A role for destabilizing amino acid replacements in light-chain amyloidosis.

@article{Hurle1994ARF,
  title={A role for destabilizing amino acid replacements in light-chain amyloidosis.},
  author={Mark Hurle and Larry R. Helms and Lin-Sheng Li and W Chan and Ronald Wetzel},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1994},
  volume={91 12},
  pages={5446-50}
}
Light-chain (L-chain) amyloidosis is characterized by deposition of fibrillar aggregates composed of the N-terminal L-chain variable region (VL) domain of an immunoglobulin, generally in individuals overproducing a monoclonal L chain. In addition to proteolytic fragmentation and high protein concentration, particular amino acid substitutions may also contribute to the tendency of an L chain to aggregate in L-chain amyloidosis, although evidence in support of this has been limited and difficult… CONTINUE READING

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