Your browser doesn't support javascript.
loading
Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases
Experimental & Molecular Medicine ; : e144-2015.
Article in English | WPRIM | ID: wpr-57305
ABSTRACT
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.
Subject(s)
Full text: Available Index: WPRIM (Western Pacific) Main subject: 2',5'-Oligoadenylate Synthetase / Biomarkers / Signal Transduction / Multigene Family / Genetic Predisposition to Disease / Polymorphism, Single Nucleotide / Disease Susceptibility / Endoribonucleases Limits: Animals / Humans Language: English Journal: Experimental & Molecular Medicine Year: 2015 Type: Article

Similar

MEDLINE

...
LILACS

LIS

Full text: Available Index: WPRIM (Western Pacific) Main subject: 2',5'-Oligoadenylate Synthetase / Biomarkers / Signal Transduction / Multigene Family / Genetic Predisposition to Disease / Polymorphism, Single Nucleotide / Disease Susceptibility / Endoribonucleases Limits: Animals / Humans Language: English Journal: Experimental & Molecular Medicine Year: 2015 Type: Article