Specific aromatic foldamers potently inhibit spontaneous and seeded Aβ42 and Aβ43 fibril assembly

Biochemical Journal

Volumn 464, Issue 1, 2014, Pages 85-98

  Seither, Katelyn M ^a   McMahon, Heather A ^a   Singh, Nikita ^a   Wang, Hejia ^a   Cushman Nick, Mimi ^a,b   Montalvo, Geronda L ^a   DeGrado, William F ^b   Shorter, James ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Alzheimer's disease; Amyloid; A 42 (amyloid 42); A 43 (amyloid 43); Foldamer; Protein misfolding

Indexed keywords

AMINOBENZOIC ACID; AMYLOID BETA PROTEIN; ARGININE; CITRULLINE; LYSINE; RNA BINDING PROTEIN; SALICYLAMIDE; AMYLOID; AMYLOID BETA-PROTEIN (1-42); AMYLOID BETA-PROTEIN (1-43); AROMATIC HYDROCARBON; PEPTIDE FRAGMENT;

ALZHEIMER DISEASE; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; ANTAGONISTS AND INHIBITORS; CHEMISTRY; DRUG DESIGN; DRUG EFFECTS; HUMAN; TUMOR CELL LINE;

AMYLOID; AMYLOID BETA-PEPTIDES; CELL LINE, TUMOR; DRUG DESIGN; HUMANS; HYDROCARBONS, AROMATIC; PEPTIDE FRAGMENTS; PROTEIN FOLDING;

EID: 84908367031     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20131609     Document Type: Article

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