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The APOBEC Protein Family: United by Structure, Divergent in Function
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APOBEC proteins play an important role in immune responses against DNA and RNA viral pathogens.
“Since APOBEC proteins play an important role in immune responses against DNA and RNA viral pathogens (Refs.19–22 and references therein), we also investigated the possible effects of the three APOBECs on SARS-CoV-2 replication and progeny production in our experimental system (Fig. 5A).”
From The roles of APOBEC-mediated RNA editing in SARS-CoV-2 mutations, replication and fitness (2022) · cites this paper as [20]
The APOBEC proteins are a family of cytosine deaminases that can deaminate cytosine to uracil (C-to-U) in single-stranded nucleic acids and function in innate and adaptive immune responses to viral pathogens.
“The APOBEC proteins are a family of cytosine deaminases that can deaminate cytosine to uracil (C-to-U) in single-stranded nucleic acids and function in a variety of biological processes, including innate and adaptive immune responses to viral pathogens (Refs.19–22 and references therein).”
From The roles of APOBEC-mediated RNA editing in SARS-CoV-2 mutations, replication and fitness (2022) · cites this paper as [20]
The pro-viral effect of A3A contrasts with the known anti-viral effect of APOBECs.
“These pro-viral effect of A3A contrast to the known anti-viral effect of APOBECs19–22.”
From The roles of APOBEC-mediated RNA editing in SARS-CoV-2 mutations, replication and fitness (2022) · cites this paper as [20]
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Ancient adaptive evolution of the primate antiviral DNA-editing enzyme APOBEC3G
Sawyer, S. L., Emerman, M., & Malik, H. S. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020275 · Cited by 485
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- Muckenfuss, 2006, APOBEC3 proteins inhibit human LINE-1 retrotransposition, J. Biol. Chem., 281, 22161, 10.1074/jbc.M601716200 · DOI
- Stenglein, 2006, APOBEC3B and APOBEC3F inhibit L1 retrotransposition by a DNA deamination-independent mechanism, J. Biol. Chem., 281, 16837, 10.1074/jbc.M602367200 · DOI
- Chiu, 2006, High-molecular-mass APOBEC3G complexes restrict Alu retrotransposition, Proc. Natl. Acad. Sci. U. S. A., 103, 15588, 10.1073/pnas.0604524103 · DOI
- Hulme, 2007, Selective inhibition of Alu retrotransposition by APOBEC3G, Gene, 390, 199, 10.1016/j.gene.2006.08.032 · DOI
- Esnault, 2005, APOBEC3G cytidine deaminase inhibits retrotransposition of endogenous retroviruses, Nature, 433, 430, 10.1038/nature03238 · DOI
- Letko, 2013, Vif proteins from diverse primate lentiviral lineages use the same binding site in APOBEC3G J, Virol., 87, 11861, 10.1128/JVI.01944-13 · DOI
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Continuous evolution of base editors with expanded target compatibility and improved activity
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Long-range single-molecule mapping of chromatin accessibility in eukaryotes
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The roles of APOBEC-mediated RNA editing in SARS-CoV-2 mutations, replication and fitness
Kim, K., Calabrese, P., Wang, S., Qin, C., Rao, Y., Feng, P., & Chen, X. S. (2022) · Scientific Reports · doi:10.1038/s41598-022-19067-x · Cited by 115
Metadata
- Authors
- Salter, J. D., Bennett, R. P., & Smith, H. C.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2016-07
- Volume
- 41
- Issue
- 7
- Pages
- 578-594
- ISSN
- 0968-0004
- PMC
- PMC4930407
- Cited by
- 408
- References
- 1
- Language
- en
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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