메뉴 건너뛰기




Volumn 332, Issue 5, 2003, Pages 1131-1141

The N-terminal domain of p53 is natively unfolded

Author keywords

CD spectroscopy; IUP; Mdm2; NMR spectroscopy; p53

Indexed keywords

PROTEIN MDM2; PROTEIN P53;

EID: 0041384333     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.08.008     Document Type: Article
Times cited : (204)

References (89)
  • 1
    • 0027109075 scopus 로고
    • Cancer. p53, guardian of the genome
    • Lane D.P. Cancer. p53, guardian of the genome. Nature. 358:1992;15-16.
    • (1992) Nature , vol.358 , pp. 15-16
    • Lane, D.P.1
  • 2
    • 0030941458 scopus 로고    scopus 로고
    • P53, the cellular gatekeeper for growth and division
    • Levine A.J. p53, the cellular gatekeeper for growth and division. Cell. 88:1997;323-331.
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 3
    • 0027749169 scopus 로고
    • A proteolytic fragment from the central region of p53 has marked sequence-specific DNA-binding activity when generated from wild-type but not from oncogenic mutant p53 protein
    • Bargonetti J., Manfredi J.J., Chen X., Marshak D.R., Prives C. A proteolytic fragment from the central region of p53 has marked sequence-specific DNA-binding activity when generated from wild-type but not from oncogenic mutant p53 protein. Genes Dev. 7:1993;2565-2574.
    • (1993) Genes Dev. , vol.7 , pp. 2565-2574
    • Bargonetti, J.1    Manfredi, J.J.2    Chen, X.3    Marshak, D.R.4    Prives, C.5
  • 4
    • 0027771333 scopus 로고
    • The DNA-binding domain of p53 contains the four conserved regions and the major mutation hot spots
    • Pavletich N.P., Chambers K.A., Pabo C.O. The DNA-binding domain of p53 contains the four conserved regions and the major mutation hot spots. Genes Dev. 7:1993;2556-2564.
    • (1993) Genes Dev. , vol.7 , pp. 2556-2564
    • Pavletich, N.P.1    Chambers, K.A.2    Pabo, C.O.3
  • 5
    • 0027744051 scopus 로고
    • P53 domains: Identification and characterization of two autonomous DNA-binding regions
    • Wang Y., Reed M., Wang P., Stenger J.E., Mayr G., Anderson M.E., et al. p53 domains: identification and characterization of two autonomous DNA-binding regions. Genes Dev. 7:1993;2575-2586.
    • (1993) Genes Dev. , vol.7 , pp. 2575-2586
    • Wang, Y.1    Reed, M.2    Wang, P.3    Stenger, J.E.4    Mayr, G.5    Anderson, M.E.6
  • 6
    • 0037007442 scopus 로고    scopus 로고
    • Refolding and structural characterization of the human p53 tumor suppressor protein
    • Bell S., Hansen S., Buchner J. Refolding and structural characterization of the human p53 tumor suppressor protein. Biophys. Chem. 96:2002;243-257.
    • (2002) Biophys. Chem. , vol.96 , pp. 243-257
    • Bell, S.1    Hansen, S.2    Buchner, J.3
  • 7
    • 0025024469 scopus 로고
    • Presence of a potent transcription activating sequence in the p53 protein
    • Fields S., Jang S.K. Presence of a potent transcription activating sequence in the p53 protein. Science. 249:1990;1046-1049.
    • (1990) Science , vol.249 , pp. 1046-1049
    • Fields, S.1    Jang, S.K.2
  • 8
    • 0025193635 scopus 로고
    • Transcriptional activation by wild-type but not transforming mutants of the p53 anti-oncogene
    • Raycroft L., Wu H.Y., Lozano G. Transcriptional activation by wild-type but not transforming mutants of the p53 anti-oncogene. Science. 249:1990;1049-1051.
    • (1990) Science , vol.249 , pp. 1049-1051
    • Raycroft, L.1    Wu, H.Y.2    Lozano, G.3
  • 10
    • 0026637484 scopus 로고
    • A C-terminal alpha-helix plus basic region motif is the major structural determinant of p53 tetramerization
    • Sturzbecher H.W., Brain R., Addison C., Rudge K., Remm M., Grimaldi M., et al. A C-terminal alpha-helix plus basic region motif is the major structural determinant of p53 tetramerization. Oncogene. 7:1992;1513-1523.
    • (1992) Oncogene , vol.7 , pp. 1513-1523
    • Sturzbecher, H.W.1    Brain, R.2    Addison, C.3    Rudge, K.4    Remm, M.5    Grimaldi, M.6
  • 11
    • 0027174586 scopus 로고
    • Use of the two-hybrid system to identify the domain of p53 involved in oligomerization
    • Iwabuchi K., Li B., Bartel P., Fields S. Use of the two-hybrid system to identify the domain of p53 involved in oligomerization. Oncogene. 8:1993;1693-1696.
    • (1993) Oncogene , vol.8 , pp. 1693-1696
    • Iwabuchi, K.1    Li, B.2    Bartel, P.3    Fields, S.4
  • 12
    • 0030011897 scopus 로고    scopus 로고
    • New insights into p53 function from structural studies
    • Arrowsmith C.H., Morin P. New insights into p53 function from structural studies. Oncogene. 12:1996;1379-1385.
    • (1996) Oncogene , vol.12 , pp. 1379-1385
    • Arrowsmith, C.H.1    Morin, P.2
  • 13
    • 0033387525 scopus 로고    scopus 로고
    • Structure and function in the p53 family
    • Arrowsmith C.H. Structure and function in the p53 family. Cell Death Differ. 6:1999;1169-1173.
    • (1999) Cell Death Differ. , vol.6 , pp. 1169-1173
    • Arrowsmith, C.H.1
  • 14
    • 0034862475 scopus 로고    scopus 로고
    • The C-terminus of p53: The more you learn the less you know
    • Ahn J., Prives C. The C-terminus of p53: the more you learn the less you know. Nature Struct. Biol. 8:2001;730-732.
    • (2001) Nature Struct. Biol. , vol.8 , pp. 730-732
    • Ahn, J.1    Prives, C.2
  • 15
    • 0033945124 scopus 로고    scopus 로고
    • Structure of the negative regulatory domain of p53 bound to S100B(betabeta)
    • Rustandi R.R., Baldisseri D.M., Weber D.J. Structure of the negative regulatory domain of p53 bound to S100B(betabeta). Nature Struct. Biol. 7:2000;570-574.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 570-574
    • Rustandi, R.R.1    Baldisseri, D.M.2    Weber, D.J.3
  • 16
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
    • Cho Y., Gorina S., Jeffrey P.D., Pavletich N.P. Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Science. 265:1994;346-355.
    • (1994) Science , vol.265 , pp. 346-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 21
    • 0035966083 scopus 로고    scopus 로고
    • NMR spectroscopy reveals the solution dimerization interface of p53 core domains bound to their consensus DNA
    • Klein C., Planker E., Diercks T., Kessler H., Kunkele K.P., Lang K., et al. NMR spectroscopy reveals the solution dimerization interface of p53 core domains bound to their consensus DNA. J. Biol. Chem. 276:2001;49020-49027.
    • (2001) J. Biol. Chem. , vol.276 , pp. 49020-49027
    • Klein, C.1    Planker, E.2    Diercks, T.3    Kessler, H.4    Kunkele, K.P.5    Lang, K.6
  • 22
    • 0037418548 scopus 로고    scopus 로고
    • Structure, function, and aggregation of the zinc-free form of the p53 DNA binding domain
    • Butler J.S., Loh S.N. Structure, function, and aggregation of the zinc-free form of the p53 DNA binding domain. Biochemistry. 42:2003;2396-2403.
    • (2003) Biochemistry , vol.42 , pp. 2396-2403
    • Butler, J.S.1    Loh, S.N.2
  • 23
    • 0035853734 scopus 로고    scopus 로고
    • Crystal structure of the mouse p53 core DNA-binding domain at 2.7 Å resolution
    • Zhao K., Chai X., Johnston K., Clements A., Marmorstein R. Crystal structure of the mouse p53 core DNA-binding domain at 2.7 Å resolution. J. Biol. Chem. 276:2001;12120-12127.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12120-12127
    • Zhao, K.1    Chai, X.2    Johnston, K.3    Clements, A.4    Marmorstein, R.5
  • 25
    • 0028952841 scopus 로고
    • Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms
    • Jeffrey P.D., Gorina S., Pavletich N.P. Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms. Science. 267:1995;1498-1502.
    • (1995) Science , vol.267 , pp. 1498-1502
    • Jeffrey, P.D.1    Gorina, S.2    Pavletich, N.P.3
  • 26
    • 0030575866 scopus 로고    scopus 로고
    • Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2
    • Gorina S., Pavletich N.P. Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2. Science. 274:1996;1001-1005.
    • (1996) Science , vol.274 , pp. 1001-1005
    • Gorina, S.1    Pavletich, N.P.2
  • 27
    • 0031951844 scopus 로고    scopus 로고
    • Crystallization and structure solution of p53 (residues 326-356) by molecular replacement using an NMR model as template
    • Mittl P.R., Chene P., Grutter M.G. Crystallization and structure solution of p53 (residues 326-356) by molecular replacement using an NMR model as template. Acta Crystallog. sect. D. 54:1998;86-89.
    • (1998) Acta Crystallog. sect. D , vol.54 , pp. 86-89
    • Mittl, P.R.1    Chene, P.2    Grutter, M.G.3
  • 28
    • 0031303353 scopus 로고    scopus 로고
    • Solution conformation of an essential region of the p53 transactivation domain
    • Botuyan M.V., Momand J., Chen Y. Solution conformation of an essential region of the p53 transactivation domain. Fold. Des. 2:1997;331-342.
    • (1997) Fold. Des. , vol.2 , pp. 331-342
    • Botuyan, M.V.1    Momand, J.2    Chen, Y.3
  • 29
    • 0028812627 scopus 로고
    • Transactivation ability of p53 transcriptional activation domain is directly related to the binding affinity to TATA-binding protein
    • Chang J., Kim D.H., Lee S.W., Choi K.Y., Sung Y.C. Transactivation ability of p53 transcriptional activation domain is directly related to the binding affinity to TATA-binding protein. J. Biol. Chem. 270:1995;25014-25019.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25014-25019
    • Chang, J.1    Kim, D.H.2    Lee, S.W.3    Choi, K.Y.4    Sung, Y.C.5
  • 30
    • 0034703040 scopus 로고    scopus 로고
    • Local structural elements in the mostly unstructured transcriptional activation domain of human p53
    • Lee H., Mok K.H., Muhandiram R., Park K.H., Suk J.E., Kim D.H., et al. Local structural elements in the mostly unstructured transcriptional activation domain of human p53. J. Biol. Chem. 275:2000;29426-29432.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29426-29432
    • Lee, H.1    Mok, K.H.2    Muhandiram, R.3    Park, K.H.4    Suk, J.E.5    Kim, D.H.6
  • 31
    • 0030564943 scopus 로고    scopus 로고
    • Structural aspects of the p53 protein in relation to gene evolution: A second look
    • Soussi T., May P. Structural aspects of the p53 protein in relation to gene evolution: a second look. J. Mol. Biol. 260:1996;623-637.
    • (1996) J. Mol. Biol. , vol.260 , pp. 623-637
    • Soussi, T.1    May, P.2
  • 32
    • 0030798557 scopus 로고    scopus 로고
    • The polyproline region of p53 is required to activate apoptosis but not growth arrest
    • Sakamuro D., Sabbatini P., White E., Prendergast G.C. The polyproline region of p53 is required to activate apoptosis but not growth arrest. Oncogene. 15:1997;887-898.
    • (1997) Oncogene , vol.15 , pp. 887-898
    • Sakamuro, D.1    Sabbatini, P.2    White, E.3    Prendergast, G.C.4
  • 33
    • 0030448650 scopus 로고    scopus 로고
    • Identification of a novel p53 functional domain that is necessary for efficient growth suppression
    • Walker K.K., Levine A.J. Identification of a novel p53 functional domain that is necessary for efficient growth suppression. Proc. Natl Acad. Sci. USA. 93:1996;15335-15340.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 15335-15340
    • Walker, K.K.1    Levine, A.J.2
  • 34
    • 0032541325 scopus 로고    scopus 로고
    • The requirement for the p53 proline-rich functional domain for mediation of apoptosis is correlated with specific PIG3 gene transactivation and with transcriptional repression
    • Venot C., Maratrat M., Dureuil C., Conseiller E., Bracco L., Debussche L. The requirement for the p53 proline-rich functional domain for mediation of apoptosis is correlated with specific PIG3 gene transactivation and with transcriptional repression. EMBO J. 17:1998;4668-4679.
    • (1998) EMBO J. , vol.17 , pp. 4668-4679
    • Venot, C.1    Maratrat, M.2    Dureuil, C.3    Conseiller, E.4    Bracco, L.5    Debussche, L.6
  • 35
    • 0028979005 scopus 로고
    • Human TAFII31 protein is a transcriptional coactivator of the p53 protein
    • Lu H., Levine A.J. Human TAFII31 protein is a transcriptional coactivator of the p53 protein. Proc. Natl Acad. Sci. USA. 92:1995;5154-5158.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5154-5158
    • Lu, H.1    Levine, A.J.2
  • 36
    • 0028922929 scopus 로고
    • P53 transcriptional activation mediated by coactivators TAFII40 and TAFII60
    • Thut C.J., Chen J.L., Klemm R., Tjian R. p53 transcriptional activation mediated by coactivators TAFII40 and TAFII60. Science. 267:1995;100-104.
    • (1995) Science , vol.267 , pp. 100-104
    • Thut, C.J.1    Chen, J.L.2    Klemm, R.3    Tjian, R.4
  • 39
    • 0033592822 scopus 로고    scopus 로고
    • The alpha-helical FXXPhiPhi motif in p53: TAF interaction and discrimination by MDM2
    • Uesugi M., Verdine G.L. The alpha-helical FXXPhiPhi motif in p53: TAF interaction and discrimination by MDM2. Proc. Natl Acad. Sci. USA. 96:1999;14801-14806.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 14801-14806
    • Uesugi, M.1    Verdine, G.L.2
  • 40
    • 0027673764 scopus 로고
    • The p53-mdm2 autoregulatory feedback loop: A paradigm for the regulation of growth control by p53?
    • Picksley S.M., Lane D.P. The p53-mdm2 autoregulatory feedback loop: a paradigm for the regulation of growth control by p53? Bioessays. 15:1993;689-690.
    • (1993) Bioessays , vol.15 , pp. 689-690
    • Picksley, S.M.1    Lane, D.P.2
  • 41
    • 0027244853 scopus 로고
    • The p53-mdm-2 autoregulatory feedback loop
    • Wu X., Bayle J.H., Olson D., Levine A.J. The p53-mdm-2 autoregulatory feedback loop. Genes Dev. 7:1993;1126-1132.
    • (1993) Genes Dev. , vol.7 , pp. 1126-1132
    • Wu, X.1    Bayle, J.H.2    Olson, D.3    Levine, A.J.4
  • 42
    • 0037317840 scopus 로고    scopus 로고
    • Inhibiting the p53-MDM2 interaction: An important target for cancer therapy
    • Chene P. Inhibiting the p53-MDM2 interaction: an important target for cancer therapy. Nature Rev. Cancer. 3:2003;102-109.
    • (2003) Nature Rev. Cancer , vol.3 , pp. 102-109
    • Chene, P.1
  • 43
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y., Maya R., Kazaz A., Oren M. Mdm2 promotes the rapid degradation of p53. Nature. 387:1997;296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 44
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • Kubbutat M.H., Jones S.N., Vousden K.H. Regulation of p53 stability by Mdm2. Nature. 387:1997;299-303.
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutat, M.H.1    Jones, S.N.2    Vousden, K.H.3
  • 45
    • 0027222956 scopus 로고
    • Mapping of the p53 and mdm-2 interaction domains
    • Chen J., Marechal V., Levine A.J. Mapping of the p53 and mdm-2 interaction domains. Mol. Cell Biol. 13:1993;4107-4114.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 4107-4114
    • Chen, J.1    Marechal, V.2    Levine, A.J.3
  • 46
    • 0027964904 scopus 로고
    • Immunochemical analysis of the interaction of p53 with MDM2; - Fine mapping of the MDM2 binding site on p53 using synthetic peptides
    • Picksley S.M., Vojtesek B., Sparks A., Lane D.P. Immunochemical analysis of the interaction of p53 with MDM2; - fine mapping of the MDM2 binding site on p53 using synthetic peptides. Oncogene. 9:1994;2523-2529.
    • (1994) Oncogene , vol.9 , pp. 2523-2529
    • Picksley, S.M.1    Vojtesek, B.2    Sparks, A.3    Lane, D.P.4
  • 48
    • 0028303752 scopus 로고
    • Several hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 E1B 55-kD protein
    • Lin J., Chen J., Elenbaas B., Levine A.J. Several hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 E1B 55-kD protein. Genes Dev. 8:1994;1235-1246.
    • (1994) Genes Dev. , vol.8 , pp. 1235-1246
    • Lin, J.1    Chen, J.2    Elenbaas, B.3    Levine, A.J.4
  • 49
  • 50
    • 0036415663 scopus 로고    scopus 로고
    • P53 contains large unstructured regions in its native state
    • Bell S., Klein C., Muller L., Hansen S., Buchner J. p53 contains large unstructured regions in its native state. J. Mol. Biol. 322:2002;917-927.
    • (2002) J. Mol. Biol. , vol.322 , pp. 917-927
    • Bell, S.1    Klein, C.2    Muller, L.3    Hansen, S.4    Buchner, J.5
  • 51
    • 0037014618 scopus 로고    scopus 로고
    • Amino acid determinants of alpha-synuclein aggregation: Putting together pieces of the puzzle
    • Uversky V.N., Fink A.L. Amino acid determinants of alpha-synuclein aggregation: putting together pieces of the puzzle. FEBS Letters. 522:2002;9-13.
    • (2002) FEBS Letters , vol.522 , pp. 9-13
    • Uversky, V.N.1    Fink, A.L.2
  • 52
    • 0034328380 scopus 로고    scopus 로고
    • HYDRONMR: Prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations
    • de la Torre J.G., Huertas M.L.C.B. HYDRONMR: prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations. J. Magn. Reson. 147:2000;138-146.
    • (2000) J. Magn. Reson. , vol.147 , pp. 138-146
    • De la Torre, J.G.1    Huertas, M.L.C.B.2
  • 54
    • 33646376290 scopus 로고
    • Spin diffusion measurements - Spin echoes in presence of a time-dependent field gradient
    • Stejskal E.O., Tanner J.E. Spin diffusion measurements - spin echoes in presence of a time-dependent field gradient. J. Chem. Phys. 42:1965;288.
    • (1965) J. Chem. Phys. , vol.42 , pp. 288
    • Stejskal, E.O.1    Tanner, J.E.2
  • 56
    • 0030974359 scopus 로고    scopus 로고
    • On the interaction between p53 and MDM2: Transfer NOE study of a p53-derived peptide ligated to MDM2
    • Blommers M.J.J., Fendrich G., Garcia-Echeverria C., Chene P. On the interaction between p53 and MDM2: transfer NOE study of a p53-derived peptide ligated to MDM2. J. Am. Chem. Soc. 119:1997;3425-3426.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 3425-3426
    • Blommers, M.J.J.1    Fendrich, G.2    Garcia-Echeverria, C.3    Chene, P.4
  • 57
    • 0034664684 scopus 로고    scopus 로고
    • Thermodynamics of p53 binding to hdm2(1-126): Effects of phosphorylation and p53 peptide length
    • Lai Z., Auger K.R., Manubay C.M., Copeland R.A. Thermodynamics of p53 binding to hdm2(1-126): effects of phosphorylation and p53 peptide length. Arch. Biochem. Biophys. 381:2000;278-284.
    • (2000) Arch. Biochem. Biophys. , vol.381 , pp. 278-284
    • Lai, Z.1    Auger, K.R.2    Manubay, C.M.3    Copeland, R.A.4
  • 58
    • 0037081033 scopus 로고    scopus 로고
    • A fluorescence polarization assay for the identification of inhibitors of the p53-DM2 protein-protein interaction
    • Knight S.M., Umezawa N., Lee H.S., Gellman S.H., Kay B.K. A fluorescence polarization assay for the identification of inhibitors of the p53-DM2 protein-protein interaction. Anal. Biochem. 300:2002;230-236.
    • (2002) Anal. Biochem. , vol.300 , pp. 230-236
    • Knight, S.M.1    Umezawa, N.2    Lee, H.S.3    Gellman, S.H.4    Kay, B.K.5
  • 59
    • 0034737438 scopus 로고    scopus 로고
    • Damage-mediated phosphorylation of human p53 threonine 18 through a cascade mediated by a casein 1-like kinase. Effect on Mdm2 binding
    • Sakaguchi K., Saito S., Higashimoto Y., Roy S., Anderson C.W., Appella E. Damage-mediated phosphorylation of human p53 threonine 18 through a cascade mediated by a casein 1-like kinase. Effect on Mdm2 binding. J. Biol. Chem. 275:2000;9278-9283.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9278-9283
    • Sakaguchi, K.1    Saito, S.2    Higashimoto, Y.3    Roy, S.4    Anderson, C.W.5    Appella, E.6
  • 60
    • 0034664684 scopus 로고    scopus 로고
    • Thermodynamics of p53 binding to hdm2(1-126): Effects of phosphorylation and p53 peptide length
    • Lai Z., Auger K.R., Manubay C.M., Copeland R.A. Thermodynamics of p53 binding to hdm2(1-126): effects of phosphorylation and p53 peptide length. Arch. Biochem. Biophys. 381:2000;278-284.
    • (2000) Arch. Biochem. Biophys. , vol.381 , pp. 278-284
    • Lai, Z.1    Auger, K.R.2    Manubay, C.M.3    Copeland, R.A.4
  • 61
    • 0037047345 scopus 로고    scopus 로고
    • The conformationally flexible S9-S10 linker region in the core domain of p53 contains a novel MDM2 binding site whose mutation increases ubiquitination of p53 in vivo
    • Shimizu H., Burch L.R., Smith A.J., Dornan D., Wallace M., Ball K.L., Hupp T.R. The conformationally flexible S9-S10 linker region in the core domain of p53 contains a novel MDM2 binding site whose mutation increases ubiquitination of p53 in vivo. J. Biol. Chem. 277:2002;28446-28458.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28446-28458
    • Shimizu, H.1    Burch, L.R.2    Smith, A.J.3    Dornan, D.4    Wallace, M.5    Ball, K.L.6    Hupp, T.R.7
  • 62
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P. Intrinsically unstructured proteins. Trends Biochem. Sci. 27:2002;527-533.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 527-533
    • Tompa, P.1
  • 65
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson H.J., Wright P.E. Coupling of folding and binding for unstructured proteins. Curr. Opin. Struct. Biol. 12:2002;54-60.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 66
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • Uversky V.N. What does it mean to be natively unfolded? Eur. J. Biochem. 269:2002;2-12.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 67
    • 0027474991 scopus 로고
    • Left-handed polyproline II helices commonly occur in globular proteins
    • Adzhubei A.A., Sternberg M.J. Left-handed polyproline II helices commonly occur in globular proteins. J. Mol. Biol. 229:1993;472-493.
    • (1993) J. Mol. Biol. , vol.229 , pp. 472-493
    • Adzhubei, A.A.1    Sternberg, M.J.2
  • 68
    • 0028808762 scopus 로고
    • An approach to protein homology modelling based on an ensemble of NMR structures: Application to the Sox-5 HMG-box protein
    • Adzhubei A.A., Laughton C.A., Neidle S. An approach to protein homology modelling based on an ensemble of NMR structures: application to the Sox-5 HMG-box protein. Protein Eng. 8:1995;615-625.
    • (1995) Protein Eng. , vol.8 , pp. 615-625
    • Adzhubei, A.A.1    Laughton, C.A.2    Neidle, S.3
  • 69
    • 0028097921 scopus 로고
    • The structure and function of proline-rich regions in proteins
    • Williamson M.P. The structure and function of proline-rich regions in proteins. Biochem. J. 297:1994;249-260.
    • (1994) Biochem. J. , vol.297 , pp. 249-260
    • Williamson, M.P.1
  • 70
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains
    • Kay B.K., Williamson M.P., Sudol M. The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J. 14:2000;231-241.
    • (2000) FASEB J. , vol.14 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 71
    • 0035030510 scopus 로고    scopus 로고
    • SH3 domains: Complexity in moderation
    • Mayer B.J. SH3 domains: complexity in moderation. J. Cell Sci. 114:2001;1253-1263.
    • (2001) J. Cell Sci. , vol.114 , pp. 1253-1263
    • Mayer, B.J.1
  • 72
    • 0033552638 scopus 로고    scopus 로고
    • Twenty years of p53 research: Structural and functional aspects of the p53 protein
    • May P., May E. Twenty years of p53 research: structural and functional aspects of the p53 protein. Oncogene. 18:1999;7621-7636.
    • (1999) Oncogene , vol.18 , pp. 7621-7636
    • May, P.1    May, E.2
  • 73
    • 0029972806 scopus 로고    scopus 로고
    • P53: Puzzle and paradigm
    • Ko L.J., Prives C. p53: puzzle and paradigm. Genes Dev. 10:1996;1054-1072.
    • (1996) Genes Dev. , vol.10 , pp. 1054-1072
    • Ko, L.J.1    Prives, C.2
  • 74
    • 0027311259 scopus 로고
    • Close encounters: Why unstructured, polymeric domains can increase rates of specific macromolecular association
    • Pontius B.W. Close encounters: why unstructured, polymeric domains can increase rates of specific macromolecular association. Trends Biochem. Sci. 18:1993;181-186.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 181-186
    • Pontius, B.W.1
  • 75
    • 0034867975 scopus 로고    scopus 로고
    • The protein trinity - Linking function and disorder
    • Dunker A.K., Obradovic Z. The protein trinity - linking function and disorder. Nature Biotechnol. 19:2001;805-806.
    • (2001) Nature Biotechnol. , vol.19 , pp. 805-806
    • Dunker, A.K.1    Obradovic, Z.2
  • 76
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright P.E., Dyson H.J. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293:1999;321-331.
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 77
    • 0026540830 scopus 로고
    • Purification and characterization of the carboxyl-terminal transactivation domain of Vmw65 from herpes simplex virus type 1
    • Donaldson L., Capone J.P. Purification and characterization of the carboxyl-terminal transactivation domain of Vmw65 from herpes simplex virus type 1. J. Biol. Chem. 267:1992;1411-1414.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1411-1414
    • Donaldson, L.1    Capone, J.P.2
  • 79
    • 0029662315 scopus 로고    scopus 로고
    • Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: Conformational disorder mediates binding diversity
    • Kriwacki R.W., Hengst L., Tennant L., Reed S.I., Wright P.E. Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. Proc. Natl Acad. Sci. USA. 93:1996;11504-11509.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 11504-11509
    • Kriwacki, R.W.1    Hengst, L.2    Tennant, L.3    Reed, S.I.4    Wright, P.E.5
  • 80
    • 0028970090 scopus 로고
    • Structure and function of transcriptional activation domains
    • Triezenberg S.J. Structure and function of transcriptional activation domains. Curr. Opin. Genet. Dev. 5:1995;190-196.
    • (1995) Curr. Opin. Genet. Dev. , vol.5 , pp. 190-196
    • Triezenberg, S.J.1
  • 81
    • 0024825088 scopus 로고
    • High-level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene product
    • Brinkmann U., Mattes R.E., Buckel P. High-level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene product. Gene. 85:1989;109-114.
    • (1989) Gene , vol.85 , pp. 109-114
    • Brinkmann, U.1    Mattes, R.E.2    Buckel, P.3
  • 82
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S.C., von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 1989;182.
    • (1989) Anal. Biochem. , pp. 182
    • Gill, S.C.1    Von Hippel, P.H.2
  • 83
    • 0037039445 scopus 로고    scopus 로고
    • Human p53 phosphorylation mimic, S392E, increases nonspecific DNA affinity and thermal stability
    • Nichols N.M., Matthews K.S. Human p53 phosphorylation mimic, S392E, increases nonspecific DNA affinity and thermal stability. Biochemistry. 41:2002;170-178.
    • (2002) Biochemistry , vol.41 , pp. 170-178
    • Nichols, N.M.1    Matthews, K.S.2
  • 84
    • 0022555883 scopus 로고
    • Refolding and association of oligomeric proteins
    • Jaenicke R., Rudolf R. Refolding and association of oligomeric proteins. Methods Enzymol. 131:1986;218-250.
    • (1986) Methods Enzymol. , vol.131 , pp. 218-250
    • Jaenicke, R.1    Rudolf, R.2
  • 85
    • 0035895350 scopus 로고    scopus 로고
    • Chalcone derivatives antagonize interactions between the human oncoprotein MDM2 and p53
    • Stoll R., Renner C., Hansen S., Palme S., Klein C., Belling A., et al. Chalcone derivatives antagonize interactions between the human oncoprotein MDM2 and p53. Biochemistry. 40:2001;336-344.
    • (2001) Biochemistry , vol.40 , pp. 336-344
    • Stoll, R.1    Renner, C.2    Hansen, S.3    Palme, S.4    Klein, C.5    Belling, A.6
  • 87
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M., Saudek V., Sklenar V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR. 2:1992;661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 88
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky V.N., Gillespie J.R., Fink A.L. Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins: Struct. Funct. Genet. 41:2000;415-427.
    • (2000) Proteins: Struct. Funct. Genet. , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.