Polymorphic C-terminal β-sheet interactions determine the formation of fibril or amyloid β-derived diffusible ligand-like globulomer for the Alzheimer Aβ42 dodecamer

Journal of Biological Chemistry

Volumn 285, Issue 47, 2010, Pages 37102-37110

  Ma, Buyong ^a   Nussinov, Ruth ^a,b  

^a NATIONAL CANCER INSTITUTE   (United States)

^b TEL AVIV UNIVERSITY   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER; AMYLOID DEPOSITION; CELLULAR TOXICITIES; DODECAMER; EXPERIMENTAL DATA; EXPERIMENTAL OBSERVATION; FIBRIL FORMATION; N-TERMINALS; NMR DATA; PROTOFIBRILS; SINGLE LAYER; STABLE SPECIES; STRUCTURAL SIMILARITY;

COMPUTER SIMULATION; GLYCOPROTEINS; LIGANDS; PROTEINS; TOXICITY;

OLIGOMERS;

AMYLOID BETA DERIVED DIFFUSIBLE LIGAND; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; METHIONINE; OLIGOMER; UNCLASSIFIED DRUG;

ARTICLE; BETA SHEET; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; HYDROPHOBICITY; MOLECULAR INTERACTION; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN STRUCTURE; SIMULATION;

AMYLOID BETA-PEPTIDES; HUMANS; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; MONTE CARLO METHOD; NEUROFIBRILLARY TANGLES; PLAQUE, AMYLOID; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY;

EID: 78449240570     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.133488     Document Type: Article

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