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Volumn 44, Issue 36, 2005, Pages 12009-12021

Structure and biochemical properties of PRL-1, a phosphatase implicated in cell growth, differentiation, and tumor invasion

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CATALYSIS; CELL CULTURE; CHEMICAL BONDS; HYDROGEN PEROXIDE; OXYGEN; TUMORS;

EID: 24644519820     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0509191     Document Type: Article
Times cited : (77)

References (63)
  • 1
    • 0032577051 scopus 로고    scopus 로고
    • The phosphorylation of proteins on tyrosine: Its role in cell growth and disease
    • Hunter, T. (1998) The phosphorylation of proteins on tyrosine: its role in cell growth and disease, Philos. Trans. R. Soc. London, Ser. B 353, 583-605.
    • (1998) Philos. Trans. R. Soc. London, Ser. B , vol.353 , pp. 583-605
    • Hunter, T.1
  • 3
    • 0035415662 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: Prospects for therapeutics
    • Zhang, Z.-Y. (2001) Protein tyrosine phosphatases: prospects for therapeutics, Curr. Opin. Chem. Biol. 5, 416-423.
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 416-423
    • Zhang, Z.-Y.1
  • 4
    • 0028359370 scopus 로고
    • PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth
    • Diamond, R. H., Cressman, D. E., Laz, T. M., Abrams, C. S., and Taub, R. (1994) PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth, Mol. Cell. Biol. 14, 3752-3762.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3752-3762
    • Diamond, R.H.1    Cressman, D.E.2    Laz, T.M.3    Abrams, C.S.4    Taub, R.5
  • 6
    • 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
    • Zeng, Q., Si, X., Horstmann, H., Xu, Y., Hong, W., and Pallen, C. J. (2000) Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome, J. Biol. Chem. 275, 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
  • 8
    • 0037195808 scopus 로고    scopus 로고
    • The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosis
    • Wang, J., Kirby, C. E., and Herbst, R. (2002) The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosis, J. Biol. Chem. 277, 46659-46668.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46659-46668
    • Wang, J.1    Kirby, C.E.2    Herbst, R.3
  • 10
    • 0033826071 scopus 로고    scopus 로고
    • PRL-1 PTPase expression is developmentally regulated with tissue-specific patterns in epithelial tissues
    • Kong, W., Swain, G. P., Li, S., and Diamond, R. H. (2000) PRL-1 PTPase expression is developmentally regulated with tissue-specific patterns in epithelial tissues, Am. J. Physiol. 279, G613-621.
    • (2000) Am. J. Physiol. , vol.279
    • Kong, W.1    Swain, G.P.2    Li, S.3    Diamond, R.H.4
  • 11
    • 0033134685 scopus 로고    scopus 로고
    • Developmental expression of the murine Prl-1 protein tyrosine phosphatase gene
    • Rundle, C. H., and Kappen, C. (1999) Developmental expression of the murine Prl-1 protein tyrosine phosphatase gene, J. Exp. Zool. 253, 612-617.
    • (1999) J. Exp. Zool. , vol.253 , pp. 612-617
    • Rundle, C.H.1    Kappen, C.2
  • 14
    • 0344009730 scopus 로고    scopus 로고
    • Enhanced cell cycle progression and down regulation of p21(Cip1/Waf1) by PRL tyrosine phosphatases
    • Werner, S. R., Lee, P. A., DeCamp, M. W., Crowell, D. N., Randall, S. K., and Crowell, P. L. (2003) Enhanced cell cycle progression and down regulation of p21(Cip1/Waf1) by PRL tyrosine phosphatases. Cancer Lett. 202, 201-211.
    • (2003) Cancer Lett. , vol.202 , pp. 201-211
    • Werner, S.R.1    Lee, P.A.2    DeCamp, M.W.3    Crowell, D.N.4    Randall, S.K.5    Crowell, P.L.6
  • 15
    • 0037049883 scopus 로고    scopus 로고
    • Analysis of stromal-epithelial interactions in prostate cancer identifies PTPCAAX2 as a potential oncogene
    • Wang, Q., Holmes, D. I., Powell, S. M., Lu, Q. L., and Waxman, J. (2002) Analysis of stromal-epithelial interactions in prostate cancer identifies PTPCAAX2 as a potential oncogene, Cancer Lett. 175, 63-69.
    • (2002) Cancer Lett. , vol.175 , pp. 63-69
    • Wang, Q.1    Holmes, D.I.2    Powell, S.M.3    Lu, Q.L.4    Waxman, J.5
  • 17
    • 8444228839 scopus 로고    scopus 로고
    • High expression of PRL-3 promotes cancer cell motility and liver metastasis in human colorectal cancer: A predictive molecular marker of metachronous liver and lung metastases
    • Kato, H., Semba, S., Miskad, U. A., Seo, Y., Kasuga, M., and Yokozaki, H. (2004) High expression of PRL-3 promotes cancer cell motility and liver metastasis in human colorectal cancer: a predictive molecular marker of metachronous liver and lung metastases, Clin. Cancer Res. 10, 7318-7328.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 7318-7328
    • Kato, H.1    Semba, S.2    Miskad, U.A.3    Seo, Y.4    Kasuga, M.5    Yokozaki, H.6
  • 18
    • 3242759991 scopus 로고    scopus 로고
    • Expression of PRL-3 phosphatase in human gastric carcinomas: Close correlation with invasion and metastasis
    • Miskad, U. A., Semba, S., Kato, H., and Yokozaki, H. (2004) Expression of PRL-3 phosphatase in human gastric carcinomas: close correlation with invasion and metastasis, Pathobiology 71, 176-184.
    • (2004) Pathobiology , vol.71 , pp. 176-184
    • Miskad, U.A.1    Semba, S.2    Kato, H.3    Yokozaki, H.4
  • 19
    • 2442655501 scopus 로고    scopus 로고
    • Phosphatase of regenerating liver-3 promotes motility and metastasis of mouse melanoma cells
    • Wu, X., Zeng, H., Zhang, X., Zhao, Y., Sha, H., Ge, X., Zhang, M., Gao, X., and Xu, Q. (2004) Phosphatase of regenerating liver-3 promotes motility and metastasis of mouse melanoma cells, Am. J. Pathol 164, 2039-2054.
    • (2004) Am. J. Pathol , vol.164 , pp. 2039-2054
    • Wu, X.1    Zeng, H.2    Zhang, X.3    Zhao, Y.4    Sha, H.5    Ge, X.6    Zhang, M.7    Gao, X.8    Xu, Q.9
  • 20
    • 16844373567 scopus 로고    scopus 로고
    • Catalytic domain of PRL-3 plays an essential role in tumor metastasis: Formation of PRL-3 tumors inside the blood vessels
    • Guo, K., Li, J., Tang, J. P., Koh, V., Gan, B. Q., and Zeng, Q. (2004) Catalytic domain of PRL-3 plays an essential role in tumor metastasis: formation of PRL-3 tumors inside the blood vessels, Cancer Biol. Ther. 3, 945-951.
    • (2004) Cancer Biol. Ther. , vol.3 , pp. 945-951
    • Guo, K.1    Li, J.2    Tang, J.P.3    Koh, V.4    Gan, B.Q.5    Zeng, Q.6
  • 21
    • 1642482862 scopus 로고    scopus 로고
    • Structural insights into molecular function of the metastasis-associated phosphatase PRL-3
    • Kozlov, G., Cheng, J., Ziomek, E., Banville, D., Gehring, K., and Ekiel, I. (2004) Structural insights into molecular function of the metastasis-associated phosphatase PRL-3, J. Biol. Chem. 279, 11882-11889.
    • (2004) J. Biol. Chem. , vol.279 , pp. 11882-11889
    • Kozlov, G.1    Cheng, J.2    Ziomek, E.3    Banville, D.4    Gehring, K.5    Ekiel, I.6
  • 22
    • 9644295701 scopus 로고    scopus 로고
    • Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms
    • Jeong, D. G., Kim, S. J., Kim, J. H., Son, J. H., Park, M. R., Lim, S. M., Yoon, T. S., and Ryu, S. E. (2005) Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms, J. Mol. Biol. 345, 401-413.
    • (2005) J. Mol. Biol. , vol.345 , pp. 401-413
    • Jeong, D.G.1    Kim, S.J.2    Kim, J.H.3    Son, J.H.4    Park, M.R.5    Lim, S.M.6    Yoon, T.S.7    Ryu, S.E.8
  • 23
    • 0025976707 scopus 로고
    • Pre-steady-state and steady-state kinetic analysis of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart
    • Zhang, Z.-Y., and Van Etten, R. L. (1991) Pre-steady-state and steady-state kinetic analysis of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart, J. Biol. Chem. 266, 1516-1525.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1516-1525
    • Zhang, Z.-Y.1    Van Etten, R.L.2
  • 24
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol. 176, 307-326.
    • (1997) Methods Enzymol. , vol.176 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 26
    • 0001940082 scopus 로고
    • MAD phasing: Treatment of dispersive differences as isomorphous replacement information
    • Terwilliger, T. C. (1994) MAD phasing: treatment of dispersive differences as isomorphous replacement information, Acta Crystallogr., Sect. D: Biol. Crystallogr. 50, 17-23.
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 17-23
    • Terwilliger, T.C.1
  • 30
    • 3142711567 scopus 로고    scopus 로고
    • Kinetic and mechanistic studies of a cell cycle protein phosphatase Cdc14
    • Wang, W.-Q., Bembenek, J., Gee, K. R., Yu, H., Charbonneau, H., and Zhang, Z.-Y. (2004) Kinetic and Mechanistic Studies of a Cell Cycle Protein Phosphatase Cdc14, J. Biol. Chem. 279, 30459-30468.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30459-30468
    • Wang, W.-Q.1    Bembenek, J.2    Gee, K.R.3    Yu, H.4    Charbonneau, H.5    Zhang, Z.-Y.6
  • 31
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L., and Sander, C (1993) Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 32
    • 0041312681 scopus 로고    scopus 로고
    • The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase
    • Gray, C. H., Good, V. M., Tonks, N. K., and Barford, D. (2003) The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase, EMBO J. 22, 3524-3535.
    • (2003) EMBO J. , vol.22 , pp. 3524-3535
    • Gray, C.H.1    Good, V.M.2    Tonks, N.K.3    Barford, D.4
  • 33
    • 0035265679 scopus 로고    scopus 로고
    • Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2
    • Song, H., Hanlon, N., Brown, N. R., Noble, M. E., Johnson, L. N., and Barford, D. (2001) Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2, Mol. Cell 7, 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
  • 34
    • 0033615538 scopus 로고    scopus 로고
    • Crystal structure of the PTEN tumor suppressor: Implications for its phosphoinositide phosphatase activity and membrane association
    • Lee, J. O., Yang, H., Georgescu, M. M., Di Cristofano, A., Maehama, T., Shi, Y., Dixon, J. E., Pandolfi, P., and Pavletich, N. P. (1999) Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association, Cell 99, 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
  • 35
    • 0029975476 scopus 로고    scopus 로고
    • Crystal structure of the dual specificity protein phosphatase VHR
    • Yuvaniyama, J., Denu, J. M., Dixon, J. E., and Saper, M. A. (1996) Crystal structure of the dual specificity protein phosphatase VHR, Science 272, 1328-1331.
    • (1996) Science , vol.272 , pp. 1328-1331
    • Yuvaniyama, J.1    Denu, J.M.2    Dixon, J.E.3    Saper, M.A.4
  • 37
    • 0025013547 scopus 로고
    • A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane
    • Hancock, J. F., Paterson, H., Marshall, C. J. (1990) A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane, Cell 63, 133-139.
    • (1990) Cell , vol.63 , pp. 133-139
    • Hancock, J.F.1    Paterson, H.2    Marshall, C.J.3
  • 38
    • 0031571632 scopus 로고    scopus 로고
    • Electrostatic interaction of myristoylated proteins with membranes: Simple physics, complicated biology
    • Murray, D., Ben-Tal, N., Honig, B., and McLaughlin, S. (1997) Electrostatic interaction of myristoylated proteins with membranes: simple physics, complicated biology, Structure 5, 985-989.
    • (1997) Structure , vol.5 , pp. 985-989
    • Murray, D.1    Ben-Tal, N.2    Honig, B.3    McLaughlin, S.4
  • 40
    • 0029015718 scopus 로고
    • Kinetic and mechanistic characterization of a mammalian protein tyrosine phosphatase, PTP1
    • Zhang, Z.-Y. (1995) Kinetic and mechanistic characterization of a mammalian protein tyrosine phosphatase, PTP1, J. Biol. Chem. 270, 11199-11204.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11199-11204
    • Zhang, Z.-Y.1
  • 41
    • 0028239771 scopus 로고
    • The nature of the rate-determining steps of the Yersinia protein tyrosine phosphatase-catalyzed reactions
    • Zhang, Z.-Y., Malachowski, W. P., Van Etten, R. L., and Dixon, J. E. (1994) The nature of the rate-determining steps of the Yersinia protein tyrosine phosphatase-catalyzed reactions, J. Biol. Chem. 269, 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
  • 42
    • 0028858055 scopus 로고
    • Transition state and rate-limiting step of the reaction catalyzed by the human dual specificity phosphatase, VHR
    • Zhang, Z.-Y., Wu, L., and Chen, L. (1995) Transition state and rate-limiting step of the reaction catalyzed by the human dual specificity phosphatase, VHR, Biochemistry 34, 16088-16096.
    • (1995) Biochemistry , vol.34 , pp. 16088-16096
    • Zhang, Z.-Y.1    Wu, L.2    Chen, L.3
  • 43
    • 2542559631 scopus 로고    scopus 로고
    • Mechanistic studies on protein tyrosine phosphatases
    • Zhang, Z.-Y. (2003) Mechanistic studies on protein tyrosine phosphatases, Prog. Nucleic Acid Res. Mol. Biol. 73, 171-220.
    • (2003) Prog. Nucleic Acid Res. Mol. Biol. , vol.73 , pp. 171-220
    • Zhang, Z.-Y.1
  • 45
    • 0029739468 scopus 로고    scopus 로고
    • VHR and PTP1 protein phosphatases exhibit remarkably different active site specificities toward low molecular weight nonpeptidic substrates
    • Chen, L., Montserat, J., Lawrence, D. S., and Zhang, Z.-Y. (1996) VHR and PTP1 protein phosphatases exhibit remarkably different active site specificities toward low molecular weight nonpeptidic substrates, Biochemistry 35, 9349-9354.
    • (1996) Biochemistry , vol.35 , pp. 9349-9354
    • Chen, L.1    Montserat, J.2    Lawrence, D.S.3    Zhang, Z.-Y.4
  • 47
    • 0033544855 scopus 로고    scopus 로고
    • Mechanism of mitogen-activated protein kinase phosphatase-3 activation by ERK2
    • Zhou, B., and Zhang, Z.-Y. (1999) Mechanism of mitogen-activated protein kinase phosphatase-3 activation by ERK2, J. Biol. Chem. 274, 35526-35534.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35526-35534
    • Zhou, B.1    Zhang, Z.-Y.2
  • 48
    • 0034629559 scopus 로고    scopus 로고
    • Mechanistic basis for catalytic activation of mitogen-activated protein kinase phosphatase 3 by extracellular signal-regulated kinase
    • Fjeld, C. C., Rice, A. E., Kim, Y., Gee, K. R., and Denu, J. M. (2000) Mechanistic basis for catalytic activation of mitogen-activated protein kinase phosphatase 3 by extracellular signal-regulated kinase, J. Biol. Chem. 275, 6749-6757.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6749-6757
    • Fjeld, C.C.1    Rice, A.E.2    Kim, Y.3    Gee, K.R.4    Denu, J.M.5
  • 49
    • 0035253383 scopus 로고    scopus 로고
    • Specificity of natural and artificial substrates for human Cdc25A
    • Rudolph, J., Epstein, D. M., Parker, L., and Eckstein, J. (2001) Specificity of natural and artificial substrates for human Cdc25A, Anal. Biochem. 289, 43-51.
    • (2001) Anal. Biochem. , vol.289 , pp. 43-51
    • Rudolph, J.1    Epstein, D.M.2    Parker, L.3    Eckstein, J.4
  • 51
    • 0037174872 scopus 로고    scopus 로고
    • Probing the molecular basis for potent and selective protein tyrosine phosphatase 1B inhibition
    • Guo, X.-L., Shen, K., Wang, F., Lawrence, D. S., and Zhang, Z.-Y. (2002) Probing the molecular basis for potent and selective protein tyrosine phosphatase 1B inhibition, J. Biol. Chem. 277, 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
  • 52
    • 0032910476 scopus 로고    scopus 로고
    • Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation
    • Stewart, A. E., Dowd, S., Keyse, S. M., and McDonald, N. Q. (1999) Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation, Nat. Struct. Biol. 6, 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
  • 53
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implications for redox regulation
    • Denu, J. M., and Tanner, K. G. (1998) Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation, Biochemistry 37, 5633-5642.
    • (1998) Biochemistry , vol.37 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 54
    • 0038749600 scopus 로고    scopus 로고
    • Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
    • van Montfort, R. L., Congreve, M., Tisi, D., Carr, R., and Jhoti, H. (2003) Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B, Nature 423, 773-737.
    • (2003) Nature , vol.423 , pp. 773-1737
    • Van Montfort, R.L.1    Congreve, M.2    Tisi, D.3    Carr, R.4    Jhoti, H.5
  • 55
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • Salmeen, A., Andersen, J. N., Myers, M. P., Meng, T. C., Hinks, J. A., Tonks, N. K., and Barford, D. (2003) Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate, Nature 423, 769-773.
    • (2003) Nature , vol.423 , pp. 769-773
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Meng, T.C.4    Hinks, J.A.5    Tonks, N.K.6    Barford, D.7
  • 58
    • 0032738102 scopus 로고    scopus 로고
    • Crystal structure of the catalytic subunit of Cdc25B required for G2/M phase transition of the cell cycle
    • Reynolds, R. A., Yem, A. W., Wolfe, C. L., Deibel, M. R., Jr., Chidester, C. G., and Watenpaugh, K. D. (1999) Crystal structure of the catalytic subunit of Cdc25B required for G2/M phase transition of the cell cycle, J. Mol. Biol. 293, 559-568.
    • (1999) J. Mol. Biol. , vol.293 , pp. 559-568
    • Reynolds, R.A.1    Yem, A.W.2    Wolfe, C.L.3    Deibel Jr., M.R.4    Chidester, C.G.5    Watenpaugh, K.D.6
  • 59
    • 0035823539 scopus 로고    scopus 로고
    • Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phosphatase in response to platelet-derived growth factor receptor stimulation
    • Chiarugi, P., Fiaschi, T., Taddei, M. L., Talini, D., Giannoni, E., Raugei, G., and Ramponi, G. (2001) Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phosphatase in response to platelet-derived growth factor receptor stimulation, J. Biol. Chem. 276, 33478-33487.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33478-33487
    • Chiarugi, P.1    Fiaschi, T.2    Taddei, M.L.3    Talini, D.4    Giannoni, E.5    Raugei, G.6    Ramponi, G.7
  • 60
    • 24644460381 scopus 로고
    • (Ahern, T. J., and Manning, M. C., Eds.), Plenum Press, New York
    • Kosen, P. A. (1992) in Stability of Protein Pharmaceuticals (Ahern, T. J., and Manning, M. C., Eds.) p 34, Plenum Press, New York.
    • (1992) Stability of Protein Pharmaceuticals , pp. 34
    • Kosen, P.A.1
  • 61
    • 0037376674 scopus 로고    scopus 로고
    • Oxidant signals and oxidative stress
    • Finkel, T. (2003) Oxidant signals and oxidative stress, Curr. Opin. Cell Biol. 15, 247-254.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 247-254
    • Finkel, T.1
  • 62
    • 0642276003 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatases during receptor tyrosine kinase signal transduction
    • Chiarugi, P., and Cirri, P. (2003) Redox regulation of protein tyrosine phosphatases during receptor tyrosine kinase signal transduction, Trends Biochem. Sci. 28, 509-514.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 509-514
    • Chiarugi, P.1    Cirri, P.2
  • 63
    • 84986486656 scopus 로고
    • A rapid finite difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation
    • Nicholls, A., and Honig, B. (1991) A rapid finite difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation, J. Comput. Chem. 12, 435-445.
    • (1991) J. Comput. Chem. , vol.12 , pp. 435-445
    • Nicholls, A.1    Honig, B.2


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