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Volumn 109, Issue 34, 2012, Pages 13590-13595

First-order rate-determining aggregation mechanism of p53 and its implications

Author keywords

Amyloid; Folding; Kinetics; Misfolding

Indexed keywords

EDETIC ACID; MONOMER; PROTEIN P53; THIOFLAVINE;

EID: 84865293745     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1211557109     Document Type: Article
Times cited : (59)

References (20)
  • 1
    • 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 USA 109:13584-13589.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 13584-13589
    • Wilcken, R.1    Wang, G.2    Boeckler, F.M.3    Fersht, A.R.4
  • 2
    • 57749098600 scopus 로고    scopus 로고
    • Amyloid formation by globular proteins under native conditions
    • Chiti F, Dobson CM (2009) Amyloid formation by globular proteins under native conditions. Nat Chem Biol 5:15-22.
    • (2009) Nat Chem Biol , vol.5 , pp. 15-22
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of proteins in human diseases
    • Eisenberg D, Jucker M (2012) The amyloid state of proteins in human diseases. Cell 148:1188-1203.
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 4
    • 59349083966 scopus 로고    scopus 로고
    • Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature
    • Morris AM, Watzky MA, Finke RG (2009) Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature. Biochim Biophys Acta 1794:375-397.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 375-397
    • Morris, A.M.1    Watzky, M.A.2    Finke, R.G.3
  • 5
    • 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
  • 6
    • 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
  • 7
    • 73649087901 scopus 로고    scopus 로고
    • Folding of tetrameric p53: Oligomerization and tumorigenic mutations induce misfolding and loss of function
    • Lubin DJ, Butler JS, Loh SN (2010) Folding of tetrameric p53: Oligomerization and tumorigenic mutations induce misfolding and loss of function. J Mol Biol 395:705-716.
    • (2010) J Mol Biol , vol.395 , pp. 705-716
    • Lubin, D.J.1    Butler, J.S.2    Loh, S.N.3
  • 8
    • 0027269545 scopus 로고
    • A structural role for metal ions in the "wild-type" conformation of the tumor suppressor protein p53
    • Hainaut P, Milner J (1993) A structural role for metal ions in the "wild-type" conformation of the tumor suppressor protein p53. Cancer Res 53:1739-1742.
    • (1993) Cancer Res , vol.53 , pp. 1739-1742
    • Hainaut, P.1    Milner, J.2
  • 9
    • 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
  • 10
    • 0037418548 scopus 로고    scopus 로고
    • Structure, function, and aggregation of the zinc-free form of the p53 DNA binding domain
    • Butler JS, Loh SN (2003) Structure, function, and aggregation of the zinc-free form of the p53 DNA binding domain. Biochemistry 42:2396-2403.
    • (2003) Biochemistry , vol.42 , pp. 2396-2403
    • Butler, J.S.1    Loh, S.N.2
  • 11
    • 0031447171 scopus 로고    scopus 로고
    • Thermodynamic stability of wild-type and mutant p53 core domain
    • Bullock AN, et al. (1997) Thermodynamic stability of wild-type and mutant p53 core domain. Proc Natl Acad Sci USA 94:14338-14342.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14338-14342
    • Bullock, A.N.1
  • 12
    • 84859993146 scopus 로고    scopus 로고
    • Halogen-enriched fragment libraries as leads for drug rescue of mutant p53
    • Wilcken R, et al. (2012) Halogen-enriched fragment libraries as leads for drug rescue of mutant p53. J Am Chem Soc 134:6810-6818.
    • (2012) J Am Chem Soc , vol.134 , pp. 6810-6818
    • Wilcken, R.1
  • 13
    • 79953723488 scopus 로고    scopus 로고
    • Single-Molecule characterization of oligomerization kinetics and equilibria of the tumor suppressor p53
    • Rajagopalan S, Huang F, Fersht AR (2011) Single-Molecule characterization of oligomerization kinetics and equilibria of the tumor suppressor p53. Nucleic Acids Res 39:2294-2303.
    • (2011) Nucleic Acids Res , vol.39 , pp. 2294-2303
    • Rajagopalan, S.1    Huang, F.2    Fersht, A.R.3
  • 14
    • 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, 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
  • 15
    • 34250834054 scopus 로고    scopus 로고
    • A Lumry-Eyring nucleated polymerization model of protein aggregation kinetics: 1. Aggregation with pre-equilibrated unfolding
    • Andrews JM, Roberts CJ (2007) A Lumry-Eyring nucleated polymerization model of protein aggregation kinetics: 1. Aggregation with pre-equilibrated unfolding. J Phys Chem B 111:7897-7913.
    • (2007) J Phys Chem B , vol.111 , pp. 7897-7913
    • Andrews, J.M.1    Roberts, C.J.2
  • 16
    • 67650072650 scopus 로고    scopus 로고
    • Lumry-Eyring nucleated-polymerization model of protein aggregation kinetics. 2. Competing growth via condensation and chain polymerization
    • Li Y, Roberts CJ (2009) Lumry-Eyring nucleated-polymerization model of protein aggregation kinetics. 2. Competing growth via condensation and chain polymerization. J Phys Chem B 113:7020-7032.
    • (2009) J Phys Chem B , vol.113 , pp. 7020-7032
    • Li, Y.1    Roberts, C.J.2
  • 17
    • 79955054710 scopus 로고    scopus 로고
    • Gain of function of mutant p53 by coaggregation with multiple tumor suppressors
    • Xu J, et al. (2011) Gain of function of mutant p53 by coaggregation with multiple tumor suppressors. Nat Chem Biol 7:285-295.
    • (2011) Nat Chem Biol , vol.7 , pp. 285-295
    • Xu, J.1
  • 18
    • 79955702054 scopus 로고    scopus 로고
    • Electrocatalytic monitoring of metal binding and mutation-induced conformational changes in p53 at picomole level
    • Palecek E, Ostatna V, Cernocka H, Joerger AC, Fersht AR (2011) Electrocatalytic monitoring of metal binding and mutation-induced conformational changes in p53 at picomole level. J Am Chem Soc 133:7190-7196.
    • (2011) J Am Chem Soc , vol.133 , pp. 7190-7196
    • Palecek, E.1    Ostatna, V.2    Cernocka, H.3    Joerger, A.C.4    Fersht, A.R.5
  • 20
    • 0022051541 scopus 로고
    • The use of 4-(2-pyridylazo)resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase
    • Hunt JB, Neece SH, Ginsburg A (1985) The use of 4-(2-pyridylazo) resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase. Anal Biochem 146:150-157.
    • (1985) Anal Biochem , vol.146 , pp. 150-157
    • Hunt, J.B.1    Neece, S.H.2    Ginsburg, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.