"Cytidine 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 enzyme that catalyzes the deamination of cytidine, forming uridine. EC 3.5.4.5.
| Descriptor ID |
D003564
|
| MeSH Number(s) |
D08.811.277.151.486.250
|
| Concept/Terms |
Cytidine Deaminase- Cytidine Deaminase
- Deaminase, Cytidine
- Cytidine Aminohydrolase
- Aminohydrolase, Cytidine
|
Below are MeSH descriptors whose meaning is more general than "Cytidine Deaminase".
Below are MeSH descriptors whose meaning is more specific than "Cytidine Deaminase".
This graph shows the total number of publications written about "Cytidine Deaminase" by people in this website by year, and whether "Cytidine Deaminase" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2007 | 1 | 0 | 1 |
| 2010 | 0 | 1 | 1 |
| 2014 | 0 | 1 | 1 |
| 2015 | 1 | 0 | 1 |
| 2017 | 1 | 0 | 1 |
| 2018 | 1 | 0 | 1 |
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Below are the most recent publications written about "Cytidine Deaminase" by people in Profiles.
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Silvas TV, Hou S, Myint W, Nalivaika E, Somasundaran M, Kelch BA, Matsuo H, Kurt Yilmaz N, Schiffer CA. Substrate sequence selectivity of APOBEC3A implicates intra-DNA interactions. Sci Rep. 2018 05 14; 8(1):7511.
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Bou Samra E, Buhagiar-Labarch?de G, Machon C, Guitton J, Onclercq-Delic R, Green MR, Alibert O, Gazin C, Veaute X, Amor-Gu?ret M. A role for Tau protein in maintaining ribosomal DNA stability and cytidine deaminase-deficient cell survival. Nat Commun. 2017 09 25; 8(1):693.
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Kouno T, Silvas TV, Hilbert BJ, Shandilya SMD, Bohn MF, Kelch BA, Royer WE, Somasundaran M, Kurt Yilmaz N, Matsuo H, Schiffer CA. Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity. Nat Commun. 2017 04 28; 8:15024.
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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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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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Khair L, Baker RE, Linehan EK, Schrader CE, Stavnezer J. Nbs1 ChIP-Seq Identifies Off-Target DNA Double-Strand Breaks Induced by AID in Activated Splenic B Cells. PLoS Genet. 2015 Aug; 11(8):e1005438.
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Bohn MF, Shandilya SMD, Silvas TV, Nalivaika EA, Kouno T, Kelch BA, Ryder SP, Kurt-Yilmaz N, Somasundaran M, Schiffer CA. The ssDNA Mutator APOBEC3A Is Regulated by Cooperative Dimerization. Structure. 2015 May 05; 23(5):903-911.
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Shandilya SM, Bohn MF, Schiffer CA. A computational analysis of the structural determinants of APOBEC3's catalytic activity and vulnerability to HIV-1 Vif. Virology. 2014 Dec; 471-473:105-16.
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Maul RW, Cao Z, Venkataraman L, Giorgetti CA, Press JL, Denizot Y, Du H, Sen R, Gearhart PJ. Spt5 accumulation at variable genes distinguishes somatic hypermutation in germinal center B cells from ex vivo-activated cells. J Exp Med. 2014 Oct 20; 211(11):2297-306.
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Ucher AJ, Ranjit S, Kadungure T, Linehan EK, Khair L, Xie E, Limauro J, Rauch KS, Schrader CE, Stavnezer J. Mismatch repair proteins and AID activity are required for the dominant negative function of C-terminally deleted AID in class switching. J Immunol. 2014 Aug 01; 193(3):1440-50.