000061816 001__ 61816
000061816 005__ 20170713115235.0
000061816 0247_ $$2doi$$a10.1186/1471-2164-15-102
000061816 0248_ $$2sideral$$a85254
000061816 037__ $$aART-2014-85254
000061816 041__ $$aeng
000061816 100__ $$0(orcid)0000-0002-3268-8730$$aEspinosa Angarica, V.
000061816 245__ $$aPrionScan: An online database of predicted prion domains in complete proteomes
000061816 260__ $$c2014
000061816 5060_ $$aAccess copy available to the general public$$fUnrestricted
000061816 5203_ $$aBackground: 
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.
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.
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.
000061816 536__ $$9info:eu-repo/grantAgreement/ES/DGA/CTPR02-09$$9info:eu-repo/grantAgreement/ES/DGA/PI078-08$$9info:eu-repo/grantAgreement/ES/MICINN/BFU2010-16297
000061816 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000061816 590__ $$a3.986$$b2014
000061816 591__ $$aGENETICS & HEREDITY$$b39 / 166 = 0.235$$c2014$$dQ1$$eT1
000061816 591__ $$aBIOTECHNOLOGY & APPLIED MICROBIOLOGY$$b26 / 163 = 0.16$$c2014$$dQ1$$eT1
000061816 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000061816 700__ $$aAngulo, A.
000061816 700__ $$0(orcid)0000-0002-9708-4647$$aGiner, A.
000061816 700__ $$0(orcid)0000-0002-6518-1477$$aLosilla, G.
000061816 700__ $$aVentura, S.
000061816 700__ $$0(orcid)0000-0002-2879-9200$$aSancho, J.$$uUniversidad de Zaragoza
000061816 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDepartamento de Bioquímica y Biología Molecular y Celular$$cBioquímica y Biología Molecular
000061816 773__ $$g15, 1 (2014), 102 [9 pp]$$pBMC genomics$$tBMC Genomics$$x1471-2164
000061816 8564_ $$s1555082$$uhttps://zaguan.unizar.es/record/61816/files/texto_completo.pdf$$yVersión publicada
000061816 8564_ $$s107175$$uhttps://zaguan.unizar.es/record/61816/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000061816 909CO $$ooai:zaguan.unizar.es:61816$$particulos$$pdriver
000061816 951__ $$a2017-07-13-11:11:33
000061816 980__ $$aARTICLE