Evidence map›Paper›PMID 24500713›Full record

ArticleThe Journal of biological chemistry2014

Evidence that the DNA endonuclease ARTEMIS also has intrinsic 5'-exonuclease activity.

Sicong Li, Howard H Chang, Doris Niewolik, Michael P Hedrick, Anthony B Pinkerton, Christian A Hassig, Klaus Schwarz, Michael R Lieber

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

37 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Structure and Function of SNM1 Family Nucleases.Advances in experimental medicine and biology · 2023
    Review
  10. Article
  11. Critical DNA damaging pathways in tumorigenesis.Seminars in cancer biology · 2022
    Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
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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 2 countries.

Sicong LiFrom the Departments of Pathology, Biochemistry and Molecular Biology, Biological Sciences, and Molecular Microbiology and Immunology, University of Southern California Keck School of Medicine, Norris Comprehensive Cancer Center, Los Angeles, California 90089-9176.
Howard H Chang
Doris Niewolik
Michael P Hedrick
Anthony B Pinkerton
Christian A Hassig
Klaus Schwarz
Michael R Lieber
Sanford Burnham Prebys Medical Discovery Institute · USUniversity of Southern California · USUniversity Hospital Ulm · DE

Funding

MECHANISM AND REGULATION OF NONHOMOLOGOUS DNA ENDJOININGR01CA100504 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LIEBER, MICHAEL R · 2003 to 2021
$5.0M
HUMAN VDJ RECOMBINASE IN NEOPLASTIC AND PRIMARY CELLSR01CA051105 · NCI · WASHINGTON UNIVERSITY · PI LIEBER, MICHAEL R · 1990 to 2004
$1.6M
NCI NIH HHS R01 CA051105NCI NIH HHS R01 CA100504NCI NIH HHS R01 CA51105
6 · The paper itself

Abstract

ARTEMIS is a member of the metallo-β-lactamase protein family. ARTEMIS has endonuclease activity at DNA hairpins and at 5'- and 3'-DNA overhangs of duplex DNA, and this endonucleolytic activity is dependent upon DNA-PKcs. There has been uncertainty about whether ARTEMIS also has 5'-exonuclease activity on single-stranded DNA and 5'-overhangs, because this 5'-exonuclease is not dependent upon DNA-PKcs. Here, we show that the 5'-exonuclease and the endonuclease activities co-purify. Second, we show that a point mutant of ARTEMIS at a putative active site residue (H115A) markedly reduces both the endonuclease activity and the 5'-exonuclease activity. Third, divalent cation effects on the 5'-exonuclease and the endonuclease parallel one another. Fourth, both the endonuclease activity and 5'-exonuclease activity of ARTEMIS can be blocked in parallel by small molecule inhibitors, which do not block unrelated nucleases. We conclude that the 5'-exonuclease is intrinsic to ARTEMIS, making it relevant to the role of ARTEMIS in nonhomologous DNA end joining.

Indexed as

ChromatographyCircular DichroismDeoxyribonuclease IDNADNA-Binding ProteinsDNA End-Joining RepairEndonucleasesExodeoxyribonucleasesHEK293 CellsHumansMutagenesisNuclear ProteinsNucleotidasesOligonucleotidesPoint MutationTransfectionDCLRE1C protein, humanDeoxyribonuclease IDNADNA-Binding ProteinsEndonucleasesExodeoxyribonucleasesNuclear ProteinsNucleotidasesOligonucleotidesDNA RepairNonhomologous DNA End JoiningNucleic AcidNucleic Acid EnzymologyNucleic Acid StructureProtein DNA-Interaction

Identifiers

PMID24500713
PMCPMC3953294
OpenAlexW1973310934

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.