Prefibrillar Amyloid Protein Aggregates Share Common Features of Cytotoxicity*

@article{Bucciantini2004PrefibrillarAP,
  title={Prefibrillar Amyloid Protein Aggregates Share Common Features of Cytotoxicity*},
  author={M. Bucciantini and G. Calloni and F. Chiti and L. Formigli and D. Nosi and C. Dobson and M. Stefani},
  journal={Journal of Biological Chemistry},
  year={2004},
  volume={279},
  pages={31374 - 31382}
}
The intracellular free Ca2+ concentration and redox status of murine fibroblasts exposed to prefibrillar aggregates of the HypF N-terminal domain have been investigated in vitro and in vivo using a range of fluorescent probes. Aggregate entrance into the cytoplasm is followed by an early rise of reactive oxygen species and free Ca2+ levels and eventually by cell death. Such changes correlate directly with the viability of the cells and are not observed when cell are cultured in the presence of… Expand
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Proteomic analysis of cells exposed to prefibrillar aggregates of HypF-N.
A comparison of the biochemical modifications caused by toxic and non-toxic protein oligomers in cells
Glycosaminoglycans (GAGs) suppress the toxicity of HypF-N prefibrillar aggregates.
Amyloid-linked cellular toxicity triggered by bacterial inclusion bodies.
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