Aggregation of the acylphosphatase from Sulfolobus solfataricus: The folded and partially unfolded states can both be precursors for amyloid formation

Journal of Biological Chemistry

Volumn 279, Issue 14, 2004, Pages 14111-14119

  Plakoutsi, Georgia ^a   Taddei, Niccolò ^a   Stefani, Massimo ^a   Chiti, Fabrizio ^a  

^a UNIVERSITY OF FLORENCE   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATES; CONFORMATIONS; DISEASES; ELECTRON MICROSCOPY; ENZYMES; PATHOLOGY;

ENZYMATIC ACTIVITY; FIBRIL FORMATION;

BIOCHEMISTRY;

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ACYLPHOSPHATASE; AMYLOID PROTEIN; CONGO RED; THIOFLAVINE; TRIFLUOROETHANOL;

ALZHEIMER DISEASE; AMYLOIDOSIS; ARCHAEBACTERIUM; ARTICLE; CIRCULAR DICHROISM; CREUTZFELDT JAKOB DISEASE; ELECTRON MICROSCOPY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; LIGHT SCATTERING; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN FOLDING; SULFOLOBUS SOLFATARICUS;

ACID ANHYDRIDE HYDROLASES; AMINO ACID SEQUENCE; ARCHAEAL PROTEINS; CIRCULAR DICHROISM; CLONING, MOLECULAR; COLORING AGENTS; ENERGY TRANSFER; MICROSCOPY, ELECTRON; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; SULFOLOBUS;

ARCHAEA; SULFOLOBUS; SULFOLOBUS SOLFATARICUS;

EID: 1842790837     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M312961200     Document Type: Article

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