메뉴 건너뛰기




Volumn 9, Issue 10, 2014, Pages 2309-2317

Toxicity of protein oligomers is rationalized by a function combining size and surface hydrophobicity

Author keywords

[No Author keywords available]

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; AMINO ACID; ARGININE; ESCHERICHIA COLI PROTEIN; GLUTAMIC ACID; HOE 33342; LEUCINE; OLIGOMER; PROTEIN; HYPF PROTEIN, E COLI; TRANSFERASE;

EID: 84908211476     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb500505m     Document Type: Article
Times cited : (171)

References (33)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F., and Dobson, C. M. (2006) Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75, 333-366.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 84858978818 scopus 로고    scopus 로고
    • Protein misfolded oligomers: Experimental approaches, mechanism of formation, and structure-toxicity relationships
    • Bemporad, F., and Chiti, F. (2012) Protein misfolded oligomers: Experimental approaches, mechanism of formation, and structure-toxicity relationships. Chem. Biol. 19, 315-327.
    • (2012) Chem. Biol. , vol.19 , pp. 315-327
    • Bemporad, F.1    Chiti, F.2
  • 4
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • Haass, C., and Selkoe, D. J. (2007) Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide. Nat. Rev. Mol. Cell Biol. 8, 101-112.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 12
    • 0035187228 scopus 로고    scopus 로고
    • Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF Nterminal domain
    • Chiti, F., Bucciantini, M., Capanni, C., Taddei, N., Dobson, C. M., and Stefani, M. (2001) Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF Nterminal domain. Protein Sci. 10, 2541-2547.
    • (2001) Protein Sci. , vol.10 , pp. 2541-2547
    • Chiti, F.1    Bucciantini, M.2    Capanni, C.3    Taddei, N.4    Dobson, C.M.5    Stefani, M.6
  • 14
    • 14644406760 scopus 로고    scopus 로고
    • Amyloid formation from HypF-N under conditions in which the protein is initially in its native state
    • Marcon, G., Plakoutsi, G., Canale, C., Relini, A., Taddei, N., Dobson, C. M., Ramponi, G., and Chiti, F. (2005) Amyloid formation from HypF-N under conditions in which the protein is initially in its native state. J. Mol. Biol. 347, 323-335.
    • (2005) J. Mol. Biol. , vol.347 , pp. 323-335
    • Marcon, G.1    Plakoutsi, G.2    Canale, C.3    Relini, A.4    Taddei, N.5    Dobson, C.M.6    Ramponi, G.7    Chiti, F.8
  • 17
    • 33846160381 scopus 로고    scopus 로고
    • Polymorphism in the intermediates and products of amyloid assembly
    • Kodali, R., and Wetzel, R. (2007) Polymorphism in the intermediates and products of amyloid assembly. Curr. Opin. Struct. Biol. 17, 48-57.
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 48-57
    • Kodali, R.1    Wetzel, R.2
  • 18
    • 0026514355 scopus 로고
    • Spectrofluorimetric assessment of the surface hydrophobicity of proteins
    • Cardamone, M., and Puri, N. K. (1992) Spectrofluorimetric assessment of the surface hydrophobicity of proteins. Biochem. J. 282, 589-593.
    • (1992) Biochem. J. , vol.282 , pp. 589-593
    • Cardamone, M.1    Puri, N.K.2
  • 19
    • 24344467958 scopus 로고    scopus 로고
    • Insights into the molecular basis of the differing susceptibility of varying cell types to the toxicity of amyloid aggregates
    • Cecchi, C., Baglioni, S., Fiorillo, C., Pensalfini, A., Liguri, G., Nosi, D., Rigacci, S., Bucciantini, M., and Stefani, M. (2005) Insights into the molecular basis of the differing susceptibility of varying cell types to the toxicity of amyloid aggregates. J. Cell Sci. 118, 3459-3470.
    • (2005) J. Cell Sci. , vol.118 , pp. 3459-3470
    • Cecchi, C.1    Baglioni, S.2    Fiorillo, C.3    Pensalfini, A.4    Liguri, G.5    Nosi, D.6    Rigacci, S.7    Bucciantini, M.8    Stefani, M.9
  • 20
    • 0034702813 scopus 로고    scopus 로고
    • Correlation of β-amyloid aggregate size and hydrophobicity with decreased bilayer fluidity of model membranes
    • Kremer, J. J., Pallitto, M. M., Sklansky, D. J., and Murphy, R. M. (2000) Correlation of β-amyloid aggregate size and hydrophobicity with decreased bilayer fluidity of model membranes. Biochemistry 39, 10309-10318.
    • (2000) Biochemistry , vol.39 , pp. 10309-10318
    • Kremer, J.J.1    Pallitto, M.M.2    Sklansky, D.J.3    Murphy, R.M.4
  • 21
    • 14844361744 scopus 로고    scopus 로고
    • Comparative analysis of the cytotoxicity of homopolymeric amino acids. Biochim
    • Oma, Y., Kino, Y., Sasagawa, N., and Ishiura, S. (2005) Comparative analysis of the cytotoxicity of homopolymeric amino acids. Biochim. Biophys. Acta 1748, 174-179.
    • (2005) Biophys. Acta , vol.1748 , pp. 174-179
    • Oma, Y.1    Kino, Y.2    Sasagawa, N.3    Ishiura, S.4
  • 22
    • 34848929022 scopus 로고    scopus 로고
    • Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils
    • Cheon, M., Chang, I., Mohanty, S., Luheshi, L. M., Dobson, C. M., Vendruscolo, M., and Favrin, G. (2007) Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils. PLOS Comput. Biol. 3, 1727-1738.
    • (2007) PLOS Comput. Biol. , vol.3 , pp. 1727-1738
    • Cheon, M.1    Chang, I.2    Mohanty, S.3    Luheshi, L.M.4    Dobson, C.M.5    Vendruscolo, M.6    Favrin, G.7
  • 30
    • 79952796718 scopus 로고    scopus 로고
    • Aromatic small molecules remodel toxic soluble oligomers of amyloid β through three independent pathways
    • Ladiwala, A. R., Dordick, J. S., and Tessier, P. M. (2011) Aromatic small molecules remodel toxic soluble oligomers of amyloid β through three independent pathways. J. Biol. Chem. 286, 3209-3218.
    • (2011) J. Biol. Chem. , vol.286 , pp. 3209-3218
    • Ladiwala, A.R.1    Dordick, J.S.2    Tessier, P.M.3
  • 31
    • 79960298697 scopus 로고    scopus 로고
    • Sequestration of toxic oligomers by HspB1 as a cytoprotective mechanism
    • Ojha, J., Masilamoni, G., Dunlap, D., Udoff, R. A., and Cashikar, A. G. (2011) Sequestration of toxic oligomers by HspB1 as a cytoprotective mechanism. Mol. Cell. Biol. 31, 3146-3157.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 3146-3157
    • Ojha, J.1    Masilamoni, G.2    Dunlap, D.3    Udoff, R.A.4    Cashikar, A.G.5
  • 32
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • Chiti, F., Stefani, M., Taddei, N., Ramponi, G., and Dobson, C. M. (2003) Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424, 805-808.
    • (2003) Nature , vol.424 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddei, N.3    Ramponi, G.4    Dobson, C.M.5
  • 33
    • 0002179519 scopus 로고    scopus 로고
    • Effects of sample geometry
    • (Lakowicz, J. R., Ed) 2nd ed., Kluwer Academic/Plenum Publishers, New York
    • Lakowicz, J. R. (1999) Effects of sample geometry. In Principles of fluorescence spectroscopy (Lakowicz, J. R., Ed) 2nd ed., p 54, Kluwer Academic/Plenum Publishers, New York.
    • (1999) Principles of Fluorescence Spectroscopy , pp. p54
    • Lakowicz, J.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.