In silico characterization of human prion-like proteins: beyond neurological diseases

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....

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Detalles Bibliográficos
Autores: Iglesias, Valentin, Paladin, Lisanna, Juan Blanco, Teresa, 1989-, Pallarès, Irantzu, Aloy, Patrick, 1972-, Tosatto, Silvio C.E., Ventura, Salvador
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2019
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:10230/44014
Acceso en línea:http://hdl.handle.net/10230/44014
http://dx.doi.org/10.3389/fphys.2019.00314
Access Level:acceso abierto
Palabra clave:Amyloid
Bioinformatics
Disease
Prion-like proteins
Protein aggregation
Protein–protein interaction
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spelling In silico characterization of human prion-like proteins: beyond neurological diseasesIglesias, ValentinPaladin, LisannaJuan Blanco, Teresa, 1989-Pallarès, IrantzuAloy, Patrick, 1972-Tosatto, Silvio C.E.Ventura, SalvadorAmyloidBioinformaticsDiseasePrion-like proteinsProtein aggregationProtein–protein interactionPrion-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.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.Frontiers202020202019info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttp://hdl.handle.net/10230/44014http://dx.doi.org/10.3389/fphys.2019.00314reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésFront Physiol. 2019; 10:314info:eu-repo/grantAgreement/ES/1PE/BIO2016-78310-Rinfo:eu-repo/grantAgreement/ES/1PE/BIO2016-77038-Rinfo:eu-repo/grantAgreement/EC/FP7/614944© 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.http://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:recercat.cat:10230/440142026-05-29T05:05:01Z
dc.title.none.fl_str_mv In silico characterization of human prion-like proteins: beyond neurological diseases
title In silico characterization of human prion-like proteins: beyond neurological diseases
spellingShingle In silico characterization of human prion-like proteins: beyond neurological diseases
Iglesias, Valentin
Amyloid
Bioinformatics
Disease
Prion-like proteins
Protein aggregation
Protein–protein interaction
title_short In silico characterization of human prion-like proteins: beyond neurological diseases
title_full In silico characterization of human prion-like proteins: beyond neurological diseases
title_fullStr In silico characterization of human prion-like proteins: beyond neurological diseases
title_full_unstemmed In silico characterization of human prion-like proteins: beyond neurological diseases
title_sort In silico characterization of human prion-like proteins: beyond neurological diseases
dc.creator.none.fl_str_mv Iglesias, Valentin
Paladin, Lisanna
Juan Blanco, Teresa, 1989-
Pallarès, Irantzu
Aloy, Patrick, 1972-
Tosatto, Silvio C.E.
Ventura, Salvador
author Iglesias, Valentin
author_facet Iglesias, Valentin
Paladin, Lisanna
Juan Blanco, Teresa, 1989-
Pallarès, Irantzu
Aloy, Patrick, 1972-
Tosatto, Silvio C.E.
Ventura, Salvador
author_role author
author2 Paladin, Lisanna
Juan Blanco, Teresa, 1989-
Pallarès, Irantzu
Aloy, Patrick, 1972-
Tosatto, Silvio C.E.
Ventura, Salvador
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Amyloid
Bioinformatics
Disease
Prion-like proteins
Protein aggregation
Protein–protein interaction
topic Amyloid
Bioinformatics
Disease
Prion-like proteins
Protein aggregation
Protein–protein interaction
description 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.
publishDate 2019
dc.date.none.fl_str_mv 2019
2020
2020
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10230/44014
http://dx.doi.org/10.3389/fphys.2019.00314
url http://hdl.handle.net/10230/44014
http://dx.doi.org/10.3389/fphys.2019.00314
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Front Physiol. 2019; 10:314
info:eu-repo/grantAgreement/ES/1PE/BIO2016-78310-R
info:eu-repo/grantAgreement/ES/1PE/BIO2016-77038-R
info:eu-repo/grantAgreement/EC/FP7/614944
dc.rights.none.fl_str_mv http://creativecommons.org/licenses/by/4.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Frontiers
publisher.none.fl_str_mv Frontiers
dc.source.none.fl_str_mv reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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