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The Human 2',5'-Oligoadenylate Synthetase Family: Interferon-Induced Proteins with Unique Enzymatic Properties
Abstract
2',5'-Oligoadenylate synthetase (2',5'-OAS) was discovered and characterized as an interferon (IFN)-induced enzyme that in the presence of double-stranded (ds) RNA converts ATP into 2',5'-linked oligomers of adenosine with the general formula pppA(2'p'A)n, n > or = 1. The product is pppG2'p5'G when GTP is used as a substrate. Now, 20 years later, this activity is attributed to several well-characterized, homologous, and IFN-induced proteins in human cells. Three distinct forms of 2',5'-OAS exist, small, medium, and large, which contain 1, 2, and 3 OAS units, respectively, and are encoded by distinct genes clustered on the 2',5'-OAS locus on human chromosome 12. Recently, other IFN-induced proteins homologous to the OAS unit but devoid of the typical 2',5'-OAS catalytic activity have been described. These OAS-related proteins are encoded by a gene located at the proximity of the 2',5'-OAS locus. These findings illustrate the apparent structural and functional complexity of the human 2',5'-OAS family.
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Cited by
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Metadata
- Authors
- Rebouillat, D., & Hovanessian, A. G.
- Venue
- Journal of Interferon & Cytokine Research
- Publisher
- SAGE Publications
- Published
- 1999-04
- Volume
- 19
- Issue
- 4
- Pages
- 295-308
- ISSN
- 1079-9907 (ISSN-L)
- 1557-7465
- OpenAlex
- W2120696122
- Cited by
- 232
- References
- 0
- FWCI
- 5.02
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: The Human 2',5'-Oligoadenylate Synthetase Family: Interferon-Induced Proteins with Unique Enzymatic Properties. https://app.cochat.ai/papers/10.1089/107999099313992
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- Rebouillat, D., & Hovanessian, A. G. (1999). The Human 2',5'-Oligoadenylate Synthetase Family: Interferon-Induced Proteins with Unique Enzymatic Properties. Journal of Interferon & Cytokine Research. https://doi.org/10.1089/107999099313992
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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