The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions

Biochemistry

Volumn 38, Issue 41, 1999, Pages 13560-13573

  Lashuel, Hilal A ^a   Wurth, Christine ^b   Woo, Linda ^a   Kelly, Jeffery W ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b ETH ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; PREALBUMIN;

ACIDIFICATION; AMYLOIDOSIS; ARTICLE; DISEASE ASSOCIATION; DISSOCIATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

AMYLOID; AMYLOID NEUROPATHIES; ANILINO NAPHTHALENESULFONATES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HUMANS; HYDROGEN-ION CONCENTRATION; LEUCINE; MICROSCOPY, ELECTRON; PREALBUMIN; PROLINE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; SPECTROMETRY, FLUORESCENCE; SURFACE PROPERTIES; ULTRACENTRIFUGATION;

EID: 0033550075     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi991021c     Document Type: Article

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