Evidence map›Paper›PMID 11557818›Full record

ArticleNucleic acids research2001

A kinetic analysis of substrate recognition by uracil-DNA glycosylase from herpes simplex virus type 1.

S R Bellamy, G S Baldwin

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.9field-weighted citation impact, top 25% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Structural basis for the recognition and cleavage of abasic DNA in Neisseria meningitidis.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Suppressed catalytic activity of base excision repair enzymes on rotationally positioned uracil in nucleosomes.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  16. Review
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

S R BellamyImperial College of Science, Technology and Medicine, Department of Biological Sciences, Sir Alexander Fleming Building, Imperial College Road, London SW7 2AZ, UK.
G S Baldwin
Imperial College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Uracil-DNA glycosylase (UDG) is responsible for the removal of uracil from DNA. It has previously been demonstrated that UDG exhibits some sequence dependence in its activity, although this has not been well characterised. This study has investigated the sequence-dependent activity of UDG from herpes simplex virus type-1 (HSV-1). A more detailed analysis has been possible by using both kinetic and binding assays with a variety of different oligonucleotide substrates. The target uracil has been placed in substrates with either A-T-rich or G-C-rich flanking sequences and analyses have been performed on both the single- and double-stranded forms of each substrate. In the latter the uracil has been placed in both a U.A base pair and a U.G mismatch. It is observed that the sequences flanking the target uracil have a greater effect on UDG activity than the partner base of the uracil. Furthermore, the sequence context effects extend to single-stranded DNA. Systematic examination of the kinetics and binding of UDG with these different substrates has enabled us to examine the origin of the sequence preferences. We conclude that the damage recognition step in the HSV-1 UDG reaction pathway is modulated by local DNA sequence.

Indexed as

DNA Glycosylases2-AminopurineAmino Acid SubstitutionBase SequenceFluorescenceHerpesvirus 1, HumanKineticsMutationN-Glycosyl HydrolasesOligonucleotidesProtein BindingSubstrate SpecificityUracilUracil-DNA Glycosidase2-AminopurineDNA GlycosylasesN-Glycosyl HydrolasesOligonucleotidesUracilUracil-DNA Glycosidase

Identifiers

PMID11557818
PMCPMC55908
OpenAlexW2116752163

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.