Title |
PrionScan: an online database of predicted prion domains in complete proteomes
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Published in |
BMC Genomics, February 2014
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DOI | 10.1186/1471-2164-15-102 |
Pubmed ID | |
Authors |
Vladimir Espinosa Angarica, Alfonso Angulo, Arturo Giner, Guillermo Losilla, Salvador Ventura, Javier Sancho |
Abstract |
Prions are a particular type of amyloids related to a large variety of important processes in cells, but also responsible for serious diseases in mammals and humans. The number of experimentally characterized prions is still low and corresponds to a handful of examples in microorganisms and mammals. Prion aggregation is mediated by specific protein domains with a remarkable compositional bias towards glutamine/asparagine and against charged residues and prolines. These compositional features have been used to predict new prion proteins in the genomes of different organisms. Despite these efforts, there are only a few available data sources containing prion predictions at a genomic scale. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Italy | 1 | 2% |
Unknown | 60 | 98% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Researcher | 13 | 21% |
Student > Ph. D. Student | 9 | 15% |
Student > Bachelor | 8 | 13% |
Student > Master | 7 | 11% |
Professor > Associate Professor | 5 | 8% |
Other | 11 | 18% |
Unknown | 8 | 13% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 24 | 39% |
Biochemistry, Genetics and Molecular Biology | 20 | 33% |
Medicine and Dentistry | 4 | 7% |
Nursing and Health Professions | 1 | 2% |
Earth and Planetary Sciences | 1 | 2% |
Other | 3 | 5% |
Unknown | 8 | 13% |