Stepwise organization of the β-structure identifies key regions essential for the propagation and cytotoxicity of insulin amyloid fibrils

Journal of Biological Chemistry

Volumn 289, Issue 15, 2014, Pages 10399-10410

  Chatani, Eri ^a   Imamura, Hiroshi ^b   Yamamoto, Naoki ^b   Kato, Minoru ^b  

^a KOBE UNIVERSITY   (Japan)

^b RITSUMEIKAN UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGEN BONDS;

AMYLOID FIBRIL; CELLULAR TOXICITIES; FOURIER TRANSFORM INFRARED SPECTRA; HUNTINGTON DISEASE; INSULIN AMYLOID FIBRILS; PROTOFIBRILS; STRUCTURAL ORGANIZATION; SUPRAMOLECULAR ASSEMBLIES;

GLYCOPROTEINS;

AMYLOID; INSULIN; INSULIN AMYLOID FIBRIL; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

ARTICLE; BETA SHEET; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; CYTOTOXICITY; HYDROGEN BOND; INFRARED SPECTROSCOPY; MOLECULAR MECHANICS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN SYNTHESIS; SIGNAL TRANSDUCTION;

AMYLOID; CYTOTOXICITY; INSULIN; PREFIBRILLAR INTERMEDIATE; PROPAGATION; PROTEIN AGGREGATION; PROTEIN MISFOLDING; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; AMYLOID; ANIMALS; HOT TEMPERATURE; HYDROGEN BONDING; INSULIN; MASS SPECTROMETRY; MICROSCOPY, ATOMIC FORCE; MOLECULAR SEQUENCE DATA; PC12 CELLS; PROTEIN STRUCTURE, SECONDARY; RATS; SALTS; SODIUM CHLORIDE; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TEMPERATURE; TIME FACTORS;

EID: 84898669502     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.520874     Document Type: Article

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