SCOPUS 정보 검색 플랫폼

Journal of the American Chemical Society

Volumn 134, Issue 14, 2012, Pages 6061-6063

The crowded environment of a reverse micelle induces the formation of β-strand seed structures for nucleating amyloid fibril formation

(2) Yeung, Priscilla S W a Axelsen, Paul H a

a UNIVERSITY OF PENNSYLVANIA (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER'S DISEASE; AMYLOID BETAS; AMYLOID FIBRIL; AMYLOID FIBRIL FORMATION; HUMAN BRAIN; INSOLUBLE FIBRILS; MACROMOLECULAR CROWDING; PLAUSIBLE MECHANISMS; REVERSE MICELLES; SCRAMBLED SEQUENCE; SEED STRUCTURE; SHEET STRUCTURE;

GLYCOPROTEINS; MACROMOLECULES; MICELLES;

PROTEINS;

AMYLOID; AMYLOID BETA PROTEIN; SODIUM ION;

ARTICLE; CHEMICAL BOND; CIRCULAR DICHROISM; CONCENTRATION (PARAMETERS); ENCAPSULATION; ENVIRONMENTAL ASPECTS AND RELATED PHENOMENA; HUMAN; HYDROGEN BOND; INFRARED SPECTROSCOPY; LIPID MEMBRANE; MACROMOLECULAR ENVIRONMENT; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; REVERSE MICELLE;

ALZHEIMER DISEASE; AMYLOID; HISTONES; HUMANS; MACROMOLECULAR SUBSTANCES; MICELLES; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 84859602872 PISSN: 00027863 EISSN: 15205126 Source Type: Journal
DOI: 10.1021/ja3004478 Document Type: Article

Times cited : (28)

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