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Volumn 45, Issue 39, 2006, Pages 12125-12135

Thermodynamics of phosphopeptide binding to the human peptidyl prolyl cis/trans isomerase pin1

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BINDING ENTHALPIES; BOUND INHIBITORS; CONFORMATIONAL TRANSITIONS; DIRECT ANALYSIS; DISSOCIATION CONSTANT; ENZYMATIC ACTIVITIES; ISOMERASES; ISOTHERMAL TITRATION CALORIMETRY; PHOSPHOPEPTIDES; PHYSIOLOGICAL IONIC STRENGTH; REGULATORY PROCESS; SUBSTRATE PROTEINS; THERMODYNAMIC PARAMETER; TRANSITION STATE; TRANSITION-STATE ANALOGUES; WW DOMAIN;

EID: 33750701178     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi0608820     Document Type: Article
Times cited : (24)

References (49)
  • 1
    • 0023236959 scopus 로고
    • Catalysis of protein folding by prolyl isomerase
    • DOI 10.1038/329268a0
    • Lang, K., Schmid, F. X., and Fischer, G. (1987) Catalysis of protein folding by prolyl isomerase, Nature 329, 268-270. (Pubitemid 17128975)
    • (1987) Nature , vol.329 , Issue.6136 , pp. 268-270
    • Lang, K.1    Schmid, F.X.2    Fischer, G.3
  • 3
    • 0032554636 scopus 로고    scopus 로고
    • Role of phosphorylation in determining the backbone dynamics of the serine/threonine-proline motif and Pin1 substrate recognition
    • DOI 10.1021/bi973060z
    • Schutkowski, M., Bernhardt, A., Zhou, X. Z., Shen, M., Reimer, U., Rahfeld, J. U., Lu, K. P., and Fischer, G. (1998) Role of phosphorylation in determining the backbone dynamics of the serine/threonine-proline motif and Pin1 substrate recognition, Biochemistry 37, 5566-5575. (Pubitemid 28241940)
    • (1998) Biochemistry , vol.37 , Issue.16 , pp. 5566-5575
    • Schutkowski, M.1    Bernhardt, A.2    Zhou, X.Z.3    Shen, M.4    Reimer, U.5    Rahfeld, J.-U.6    Lu, K.P.7    Fischer, G.8
  • 4
    • 0040017910 scopus 로고    scopus 로고
    • Function of WW domains as phosphoserine- Or phosphothreonine-binding modules
    • Lu, P. J., Zhou, X. Z., Shen, M., and Lu, K. P. (1999) Function of WW domains as phosphoserine- or phosphothreonine-binding modules, Science 283, 1325-1328.
    • (1999) Science , vol.283 , pp. 1325-1328
    • Lu, P.J.1    Zhou, X.Z.2    Shen, M.3    Lu, K.P.4
  • 5
    • 0033885803 scopus 로고    scopus 로고
    • Structural basis for phosphoserine-proline recognition by group IV WW domains
    • DOI 10.1038/77929
    • Verdecia, M. A., Bowman, M. E., Lu, K. P., Hunter, T., and Noel, J. P. (2000) Structural basis for phosphoserine-proline recognition by group IV WW domains, Nat. Struct. Biol. 7, 639-643. (Pubitemid 30636673)
    • (2000) Nature Structural Biology , vol.7 , Issue.8 , pp. 639-643
    • Verdecia, M.A.1    Bowman, M.E.2    Lu, K.P.3    Hunter, T.4    Noel, J.P.5
  • 7
    • 0035947078 scopus 로고    scopus 로고
    • Pin1 acts catalytically to promote a conformational change in Cdc25
    • DOI 10.1016/S1097-2765(01)00245-3
    • Stukenberg, P. T., and Kirschner, M. W. (2001) Pin1 acts catalytically to promote a conformational change in Cdc25, Mol. Cell 7, 1071-1083. (Pubitemid 32525753)
    • (2001) Molecular Cell , vol.7 , Issue.5 , pp. 1071-1083
    • Stukenberg, P.T.1    Kirschner, M.W.2
  • 8
    • 18644384688 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 is a regulator of p53 in genotoxic response
    • DOI 10.1038/nature01116
    • Zheng, H., You, H., Zhou, X. Z., Murray, S. A., Uchida, T., Wulf, G., Gu, L., Tang, X., Lu, K. P., and Xiao, Z. X. (2002) The prolyl isomerase Pin1 is a regulator of p53 in genotoxic response, Nature 419, 849-853. (Pubitemid 35238572)
    • (2002) Nature , vol.419 , Issue.6909 , pp. 849-853
    • Zheng, H.1    You, H.2    Zhou, X.Z.3    Murray, S.A.4    Uchida, T.5    Wulf, G.6    Gu, L.7    Tang, X.8    Lu, K.P.9    Xiao, Z.-X.J.10
  • 9
    • 18644384283 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 reveals a mechanism to control p53 functions after genotoxic insults
    • DOI 10.1038/nature01120
    • Zacchi, P., Gostissa, M., Uchida, T., Salvagno, C., Avolio, F., Volinia, S., Ronai, Z., Blandino, G., Schneider, C., and Del Sal, G. (2002) The prolyl isomerase Pin1 reveals a mechanism to control p53 functions after genotoxic insults, Nature 419, 853-857. (Pubitemid 35238573)
    • (2002) Nature , vol.419 , Issue.6909 , pp. 853-857
    • Zacchi, P.1    Gostissa, M.2    Uchida, T.3    Salvagno, C.4    Avolio, F.5    Volinia, S.6    Ronai, Z.7    Blandino, G.8    Schneider, C.9    Del, S.G.10
  • 10
    • 0037181170 scopus 로고    scopus 로고
    • Pin1 modulates the dephosphorylation of the RNA polymerase II C-terminal domain by yeast Fcp1
    • DOI 10.1016/S0014-5793(02)02288-3, PII S0014579302022883
    • Kops, O., Zhou, X. Z., and Lu, K. P. (2002) Pin1 modulates the dephosphorylation of the RNA polymerase II C-terminal domain by yeast Fcp1, FEBS Lett. 513, 305-311. (Pubitemid 34251283)
    • (2002) FEBS Letters , vol.513 , Issue.2-3 , pp. 305-311
    • Kops, O.1    Zhou, X.Z.2    Lu, K.P.3
  • 11
    • 0029916122 scopus 로고    scopus 로고
    • A human peptidyl-prolyl isomerase essential for regulation of mitosis
    • DOI 10.1038/380544a0
    • Lu, K. P., Hanes, S. D., and Hunter, T. (1996) A human peptidylprolyl isomerase essential for regulation of mitosis, Nature 380, 544-547. (Pubitemid 26111332)
    • (1996) Nature , vol.380 , Issue.6574 , pp. 544-547
    • Lu, K.P.1    Hanes, S.D.2    Hunter, T.3
  • 12
    • 0032473350 scopus 로고    scopus 로고
    • The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1
    • DOI 10.1093/emboj/17.5.1315
    • Crenshaw, D. G., Yang, J., Means, A. R., and Kornbluth, S. (1998) The mitotic peptidyl-prolyl isomerase, Pin1, interacts with CDC25 and Plx, EMBO J. 17, 1315-1327. (Pubitemid 28105511)
    • (1998) EMBO Journal , vol.17 , Issue.5 , pp. 1315-1327
    • Crenshaw, D.G.1    Yang, J.2    Means, A.R.3    Kornbluth, S.4
  • 13
    • 0034050649 scopus 로고    scopus 로고
    • Requirement of the prolyl isomerase Pin1 for the replication checkpoint
    • DOI 10.1126/science.287.5458.1644
    • Winkler, K. E., Swenson, K. I., Kornbluth, S., and Means, A. R. (2000) Requirement of the prolyl isomerase Pin1 for the replication checkpoint, Science 287, 1644-1647. (Pubitemid 30127764)
    • (2000) Science , vol.287 , Issue.5458 , pp. 1644-1647
    • Winkler, K.E.1    Swenson, K.I.2    Kornbluth, S.3    Means, A.R.4
  • 14
    • 0033619755 scopus 로고    scopus 로고
    • Mice lacking Pin1 develop normally, but are defective in entering cell cycle from G(0) arrest
    • Fujimori, F., Takahashi, K., Uchida, C., and Uchida, T. (1999) Mice lacking Pin1 develop normally, but are defective in entering cell cycle from G(0) arrest, Biochem. Biophys. Res. Commun. 265, 658-663.
    • (1999) Biochem. Biophys. Res. Commun. , vol.265 , pp. 658-663
    • Fujimori, F.1    Takahashi, K.2    Uchida, C.3    Uchida, T.4
  • 16
    • 27144524092 scopus 로고    scopus 로고
    • Stable suppression of tumorigenicity by Pin1-targeted RNA interference in prostate cancer
    • DOI 10.1158/1078-0432.CCR-05-0457
    • Ryo, A., Uemura, H., Ishiguro, H., Saitoh, T., Yamaguchi, A., Perrem, K., Kubota, Y., Lu, K. P., and Aoki, I. (2005) Stable suppression of tumorigenicity by pin1-targeted RNA interference in prostate cancer, Clin. Cancer Res. 11, 7523-7531. (Pubitemid 41507714)
    • (2005) Clinical Cancer Research , vol.11 , Issue.20 , pp. 7523-7531
    • Ryo, A.1    Uemura, H.2    Ishiguro, H.3    Saitoh, T.4    Yamaguchi, A.5    Perrem, K.6    Kubota, Y.7    Lu, K.P.8    Aoki, I.9
  • 17
    • 0037351048 scopus 로고    scopus 로고
    • Prolyl isomerase Pin1: A catalyst for oncogenesis and a potential therapeutic target in cancer
    • DOI 10.1242/jcs.00276
    • Ryo, A., Liou, Y. C., Lu, K. P., and Wulf, G. (2003) Prolyl isomerase Pin1: a catalyst for oncogenesis and a potential therapeutic target in cancer, J. Cell Sci. 116, 773-783. (Pubitemid 36367627)
    • (2003) Journal of Cell Science , vol.116 , Issue.5 , pp. 773-783
    • Ryo, A.1    Liou, Y.-C.2    Lu, K.P.3    Wulf, G.4
  • 18
    • 0035796405 scopus 로고    scopus 로고
    • Pin1 is overexpressed in breast cancer and cooperates with Ras signaling in increasing the transcriptional activity of c-Jun towards cyclin D1
    • DOI 10.1093/emboj/20.13.3459
    • Wulf, G. M., Ryo, A., Wulf, G. G., Lee, S. W., Niu, T., Petkova, V., and Lu, K. P. (2001) Pin1 is overexpressed in breast cancer and cooperates with Ras signaling in increasing the transcriptional activity of c-Jun towards cyclin D1, EMBO J. 20, 3459-3472. (Pubitemid 32634353)
    • (2001) EMBO Journal , vol.20 , Issue.13 , pp. 3459-3472
    • Wulf, G.M.1    Ryo, A.2    Wulf, G.G.3    Lee, S.W.4    Niu, T.5    Petkova, V.6    Lu, K.P.7
  • 19
    • 4444309643 scopus 로고    scopus 로고
    • Modeling breast cancer in vivo and ex vivo reveals an essential role of Pin1 in tumorigenesis
    • DOI 10.1038/sj.emboj.7600323
    • Wulf, G., Garg, P., Liou, Y. C., Iglehart, D., and Lu, K. P. (2004) Modeling breast cancer in vivo and ex vivo reveals an essential role of Pin1 in tumorigenesis, EMBO J. 23, 3397-3407. (Pubitemid 39209163)
    • (2004) EMBO Journal , vol.23 , Issue.16 , pp. 3397-3407
    • Wulf, G.1    Garg, P.2    Liou, Y.-C.3    Iglehart, D.4    Lu, K.P.5
  • 21
    • 10944246574 scopus 로고    scopus 로고
    • Pinning down phosphorylated tau and tauopathies
    • Lim, J. N. and Lu, K. P. (2005) Pinning down phosphorylated tau and tauopathies, Biochim. Biophys. Acta 1739, 311-322.
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 311-322
    • Lim, J.N.1    Lu, K.P.2
  • 22
    • 30044436160 scopus 로고    scopus 로고
    • The peptidyl-prolyl isomerase Pin1 regulates the stability of granulocyte-macrophage colony-stimulating factor mRNA in activated eosinophils
    • DOI 10.1038/ni1266, PII N1266
    • Shen, Z. J., Esnault, S., and Malter, J. S. (2005) The peptidylprolyl isomerase Pin1 regulates the stability of granulocytemacrophage colony-stimulating factor mRNA in activated eosinophils, Nature Immunol. 6, 1280-1287. (Pubitemid 43045640)
    • (2005) Nature Immunology , vol.6 , Issue.12 , pp. 1280-1287
    • Shen, Z.-J.1    Esnault, S.2    Malter, J.S.3
  • 25
    • 0008233581 scopus 로고    scopus 로고
    • Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent
    • Ranganathan, R., Lu, K. P., Hunter, T., and Noel, J. P. (1997) Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent, Cell 89, 875-886. (Pubitemid 27513514)
    • (1997) Cell , vol.89 , Issue.6 , pp. 875-886
    • Ranganathan, R.1    Lu, K.P.2    Hunter, T.3    Noel, J.P.4
  • 26
    • 22544455987 scopus 로고    scopus 로고
    • Regulation of Pin1 peptidyl-prolyl cis/trans isomerase activity by its WW binding module on a multi-phosphorylated peptide of Tau protein
    • DOI 10.1016/j.febslet.2005.06.048, PII S0014579305007891
    • Smet, C., Wieruszeski, J. M., Buee, L., Landrieu, I., and Lippens, G. (2005) Regulation of Pin1 peptidyl-prolyl cis/trans isomerase activity by its WW binding module on a multi-phosphorylated peptide of Tau protein, FEBS Lett. 579, 4159-4164. (Pubitemid 41021806)
    • (2005) FEBS Letters , vol.579 , Issue.19 , pp. 4159-4164
    • Smet, C.1    Wieruszeski, J.-M.2    Buee, L.3    Landrieu, I.4    Lippens, G.5
  • 27
    • 0035943020 scopus 로고    scopus 로고
    • Phosphorylation of RNA polymerase II CTD fragments results in tight binding to the WW domain from the yeast prolyl isomerase Ess1
    • DOI 10.1021/bi0027884
    • Myers, J. K., Morris, D. P., Greenleaf, A. L., and Oas, T. G. (2001) Phosphorylation of RNA polymerase II CTD fragments results in tight binding to the WW domain from the yeast prolyl isomerase Ess1, Biochemistry 40, 8479-8486. (Pubitemid 32667252)
    • (2001) Biochemistry , vol.40 , Issue.29 , pp. 8479-8486
    • Myers, J.K.1    Morris, D.P.2    Greenleaf, A.L.3    Oas, T.G.4
  • 29
    • 0031572824 scopus 로고    scopus 로고
    • A protease-free assay for peptidyl prolyl cis/trans isomerases using standard peptide substrates
    • DOI 10.1006/abio.1997.2330
    • Janowski, B., Wöllner, S., Schutkowski, M., and Fischer, G. (1997) A protease-free assay for peptidyl prolyl cis/trans isomerases using standard peptide substrates, Anal. Biochem 252, 299-307. (Pubitemid 27449713)
    • (1997) Analytical Biochemistry , vol.252 , Issue.2 , pp. 299-307
    • Janowski, B.1    Wollner, S.2    Schutkowski, M.3    Fischer, G.4
  • 30
    • 0021668676 scopus 로고
    • NACHWEIS EINER ENZYMKATALYSE FUR DIE CIS-TRANS-ISOMERISIERUNG DER PEPTIDBINDUNG IN PROLINHALTIGEN PEPTIDEN
    • Fischer, G., Bang, H., and Mech, C. (1984) Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in proline-containing peptides, Biomed. Biochim. Acta 43, 1101-1111. (Pubitemid 15221717)
    • (1984) Biomedica Biochimica Acta , vol.43 , Issue.10 , pp. 1101-1111
    • Fischer, G.1    Bang, H.2    Mech, C.3
  • 31
    • 0020345697 scopus 로고
    • Buffers of constant ionic strength for studying pH-dependent processes
    • Ellis, K. J., and Morrison, J. F. (1982) Buffers of constant ionic strength for studying pH-dependent processes, Methods Enzymol. 87, 405-426.
    • (1982) Methods Enzymol. , vol.87 , pp. 405-426
    • Ellis, K.J.1    Morrison, J.F.2
  • 32
    • 0028146012 scopus 로고
    • Structure based prediction of protein folding intermediates
    • DOI 10.1006/jmbi.1994.1557
    • Xie, D., and Freire, E. (1994) Structure based prediction of protein folding intermediates, J. Mol. Biol. 242, 62-80. (Pubitemid 24285439)
    • (1994) Journal of Molecular Biology , vol.242 , Issue.1 , pp. 62-80
    • Xie, D.1    Freire, E.2
  • 33
    • 4143121554 scopus 로고    scopus 로고
    • Free energy of ligand binding to protein: Evaluation of the contribution of water molecules by computational methods
    • Cozzini, P., Fornabaio, M., Marabotti, A., Abraham, D. J., Kellogg, G. E., and Mozzarelli, A. (2004) Free energy of ligand binding to protein: evaluation of the contribution of water molecules by computational methods, Curr. Med. Chem. 11, 3093-3118. (Pubitemid 39545578)
    • (2004) Current Medicinal Chemistry , vol.11 , Issue.23 , pp. 3093-3118
    • Cozzini, P.1    Fornabaio, M.2    Marabotti, A.3    Abraham, D.J.4    Kellogs, G.E.5    Mozzarelli, A.6
  • 34
    • 0021093448 scopus 로고
    • Enthalpy - Entropy compensation and heat capacity changes for protein - ligand interactions: General thermodynamic models and data for the binding of nucleotides to ribonuclease A
    • Eftink, M. R., Anusiem, A. C., and Biltonen, R. L. (1983) Enthalpy - entropy compensation and heat capacity changes for protein - ligand interactions: general thermodynamic models and data for the binding of nucleotides to ribonuclease A, Biochemistry 22, 3884-3896.
    • (1983) Biochemistry , vol.22 , pp. 3884-3896
    • Eftink, M.R.1    Anusiem, A.C.2    Biltonen, R.L.3
  • 35
    • 0038448924 scopus 로고    scopus 로고
    • Structural analysis of the mitotic regulator hPin1 in solution: Insights into domain architecture and substrate binding
    • DOI 10.1074/jbc.M300721200
    • Bayer, E., Goettsch, S., Mueller, J. W., Griewel, B., Guiberman, E., Mayr, L. M., and Bayer, P. (2003) Structural analysis of the mitotic regulator Pin1 in solution: insights into domain architecture and substrate binding, J. Biol. Chem. 278, 26183-26193. (Pubitemid 36835387)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.28 , pp. 26183-26193
    • Bayer, E.1    Goettsch, S.2    Mueller, J.W.3    Griewel, B.4    Guiberman, E.5    Mayr, L.M.6    Bayer, P.7
  • 36
    • 0030876333 scopus 로고    scopus 로고
    • Rotational barriers of cis/trans isomerization of proline analogues and their catalysis by cyclophilin
    • DOI 10.1021/ja970606w
    • Kern, D., Schutkowski, M., and Drakenberg, T. (1997) Rotational barriers of cis/trans isomerization of proline analogues and their catalysis by cyclophilin, J. Am. Chem. Soc. 119, 8403-8408. (Pubitemid 27404565)
    • (1997) Journal of the American Chemical Society , vol.119 , Issue.36 , pp. 8403-8408
    • Kern, D.1    Schutkowski, M.2    Drakenberg, T.3
  • 37
    • 0031718528 scopus 로고    scopus 로고
    • Mapping the stereospecificity of peptidyl prolyl cis/trans isomerases
    • DOI 10.1016/S0014-5793(98)00871-0, PII S0014579398008710
    • Schiene, C., Reimer, U., Schutkowski, M., and Fischer, G. (1998) Mapping the stereospecificity of peptidyl prolyl cis/trans isomerases, FEBS Lett. 432, 202-206. (Pubitemid 28473275)
    • (1998) FEBS Letters , vol.432 , Issue.3 , pp. 202-206
    • Schiene, C.1    Reimer, U.2    Schutkowski, M.3    Fischer, G.4
  • 38
    • 0037438354 scopus 로고    scopus 로고
    • Thermodynamic characterization of the interaction of human cyclophilin 18 with cyclosporin A
    • DOI 10.1016/S0301-4622(02)00292-2, PII S0301462202002922
    • Fanghänel, J., and Fischer, G. (2003) Thermodynamic characterization of the interaction of human cyclophilin 18 with cyclosporin A, Biophys. Chem. 100, 351-366. (Pubitemid 36338052)
    • (2003) Biophysical Chemistry , vol.100 , Issue.1-3 , pp. 351-366
    • Fanghanel, J.1    Fischer, G.2
  • 39
    • 0029395478 scopus 로고
    • Win some, lose some: Enthalpy-entropy compensation in weak intermolecular interactions
    • Dunitz, J. D. (1995) Win some, lose some: enthalpy-entropy compensation in weak intermolecular interactions, Chem. Biol. 2, 709-712.
    • (1995) Chem. Biol. , vol.2 , pp. 709-712
    • Dunitz, J.D.1
  • 40
    • 3543005385 scopus 로고    scopus 로고
    • Thermodynamics of protein-ligand interactions: History, presence, and future aspects
    • DOI 10.1081/RRS-120037896
    • Perozzo, R., Folkers, G., and Scapozza, L. (2004) Thermodynamics of protein-ligand interactions: history, presence, and future aspects, J. Recept. Signal Transduction Res. 24, 1-52. (Pubitemid 39011288)
    • (2004) Journal of Receptors and Signal Transduction , vol.24 , Issue.1-2 , pp. 1-52
    • Perozzo, R.1    Folkers, G.2    Scapozza, L.3
  • 41
    • 14744268745 scopus 로고    scopus 로고
    • Heat capacity effects in protein folding and ligand binding: A re-evaluation of the role of water in biomolecular thermodynamics
    • Cooper, A. (2005) Heat capacity effects in protein folding and ligand binding: a re-evaluation of the role of water in biomolecular thermodynamics, Biophys. Chem. 115, 89-97.
    • (2005) Biophys. Chem. , vol.115 , pp. 89-97
    • Cooper, A.1
  • 42
    • 22544455987 scopus 로고    scopus 로고
    • Regulation of Pin1 peptidyl-prolyl cis/trans isomerase activity by its WW binding module on a multi-phosphorylated peptide of Tau protein
    • DOI 10.1016/j.febslet.2005.06.048, PII S0014579305007891
    • Smet, C., Wieruszeski, J. M., Buee, L., Landrieu, I., and Lippens, G. (2005) Regulation of Pin1 peptidyl-prolyl cis/trans isomerase activity by its WW binding module on a multi-phosphorylated peptide of Tau protein, FEBS Lett. 579, 4159-4164. (Pubitemid 41021806)
    • (2005) FEBS Letters , vol.579 , Issue.19 , pp. 4159-4164
    • Smet, C.1    Wieruszeski, J.-M.2    Buee, L.3    Landrieu, I.4    Lippens, G.5
  • 44
    • 13444259420 scopus 로고    scopus 로고
    • nrb is multiphosphorylated in mitosis and interacts with the mitotic regulator Pin1
    • DOI 10.1016/j.jmb.2004.12.034
    • Proteau, A., Blier, S., Albert, A. L., Lavoie, S. B., Traish, A. M., and Vincent, M. (2005) The multifunctional nuclear protein p54-(nrb) is multiphosphorylated in mitosis and interacts with the mitotic regulator Pin1, J. Mol. Biol. 346, 1163-1172. (Pubitemid 40215536)
    • (2005) Journal of Molecular Biology , vol.346 , Issue.4 , pp. 1163-1172
    • Proteau, A.1    Blier, S.2    Albert, A.L.3    Lavoie, S.B.4    Traish, A.M.5    Vincent, M.6
  • 46
    • 17644413069 scopus 로고    scopus 로고
    • Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae
    • DOI 10.1074/jbc.M412172200
    • Gemmill, T. R., Wu, X., and Hanes, S. D. (2005) Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae, J. Biol. Chem. 280, 15510-15517. (Pubitemid 40616666)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.16 , pp. 15510-15517
    • Gemmill, T.R.1    Wu, X.2    Hanes, S.D.3
  • 48
    • 0032574832 scopus 로고    scopus 로고
    • Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone
    • DOI 10.1021/bi973162p
    • Hennig, L., Christner, C., Kipping, M., Schelbert, B., Rücknagel, K. P., Grabley, S., Küllertz, G., and Fischer, G. (1998) Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone, Biochemistry 37, 5953-5960. (Pubitemid 28196748)
    • (1998) Biochemistry , vol.37 , Issue.17 , pp. 5953-5960
    • Hennig, L.1    Christner, C.2    Kipping, M.3    Schelbert, B.4    Rucknagel, K.P.5    Grabley, S.6    Kullertz, G.7    Fischer, G.8
  • 49
    • 0141448966 scopus 로고    scopus 로고
    • Thermodynamic and extrathermodynamic requirements of enzyme catalysis
    • Wolfenden, R. (2003) Thermodynamic and extrathermodynamic requirements of enzyme catalysis, Biophys. Chem. 105, 559-572.
    • (2003) Biophys. Chem. , vol.105 , pp. 559-572
    • Wolfenden, R.1


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