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 Ludmilla A. 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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References

SHOWING 1-10 OF 52 REFERENCES
Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants.
  • 269
Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants.
  • 155
The preaggregated state of an amyloidogenic protein: hydrostatic pressure converts native transthyretin into the amyloidogenic state.
  • 191
  • PDF
Human lysozyme gene mutations cause hereditary systemic amyloidosis
  • 536
  • Highly Influential
Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy
  • 30
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
  • 2,248
Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme
  • 199
  • PDF
Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
  • 401
...
1
2
3
4
5
...