Evidence map›Paper›PMID 24841533›Full record

ArticleJournal of the American Chemical Society2014

A zinc linchpin motif in the MUTYH glycosylase interdomain connector is required for efficient repair of DNA damage.

Lisa M Engstrom, Megan K Brinkmeyer, Yang Ha, Alan G Raetz, Britt Hedman, Keith O Hodgson, Edward I Solomon, Sheila S David

Open access · bronzeAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

22 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Noncatalytic Domains in DNA Glycosylases.International journal of molecular sciences · 2022
    Review
  8. Review
  9. Article
  10. Article
  11. MUTYH: Not just polyposis.World journal of clinical oncology · 2020
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Base Excision Repair of NBiochemistry · 2016
    Article
  20. Article
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 1 country.

Lisa M EngstromDepartment of Chemistry, University of California, Davis , One Shields Avenue, Davis, California 95616, United States.
Megan K Brinkmeyer
Yang Ha
Alan G Raetz
Britt Hedman
Keith O Hodgson
Edward I Solomon
Sheila S David
University of California, Davis · USStanford Synchrotron Radiation Lightsource · USStanford University · US

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
ENVIRONMENTAL TOXICOLOGYT32ES007059 · NIEHS · UNIVERSITY OF CALIFORNIA DAVIS · PI Laura S Van Winkle · 1985 to 2026
$7.9M
RECOGNITION AND REPAIR OF MISMATCHED DNA BY MUTYR01CA067985 · NCI · UNIVERSITY OF UTAH · PI DAVID, SHEILA SUE · 2000 to 2025
$5.6M
NCI NIH HHS CA069785NCI NIH HHS R01 CA067985NIEHS NIH HHS T32 ES007058NIEHS NIH HHS T32 ES007059NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41GM103393
6 · The paper itself

Abstract

Mammalian MutY glycosylases have a unique architecture that features an interdomain connector (IDC) that joins the catalytic N-terminal domain and 8-oxoguanine (OG) recognition C-terminal domain. The IDC has been shown to be a hub for interactions with protein partners involved in coordinating downstream repair events and signaling apoptosis. Herein, a previously unidentified zinc ion and its coordination by three Cys residues of the IDC region of eukaryotic MutY organisms were characterized by mutagenesis, ICP-MS, and EXAFS. In vitro kinetics and cellular assays on WT and Cys to Ser mutants have revealed an important function for zinc coordination on overall protein stability, iron-sulfur cluster insertion, and ability to mediate DNA damage repair. We propose that this "zinc linchpin" motif serves to structurally organize the IDC and coordinate the damage recognition and base excision functions of the C- and N-terminal domains.

Indexed as

Amino Acid SequenceAnimalsCysteineDNA DamageDNA GlycosylasesDNA Repair EnzymesHumansKineticsMiceModels, MolecularMolecular Sequence DataMutagenesisProtein ConformationSerineZinc CompoundsCysteineDNA GlycosylasesDNA Repair EnzymesmutY adenine glycosylaseSerineZinc Compounds

Identifiers

PMID24841533
PMCPMC4063174
OpenAlexW2027416721

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.