Solution structure of the Alzheimer amyloid β-peptide (1-42) in an apolar microenvironment: Similarity with a virus fusion domain

European Journal of Biochemistry

Volumn 269, Issue 22, 2002, Pages 5642-5648

  Crescenzi, Orlando ^a   Tomaselli, Simona ^a   Guerrini, Remo ^b   Salvadori, Severo ^b   D'Ursi, Anna M ^c   Temussi, Piero Andrea ^a   Picone, Delia ^a  

^a UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^b UNIVERSITY OF FERRARA   (Italy)

^c UNIVERSITY OF SALERNO   (Italy)

Author keywords

Alzheimer disease; Amyloid peptides; Conformational analysis; Fusion domain; NMR

Indexed keywords

AMYLOID BETA PROTEIN; INFLUENZA VIRUS HEMAGGLUTININ; SOLVENT; TRIFLUOROETHANOL;

ACCURACY; ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AQUEOUS SOLUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; MICELLE; MICROENVIRONMENT; NEUROTOXICITY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN STRUCTURE;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN; CIRCULAR DICHROISM; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE BIOSYNTHESIS; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID;

INFLUENZA VIRUS;

EID: 0036438914     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03271.x     Document Type: Article

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