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Volumn 427, Issue 2, 2015, Pages 287-290

Assembly of Aβ proceeds via monomeric nuclei

Author keywords

Alzheimer's disease; Lag time; Nucleation; Polymerization; Protein folding

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; DIMER; MONOMER; POLYGLUTAMINE; POLYMER; MACROMOLECULE; PEPTIDE; PROTEIN AGGREGATE;

EID: 84920773998     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.10.028     Document Type: Article
Times cited : (31)

References (18)
  • 1
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson CM. Protein folding and misfolding. Nature 2003;426:884-90.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 2
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid betapeptide
    • Haass C, Selkoe DJ. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid betapeptide. Nat Rev Mol Cell Biol 2007;8:101-12.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 3
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, Cotman CW, et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 2003;300:486-9.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6
  • 6
    • 84903696629 scopus 로고    scopus 로고
    • Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Abeta40 and Abeta42 peptides
    • Meisl G, Yang X, Hellstrand E, Frohm B, Kirkegaard JB, Cohen SI, et al. Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Abeta40 and Abeta42 peptides. Proc Natl Acad Sci U S A 2014;111:9384-9.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 9384-9389
    • Meisl, G.1    Yang, X.2    Hellstrand, E.3    Frohm, B.4    Kirkegaard, J.B.5    Cohen, S.I.6
  • 8
    • 0021837479 scopus 로고
    • Kinetics of sickle hemoglobin polymerization II: A double nucleation mechanism
    • Ferrone FA, Hofrichter J, Eaton WA. Kinetics of sickle hemoglobin polymerization II: a double nucleation mechanism. J Mol Biol 1985;183:611-31.
    • (1985) J Mol Biol , vol.183 , pp. 611-631
    • Ferrone, F.A.1    Hofrichter, J.2    Eaton, W.A.3
  • 10
    • 0021527508 scopus 로고
    • Kinetics of nucleation controlled polymerization: A perturbation treatment for use with a secondary pathway
    • Bishop MF, Ferrone FA. Kinetics of nucleation controlled polymerization: a perturbation treatment for use with a secondary pathway. Biophys J 1984;46:631-44.
    • (1984) Biophys J , vol.46 , pp. 631-644
    • Bishop, M.F.1    Ferrone, F.A.2
  • 11
    • 0028920158 scopus 로고
    • Nucleation, fiber growth and melting, and domain formation and structure in sickle cell hemoglobin gels
    • Briehl R. Nucleation, fiber growth and melting, and domain formation and structure in sickle cell hemoglobin gels. J Mol Biol 1995;245:710-23.
    • (1995) J Mol Biol , vol.245 , pp. 710-723
    • Briehl, R.1
  • 12
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of protein aggregation kinetics
    • Ferrone F. Analysis of protein aggregation kinetics. Methods Enzymol 1999;309:256-74.
    • (1999) Methods Enzymol , vol.309 , pp. 256-274
    • Ferrone, F.1
  • 13
    • 0014190760 scopus 로고
    • Self-replication and scrapie
    • Griffith JS. Self-replication and scrapie. Nature 1967;215:1043-4.
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 14
    • 0037015081 scopus 로고    scopus 로고
    • Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation
    • Chen S, Ferrone FA, Wetzel R. Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation. Proc Natl Acad Sci U S A 2002;99:11884-9.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 11884-11889
    • Chen, S.1    Ferrone, F.A.2    Wetzel, R.3
  • 15
    • 79952360891 scopus 로고    scopus 로고
    • Critical nucleus size for disease-related polyglutamine aggregation is repeat-length dependent
    • Kar K, Jayaraman M, Sahoo B, Kodali R, Wetzel R. Critical nucleus size for disease-related polyglutamine aggregation is repeat-length dependent. Nat Struct Mol Biol 2011;18:328-36.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 328-336
    • Kar, K.1    Jayaraman, M.2    Sahoo, B.3    Kodali, R.4    Wetzel, R.5
  • 16
    • 33947586837 scopus 로고    scopus 로고
    • Mechanisms of ataxin-3 misfolding and fibril formation: Kinetic analysis of a disease-associated polyglutamine protein
    • Ellisdon AM, Pearce MC, Bottomley SP. Mechanisms of ataxin-3 misfolding and fibril formation: kinetic analysis of a disease-associated polyglutamine protein. J Mol Biol 2007;368:595-605.
    • (2007) J Mol Biol , vol.368 , pp. 595-605
    • Ellisdon, A.M.1    Pearce, M.C.2    Bottomley, S.P.3
  • 18
    • 33745757474 scopus 로고    scopus 로고
    • The kinetics of nucleated polymerizations at high concentrations: Amyloid fibril formation near and above the "supercritical concentration"
    • Powers ET, Powers DL. The kinetics of nucleated polymerizations at high concentrations: amyloid fibril formation near and above the "supercritical concentration". Biophys J 2006;91:122-32.
    • (2006) Biophys J , vol.91 , pp. 122-132
    • Powers, E.T.1    Powers, D.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.