Title |
Genomic Clustering and Homology between HET-S and the NWD2 STAND Protein in Various Fungal Genomes
|
---|---|
Published in |
PLOS ONE, April 2012
|
DOI | 10.1371/journal.pone.0034854 |
Pubmed ID | |
Authors |
Asen Daskalov, Mathieu Paoletti, Frédérique Ness, Sven J. Saupe |
Abstract |
Prions are infectious proteins propagating as self-perpetuating amyloid polymers. The [Het-s] prion of Podospora anserina is involved in a cell death process associated with non-self recognition. The prion forming domain (PFD) of HET-s adopts a β-solenoid amyloid structure characterized by the two fold repetition of an elementary triangular motif. [Het-s] induces cell death when interacting with HET-S, an allelic variant of HET-s. When templated by [Het-s], HET-S undergoes a trans-conformation, relocates to the cell membrane and induces toxicity. |
Mendeley readers
The data shown below were compiled from readership statistics for 61 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
Country | Count | As % |
---|---|---|
United States | 1 | 2% |
Italy | 1 | 2% |
Unknown | 59 | 97% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 17 | 28% |
Researcher | 9 | 15% |
Student > Bachelor | 9 | 15% |
Professor | 5 | 8% |
Student > Master | 3 | 5% |
Other | 7 | 11% |
Unknown | 11 | 18% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 31 | 51% |
Biochemistry, Genetics and Molecular Biology | 10 | 16% |
Immunology and Microbiology | 3 | 5% |
Neuroscience | 2 | 3% |
Computer Science | 1 | 2% |
Other | 3 | 5% |
Unknown | 11 | 18% |