Amyloid formation from HypF-N under conditions in which the protein is initially in its native state

Journal of Molecular Biology

Volumn 347, Issue 2, 2005, Pages 323-335

  Marcon, Giordana ^a   Plakoutsi, Georgia ^a   Canale, Claudio ^b   Relini, Annalisa ^b   Taddei, Niccolò ^a,c   Dobson, Christopher M ^d   Ramponi, Giampietro ^a,c   Chiti, Fabrizio ^a,c  

^a UNIVERSITY OF FLORENCE   (Italy)

^b UNIVERSITY OF GENOA   (Italy)

^c Centro di Ricerca   (Italy)

^d UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Amyloid; Disease; HypF; Misfolding; Oligomers

Indexed keywords

ACRYLAMIDE; AMYLOID PROTEIN; GLOBULAR PROTEIN; THIOFLAVINE; TRIFLUOROETHANOL; TRYPTOPHAN;

AMINO TERMINAL SEQUENCE; ARTICLE; ATOMIC FORCE MICROSCOPY; CELL CULTURE; CIRCULAR DICHROISM; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; ULTRAVIOLET RADIATION;

EID: 14644406760     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.01.034     Document Type: Article

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