Amyloid fibril formation from full-length and fragments of amylin

Journal of Structural Biology

Volumn 130, Issue 2-3, 2000, Pages 352-362

  Goldsbury, C ^a,b   Goldie, K ^d   Pellaud, J ^a   Seelig, J ^a   Frey, P ^e   Muller S A ^a   Kistler, J ^b   Cooper, G J S ^b,c   Aebi, U ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

^b UNIVERSITY OF AUCKLAND   (New Zealand)

^c UNIVERSITY OF AUCKLAND   (New Zealand)

^d EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^e NOVARTIS PHARMA AG   (Switzerland)

Author keywords

Amylin; Amyloid; Circular dichroism spectroscopy; Diabetes mellitus; Fibril structure; IAPP; Polymorphism; Scanning transmission electron microscopy (STEM); Transmission electron microscopy (TEM)

Indexed keywords

AMYLIN; AMYLOID;

AMINO ACID SEQUENCE; AMYLOIDOSIS; ARTICLE; CIRCULAR DICHROISM; DIABETES MELLITUS; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; SCANNING ELECTRON MICROSCOPY; TRANSMISSION ELECTRON MICROSCOPY;

EID: 0033856165     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.2000.4268     Document Type: Article

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