Features of Distribution of the Allelic Variant of the OAS1 Gene Associated with Severe Form of the Coronavirus Infection in the Russian and Global Populations
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Biochemistry, Genetics and Molecular Biology,General Medicine
Link
https://link.springer.com/content/pdf/10.1007/s10517-024-05994-4.pdf
Reference15 articles.
1. Schwartz SL, Park EN, Vachon VK, Danzy S, Lowen AC, Conn GL. Human OAS1 activation is highly dependent on both RNA sequence and context of activating RNA motifs. Nucleic Acids Res. 2020;48(13):7520-7531. doi: https://doi.org/10.1093/nar/gkaa513
2. Justesen J, Hartmann R, Kjeldgaard NO. Gene structure and function of the 2’-5’-oligoadenylate synthetase family. Cell. Mol. Life Sci. 2000;57(11):1593-1612. doi: https://doi.org/10.1007/pl00000644
3. Bonnevie-Nielsen V, Field LL, Lu S, Zheng DJ, Li M, Martensen PM, Nielsen TB, Beck-Nielsen H, Lau YL, Pociot F. Variation in antiviral 2’,5’-oligoadenylate synthetase (2’5’AS) enzyme activity is controlled by a single-nucleotide polymorphism at a splice-acceptor site in the OAS1 gene. Am. J. Hum. Genet. 2005;76(4):623-633. doi: https://doi.org/10.1086/429391
4. Kjær KH, Pahus J, Hansen MF, Poulsen JB, Christensen EI, Justesen J, Martensen PM. Mitochondrial localization of the OAS1 p46 isoform associated with a common single nucleotide polymorphism. BMC Cell Biol. 2014;15:33. doi: https://doi.org/10.1186/1471-2121-15-33
5. Zhao Y, Kang H, Ji Y, Chen X. Evaluate the relationship between polymorphisms of OAS1 gene and susceptibility to chronic hepatitis C with high resolution melting analysis. Clin. Exp. Med. 2013;13(3):171-176. doi: https://doi.org/10.1007/s10238-012-0193-6
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