Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina.

@article{Balguerie2003DomainOA,
  title={Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina.},
  author={Axelle Balguerie and Suzana Dos Reis and Christiane Ritter and St{\'e}phane Chaignepain and B{\'e}n{\'e}dicte Coulary-Salin and Vincent Forge and Katell Bathany and Ioan Lascu and Jean-Marie Schmitter and Roland Riek and Sven J. Saupe},
  journal={The EMBO journal},
  year={2003},
  volume={22 9},
  pages={
          2071-81
        }
}
The [Het-s] infectious element of the fungus Podospora anserina is a prion protein involved in a genetically controlled cell death reaction termed heterokaryon incompatibility. Previous analyses indicate that [Het-s] propagates as a self-perpetuating amyloid aggregate. The HET-s protein is 289 amino acids in length. Herein, we identify the region of the HET-s protein that is responsible for amyloid formation and prion propagation. The region of HET-s spanning residues 218-289 forms amyloid… CONTINUE READING
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