ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
Structure of the uracil complex of Vaccinia virus uracil DNA glycosylase.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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
6 citing papers in PubMed, 7 citations in OpenAlex.
- Correlated Target Search by Vaccinia Virus Uracil-DNA Glycosylase, a DNA Repair Enzyme and a Processivity Factor of Viral Replication Machinery.International journal of molecular sciences · 2023Article
- The vaccinia virus DNA polymerase and its processivity factor.Virus research · 2017Review
- Poxvirus uracil-DNA glycosylase-An unusual member of the family I uracil-DNA glycosylases.Protein science : a publication of the Protein Society · 2016Review
- Crystal Structure of the Vaccinia Virus Uracil-DNA Glycosylase in Complex with DNA.The Journal of biological chemistry · 2015Article
- Binding of undamaged double stranded DNA to vaccinia virus uracil-DNA Glycosylase.BMC structural biology · 2015Article
- Uracil-DNA glycosylases-structural and functional perspectives on an essential family of DNA repair enzymes.Protein science : a publication of the Protein Society · 2014Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Poxvirus uracil DNA glycosylases are the most diverse members of the family I uracil DNA glycosylases (UNGs). The crystal structure of the uracil complex of Vaccinia virus uracil DNA glycosylase (D4) was determined at 2.03 Å resolution. One uracil molecule was located in the active-site pocket in each of the 12 noncrystallographic symmetry-related D4 subunits. Although the UNGs of the poxviruses (including D4) feature significant differences in the characteristic motifs designated for uracil recognition and in the base-excision mechanism, the architecture of the active-site pocket in D4 is very similar to that in UNGs of other organisms. Overall, the interactions of the bound uracil with the active-site residues are also similar to the interactions previously observed in the structures of human and Escherichia coli UNG.
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Registered trials
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