Hydration and Packing are Crucial to Amyloidogenesis as Revealed by Pressure Studies on Transthyretin Variants that Either Protect or Worsen Amyloid Disease

Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å

C. C. F. Blake, Michael J. Geisow, Stuart J. Oatley et al. · Journal of Molecular Biology · 1978 · 793 citations

Biochemistry, Protein Folding, Natural Sciences +7

Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components

Serge N. Timasheff · Proceedings of the National Academy of Sciences · 2002 · 696 citations · Full text

Engineering, Protein Phase Separation, Solution (Chemistry) +18

Fibril in senile systemic amyloidosis is derived from normal transthyretin.

Per Westermark, Knut Sletten, Gibbons G. Cornwell · Proceedings of the National Academy of Sciences · 1990 · 691 citations

Amyloid Fibril, Alzheimer's Disease, Senile Systemic Amyloidosis +8

The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins

Gerhard Hummer, Shekhar Garde, Angel E. Garcı́a et al. · Proceedings of the National Academy of Sciences · 1998 · 587 citations · Full text

Proteinlipid Interaction, High Hydrostatic Pressure, Protein Assembly +16

The Acid-Mediated Denaturation Pathway of Transthyretin Yields a Conformational Intermediate That Can Self-Assemble into Amyloid

Zhihong Lai, Wilfredo Colón, Jeffery W. Kelly · Biochemistry · 1996 · 562 citations