Evidence map›Paper›PMID 22219368›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Strandwise translocation of a DNA glycosylase on undamaged DNA.

Yan Qi, Kwangho Nam, Marie C Spong, Anirban Banerjee, Rou-Jia Sung, Michael Zhang, Martin Karplus, Gregory L Verdine

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Revealing atomic-scale molecular diffusion of a plant-transcription factor WRKY domain protein along DNA.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Visualizing the Search for Radiation-damaged DNA Bases in Real Time.Radiation physics and chemistry (Oxford, England : 1993) · 2016
    Article
  10. Article
  11. Article
  12. Article
  13. Two glycosylase families diffusively scan DNA using a wedge residue to probe for and identify oxidatively damaged bases.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  14. DNA glycosylases search for and remove oxidized DNA bases.Environmental and molecular mutagenesis · 2013
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 3 countries.

Yan QiProgram in Biophysics, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
Kwangho Nam
Marie C Spong
Anirban Banerjee
Rou-Jia Sung
Michael Zhang
Martin Karplus
Gregory L Verdine
Harvard University · USInstitute for Stem Cell Biology and Regenerative Medicine · INInstitut de Science et d'Ingénierie Supramoléculaires · FR

Funding

FUNCTIONALLY TETHERED OLIGONUCLEOTIDESR01GM044853 · NIGMS · HARVARD UNIVERSITY · PI VERDINE, GREGORY LAWRENCE · 1990 to 2011
$5.1M
Structure and Mechanism of Base-Excision DNA RepairR01CA100742 · NCI · HARVARD UNIVERSITY · PI VERDINE, GREGORY LAWRENCE · 2003 to 2013
$3.9M
THEORETICAL SUTDIES OF BIOMOLECULESR01GM030804 · NIGMS · HARVARD UNIVERSITY · PI KARPLUS, MARTIN · 1985 to 2011
$2.7M
THEORETICAL STUDIES OF BIOMOLECULESR37GM030804 · NIGMS · HARVARD UNIVERSITY · PI KARPLUS, MARTIN · 1988 to 1997
–
Howard Hughes Medical InstituteNCI NIH HHS R01 CA100742NIGMS NIH HHS GM030804NIGMS NIH HHS GM044853NIGMS NIH HHS R01 GM030804NIGMS NIH HHS R01 GM044853
6 · The paper itself

Abstract

Base excision repair of genotoxic nucleobase lesions in the genome is critically dependent upon the ability of DNA glycosylases to locate rare sites of damage embedded in a vast excess of undamaged DNA, using only thermal energy to fuel the search process. Considerable interest surrounds the question of how DNA glycosylases translocate efficiently along DNA while maintaining their vigilance for target damaged sites. Here, we report the observation of strandwise translocation of 8-oxoguanine DNA glycosylase, MutM, along undamaged DNA. In these complexes, the protein is observed to translocate by one nucleotide on one strand while remaining untranslocated on the complementary strand. We further report that alterations of single base-pairs or a single amino acid substitution (R112A) can induce strandwise translocation. Molecular dynamics simulations confirm that MutM can translocate along DNA in a strandwise fashion. These observations reveal a previously unobserved mode of movement for a DNA-binding protein along the surface of DNA.

Indexed as

Models, MolecularCrystallizationDNADNA-Formamidopyrimidine GlycosylaseDNA RepairEscherichia coliGeobacillus stearothermophilusMolecular Dynamics SimulationMutagenesis, Site-DirectedNucleic Acid ConformationProtein ConformationProtein TransportSynchrotronsTranslocation, GeneticX-Ray DiffractionDNADNA-Formamidopyrimidine Glycosylase

Identifiers

PMID22219368
PMCPMC3268267
OpenAlexW2136777969

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.