Influence of divalent copper, manganese and zinc ions on fibril nucleation and elongation of the amyloid-like yeast prion determinant Sup35p-NM

Journal of Inorganic Biochemistry

Volumn 103, Issue 12, 2009, Pages 1711-1720

  Suhre, Michael H ^a   Hess, Simone ^b   Golser, Adrian V ^a   Scheibel, Thomas ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

^b TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

Acrylodan fluorescence; Amyloid nucleation; Copper; Fibril assembly; ITC

Indexed keywords

AMYLOID; COPPER ION; CYTOPLASM PROTEIN; MANGANESE; PRION PROTEIN; SUP35P PROTEIN; UNCLASSIFIED DRUG; ZINC ION;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING SITE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; METAL BINDING; OLIGOMERIZATION; PROTEIN AGGREGATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SACCHAROMYCES CEREVISIAE;

AMINO ACID SEQUENCE; AMYLOID; COPPER; MANGANESE; MOLECULAR SEQUENCE DATA; PEPTIDE TERMINATION FACTORS; PRIONS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; ZINC;

MAMMALIAN PRION; SACCHAROMYCES CEREVISIAE;

EID: 70350571753     PISSN: 01620134     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jinorgbio.2009.09.021     Document Type: Article

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