In silico characterization of human prion-like proteins
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....
| Autores: | , , , , , , |
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| Formato: | artículo |
| Fecha de publicación: | 2019 |
| País: | España |
| Recursos: | Universitat Autònoma de Barcelona |
| Repositorio: | Dipòsit Digital de Documents de la UAB |
| Idioma: | inglés |
| OAI Identifier: | oai:ddd.uab.cat:223543 |
| Acesso em linha: | https://ddd.uab.cat/record/223543 https://dx.doi.org/urn:doi:10.3389/fphys.2019.00314 |
| Access Level: | acceso abierto |
| Palavra-chave: | Prion-like proteins Disease Protein-protein interaction Protein aggregation Amyloid Bioinformatics |
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In silico characterization of human prion-like proteinsbeyond neurological diseasesIglesias, Valentin|||0000-0002-6133-0869Paladin, LisannaJuan Blanco, TeresaPallarès i Goitiz, Irantzu|||0000-0002-8205-2060Aloy, Patrick|||0000-0002-3557-0236Tosatto, Silvio|||0000-0003-4525-7793Ventura, Salvador|||0000-0002-9652-6351Prion-like proteinsDiseaseProtein-protein interactionProtein aggregationAmyloidBioinformaticsPrion-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. 22019-01-0120192019-01-01Articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://ddd.uab.cat/record/223543https://dx.doi.org/urn:doi:10.3389/fphys.2019.00314reponame:Dipòsit Digital de Documents de la UABinstname:Universitat Autònoma de BarcelonaInglésengEuropean Commission https://doi.org/10.13039/501100000780 614944Agencia Estatal de Investigación https://doi.org/10.13039/501100011033 BIO2016-78310-RAgencia Estatal de Investigación https://doi.org/10.13039/501100011033 BIO2016-77038-Ropen accesshttp://purl.org/coar/access_right/c_abf2Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original.https://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:ddd.uab.cat:2235432026-06-06T12:50:31Z |
| 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 |
| spellingShingle |
In silico characterization of human prion-like proteins Iglesias, Valentin|||0000-0002-6133-0869 Prion-like proteins Disease Protein-protein interaction Protein aggregation Amyloid Bioinformatics |
| title_short |
In silico characterization of human prion-like proteins |
| title_full |
In silico characterization of human prion-like proteins |
| title_fullStr |
In silico characterization of human prion-like proteins |
| title_full_unstemmed |
In silico characterization of human prion-like proteins |
| title_sort |
In silico characterization of human prion-like proteins |
| dc.creator.none.fl_str_mv |
Iglesias, Valentin|||0000-0002-6133-0869 Paladin, Lisanna Juan Blanco, Teresa Pallarès i Goitiz, Irantzu|||0000-0002-8205-2060 Aloy, Patrick|||0000-0002-3557-0236 Tosatto, Silvio|||0000-0003-4525-7793 Ventura, Salvador|||0000-0002-9652-6351 |
| author |
Iglesias, Valentin|||0000-0002-6133-0869 |
| author_facet |
Iglesias, Valentin|||0000-0002-6133-0869 Paladin, Lisanna Juan Blanco, Teresa Pallarès i Goitiz, Irantzu|||0000-0002-8205-2060 Aloy, Patrick|||0000-0002-3557-0236 Tosatto, Silvio|||0000-0003-4525-7793 Ventura, Salvador|||0000-0002-9652-6351 |
| author_role |
author |
| author2 |
Paladin, Lisanna Juan Blanco, Teresa Pallarès i Goitiz, Irantzu|||0000-0002-8205-2060 Aloy, Patrick|||0000-0002-3557-0236 Tosatto, Silvio|||0000-0003-4525-7793 Ventura, Salvador|||0000-0002-9652-6351 |
| author2_role |
author author author author author author |
| dc.subject.none.fl_str_mv |
Prion-like proteins Disease Protein-protein interaction Protein aggregation Amyloid Bioinformatics |
| topic |
Prion-like proteins Disease Protein-protein interaction Protein aggregation Amyloid Bioinformatics |
| 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 |
2 2019-01-01 2019 2019-01-01 |
| dc.type.none.fl_str_mv |
Article http://purl.org/coar/resource_type/c_6501 VoR http://purl.org/coar/version/c_970fb48d4fbd8a85 |
| dc.type.openaire.fl_str_mv |
info:eu-repo/semantics/article |
| format |
article |
| dc.identifier.none.fl_str_mv |
https://ddd.uab.cat/record/223543 https://dx.doi.org/urn:doi:10.3389/fphys.2019.00314 |
| url |
https://ddd.uab.cat/record/223543 https://dx.doi.org/urn:doi:10.3389/fphys.2019.00314 |
| dc.language.none.fl_str_mv |
Inglés eng |
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Inglés |
| language |
eng |
| dc.relation.none.fl_str_mv |
European Commission https://doi.org/10.13039/501100000780 614944 Agencia Estatal de Investigación https://doi.org/10.13039/501100011033 BIO2016-78310-R Agencia Estatal de Investigación https://doi.org/10.13039/501100011033 BIO2016-77038-R |
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open access http://purl.org/coar/access_right/c_abf2 https://creativecommons.org/licenses/by/4.0/ |
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info:eu-repo/semantics/openAccess |
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open access http://purl.org/coar/access_right/c_abf2 https://creativecommons.org/licenses/by/4.0/ |
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openAccess |
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application/pdf |
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reponame:Dipòsit Digital de Documents de la UAB instname:Universitat Autònoma de Barcelona |
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Universitat Autònoma de Barcelona |
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Dipòsit Digital de Documents de la UAB |
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Dipòsit Digital de Documents de la UAB |
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