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Volumn 343, Issue 4, 2006, Pages 1262-1271

Interaction-based evaluation of the propensity for amyloid formation with cross-β structure

Author keywords

Synuclein; 2 Microglobulin; Amyloid; Amyloid ; Amyloidogenicity; Antiparallel; Core cross ; Hydrophobic interaction; Line matching; Prion; Propensity score

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; HYDROGEN; PEPTIDE;

EID: 33744973540     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.03.089     Document Type: Article
Times cited : (22)

References (23)
  • 6
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • Fernandez-Escamilla A.-M., Rousseau F., Schymkowitz J., and Serrano L. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat. Biotech. 22 (2004) 1302-1306
    • (2004) Nat. Biotech. , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.-M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 7
    • 20444403757 scopus 로고    scopus 로고
    • Prediction of aggregation-prone and aggregation-susceptible regions in proteins associated with neurodegenerative diseases
    • Pawar A.P., DuBay K.F., Zurdo J., Chiti F., Vendruscolo M., and Dobson C.M. Prediction of aggregation-prone and aggregation-susceptible regions in proteins associated with neurodegenerative diseases. J. Mol. Biol. 350 (2005) 379-392
    • (2005) J. Mol. Biol. , vol.350 , pp. 379-392
    • Pawar, A.P.1    DuBay, K.F.2    Zurdo, J.3    Chiti, F.4    Vendruscolo, M.5    Dobson, C.M.6
  • 8
    • 17444393233 scopus 로고    scopus 로고
    • Higher-order molecular packing in amyloid-like fibrils constructed with linear arrangements of hydrophobic and hydrogen-bonding side-chains
    • Saiki M., Honda S., Kawasaki K., Zhou D., Kaito A., Konakahara T., and Morii H. Higher-order molecular packing in amyloid-like fibrils constructed with linear arrangements of hydrophobic and hydrogen-bonding side-chains. J. Mol. Biol. 348 (2005) 983-998
    • (2005) J. Mol. Biol. , vol.348 , pp. 983-998
    • Saiki, M.1    Honda, S.2    Kawasaki, K.3    Zhou, D.4    Kaito, A.5    Konakahara, T.6    Morii, H.7
  • 9
    • 0027251341 scopus 로고
    • The Greek key motif: extraction, classification and analysis
    • Hutchinson E.G., and Thornton J.M. The Greek key motif: extraction, classification and analysis. Protein Eng. 6 (1993) 233-245
    • (1993) Protein Eng. , vol.6 , pp. 233-245
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 10
    • 0033849738 scopus 로고    scopus 로고
    • Review: history of the amyloid fibril
    • Sipe J.D., and Cohen A.S. Review: history of the amyloid fibril. J. Struct. Biol. 130 (2000) 88-98
    • (2000) J. Struct. Biol. , vol.130 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.S.2
  • 11
    • 0028566270 scopus 로고
    • A revised set of potentials for β-turn formation in proteins
    • Hutchinson E.G., and Thornton J.M. A revised set of potentials for β-turn formation in proteins. Protein Sci. 3 (1994) 2207-2216
    • (1994) Protein Sci. , vol.3 , pp. 2207-2216
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 12
    • 0028088517 scopus 로고
    • Hydrophobicity, expressivity and aromaticity are the major trends of amino-acid usage in 999 Escherichia coli chromosome-encoded genes
    • Lobry J.R., and Gautier C. Hydrophobicity, expressivity and aromaticity are the major trends of amino-acid usage in 999 Escherichia coli chromosome-encoded genes. Nucleic Acids Res. 22 (1994) 3174-3180
    • (1994) Nucleic Acids Res. , vol.22 , pp. 3174-3180
    • Lobry, J.R.1    Gautier, C.2
  • 15
    • 0034649352 scopus 로고    scopus 로고
    • Amyloid fibril formation by Aβ(16-22), a seven-residue fragment of the Alzheimer's β-amyloid peptide, and structural characterization by solid state NMR
    • Balbach J.J., Ishii Y., Antzutkin O.N., Leapman R.D., Rizzo N.W., Dyda F., Reed J., and Tycko R. Amyloid fibril formation by Aβ(16-22), a seven-residue fragment of the Alzheimer's β-amyloid peptide, and structural characterization by solid state NMR. Biochemistry 39 (2000) 13748-13759
    • (2000) Biochemistry , vol.39 , pp. 13748-13759
    • Balbach, J.J.1    Ishii, Y.2    Antzutkin, O.N.3    Leapman, R.D.4    Rizzo, N.W.5    Dyda, F.6    Reed, J.7    Tycko, R.8
  • 18
    • 0037227173 scopus 로고    scopus 로고
    • 2-microglobulin-Insights into the mechanism of fibril formation in vitro
    • 2-microglobulin-Insights into the mechanism of fibril formation in vitro. J. Mol. Biol. 325 (2003) 249-257
    • (2003) J. Mol. Biol. , vol.325 , pp. 249-257
    • Jones, S.1    Manning, J.2    Kad, N.M.3    Radford, S.E.4
  • 20
    • 0029257497 scopus 로고
    • The core Alzheimer's peptide Nac forms amyloid fibrils which seed and are seeded by β-amyloid-is Nac a common trigger or target in neuro-degenerative disease
    • Han H.Y., Weinreb P.H., and Lansbury P.T. The core Alzheimer's peptide Nac forms amyloid fibrils which seed and are seeded by β-amyloid-is Nac a common trigger or target in neuro-degenerative disease. Chem. Biol. 2 (1995) 163-169
    • (1995) Chem. Biol. , vol.2 , pp. 163-169
    • Han, H.Y.1    Weinreb, P.H.2    Lansbury, P.T.3
  • 21
    • 0036670712 scopus 로고    scopus 로고
    • Aggregation and neurotoxicity of alpha-synuclein and related peptides
    • El-Agnaf O.M.A., and Irvine G.B. Aggregation and neurotoxicity of alpha-synuclein and related peptides. Biochem. Soc. Trans. 30 (2002) 559-565
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 559-565
    • El-Agnaf, O.M.A.1    Irvine, G.B.2
  • 22
    • 0141733169 scopus 로고    scopus 로고
    • Structural organization of alpha-synuclein fibrils studied by site directed spin labeling
    • Der-Sarkissian A., Jao C.C., Chen J., and Langen R. Structural organization of alpha-synuclein fibrils studied by site directed spin labeling. J. Biol. Chem. 278 (2003) 37530-37535
    • (2003) J. Biol. Chem. , vol.278 , pp. 37530-37535
    • Der-Sarkissian, A.1    Jao, C.C.2    Chen, J.3    Langen, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.