Formation of amyloid aggregates from human lysozyme and its disease‐associated variants using hydrostatic pressure

@article{Felice2004FormationOA,
  title={Formation of amyloid aggregates from human lysozyme and its disease‐associated variants using hydrostatic pressure},
  author={F. G. Felice and Marcelo N N Vieira and M. Meirelles and L. Morozova-Roche and C. Dobson and S. Ferreira},
  journal={The FASEB Journal},
  year={2004},
  volume={18}
}
Formation of amyloid deposits from the Ile56Thr or Asp67His variants of human lysozyme is a hallmark of autosomal hereditary systemic amyloidosis. It has recently been shown that amyloid fibrils can be formed in vitro from wild‐type (WT), I56T, or D67H lysozyme variants upon prolonged incubation at acidic pH and elevated temperatures (1). Here, we have used hydrostatic pressure as a tool to generate amyloidogenic states of WT and variant lysozymes at physiological pH. WT or variant lysozyme… Expand
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