Influence of residue 22 on the folding, aggregation profile, and toxicity of the Alzheimer's amyloid β peptide

Biophysical Journal

Volumn 97, Issue 1, 2009, Pages 277-285

  Perálvarez Marín, Alex ^a   Mateos, Laura ^b   Zhang, Ce ^c   Singh, Shalini ^a   Cedazo Mínguez, Ángel ^b   Visa, Neus ^a   Morozova Roche, Ludmilla ^c   Gräslund, Astrid ^a   Barth, Andreas ^a  

^a STOCKHOLM UNIVERSITY   (Sweden)

^b KAROLINSKA INSTITUTE   (Sweden)

^c UMEÅ UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; ATOMIC FORCE MICROSCOPY; BETA SHEET; CELL STRUCTURE; CELL VIABILITY; CONTROLLED STUDY; HUMAN; HUMAN CELL; HYDROPHOBICITY; NEUROBLASTOMA CELL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; THERMOSTABILITY; TRANSMISSION ELECTRON MICROSCOPY;

AGING; AMYLOID BETA-PEPTIDES; CELL LINE, TUMOR; CELL SURVIVAL; CIRCULAR DICHROISM; CONGO RED; HUMANS; MICROSCOPY, ATOMIC FORCE; MICROSCOPY, ELECTRON, TRANSMISSION; NEUROBLASTOMA; PEPTIDE FRAGMENTS; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TEMPERATURE;

EID: 68949149540     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.04.017     Document Type: Article

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