4.7 Review

Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases

期刊

出版社

NATURE PUBLISHING GROUP
DOI: 10.1038/emm.2014.110

关键词

-

资金

  1. Global Research Laboratory Program of the National Research Foundation (NRF) - Ministry of Science, ICT and Future Planning (MEST) [K20705000006-12A0500-00610]
  2. Bio and Medical Technology Development Program of the National Research Foundation (NRF) - Ministry of Science, ICT and Future Planning (MEST) [2012028272]
  3. Korea Health Technology R&D Project through the Korea Health Industry Development Institute (KHIDI) - Ministry of Health and Welfare, Republic of Korea [HI13C08470200]

向作者/读者索取更多资源

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.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.7
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据