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Genomic Clustering and Homology between HET-S and the NWD2 STAND Protein in Various Fungal Genomes

Overview of attention for article published in PLOS ONE, April 2012
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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

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%