Amyloidogenic mutations in human apolipoprotein A-I are not necessarily destabilizing - a common mechanism of apolipoprotein A-I misfolding in familial amyloidosis and atherosclerosis.

@article{Das2014AmyloidogenicMI,
  title={Amyloidogenic mutations in human apolipoprotein A-I are not necessarily destabilizing - a common mechanism of apolipoprotein A-I misfolding in familial amyloidosis and atherosclerosis.},
  author={Madhurima Das and Xiaohu Mei and Shobini Jayaraman and David Atkinson and Olga Gursky},
  journal={The FEBS journal},
  year={2014},
  volume={281 11},
  pages={2525-42}
}
High-density lipoproteins and their major protein, apolipoprotein A-I (apoA-I), remove excess cellular cholesterol and protect against atherosclerosis. However, in acquired amyloidosis, nonvariant full-length apoA-I deposits as fibrils in atherosclerotic plaques; in familial amyloidosis, N-terminal fragments of variant apoA-I deposit in vital organs, damaging them. Recently, we used the crystal structure of Δ(185-243)apoA-I to show that amyloidogenic mutations destabilize apoA-I and increase… CONTINUE READING

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