SCOPUS 정보 검색 플랫폼

Volumn 52, Issue 5, 2016, Pages 882-885

Amyloid-β adopts a conserved, partially folded structure upon binding to zwitterionic lipid bilayers prior to amyloid formation

(4) Korshavn, Kyle J a Bhunia, Anirban a,b Lim, Mi Hee c Ramamoorthy, Ayyalusamy a

a UNIVERSITY OF MICHIGAN (United States)

b BOSE INSTITUTE (India)

c Ulsan National Institute of Science and Technology (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; PHOSPHATIDYLCHOLINE; AMYLOID; AMYLOID BETA PROTEIN; LIPID BILAYER;

ARTICLE; BINDING AFFINITY; FLUORESCENCE POLARIZATION; LIPID BILAYER; MEMBRANE DAMAGE; BINDING SITE; BIOSYNTHESIS; CHEMISTRY; METABOLISM; MOLECULAR MODEL; PROTEIN CONFORMATION; PROTEIN FOLDING; SURFACE PROPERTY;

AMYLOID; AMYLOID BETA-PEPTIDES; BINDING SITES; LIPID BILAYERS; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; SURFACE PROPERTIES;

EID: 84954048415 PISSN: 13597345 EISSN: 1364548X Source Type: Journal
DOI: 10.1039/c5cc08634e Document Type: Article

Times cited : (62)

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