The DOI matches its Crossref record; 56 of the 56 references it cites were found in a registry or an index.
The Oligoadenylate Synthetase Family: An Ancient Protein Family with Multiple Antiviral Activities
Abstract
The 2'-5' oligoadenylate synthetases (OAS) are interferon-induced antiviral enzymes that recognize virally produced dsRNA and initiate RNA destabilization through activation of RNase L within infected cells. However, recent evidence points toward several RNase L-independent pathways, through which members of the OAS family can exert antiviral activity. The crystal structure of OAS led to a novel insight into the catalytic mechanism, and revealed a remarkable similarity between OAS, Polyadenosine polymerase, and the class I CCA-adding enzyme from Archeoglobus fulgidus. This, combined with a variety of bioinformatic data, leads to the definition of a superfamily of template independent polymerases and proved that the OAS family are ancient proteins, which probably arose as early as the beginning of metazoan evolution.
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Cites
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An attempt to unify the structure of polymerases
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Interferon-mediated protein kinase and low-molecular-weight inhibitor of protein synthesis
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Interferon action may be mediated by activation of a nuclease by pppA2′p5′A2′p5′A
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A Unified Polymerase Mechanism for Nonhomologous DNA and RNA Polymerases
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Cited by
CGAS produces a 2′-5′-linked cyclic dinucleotide second messenger that activates STING.
Ablasser, A., Goldeck, M., Cavlar, T., Deimling, T., Witte, G., Röhl, I., Hopfner, K.-P., Ludwig, J., & Hornung, V. (2013) · Nature · doi:10.1038/nature12306 · Cited by 1,695
Interferon-Stimulated Genes: What Do They All Do?
Schoggins, J. W. (2019) · Annual Review of Virology · doi:10.1146/annurev-virology-092818-015756 · Cited by 1,036
Double-Stranded RNA Sensors and Modulators in Innate Immunity
Hur, S. (2019) · Annual Review of Immunology · doi:10.1146/annurev-immunol-042718-041356 · Cited by 420
Translation inhibition and stress granules in the antiviral immune response
McCormick, C., & Khaperskyy, D. A. (2017) · Nature Reviews Immunology · doi:10.1038/nri.2017.63 · Cited by 353
Bradley, K. C., Finsterbusch, K., Schnepf, D., Crotta, S., Llorian, M., Davidson, S., Fuchs, S. Y., Staeheli, P., & Wack, A. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.05.105 · Cited by 313
Metadata
- Authors
- Kristiansen, H., Gad, H. H., Eskildsen-Larsen, S., Despres, P., & Hartmann, R.
- Venue
- Journal of Interferon & Cytokine Research
- Publisher
- SAGE Publications
- Published
- 2011-01
- Volume
- 31
- Issue
- 1
- Pages
- 41-47
- ISSN
- 1079-9907 (ISSN-L)
- 1557-7465
- OpenAlex
- W2044635447
- Cited by
- 310
- References
- 56
- FWCI
- 3.75
- Type
- journal article
- Language
- en
- Open access
- closed
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- Kristiansen, H., Gad, H. H., Eskildsen-Larsen, S., Despres, P., & Hartmann, R. (2011). The Oligoadenylate Synthetase Family: An Ancient Protein Family with Multiple Antiviral Activities. Journal of Interferon & Cytokine Research. https://doi.org/10.1089/jir.2010.0107
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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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