ReviewBiophysical reviews2022
Structural organization, evolution, and distribution of viral pyrimidine dimer-DNA glycosylases.
Review in Biophysical reviews, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DNA glycosylases are DNA repair enzymes capable of removing damaged nitrogenous bases, including those formed as a result of UV irradiation with sunlight (approximately 300-400 нм). DNA glycosylases are common not only among bacteria, archaea, and eukaryotes, but some groups of viruses can also encode them. The best-known viral glycosylase is endonuclease V (DenV, Pdg-T4) of Escherichia virus T4, the main substrate of which is cyclobutane pyrimidine dimers. DenV is isolated separately from other large families of glycosylases; it is quite common in nature and has homologs in a number of other viruses and even bacteria. However, the ways of its origin are poorly understood. The best-known DenV homolog is the glycosylase of Chlorella virus strain, PBCV-1 (Cv-pdg). This review contains the main known data on the structure and mechanism of operation of DenV and its homologs. The issues of biological importance and distribution of the enzyme and its homologs among viruses are considered and supplemented separately. Supplementary Information: The online version contains supplementary material available at 10.1007/s12551-022-00972-4.
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