Dual role of an N-terminal amyloidogenic mutation in apolipoprotein A-I: Destabilization of helix bundle and enhancement of fibril formation

Journal of Biological Chemistry

Volumn 288, Issue 4, 2013, Pages 2848-2856

  Adachi, Emi ^a   Nakajima, Hiroyuki ^a   Mizuguchi, Chiharu ^a   Dhanasekaran, Padmaja ^c   Kawashima, Hiroyuki ^b   Nagao, Kohjiro ^a   Akaji, Kenichi ^b   Lund Katz, Sissel ^c   Phillips, Michael C ^c   Saito, Hiroyuki ^a  

^a UNIVERSITY OF TOKUSHIMA   (Japan)

^b KYOTO PHARMACEUTICAL UNIVERSITY   (Japan)

^c UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATION PROPENSITY; AMYLOID FIBRIL; AMYLOID FIBRIL FORMATION; APOLIPOPROTEIN A-I; APOLIPOPROTEINS; ARGININE RESIDUE; CONFORMATIONAL CHANGE; DUAL ROLE; FIBRIL FORMATION; FLUORESCENCE MEASUREMENTS; FULL-LENGTH PROTEINS; HEK293 CELLS; HELIX BUNDLE; HYDROPHOBIC SURFACES; INHIBITING EFFECT; INITIAL STRUCTURES; N-TERMINAL HELIX; N-TERMINALS; NATURALLY OCCURRING; NEUTRAL PH; POINT MUTATIONS; RANDOM-COIL STRUCTURES; STRUCTURAL CHANGE; THIOFLAVIN T;

AMINO ACIDS; ATOMIC FORCE MICROSCOPY; DISEASES; FLUORESCENCE; SURFACE CHEMISTRY;

PROTEINS;

AMYLOID; APOLIPOPROTEIN A1;

AMINO TERMINAL SEQUENCE; ARTICLE; ATOMIC FORCE MICROSCOPY; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CYTOTOXICITY TEST; FLUORESCENCE ANALYSIS; HYDROPHOBICITY; MUTATIONAL ANALYSIS; PHYSICAL CHEMISTRY; POINT MUTATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STABILITY; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; SURFACE PROPERTY;

AMYLOID; AMYLOIDOSIS, FAMILIAL; APOLIPOPROTEIN A-I; CIRCULAR DICHROISM; HEK293 CELLS; HUMANS; HYDROGEN-ION CONCENTRATION; MICROSCOPY, ATOMIC FORCE; MUTATION; POINT MUTATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; THERMODYNAMICS; TIME FACTORS;

EID: 84873874544     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.428052     Document Type: Article

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