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PrionScan: an online database of predicted prion domains in complete proteomes

BACKGROUND: 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...

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Autores principales: Espinosa Angarica, Vladimir, Angulo, Alfonso, Giner, Arturo, Losilla, Guillermo, Ventura, Salvador, Sancho, Javier
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3922584/
https://www.ncbi.nlm.nih.gov/pubmed/24498877
http://dx.doi.org/10.1186/1471-2164-15-102
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author Espinosa Angarica, Vladimir
Angulo, Alfonso
Giner, Arturo
Losilla, Guillermo
Ventura, Salvador
Sancho, Javier
author_facet Espinosa Angarica, Vladimir
Angulo, Alfonso
Giner, Arturo
Losilla, Guillermo
Ventura, Salvador
Sancho, Javier
author_sort Espinosa Angarica, Vladimir
collection PubMed
description BACKGROUND: 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. DESCRIPTION: Here we present PrionScan, a new database of predicted prion-like domains in complete proteomes. We have previously developed a predictive methodology to identify and score prionogenic stretches in protein sequences. In the present work, we exploit this approach to scan all the protein sequences in public databases and compile a repository containing relevant information of proteins bearing prion-like domains. The database is updated regularly alongside UniprotKB and in its present version contains approximately 28000 predictions in proteins from different functional categories in more than 3200 organisms from all the taxonomic subdivisions. PrionScan can be used in two different ways: database query and analysis of protein sequences submitted by the users. In the first mode, simple queries allow to retrieve a detailed description of the properties of a defined protein. Queries can also be combined to generate more complex and specific searching patterns. In the second mode, users can submit and analyze their own sequences. CONCLUSIONS: It is expected that this database would provide relevant insights on prion functions and regulation from a genome-wide perspective, allowing researches performing cross-species prion biology studies. Our database might also be useful for guiding experimentalists in the identification of new candidates for further experimental characterization.
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spelling pubmed-39225842014-02-13 PrionScan: an online database of predicted prion domains in complete proteomes Espinosa Angarica, Vladimir Angulo, Alfonso Giner, Arturo Losilla, Guillermo Ventura, Salvador Sancho, Javier BMC Genomics Database BACKGROUND: 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. DESCRIPTION: Here we present PrionScan, a new database of predicted prion-like domains in complete proteomes. We have previously developed a predictive methodology to identify and score prionogenic stretches in protein sequences. In the present work, we exploit this approach to scan all the protein sequences in public databases and compile a repository containing relevant information of proteins bearing prion-like domains. The database is updated regularly alongside UniprotKB and in its present version contains approximately 28000 predictions in proteins from different functional categories in more than 3200 organisms from all the taxonomic subdivisions. PrionScan can be used in two different ways: database query and analysis of protein sequences submitted by the users. In the first mode, simple queries allow to retrieve a detailed description of the properties of a defined protein. Queries can also be combined to generate more complex and specific searching patterns. In the second mode, users can submit and analyze their own sequences. CONCLUSIONS: It is expected that this database would provide relevant insights on prion functions and regulation from a genome-wide perspective, allowing researches performing cross-species prion biology studies. Our database might also be useful for guiding experimentalists in the identification of new candidates for further experimental characterization. BioMed Central 2014-02-05 /pmc/articles/PMC3922584/ /pubmed/24498877 http://dx.doi.org/10.1186/1471-2164-15-102 Text en Copyright © 2014 Espinosa Angarica et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Database
Espinosa Angarica, Vladimir
Angulo, Alfonso
Giner, Arturo
Losilla, Guillermo
Ventura, Salvador
Sancho, Javier
PrionScan: an online database of predicted prion domains in complete proteomes
title PrionScan: an online database of predicted prion domains in complete proteomes
title_full PrionScan: an online database of predicted prion domains in complete proteomes
title_fullStr PrionScan: an online database of predicted prion domains in complete proteomes
title_full_unstemmed PrionScan: an online database of predicted prion domains in complete proteomes
title_short PrionScan: an online database of predicted prion domains in complete proteomes
title_sort prionscan: an online database of predicted prion domains in complete proteomes
topic Database
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3922584/
https://www.ncbi.nlm.nih.gov/pubmed/24498877
http://dx.doi.org/10.1186/1471-2164-15-102
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