In silico characterization of human prion-like proteins: beyond neurological diseases
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- dc.contributor.author Iglesias, Valentin
- dc.contributor.author Paladin, Lisanna
- dc.contributor.author Juan Blanco, Teresa, 1989-
- dc.contributor.author Pallarès, Irantzu
- dc.contributor.author Aloy, Patrick, 1972-
- dc.contributor.author Tosatto, Silvio C.E.
- dc.contributor.author Ventura, Salvador
- dc.date.accessioned 2020-03-25T07:35:51Z
- dc.date.available 2020-03-25T07:35:51Z
- dc.date.issued 2019
- dc.description.abstract Prion-like behavior has been in the spotlight since it was first associated with the onset of mammalian neurodegenerative diseases. However, a growing body of evidence suggests that this mechanism could be behind the regulation of processes such as transcription and translation in multiple species. Here, we perform a stringent computational survey to identify prion-like proteins in the human proteome. We detected 242 candidate polypeptides and computationally assessed their function, protein-protein interaction networks, tissular expression, and their link to disease. Human prion-like proteins constitute a subset of modular polypeptides broadly expressed across different cell types and tissues, significantly associated with disease, embedded in highly connected interaction networks, and involved in the flow of genetic information in the cell. Our analysis suggests that these proteins might play a relevant role not only in neurological disorders, but also in different types of cancer and viral infections.
- dc.description.sponsorship SV was supported by Ministerio de Economía y Competitividad (MINECO) (BIO2016-78310-R) and by ICREA, ICREA ACADEMIA 2015 to SV. PA was supported by MINECO (BIO2016-77038-R) and the European Research Council Consolidator grant, SysPharmAD (614944). TJ-B is a recipient of an FPI-SO fellowship. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
- dc.format.mimetype application/pdf
- dc.identifier.citation Iglesias V, Paladin L, Juan-Blanco T, Pallarès I, Aloy P, Tosatto SCE, Ventura S. In silico characterization of human prion-like proteins: beyond neurological diseases. Front Physiol. 2019; 10:314. DOI: 10.3389/fphys.2019.00314
- dc.identifier.doi http://dx.doi.org/10.3389/fphys.2019.00314
- dc.identifier.issn 1664-042X
- dc.identifier.uri http://hdl.handle.net/10230/44014
- dc.language.iso eng
- dc.publisher Frontiers
- dc.relation.ispartof Front Physiol. 2019; 10:314
- dc.relation.projectID info:eu-repo/grantAgreement/ES/1PE/BIO2016-78310-R
- dc.relation.projectID info:eu-repo/grantAgreement/ES/1PE/BIO2016-77038-R
- dc.relation.projectID info:eu-repo/grantAgreement/EC/FP7/614944
- dc.rights © 2019 Iglesias, Paladin, Juan-Blanco, Pallarès, Aloy, Tosatto and Ventura. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
- dc.rights.accessRights info:eu-repo/semantics/openAccess
- dc.rights.uri http://creativecommons.org/licenses/by/4.0/
- dc.subject.keyword Amyloid
- dc.subject.keyword Bioinformatics
- dc.subject.keyword Disease
- dc.subject.keyword Prion-like proteins
- dc.subject.keyword Protein aggregation
- dc.subject.keyword Protein–protein interaction
- dc.title In silico characterization of human prion-like proteins: beyond neurological diseases
- dc.type info:eu-repo/semantics/article
- dc.type.version info:eu-repo/semantics/publishedVersion