A disulfide-linked amyloid-β peptide dimer forms a protofibril-like oligomer through a distinct pathway from amyloid fibril formation

Biochemistry

Volumn 49, Issue 33, 2010, Pages 7100-7107

  Yamaguchi, Takahiro ^a   Yagi, Hisashi ^b   Goto, Yuji ^b   Matsuzaki, Katsumi ^a   Hoshino, Masaru ^a  

^a KYOTO UNIVERSITY   (Japan)

^b OSAKA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER'S DISEASE; AMYLOID FIBRIL; AMYLOID FIBRIL FORMATION; CONFORMATIONAL FLEXIBILITY; DISSOCIATION RATES; FORMING PROCESS; PROTOFIBRILS; SHEET STRUCTURE; SPONTANEOUS FORMATION; THERMODYNAMICALLY STABLE; THIOFLAVIN; TRAPPED STATE;

DISSOCIATION; ELECTRON AFFINITY; PEPTIDES; TRANSMISSION ELECTRON MICROSCOPY;

GLYCOPROTEINS;

AMYLOID; AMYLOID BETA PROTEIN; DISULFIDE; OLIGOMER; THIOFLAVINE; PEPTIDE FRAGMENT;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CELL MATURATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTOFIBRIL; TRANSMISSION ELECTRON MICROSCOPY; ALZHEIMER DISEASE; CHEMISTRY; HUMAN; METABOLISM; MOLECULAR GENETICS; PROTEIN MULTIMERIZATION; PROTEIN SECONDARY STRUCTURE;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMYLOID; AMYLOID BETA-PROTEIN; DISULFIDES; HUMANS; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; AMYLOID BETA-PEPTIDES;

EID: 77955680341     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100583x     Document Type: Article

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