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Article

Function of ubiquitin-like domain of chicken 2'-5'-oligoadenylate synthetase in conformational stability.

Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research - 1 Nov 2003

Tatsumi Rie, Sekiya Sadanori, Nakanishi Ryoko, Mizutani Makoto, Kojima Shin-Ichi, Sokawa Yoshihiro

Abstract excerpt

2'-5'-Oligoadenylate synthetase (OAS), an interferon (IFN) induced enzyme, synthesizes 2'-5'-oligoadenylate (2-5A) from ATP when activated by dsRNA. Chicken OAS (ChOAS) has a ubiquitin-like (UbL) domain of two consecutive sequences (UbL1 and UbL2) at its carboxyl-terminus. The OAS gene has at least two alleles, OAS*A and OAS*B. OAS-A is the wild-type (wt) and OAS-B is a mutant deleted of a highly hydrophobic...

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PMID: 14651781
DOI: 10.1089/107999003322558809

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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