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Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases
The study of antiviral pathways to reveal methods for the effective response and clearance of virus is closely related to understanding interferon (IFN) signaling and its downstream target genes, IFN-stimulated genes. One of the key antiviral factors induced by IFNs, 2′-5′ oligoadenylate synthase (O...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4351405/ https://www.ncbi.nlm.nih.gov/pubmed/25744296 http://dx.doi.org/10.1038/emm.2014.110 |
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author | Choi, Un Yung Kang, Ji-Seon Hwang, Yune Sahng Kim, Young-Joon |
author_facet | Choi, Un Yung Kang, Ji-Seon Hwang, Yune Sahng Kim, Young-Joon |
author_sort | Choi, Un Yung |
collection | PubMed |
description | The study of antiviral pathways to reveal methods for the effective response and clearance of virus is closely related to understanding interferon (IFN) signaling and its downstream target genes, IFN-stimulated genes. One of the key antiviral factors induced by IFNs, 2′-5′ oligoadenylate synthase (OAS), is a well-known molecule that regulates the early phase of viral infection by degrading viral RNA in combination with RNase L, resulting in the inhibition of viral replication. In this review, we describe OAS family proteins from a different point of view from that of previous reviews. We discuss not only RNase L-dependent (canonical) and -independent (noncanonical) pathways but also the possibility of the OAS family members as biomarkers for various diseases and clues to non-immunological functions based on recent studies. In particular, we focus on OASL, a member of the OAS family that is relatively less well understood than the other members. We will explain its anti- and pro-viral dual roles as well as the diseases related to single-nucleotide polymorphisms in the corresponding gene. |
format | Online Article Text |
id | pubmed-4351405 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-43514052015-03-10 Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases Choi, Un Yung Kang, Ji-Seon Hwang, Yune Sahng Kim, Young-Joon Exp Mol Med Review The study of antiviral pathways to reveal methods for the effective response and clearance of virus is closely related to understanding interferon (IFN) signaling and its downstream target genes, IFN-stimulated genes. One of the key antiviral factors induced by IFNs, 2′-5′ oligoadenylate synthase (OAS), is a well-known molecule that regulates the early phase of viral infection by degrading viral RNA in combination with RNase L, resulting in the inhibition of viral replication. In this review, we describe OAS family proteins from a different point of view from that of previous reviews. We discuss not only RNase L-dependent (canonical) and -independent (noncanonical) pathways but also the possibility of the OAS family members as biomarkers for various diseases and clues to non-immunological functions based on recent studies. In particular, we focus on OASL, a member of the OAS family that is relatively less well understood than the other members. We will explain its anti- and pro-viral dual roles as well as the diseases related to single-nucleotide polymorphisms in the corresponding gene. Nature Publishing Group 2015-03 2015-03-06 /pmc/articles/PMC4351405/ /pubmed/25744296 http://dx.doi.org/10.1038/emm.2014.110 Text en Copyright © 2014 KSBMB. http://creativecommons.org/licenses/by/3.0/ This work is licensed under a Creative Commons Attribution 3.0 Unported License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/3.0/ |
spellingShingle | Review Choi, Un Yung Kang, Ji-Seon Hwang, Yune Sahng Kim, Young-Joon Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases |
title | Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases |
title_full | Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases |
title_fullStr | Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases |
title_full_unstemmed | Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases |
title_short | Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases |
title_sort | oligoadenylate synthase-like (oasl) proteins: dual functions and associations with diseases |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4351405/ https://www.ncbi.nlm.nih.gov/pubmed/25744296 http://dx.doi.org/10.1038/emm.2014.110 |
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