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Volumn 5, Issue 6, 2006, Pages 1467-1473

Functional analysis and molecular modeling show a preserved wild-type activity of p53C238Y

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN MDM2; PROTEIN P53; SERINE;

EID: 33746079646     PISSN: 15357163     EISSN: None     Source Type: Journal    
DOI: 10.1158/1535-7163.MCT-06-0012     Document Type: Article
Times cited : (17)

References (33)
  • 1
    • 18344377030 scopus 로고    scopus 로고
    • The p53 pathway: Positive and negative feedback loops
    • Harris SL, Levine AJ. The p53 pathway: positive and negative feedback loops. Oncogene 2005;24:2899-908.
    • (2005) Oncogene , vol.24 , pp. 2899-2908
    • Harris, S.L.1    Levine, A.J.2
  • 2
    • 0031724593 scopus 로고    scopus 로고
    • Nuclear export is required for degradation of enclogenous p53 by MDM2 and human papillomavirus E6
    • Freedman DA, Levine AJ. Nuclear export is required for degradation of enclogenous p53 by MDM2 and human papillomavirus E6. Mol Cell Biol 1998;18:7288-93.
    • (1998) Mol Cell Biol , vol.18 , pp. 7288-7293
    • Freedman, D.A.1    Levine, A.J.2
  • 3
    • 0028098165 scopus 로고
    • Molecular abnormalities of mdm2 and p53 genes in adult soft tissue sarcomas
    • Cordon-Cardo C, Latres E, Drobnjak N, et al. Molecular abnormalities of mdm2 and p53 genes in adult soft tissue sarcomas. Cancer Res 1994;54:794-9.
    • (1994) Cancer Res , vol.54 , pp. 794-799
    • Cordon-Cardo, C.1    Latres, E.2    Drobnjak, N.3
  • 4
    • 0031046598 scopus 로고    scopus 로고
    • Distinct mdm2/p53 expression patterns in liposarcoma subgroups: Implications for different pathogenetic mechanisms
    • Pilotti S, Della Torre G, Lavarino C, et al. Distinct mdm2/p53 expression patterns in liposarcoma subgroups: implications for different pathogenetic mechanisms. J Pathol 1997;181:14-24.
    • (1997) J Pathol , vol.181 , pp. 14-24
    • Pilotti, S.1    Della Torre, G.2    Lavarino, C.3
  • 6
    • 0034979601 scopus 로고    scopus 로고
    • Rb and TP53 pathway alterations in sporadic and NF1-related malignant peripheral nerve sheath tumors
    • Birindelli S, Perrone F, Oggionni M, et al . Rb and TP53 pathway alterations in sporadic and NF1-related malignant peripheral nerve sheath tumors. Lab Invest 2001;81:833-44.
    • (2001) Lab Invest , vol.81 , pp. 833-844
    • Birindelli, S.1    Perrone, F.2    Oggionni, M.3
  • 7
    • 3843053704 scopus 로고    scopus 로고
    • INK4a inactivation in sporadic and neurofibromatosis type 1-related malignant peripheral nerve sheath tumors
    • INK4a inactivation in sporadic and neurofibromatosis type 1-related malignant peripheral nerve sheath tumors. Clin Cancer Res 2003;9:4132-8.
    • (2003) Clin Cancer Res , vol.9 , pp. 4132-4138
    • Perrone, F.1    Tabano, S.2    Colombo, F.3
  • 8
    • 0032710531 scopus 로고    scopus 로고
    • Biochemical uncovering of mdm2/p53 complexes in liposarcomas parallels their immunohistochemical detection
    • Butò S, Pierotti MA, Tamborini E, et al. Biochemical uncovering of mdm2/p53 complexes in liposarcomas parallels their immunohistochemical detection. Diagn Mol Pathol 1999;8:125-30.
    • (1999) Diagn Mol Pathol , vol.8 , pp. 125-130
    • Butò, S.1    Pierotti, M.A.2    Tamborini, E.3
  • 10
    • 0029011701 scopus 로고
    • A second generation force field for the simulation of proteins and nucleic acids
    • Cornell WD, Cieplak P, Bayly CI, et al. A second generation force field for the simulation of proteins and nucleic acids. J Am Chem Soc 1995; 117:5179-97.
    • (1995) J Am Chem Soc , vol.117 , pp. 5179-5197
    • Cornell, W.D.1    Cieplak, P.2    Bayly, C.I.3
  • 11
    • 0030040323 scopus 로고    scopus 로고
    • Reduced surface: An efficient way to compute molecular surfaces
    • Sanner MF, Olson AJ, Spehner JC. Reduced surface: an efficient way to compute molecular surfaces. Biopolymers 1996;38:305-20.
    • (1996) Biopolymers , vol.38 , pp. 305-320
    • Sanner, M.F.1    Olson, A.J.2    Spehner, J.C.3
  • 12
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
    • Cho Y, Gorina S, Jeffrey PD, Pavletich NP. Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Science 1994;265:346-65
    • (1994) Science , vol.265 , pp. 346-365
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 13
    • 0034614387 scopus 로고    scopus 로고
    • Investigating the binding specificity of U 1A-RNA by computational mutagenesis
    • Reyes CM, Kollman PA. Investigating the binding specificity of U 1A-RNA by computational mutagenesis. J Mol Biol 2000;295:1-6.
    • (2000) J Mol Biol , vol.295 , pp. 1-6
    • Reyes, C.M.1    Kollman, P.A.2
  • 14
    • 23844553757 scopus 로고    scopus 로고
    • T3151-mutated Bcr-Abl in chronic myeloid leucemia and imatinib; insights from a computational study
    • Pricl S, Fermeglia M, Ferrone M, Tamborini E. T3151-mutated Bcr-Abl in chronic myeloid leucemia and imatinib; insights from a computational study. Mol Cancer Ther 2005;4:1167-74.
    • (2005) Mol Cancer Ther , vol.4 , pp. 1167-1174
    • Pricl, S.1    Fermeglia, M.2    Ferrone, M.3    Tamborini, E.4
  • 16
    • 33846823909 scopus 로고
    • Particle mesh Ewald-an Nlog(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L. Particle mesh Ewald-an Nlog(N) method for Ewald sums in large systems. J Chem Phys 1993;98:1089-92.
    • (1993) J Chem Phys , vol.98 , pp. 1089-1092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 17
    • 0032560959 scopus 로고
    • Continuum solvent studies of the stability of DNA, RNA, and phosphoramidate-DNA helices
    • Srinivasan J, Cheathem TE III, Cieplak P, Kollman PA, Case DA. Continuum solvent studies of the stability of DNA, RNA, and phosphoramidate-DNA helices. J Am Chem Soc 1993;120:9401-9.
    • (1993) J Am Chem Soc , vol.120 , pp. 9401-9409
    • Srinivasan, J.1    Cheathem III, T.E.2    Cieplak, P.3    Kollman, P.A.4    Case, D.A.5
  • 18
    • 84988087911 scopus 로고
    • Calculating the electrostatic potential of molecules in solution: Method and error assessment
    • Gilson MK, Sharp KA, Honig B. Calculating the electrostatic potential of molecules in solution: method and error assessment. J Comput Chem 1987;9:327-35.
    • (1987) J Comput Chem , vol.9 , pp. 327-335
    • Gilson, M.K.1    Sharp, K.A.2    Honig, B.3
  • 19
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig B, Nicholls A. Classical electrostatics in biology and chemistry. Science 1995;268:1144-9.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 20
    • 32844457567 scopus 로고
    • Accurate calculation of hydration free energies using macroscopic solvent models
    • Sitkoff D, Sharp KA, Honig B. Accurate calculation of hydration free energies using macroscopic solvent models. J Phys Chem 1994;98:1978-88.
    • (1994) J Phys Chem , vol.98 , pp. 1978-1988
    • Sitkoff, D.1    Sharp, K.A.2    Honig, B.3
  • 21
    • 0000885331 scopus 로고
    • Harmonic analysis of large systems. 1. Methodology
    • Brooks BR, Janežič D, Karplus M. Harmonic analysis of large systems. 1. Methodology. J Comput Chem 1995;16:1522-42.
    • (1995) J Comput Chem , vol.16 , pp. 1522-1542
    • Brooks, B.R.1    Janežič, D.2    Karplus, M.3
  • 23
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JIM. PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 1993;26:283-91.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.I.M.4
  • 24
    • 0031718310 scopus 로고    scopus 로고
    • Homology modeling, model and software evaluation: Three related sources
    • Rhodriguez R, Chinea G, Lopez N, Pons T, Vriend G. Homology modeling, model and software evaluation: three related sources. CABIOS 1998;14:523-8.
    • (1998) CABIOS , vol.14 , pp. 523-528
    • Rhodriguez, R.1    Chinea, G.2    Lopez, N.3    Pons, T.4    Vriend, G.5
  • 25
    • 0036415663 scopus 로고    scopus 로고
    • p53 contains large unstructured regions in its native state
    • Bell S, Klein C, Willer L, Hansen S, Buchner J. p53 contains large unstructured regions in its native state. J Mol Biol 2002;322:917-27.
    • (2002) J Mol Biol , vol.322 , pp. 917-927
    • Bell, S.1    Klein, C.2    Willer, L.3    Hansen, S.4    Buchner, J.5
  • 26
    • 0028016446 scopus 로고
    • Characterization of baculovirus recombinant wild-type p53. Dimerization of p53 is required for high-affinity DNA binding and cysteine oxidation inhibits p53 DNA binding
    • Delphin C, Cahen P, Lawrence JJ, Baudier J. Characterization of baculovirus recombinant wild-type p53. Dimerization of p53 is required for high-affinity DNA binding and cysteine oxidation inhibits p53 DNA binding. Eur J Biochem 1994;223:683-92.
    • (1994) Eur J Biochem , vol.223 , pp. 683-692
    • Delphin, C.1    Cahen, P.2    Lawrence, J.J.3    Baudier, J.4
  • 28
    • 0036606407 scopus 로고    scopus 로고
    • Redox state of tumor suppressor p53 regulates its sequence-specific DNA binding in DNA-damaged cells by cysteine 277
    • Buzek J, Latonen L, Kurki S, Peltonen K, Laiho M. Redox state of tumor suppressor p53 regulates its sequence-specific DNA binding in DNA-damaged cells by cysteine 277. Nucleic Acids Res 2002;30:2340-8.
    • (2002) Nucleic Acids Res , vol.30 , pp. 2340-2348
    • Buzek, J.1    Latonen, L.2    Kurki, S.3    Peltonen, K.4    Laiho, M.5
  • 29
    • 10744223812 scopus 로고    scopus 로고
    • Formation of disulfide bond in p53 correlates with inhibition of DNA binding and tetramerization
    • Sun XZ, Vinci C, Makmura L, et al. Formation of disulfide bond in p53 correlates with inhibition of DNA binding and tetramerization. Antioxid Redox Signal 2003;5:655-65.
    • (2003) Antioxid Redox Signal , vol.5 , pp. 655-665
    • Sun, X.Z.1    Vinci, C.2    Makmura, L.3
  • 30
    • 28444459974 scopus 로고    scopus 로고
    • Recognition of cisplatin-damaged DNA by p53 protein: Critical role of the p53 C-terminal domain
    • Pivonkova H, Brazdova M, Kasparkova J, Brabec V, Fojta M. Recognition of cisplatin-damaged DNA by p53 protein: critical role of the p53 C-terminal domain. Biochem Biophys Res Commun 2006;339:477-84.
    • (2006) Biochem Biophys Res Commun , vol.339 , pp. 477-484
    • Pivonkova, H.1    Brazdova, M.2    Kasparkova, J.3    Brabec, V.4    Fojta, M.5
  • 31
    • 0031447171 scopus 로고    scopus 로고
    • Thermodynamic stability of wild-type and mutant p53 core domain
    • Bullock AN, Henckel J, DeDecker BS, et al. Thermodynamic stability of wild-type and mutant p53 core domain. Proc Natl Acad Sci U S A 1997;94:14338-42.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 14338-14342
    • Bullock, A.N.1    Henckel, J.2    DeDecker, B.S.3
  • 32
    • 0034594995 scopus 로고    scopus 로고
    • Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: Definition of mutant states for rescue in cancer therapy
    • Bullock AN, Henckel J, Fersht AR. Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: definition of mutant states for rescue in cancer therapy. Oncogene 2000;19:1245-56.
    • (2000) Oncogene , vol.19 , pp. 1245-1256
    • Bullock, A.N.1    Henckel, J.2    Fersht, A.R.3
  • 33
    • 0035860350 scopus 로고    scopus 로고
    • Tyrosine hydrogen bends make a large contribution to protein stability
    • Pace CN, Horn G, Herbert EJ, et al. Tyrosine hydrogen bends make a large contribution to protein stability. J Mol Biol 2001;321:393-404.
    • (2001) J Mol Biol , vol.321 , pp. 393-404
    • Pace, C.N.1    Horn, G.2    Herbert, E.J.3


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