"APOBEC-3G Deaminase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
An APOBEC deaminase that functions as an inhibitor of RETROVIRIDAE replication and inhibits the mobility of RETROTRANSPOSONS via deaminase-dependent and independent mechanisms. It is selective for SINGLE-STRANDED DNA and does not deaminate double-stranded DNA or single or DOUBLE-STRANDED RNA. It exhibits potent antiviral activity against VIF PROTEIN deficient HIV-1 through the creation of hypermutations in the VIRAL DNA. It also has anti-viral activity against SIMIAN IMMUNODEFICIENCY VIRUSES and HEPATITIS B VIRUS.
| Descriptor ID |
D000071480
|
| MeSH Number(s) |
D08.811.277.151.486.250.500.750
|
| Concept/Terms |
APOBEC-3G Deaminase- APOBEC-3G Deaminase
- APOBEC 3G Deaminase
- Deaminase, APOBEC-3G
- APOBEC-Related Cytidine Deaminase
- APOBEC Related Cytidine Deaminase
- Cytidine Deaminase, APOBEC-Related
- APOBEC3G Protein
- CEM15 Protein
- APOBEC3G Deaminase
- Deaminase, APOBEC3G
- APOBEC-3G Protein
- APOBEC 3G Protein
- APOBEC-Related Protein
- APOBEC Related Protein
- APOBEC-3G dC-dU Editing Enzyme
- APOBEC 3G dC dU Editing Enzyme
|
Below are MeSH descriptors whose meaning is more general than "APOBEC-3G Deaminase".
Below are MeSH descriptors whose meaning is more specific than "APOBEC-3G Deaminase".
This graph shows the total number of publications written about "APOBEC-3G Deaminase" by people in this website by year, and whether "APOBEC-3G Deaminase" was a major or minor topic of these publications.
To see the data from this visualization as text,
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2007 | 0 | 1 | 1 |
| 2008 | 0 | 1 | 1 |
| 2009 | 0 | 1 | 1 |
| 2010 | 0 | 1 | 1 |
| 2011 | 0 | 2 | 2 |
| 2012 | 0 | 1 | 1 |
| 2015 | 0 | 3 | 3 |
| 2016 | 1 | 0 | 1 |
| 2018 | 1 | 0 | 1 |
| 2019 | 1 | 0 | 1 |
| 2020 | 1 | 0 | 1 |
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Below are the most recent publications written about "APOBEC-3G Deaminase" by people in Profiles.
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Maiti A, Myint W, Delviks-Frankenberry KA, Hou S, Kanai T, Balachandran V, Sierra Rodriguez C, Tripathi R, Kurt Yilmaz N, Pathak VK, Schiffer CA, Matsuo H. Crystal Structure of a Soluble APOBEC3G Variant Suggests ssDNA to Bind in a Channel that Extends between the Two Domains. J Mol Biol. 2020 11 20; 432(23):6042-6060.
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Solomon WC, Myint W, Hou S, Kanai T, Tripathi R, Kurt Yilmaz N, Schiffer CA, Matsuo H. Mechanism for APOBEC3G catalytic exclusion of RNA and non-substrate DNA. Nucleic Acids Res. 2019 08 22; 47(14):7676-7689.
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Maiti A, Myint W, Kanai T, Delviks-Frankenberry K, Sierra Rodriguez C, Pathak VK, Schiffer CA, Matsuo H. Crystal structure of the catalytic domain of HIV-1 restriction factor APOBEC3G in complex with ssDNA. Nat Commun. 2018 06 25; 9(1):2460.
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Polevoda B, McDougall WM, Bennett RP, Salter JD, Smith HC. Structural and functional assessment of APOBEC3G macromolecular complexes. Methods. 2016 09 01; 107:10-22.
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Prabhu P, Shandilya SM, Britan-Rosich E, Nagler A, Schiffer CA, Kotler M. Inhibition of APOBEC3G activity impedes double-stranded DNA repair. FEBS J. 2016 Jan; 283(1):112-29.
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Polevoda B, McDougall WM, Tun BN, Cheung M, Salter JD, Friedman AE, Smith HC. RNA binding to APOBEC3G induces the disassembly of functional deaminase complexes by displacing single-stranded DNA substrates. Nucleic Acids Res. 2015 Oct 30; 43(19):9434-45.
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Kouno T, Luengas EM, Shigematsu M, Shandilya SM, Zhang J, Chen L, Hara M, Schiffer CA, Harris RS, Matsuo H. Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G. Nat Struct Mol Biol. 2015 Jun; 22(6):485-91.
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Li M, Shandilya SM, Carpenter MA, Rathore A, Brown WL, Perkins AL, Harki DA, Solberg J, Hook DJ, Pandey KK, Parniak MA, Johnson JR, Krogan NJ, Somasundaran M, Ali A, Schiffer CA, Harris RS. First-in-class small molecule inhibitors of the single-strand DNA cytosine deaminase APOBEC3G. ACS Chem Biol. 2012 Mar 16; 7(3):506-17.
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McDougall WM, Smith HC. Direct evidence that RNA inhibits APOBEC3G ssDNA cytidine deaminase activity. Biochem Biophys Res Commun. 2011 Sep 09; 412(4):612-7.
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McDougall WM, Okany C, Smith HC. Deaminase activity on single-stranded DNA (ssDNA) occurs in vitro when APOBEC3G cytidine deaminase forms homotetramers and higher-order complexes. J Biol Chem. 2011 Sep 02; 286(35):30655-30661.