The extreme N-terminal region of human apolipoprotein A-I has a strong propensity to form amyloid fibrils

FEBS Letters

Volumn 588, Issue 3, 2014, Pages 389-394

  Adachi, Emi ^a   Kosaka, Asako ^a   Tsuji, Kohei ^a   Mizuguchi, Chiharu ^a   Kawashima, Hiroyuki ^b   Shigenaga, Akira ^a   Nagao, Kohjiro ^a   Akaji, Kenichi ^b   Otaka, Akira ^a   Saito, Hiroyuki ^a  

^a UNIVERSITY OF TOKUSHIMA   (Japan)

^b KYOTO PHARMACEUTICAL UNIVERSITY   (Japan)

Author keywords

Amyloid fibril; Apolipoprotein A I; Peptide; Point mutation

Indexed keywords

AMYLOID; APOLIPOPROTEIN A1;

AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CONTROLLED STUDY; FLUORESCENCE ANALYSIS; POINT MUTATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

AFM; AMYLOID FIBRIL; APOA-I; APOLIPOPROTEIN A-I; ATOMIC FORCE MICROSCOPY; ATR; ATTENUATED TOTAL REFLECTION; FOURIER TRANSFORM INFRARED SPECTROSCOPY; FTIR; HDL; HIGH-DENSITY LIPOPROTEIN; PEPTIDE; POINT MUTATION; THIOFLAVINT; THT; WAVELENGTH OF MAXIMUM FLUORESCENCE; WMF;

AMYLOID; APOLIPOPROTEIN A-I; CIRCULAR DICHROISM; HUMANS; MICROSCOPY, ATOMIC FORCE; PEPTIDE FRAGMENTS; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 84892832599     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.11.031     Document Type: Article

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