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....
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2019-03-01
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| Series: | Frontiers in Physiology |
| Subjects: | |
| Online Access: | https://www.frontiersin.org/article/10.3389/fphys.2019.00314/full |
| _version_ | 1811235647608848384 |
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| author | Valentin Iglesias Lisanna Paladin Teresa Juan-Blanco Irantzu Pallarès Patrick Aloy Patrick Aloy Silvio C. E. Tosatto Silvio C. E. Tosatto Salvador Ventura |
| author_facet | Valentin Iglesias Lisanna Paladin Teresa Juan-Blanco Irantzu Pallarès Patrick Aloy Patrick Aloy Silvio C. E. Tosatto Silvio C. E. Tosatto Salvador Ventura |
| author_sort | Valentin Iglesias |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-04-12T11:55:31Z |
| format | Article |
| id | doaj.art-0b252a4eb5814790b15de127005c4d2b |
| institution | Directory Open Access Journal |
| issn | 1664-042X |
| language | English |
| last_indexed | 2024-04-12T11:55:31Z |
| publishDate | 2019-03-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Physiology |
| spelling | doaj.art-0b252a4eb5814790b15de127005c4d2b2022-12-22T03:34:01ZengFrontiers Media S.A.Frontiers in Physiology1664-042X2019-03-011010.3389/fphys.2019.00314429179In silico Characterization of Human Prion-Like Proteins: Beyond Neurological DiseasesValentin Iglesias0Lisanna Paladin1Teresa Juan-Blanco2Irantzu Pallarès3Patrick Aloy4Patrick Aloy5Silvio C. E. Tosatto6Silvio C. E. Tosatto7Salvador Ventura8Institut de Biotecnologia i de Biomedicina, Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, Barcelona, SpainDepartment of Biomedical Sciences, University of Padua, Padua, ItalyJoint IRB-BSC-CRG Program in Computational Biology, Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Barcelona, SpainInstitut de Biotecnologia i de Biomedicina, Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, Barcelona, SpainJoint IRB-BSC-CRG Program in Computational Biology, Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Barcelona, SpainInstitució Catalana de Recerca i Estudis Avançats, Barcelona, SpainDepartment of Biomedical Sciences, University of Padua, Padua, ItalyCNR Institute of Neuroscience, Padua, ItalyInstitut de Biotecnologia i de Biomedicina, Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, Barcelona, SpainPrion-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.https://www.frontiersin.org/article/10.3389/fphys.2019.00314/fullprion-like proteinsdiseaseprotein–protein interactionprotein aggregationamyloidbioinformatics |
| spellingShingle | Valentin Iglesias Lisanna Paladin Teresa Juan-Blanco Irantzu Pallarès Patrick Aloy Patrick Aloy Silvio C. E. Tosatto Silvio C. E. Tosatto Salvador Ventura In silico Characterization of Human Prion-Like Proteins: Beyond Neurological Diseases Frontiers in Physiology prion-like proteins disease protein–protein interaction protein aggregation amyloid bioinformatics |
| title | 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_short | In silico Characterization of Human Prion-Like Proteins: Beyond Neurological Diseases |
| title_sort | in silico characterization of human prion like proteins beyond neurological diseases |
| topic | prion-like proteins disease protein–protein interaction protein aggregation amyloid bioinformatics |
| url | https://www.frontiersin.org/article/10.3389/fphys.2019.00314/full |
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