Hydration and packing are crucial to amyloidogenesis as revealed by pressure studies on transthyretin variants that either protect or worsen amyloid disease

Journal of Molecular Biology

Volumn 328, Issue 4, 2003, Pages 963-974

  Ferrão Gonzales, Astria D ^a   Palmieri, Leonardo ^a   Valory, Marcelo ^a   Silva, Jerson L ^a   Lashuel, Hilal ^b   Kelly, Jeffery W ^c   Foguel, Débora ^a  

^a FEDERAL UNIVERSITY OF RIO DE JANEIRO   (Brazil)

^b HARVARD MEDICAL SCHOOL   (United States)

^c SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Amyloid; High hydrostatic pressure; Packing defects; Thermodynamic stability; Transthyretin

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; AMYLOID; CHAPERONE; GLUCOSE; MUTANT PROTEIN; PREALBUMIN; PROTEIN SUBUNIT; SULFONIC ACID DERIVATIVE; TETRAMER;

ACIDITY; AMYLOIDOSIS; ARTICLE; COMPRESSION; DECOMPRESSION; DISEASE ASSOCIATION; DISEASE COURSE; HYDRATION; HYDROSTATIC PRESSURE; MOLECULAR INTERACTION; MUTATION; PACKAGING; PH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN VARIANT; SPECIES; WILD TYPE;

EID: 0043018095     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00368-1     Document Type: Article

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