Ontology highlight
ABSTRACT:
SUBMITTER: Ibsen MS
PROVIDER: S-EPMC4446440 | biostudies-literature | 2015 May
REPOSITORIES: biostudies-literature
Ibsen Mikkel Søes MS Gad Hans Henrik HH Andersen Line Lykke LL Hornung Veit V Julkunen Ilkka I Sarkar Saumendra N SN Hartmann Rune R
Nucleic acids research 20150429 10
The oligoadenylate synthetase (OAS) enzymes are cytoplasmic dsRNA sensors belonging to the antiviral innate immune system. Upon binding to viral dsRNA, the OAS enzymes synthesize 2'-5' linked oligoadenylates (2-5As) that initiate an RNA decay pathway to impair viral replication. The human OAS-like (OASL) protein, however, does not harbor the catalytic activity required for synthesizing 2-5As and differs from the other human OAS family members by having two C-terminal ubiquitin-like domains. In s ...[more]