
    • Substrate specificity of the protein tyrosine phosphatases
    • Zhang, Z.-Y. et al. Substrate specificity of the protein tyrosine phosphatases. Proc. natn. Acad. Sci. U.5.A. 90, 4446-4450 (1994).
    • (1994) Proc. Natn. Acad. Sci. U.5.A. , vol.90 , pp. 4446-4450
    • Zhang, Z.-Y.1
  • 42
    • 0027160287 scopus 로고
    • Substrate specificities of catalytic fragments of protein tyrosine phosphatases (HPTPb, LAR, and CD45) toward phosphotyrosyl peptide substrates and thiophosphotyrosylated peptides as inhibitors. Prot
    • Cho H. et al. Substrate specificities of catalytic fragments of protein tyrosine phosphatases (HPTPb, LAR, and CD45) toward phosphotyrosyl peptide substrates and thiophosphotyrosylated peptides as inhibitors. Prot. Sci. 2, 977-984 (1993).
    • (1993) , vol.2 , pp. 977-984
    • Cho, H.1
  • 43
    • 0027379577 scopus 로고
    • Acidic residues are involved in substrate regognition by two soluble protein tyrosine phosphatases, PTP-5 and rrbPTP-1
    • Hippen, K.L et al. Acidic residues are involved in substrate regognition by two soluble protein tyrosine phosphatases, PTP-5 and rrbPTP-1. Biochemistry 32, 12405-12412 (1993).
    • (1993) Biochemistry , vol.32 , pp. 12405-12412
    • Hippen, K.L.1
  • 44
    • 0027402515 scopus 로고    scopus 로고
    • Specificity of T-ceil protein tyrosine phosphatase toward phosphorylated synthetic peptides. Eur.J
    • Ruzzene, M. et al. Specificity of T-ceil protein tyrosine phosphatase toward phosphorylated synthetic peptides. Eur.J. Biochem. 211, 289-295.
    • Biochem , vol.211 , pp. 289-295
    • Ruzzene, M.1
  • 45
    • 0028017434 scopus 로고
    • Phosphorylated synthetic peptides as tools for studying protein phosphatases. Biochim. biophys
    • Pinna, L.A. & Donella-Deana, A. Phosphorylated synthetic peptides as tools for studying protein phosphatases. Biochim. biophys. Acta. 1222, 415-431 (1994).
    • (1994) Acta , vol.1222 , pp. 415-431
    • Pinna, L.A.1    Donella-Deana, A.2
  • 47
    • 0026342401 scopus 로고
    • Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton, D.E. et al. Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 414-420 (1991).
    • (1991) Science , vol.253 , pp. 414-420
    • Knighton, D.E.1
  • 48
    • 0028773477 scopus 로고
    • Three protein kinase structures define a common motif
    • Taylor, S.S. & Radzio-Andzelm, E. Three protein kinase structures define a common motif. Structure 2, 345-355 (1994).
    • (1994) Structure , vol.2 , pp. 345-355
    • Taylor, S.S.1    Radzio-Andzelm, E.2
  • 49
    • 0025277449 scopus 로고
    • Distinct functional roles of the two intracelular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR
    • Streuli, M., Kreuger, N.X., Thai, T, Tang, M. & Saito, H. Distinct functional roles of the two intracelular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR. EMBOJ. 9, 2399-2407 (1990).
    • (1990) EMBOJ , vol.9 , pp. 2399-2407
    • Streuli, M.1    Kreuger, N.X.2    Thai, T.3    Tang, M.4    Saito, H.5
  • 51
    • 0027399347 scopus 로고
    • Demonstration of protein tyrosine phosphatsse activity in the second of two homologous domains of CD45
    • Tan, X., Stover, D.R. & Walsh, K.A. Demonstration of protein tyrosine phosphatsse activity in the second of two homologous domains of CD45. J. biol. Chem. 268, 6835-6838 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 6835-6838
    • Tan, X.1    Stover, D.R.2    Walsh, K.A.3
  • 52
    • 0028017607 scopus 로고
    • Protein tyrosine phosphatase activity of CD45 is activated by sequential phosphorylation by two kinases. Molec. cell
    • Stover, D.R. & Walsh, K.A. Protein tyrosine phosphatase activity of CD45 is activated by sequential phosphorylation by two kinases. Molec. cell. Biol. 14, 5523-5532(1994).
    • (1994) Biol , vol.5523 , pp. 14
    • Stover, D.R.1    Walsh, K.A.2
  • 53
    • 0028540405 scopus 로고
    • Use of an oriented peptide library to determine the optimal substrates of protein kinases
    • Sonygang, Z. et al. Use of an oriented peptide library to determine the optimal substrates of protein kinases. Curr. Biol. 4, 973-982 (1994).
    • (1994) Curr. Biol , vol.4 , pp. 973-982
    • Sonygang, Z.1
  • 54
    • 0028938721 scopus 로고
    • Catalytic specificity of protein tyrosine kinases is critical for selective signalling
    • Songyang, Z. et al. Catalytic specificity of protein tyrosine kinases is critical for selective signalling. Nature 373, 536-539 (1994).
    • (1994) Nature , vol.373 , pp. 536-539
    • Songyang, Z.1
  • 55
    • 0026355413 scopus 로고
    • Protein kinase phosphorylation sites sequences and consensus specificity motifs:Tabulations. Meth
    • Pearson, R.B., Kemp, B.E. Protein kinase phosphorylation sites sequences and consensus specificity motifs:Tabulations. Meth. Enzymol. 200, 62-143 (1991).
    • (1991) Enzymol , vol.200 , pp. 62-143
    • Pearson, R.B.1    Kemp, B.E.2
  • 56
    • 0027409462 scopus 로고
    • Phosphotransferase and substrate binding mechanism of the cAMP-dependent protein kinase catalytic subunit from porcine heart deduced from the 2.0 structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PK!(524)
    • Bossemeyer, D., Engh, R.A., Kinzel, V., Ponstingl, H. & Huber, R. (1993) Phosphotransferase and substrate binding mechanism of the cAMP-dependent protein kinase catalytic subunit from porcine heart deduced from the 2.0 structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PK!(524). EMBOJ. 12, 849-859.
    • (1993) EMBOJ , vol.12 , pp. 849-859
    • Bossemeyer, D.1    Engh, R.A.2    Kinzel, V.3    Ponstingl, H.4    Huber, R.5
  • 57
    • 0028773294 scopus 로고
    • Antigenic peptide binding by class I and class II histocompatibility proteins
    • Stern, L.J. & Wiley, D.C. Antigenic peptide binding by class I and class II histocompatibility proteins. Structure 2, 245-251 (1994).
    • (1994) Structure , vol.2 , pp. 245-251
    • Stern, L.J.1    Wiley, D.C.2
  • 58
    • 0028773467 scopus 로고
    • Crystal structures of peptide complexes of the aminoterminal SH2 domain of the Syp tyrosine phosphatase
    • Lee, C.-H. Crystal structures of peptide complexes of the aminoterminal SH2 domain of the Syp tyrosine phosphatase. Structure 2, 423-438 (1994).
    • (1994) Structure , vol.2 , pp. 423-438
    • Lee, C.-H.1
  • 59
    • 0028299432 scopus 로고
    • Zip codes direct intracelluiat protein tyrosine phosphatases to the correct cellular 'addresses'. Trends biochem
    • Mauro, L.J. & Dixon, J.E. 'Zip codes' direct intracelluiat protein tyrosine phosphatases to the correct cellular 'addresses'. Trends biochem. Sci. 19, 151-155 (1994).
    • (1994) Sci , vol.19 , pp. 151-155
    • Mauro, L.J.1    Dixon, J.E.2
  • 60
    • 0028171416 scopus 로고    scopus 로고
    • The catalytic role of Cys 124 in the dual specificity phosphatase VHR. J. biol
    • Zhou, G., Denu, J.M., Wu, L. & Dixon, J.E. The catalytic role of Cys 124 in the dual specificity phosphatase VHR. J. biol. Chem. 269, 28084-28090.
    • Chem , vol.269 , pp. 28084-28090
    • Zhou, G.1    Denu, J.M.2    Wu, L.3    Dixon, J.E.4
  • 61
    • 0029043627 scopus 로고
    • Catalytic mechanism for the dual-specific phosphatases
    • Denu, J.M. & Dixon, J.E. A catalytic mechanism for the dual-specific phosphatases. Proc. natn. Acad. Sci. U.S.A. 92, 5910-5914 (1994).
    • (1994) Proc. Natn. Acad. Sci. U.S.A. , vol.92 , pp. 5910-5914
    • Denu, J.M.1    Dixon, J.2
  • 62
    • 0028239771 scopus 로고
    • Nature of the rate-determining steps of the reaction catalysed by the Yersinia Protein Tyrosine Phosphatase
    • Zhang, Z.-Y., Malachowski, W.P., Van Etten, R. & Dixon, J.E. Nature of the rate-determining steps of the reaction catalysed by the Yersinia Protein Tyrosine Phosphatase. J. biol. Chem. 269, 8140-8145 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 8140-8145
    • Zhang, Z.-Y.1    Malachowski, W.P.2    Van Etten, R.3    Dixon, J.E.4
  • 63
    • 0027358722 scopus 로고
    • MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP Kinase in vivo
    • Sun, H., Charles, C.H., Lau, L.F. & Tonks, N.K. MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP Kinase in vivo. Cell 75, 487-493 (1993).
    • (1993) Cell , vol.75 , pp. 487-493
    • Sun, H.1    Charles, C.H.2    Lau, L.F.3    Tonks, N.K.4
  • 64
    • 0027314525 scopus 로고
    • The role of Cys 12, Cys 17 and Arg 18 in the catalytic mechnism of low Mr cytosolic phosphotyrosine protein phosphatases
    • Cirri, P. et al. The role of Cys 12, Cys 17 and Arg 18 in the catalytic mechnism of low Mr cytosolic phosphotyrosine protein phosphatases. Eur. J. Biochem. 214, 647-657 (1993).
    • (1993) Eur. J. Biochem , vol.214 , pp. 647-657
    • Cirri, P.1
  • 65
    • 0028363734 scopus 로고
    • R. Kinetic and site-directed mutageneis studies of the Cysteine residues of bovine low molecular weight phosphotyrosyl protein phosphatases
    • Davis, J.P., Zhou, M.-M., & Van Etten, R. Kinetic and site-directed mutageneis studies of the Cysteine residues of bovine low molecular weight phosphotyrosyl protein phosphatases. J. biol. Chem. 269, 8734-8740 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 8734-8740
    • Davis, J.P.1    Zhou, M.-M.2    Etten, V.3
  • 66
    • 0028018098 scopus 로고
    • Aspartic-129 Is an essential residue in the catalytic mechanism of the low Mr phosphotyrosine protein phosphatase
    • Taddei, N. et al. Aspartic-129 Is an essential residue in the catalytic mechanism of the low Mr phosphotyrosine protein phosphatase. FEBS Lett. 350, 328-332 (1994).
    • (1994) FEBS Lett , vol.350 , pp. 328-332
    • Taddei, N.1
  • 67
    • 0027764344 scopus 로고
    • Protein sequence alignments: A strategy for the hierarchial analysis of residue conservation. Comput. Applic
    • Livingstone, CD. & Barton, G.J. Protein sequence alignments: a strategy for the hierarchial analysis of residue conservation. Comput. Applic. Biosci. 9, 745-756 (1993).
    • (1993) Biosci , vol.9 , pp. 745-756
    • Livingstone, C.D.1    Barton, G.J.2
  • 68
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G.J. ALSCRIPT: a tool to format multiple sequence alignments. Protein Engng. 6, 37-40 (1993).
    • (1993) Protein Engng , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 69
    • 84986486656 scopus 로고
    • Rapid finite difference alogorithm utilising successive over relaxation to solve the Poisson-Boltzman equation
    • Nicholls, A. & Honig, B. A rapid finite difference alogorithm utilising successive over relaxation to solve the Poisson-Boltzman equation. J. comput. Chem. 12, 435-445 (1991).
    • (1991) J. Comput. Chem , vol.12 , pp. 435-445
    • Nicholls, A.1    Honig, B.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.