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Volumn 7, Issue 10, 2012, Pages

Stability of p53 Homologs

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN P53; PROTEIN P73;

EID: 84868132814     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0047889     Document Type: Article
Times cited : (29)

References (45)
  • 1
    • 23944490117 scopus 로고    scopus 로고
    • Missense meanderings in sequence space: a biophysical view of protein evolution
    • DePristo MA, Weinreich DM, Hartl DL, (2005) Missense meanderings in sequence space: a biophysical view of protein evolution. Nat Rev Genet 6: 678-687.
    • (2005) Nat Rev Genet , vol.6 , pp. 678-687
    • DePristo, M.A.1    Weinreich, D.M.2    Hartl, D.L.3
  • 2
    • 8444219763 scopus 로고    scopus 로고
    • Adaptation of enzymes to temperature: searching for basic "strategies"
    • Somero GN, (2004) Adaptation of enzymes to temperature: searching for basic "strategies". Comp Biochem Physiol B Biochem Mol Biol 139: 321-333.
    • (2004) Comp Biochem Physiol B Biochem Mol Biol , vol.139 , pp. 321-333
    • Somero, G.N.1
  • 3
    • 70349901079 scopus 로고    scopus 로고
    • Stability effects of mutations and protein evolvability
    • Tokuriki N, Tawfik DS, (2009) Stability effects of mutations and protein evolvability. Curr Opin Struct Biol 19: 596-604.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 596-604
    • Tokuriki, N.1    Tawfik, D.S.2
  • 4
    • 0027441807 scopus 로고
    • Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability
    • Serrano L, Day AG, Fersht AR, (1993) Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability. J Mol Biol 233: 305-312.
    • (1993) J Mol Biol , vol.233 , pp. 305-312
    • Serrano, L.1    Day, A.G.2    Fersht, A.R.3
  • 5
    • 0028949615 scopus 로고
    • Proteins and temperature
    • Somero GN, (1995) Proteins and temperature. Annu Rev Physiol 57: 43-68.
    • (1995) Annu Rev Physiol , vol.57 , pp. 43-68
    • Somero, G.N.1
  • 6
    • 0033594485 scopus 로고    scopus 로고
    • p63 is essential for regenerative proliferation in limb, craniofacial and epithelial development
    • Yang A, Schweitzer R, Sun D, Kaghad M, Walker N, et al. (1999) p63 is essential for regenerative proliferation in limb, craniofacial and epithelial development. Nature 398: 714-718.
    • (1999) Nature , vol.398 , pp. 714-718
    • Yang, A.1    Schweitzer, R.2    Sun, D.3    Kaghad, M.4    Walker, N.5
  • 7
    • 17544363909 scopus 로고    scopus 로고
    • p73-deficient mice have neurological, pheromonal and inflammatory defects but lack spontaneous tumours
    • Yang A, Walker N, Bronson R, Kaghad M, Oosterwegel M, et al. (2000) p73-deficient mice have neurological, pheromonal and inflammatory defects but lack spontaneous tumours. Nature 404: 99-103.
    • (2000) Nature , vol.404 , pp. 99-103
    • Yang, A.1    Walker, N.2    Bronson, R.3    Kaghad, M.4    Oosterwegel, M.5
  • 8
    • 33746790624 scopus 로고    scopus 로고
    • Effects of common cancer mutations on stability and DNA binding of full-length p53 compared with isolated core domains
    • Ang HC, Joerger AC, Mayer S, Fersht AR, (2006) Effects of common cancer mutations on stability and DNA binding of full-length p53 compared with isolated core domains. J Biol Chem 281: 21934-21941.
    • (2006) J Biol Chem , vol.281 , pp. 21934-21941
    • Ang, H.C.1    Joerger, A.C.2    Mayer, S.3    Fersht, A.R.4
  • 9
    • 0035496607 scopus 로고    scopus 로고
    • Rescuing the function of mutant p53
    • Bullock AN, Fersht AR, (2001) Rescuing the function of mutant p53. Nat Rev Cancer 1: 68-76.
    • (2001) Nat Rev Cancer , vol.1 , pp. 68-76
    • Bullock, A.N.1    Fersht, A.R.2
  • 11
    • 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, (2000) Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: definition of mutant states for rescue in cancer therapy. Oncogene 19: 1245-1256.
    • (2000) Oncogene , vol.19 , pp. 1245-1256
    • Bullock, A.N.1    Henckel, J.2    Fersht, A.R.3
  • 12
  • 14
    • 0036674617 scopus 로고    scopus 로고
    • Live or let die: the cell's response to p53
    • Vousden KH, Lu X, (2002) Live or let die: the cell's response to p53. Nat Rev Cancer 2: 594-604.
    • (2002) Nat Rev Cancer , vol.2 , pp. 594-604
    • Vousden, K.H.1    Lu, X.2
  • 15
    • 70349240216 scopus 로고    scopus 로고
    • Adaptive evolution of p53 thermodynamic stability
    • Khoo KH, Andreeva A, Fersht AR, (2009) Adaptive evolution of p53 thermodynamic stability. J Mol Biol 393: 161-175.
    • (2009) J Mol Biol , vol.393 , pp. 161-175
    • Khoo, K.H.1    Andreeva, A.2    Fersht, A.R.3
  • 16
    • 0035813165 scopus 로고    scopus 로고
    • High thermostability and lack of cooperative DNA binding distinguish the p63 core domain from the homologous tumor suppressor p53
    • Klein C, Georges G, Kunkele KP, Huber R, Engh RA, et al. (2001) High thermostability and lack of cooperative DNA binding distinguish the p63 core domain from the homologous tumor suppressor p53. J Biol Chem 276: 37390-37401.
    • (2001) J Biol Chem , vol.276 , pp. 37390-37401
    • Klein, C.1    Georges, G.2    Kunkele, K.P.3    Huber, R.4    Engh, R.A.5
  • 17
    • 40549119464 scopus 로고    scopus 로고
    • The p73 DNA binding domain displays enhanced stability relative to its homologue, the tumor suppressor p53, and exhibits cooperative DNA binding
    • Patel S, Bui TT, Drake AF, Fraternali F, Nikolova PV, (2008) The p73 DNA binding domain displays enhanced stability relative to its homologue, the tumor suppressor p53, and exhibits cooperative DNA binding. Biochemistry 47: 3235-3244.
    • (2008) Biochemistry , vol.47 , pp. 3235-3244
    • Patel, S.1    Bui, T.T.2    Drake, A.F.3    Fraternali, F.4    Nikolova, P.V.5
  • 18
    • 0037591875 scopus 로고    scopus 로고
    • Kinetic instability of p53 core domain mutants: implications for rescue by small molecules
    • Friedler A, Veprintsev DB, Hansson LO, Fersht AR, (2003) Kinetic instability of p53 core domain mutants: implications for rescue by small molecules. J Biol Chem 278: 24108-24112.
    • (2003) J Biol Chem , vol.278 , pp. 24108-24112
    • Friedler, A.1    Veprintsev, D.B.2    Hansson, L.O.3    Fersht, A.R.4
  • 19
    • 0032055501 scopus 로고    scopus 로고
    • Genetic selection of intragenic suppressor mutations that reverse the effect of common p53 cancer mutations
    • Brachmann RK, Yu K, Eby Y, Pavletich NP, Boeke JD, (1998) Genetic selection of intragenic suppressor mutations that reverse the effect of common p53 cancer mutations. EMBO J 17: 1847-1859.
    • (1998) EMBO J , vol.17 , pp. 1847-1859
    • Brachmann, R.K.1    Yu, K.2    Eby, Y.3    Pavletich, N.P.4    Boeke, J.D.5
  • 20
    • 0032919288 scopus 로고    scopus 로고
    • In vitro evolution of thermostable p53 variants
    • Matsumura I, Ellington AD, (1999) In vitro evolution of thermostable p53 variants. Protein Sci 8: 731-740.
    • (1999) Protein Sci , vol.8 , pp. 731-740
    • Matsumura, I.1    Ellington, A.D.2
  • 21
    • 0032437592 scopus 로고    scopus 로고
    • Semirational design of active tumor suppressor p53 DNA binding domain with enhanced stability
    • Nikolova PV, Henckel J, Lane DP, Fersht AR, (1998) Semirational design of active tumor suppressor p53 DNA binding domain with enhanced stability. Proc Natl Acad Sci U S A 95: 14675-14680.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 14675-14680
    • Nikolova, P.V.1    Henckel, J.2    Lane, D.P.3    Fersht, A.R.4
  • 22
    • 79956071405 scopus 로고    scopus 로고
    • Interaction of the p53 DNA-Binding Domain with Its N-Terminal Extension Modulates the Stability of the p53 Tetramer
    • Natan E, Baloglu C, Pagel K, Freund SM, Morgner N, et al. (2011) Interaction of the p53 DNA-Binding Domain with Its N-Terminal Extension Modulates the Stability of the p53 Tetramer. J Mol Biol 409: 358-368.
    • (2011) J Mol Biol , vol.409 , pp. 358-368
    • Natan, E.1    Baloglu, C.2    Pagel, K.3    Freund, S.M.4    Morgner, N.5
  • 24
    • 33750470057 scopus 로고    scopus 로고
    • Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination
    • Vedadi M, Niesen FH, Allali-Hassani A, Fedorov OY, Finerty PJ Jr, et al. (2006) Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination. Proc Natl Acad Sci U S A 103: 15835-15840.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 15835-15840
    • Vedadi, M.1    Niesen, F.H.2    Allali-Hassani, A.3    Fedorov, O.Y.4    Finerty Jr., P.J.5
  • 25
    • 0035338647 scopus 로고    scopus 로고
    • The ligand affinity of proteins measured by isothermal denaturation kinetics
    • Epps DE, Sarver RW, Rogers JM, Herberg JT, Tomich PK, (2001) The ligand affinity of proteins measured by isothermal denaturation kinetics. Anal Biochem 292: 40-50.
    • (2001) Anal Biochem , vol.292 , pp. 40-50
    • Epps, D.E.1    Sarver, R.W.2    Rogers, J.M.3    Herberg, J.T.4    Tomich, P.K.5
  • 26
    • 0036199409 scopus 로고    scopus 로고
    • Determination of ligand-MurB interactions by isothermal denaturation: application as a secondary assay to complement high throughput screening
    • Sarver RW, Rogers JM, Epps DE, (2002) Determination of ligand-MurB interactions by isothermal denaturation: application as a secondary assay to complement high throughput screening. J Biomol Screen 7: 21-28.
    • (2002) J Biomol Screen , vol.7 , pp. 21-28
    • Sarver, R.W.1    Rogers, J.M.2    Epps, D.E.3
  • 27
    • 44849085505 scopus 로고    scopus 로고
    • Application of high-throughput isothermal denaturation to assess protein stability and screen for ligands
    • Senisterra GA, Soo Hong B, Park HW, Vedadi M, (2008) Application of high-throughput isothermal denaturation to assess protein stability and screen for ligands. J Biomol Screen 13: 337-342.
    • (2008) J Biomol Screen , vol.13 , pp. 337-342
    • Senisterra, G.A.1    Soo Hong, B.2    Park, H.W.3    Vedadi, M.4
  • 28
    • 84865293745 scopus 로고    scopus 로고
    • First-order rate-determining aggregation mechanism of p53 and its implications
    • Wang G, Fersht AR, (2012) First-order rate-determining aggregation mechanism of p53 and its implications. Proc Natl Acad Sci U S A 109: 13590-13595.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 13590-13595
    • Wang, G.1    Fersht, A.R.2
  • 29
    • 84865281347 scopus 로고    scopus 로고
    • Kinetic mechanism of p53 oncogenic mutant aggregation and its inhibition
    • Wilcken R, Wang G, Boeckler FM, Fersht AR, (2012) Kinetic mechanism of p53 oncogenic mutant aggregation and its inhibition. Proc Natl Acad Sci U S A 109: 13584-13589.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 13584-13589
    • Wilcken, R.1    Wang, G.2    Boeckler, F.M.3    Fersht, A.R.4
  • 30
    • 74549130412 scopus 로고    scopus 로고
    • Conservation of DNA-binding specificity and oligomerisation properties within the p53 family
    • Brandt T, Petrovich M, Joerger AC, Veprintsev DB, (2009) Conservation of DNA-binding specificity and oligomerisation properties within the p53 family. BMC Genomics 10: 628.
    • (2009) BMC Genomics , vol.10 , pp. 628
    • Brandt, T.1    Petrovich, M.2    Joerger, A.C.3    Veprintsev, D.B.4
  • 31
    • 84864999268 scopus 로고    scopus 로고
    • Mutant p53 Aggregates into Prion-like Amyloid Oligomers and Fibrils: IMPLICATIONS FOR CANCER
    • Ano Bom AP, Rangel LP, Costa DC, de Oliveira GA, Sanches D, et al. (2012) Mutant p53 Aggregates into Prion-like Amyloid Oligomers and Fibrils: IMPLICATIONS FOR CANCER. J Biol Chem 287: 28152-28162.
    • (2012) J Biol Chem , vol.287 , pp. 28152-28162
    • Ano Bom, A.P.1    Rangel, L.P.2    Costa, D.C.3    de Oliveira, G.A.4    Sanches, D.5
  • 34
    • 67650078274 scopus 로고    scopus 로고
    • Cognate DNA stabilizes the tumor suppressor p53 and prevents misfolding and aggregation
    • Ishimaru D, Ano Bom AP, Lima LM, Quesado PA, Oyama MF, et al. (2009) Cognate DNA stabilizes the tumor suppressor p53 and prevents misfolding and aggregation. Biochemistry 48: 6126-6135.
    • (2009) Biochemistry , vol.48 , pp. 6126-6135
    • Ishimaru, D.1    Ano Bom, A.P.2    Lima, L.M.3    Quesado, P.A.4    Oyama, M.F.5
  • 35
    • 41149090794 scopus 로고    scopus 로고
    • Algorithm for prediction of tumour suppressor p53 affinity for binding sites in DNA
    • Veprintsev DB, Fersht AR, (2008) Algorithm for prediction of tumour suppressor p53 affinity for binding sites in DNA. Nucleic Acids Res 36: 1589-1598.
    • (2008) Nucleic Acids Res , vol.36 , pp. 1589-1598
    • Veprintsev, D.B.1    Fersht, A.R.2
  • 36
    • 47649096991 scopus 로고    scopus 로고
    • Structural biology of the tumor suppressor p53
    • Joerger AC, Fersht AR, (2008) Structural biology of the tumor suppressor p53. Annu Rev Biochem 77: 557-582.
    • (2008) Annu Rev Biochem , vol.77 , pp. 557-582
    • Joerger, A.C.1    Fersht, A.R.2
  • 38
    • 3543110350 scopus 로고    scopus 로고
    • p63 and p73: roles in development and tumor formation
    • Moll UM, Slade N, (2004) p63 and p73: roles in development and tumor formation. Mol Cancer Res 2: 371-386.
    • (2004) Mol Cancer Res , vol.2 , pp. 371-386
    • Moll, U.M.1    Slade, N.2
  • 39
    • 0347723910 scopus 로고    scopus 로고
    • Crystal structure of a superstable mutant of human p53 core domain. Insights into the mechanism of rescuing oncogenic mutations
    • Joerger AC, Allen MD, Fersht AR, (2004) Crystal structure of a superstable mutant of human p53 core domain. Insights into the mechanism of rescuing oncogenic mutations. J Biol Chem 279: 1291-1296.
    • (2004) J Biol Chem , vol.279 , pp. 1291-1296
    • Joerger, A.C.1    Allen, M.D.2    Fersht, A.R.3
  • 40
    • 0027958323 scopus 로고
    • The peripheral subunit-binding domain of the dihydrolipoyl acetyltransferase component of the pyruvate dehydrogenase complex of Bacillus stearothermophilus: preparation and characterization of its binding to the dihydrolipoyl dehydrogenase component
    • Hipps DS, Packman LC, Allen MD, Fuller C, Sakaguchi K, et al. (1994) The peripheral subunit-binding domain of the dihydrolipoyl acetyltransferase component of the pyruvate dehydrogenase complex of Bacillus stearothermophilus: preparation and characterization of its binding to the dihydrolipoyl dehydrogenase component. Biochem J 297 (Pt 1): 137-143.
    • (1994) Biochem J , vol.297 , Issue.Pt 1 , pp. 137-143
    • Hipps, D.S.1    Packman, L.C.2    Allen, M.D.3    Fuller, C.4    Sakaguchi, K.5
  • 41
    • 33750036093 scopus 로고    scopus 로고
    • Structural basis for understanding oncogenic p53 mutations and designing rescue drugs
    • Joerger AC, Ang HC, Fersht AR, (2006) Structural basis for understanding oncogenic p53 mutations and designing rescue drugs. Proc Natl Acad Sci U S A 103: 15056-15061.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 15056-15061
    • Joerger, A.C.1    Ang, H.C.2    Fersht, A.R.3
  • 43
    • 0000887374 scopus 로고
    • The Laboratory culture of Drosophila
    • In: Ashburner M, Wright TRF, editors, London: Academic Press
    • Ashburner M, Thompson JN Jr (1978) The Laboratory culture of Drosophila. In: Ashburner M, Wright TRF, editors. The Genetics and Biology of Drosophila. London: Academic Press.
    • (1978) The Genetics and Biology of Drosophila
    • Ashburner, M.1    Thompson Jr., J.N.2
  • 44
    • 0001936490 scopus 로고    scopus 로고
    • A virtual tour of the Guide for zebrafish users
    • Matthews M, Trevarrow B, Matthews J, (2002) A virtual tour of the Guide for zebrafish users. Lab Anim (NY) 31: 34-40.
    • (2002) Lab Anim (NY) , vol.31 , pp. 34-40
    • Matthews, M.1    Trevarrow, B.2    Matthews, J.3
  • 45
    • 0028961923 scopus 로고
    • Growth of Xenopus laevis under different laboratory rearing conditions
    • Hilken G, Dimigen J, Iglauer F, (1995) Growth of Xenopus laevis under different laboratory rearing conditions. Lab Anim 29: 152-162.
    • (1995) Lab Anim , vol.29 , pp. 152-162
    • Hilken, G.1    Dimigen, J.2    Iglauer, F.3


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