Folding stability of amyloid-β 40 monomer is an important determinant of the nucleation kinetics in fibrillization

FASEB Journal

Volumn 25, Issue 4, 2011, Pages 1390-1401

  Ni, Chun Lun ^a   Shi, Hoi Ping ^a   Yu, Hui Ming ^a   Chang, Yun Chorng ^b   Chen, Yun Ru ^a  

^a GENOMICS RESEARCH CENTER   (Taiwan)

^b NATIONAL CHENG KUNG UNIVERSITY   (Taiwan)

Author keywords

Alzheimer's disease; Natively unfolded; Protein aggregation; Protein conformation

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; GUANIDINE; MONOMER; MUTANT PROTEIN; TRIFLUOROETHANOL;

ALZHEIMER DISEASE; AMYLOID FIBRILLIZATION; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; ELECTROPHORESIS; FLUORESCENCE SPECTROSCOPY; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN MODIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN VARIANT; THERMODYNAMICS; ULTRACENTRIFUGATION; UNFOLDED PROTEIN RESPONSE; WILD TYPE;

AMINO ACID SEQUENCE; AMYLOID; AMYLOID BETA-PEPTIDES; AMYLOID BETA-PROTEIN PRECURSOR; GUANIDINE; HUMANS; KINETICS; PEPTIDE FRAGMENTS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; TRIFLUOROETHANOL;

EID: 79954613385     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.10-175539     Document Type: Article

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