Structural differences between amyloid beta oligomers

Biochemical and Biophysical Research Communications

Volumn 477, Issue 4, 2016, Pages 700-705

  Breydo, Leonid ^a,b   Kurouski, Dmitry ^c   Rasool, Suhail ^a   Milton, Saskia ^a   Wu, Jessica W ^a   Uversky, Vladimir N ^b,d   Lednev, Igor K ^c   Glabe, Charles G ^a,d  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF SOUTH FLORIDA   (United States)

^c STATE UNIVERSITY OF NEW YORK   (United States)

^d KING ABDULAZIZ UNIVERSITY   (Saudi Arabia)

Author keywords

Alzheimer's disease; Amyloid beta; Oligomers; Protein aggregation

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; OLIGOMER; AMYLOID; AMYLOID BETA PROTEIN; PEPTIDE FRAGMENT;

AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; HYDROGEN BOND; HYDROPHOBICITY; MASS SPECTROMETRY; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE; WILD TYPE; CHEMISTRY; DIMERIZATION; ULTRASTRUCTURE;

AMYLOID; AMYLOID BETA-PEPTIDES; DIMERIZATION; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION;

EID: 84979673431     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2016.06.122     Document Type: Article

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