Evidence map›Paper›PMID 24754999›Full record

ReviewDNA repair2014

The cutting edges in DNA repair, licensing, and fidelity: DNA and RNA repair nucleases sculpt DNA to measure twice, cut once.

Susan E Tsutakawa, Julien Lafrance-Vanasse, John A Tainer

Abstract readReview
In one paragraph

Review in DNA repair, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

61 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Recurrent DNA nicks drive massive expansions of (GAA)Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Review
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1 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Susan E TsutakawaLife Science Division, 1 Cyclotron Road, Berkeley, CA 94720, USA.
Julien Lafrance-VanasseLife Science Division, 1 Cyclotron Road, Berkeley, CA 94720, USA.
John A TainerLife Science Division, 1 Cyclotron Road, Berkeley, CA 94720, USA; The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. Electronic address: jat@scripps.edu.
Scripps Research Institute · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
STRUCTURE AND FUNCTION OF METALLOENZYMES FOR DNA REPAIRR01GM046312 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI TAINER, JOHN A. · 1991 to 2012
$5.9M
Mre11/Rad50 Structural Biology for DNA Damage ResponsesR01CA117638 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI RUSSELL, PAUL, TAINER, JOHN A. · 2005 to 2019
$5.6M
FEN1 STRUCTURES AND HUMAN GENOME STABILITYR01CA081967 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI TAINER, JOHN A. · 1999 to 2013
$4.2M
CIHRNCI NIH HHS P01 CA092584NCI NIH HHS P01CA092584NCI NIH HHS R01 CA081967NCI NIH HHS R01CA081967NCI NIH HHS R01 CA117638NIGMS NIH HHS R01 GM046312NIGMS NIH HHS R01GM46312
6 · The paper itself

Abstract

To avoid genome instability, DNA repair nucleases must precisely target the correct damaged substrate before they are licensed to incise. Damage identification is a challenge for all DNA damage response proteins, but especially for nucleases that cut the DNA and necessarily create a cleaved DNA repair intermediate, likely more toxic than the initial damage. How do these enzymes achieve exquisite specificity without specific sequence recognition or, in some cases, without a non-canonical DNA nucleotide? Combined structural, biochemical, and biological analyses of repair nucleases are revealing their molecular tools for damage verification and safeguarding against inadvertent incision. Surprisingly, these enzymes also often act on RNA, which deserves more attention. Here, we review protein-DNA structures for nucleases involved in replication, base excision repair, mismatch repair, double strand break repair (DSBR), and telomere maintenance: apurinic/apyrimidinic endonuclease 1 (APE1), Endonuclease IV (Nfo), tyrosyl DNA phosphodiesterase (TDP2), UV Damage endonuclease (UVDE), very short patch repair endonuclease (Vsr), Endonuclease V (Nfi), Flap endonuclease 1 (FEN1), exonuclease 1 (Exo1), RNase T and Meiotic recombination 11 (Mre11). DNA and RNA structure-sensing nucleases are essential to life with roles in DNA replication, repair, and transcription. Increasingly these enzymes are employed as advanced tools for synthetic biology and as targets for cancer prognosis and interventions. Currently their structural biology is most fully illuminated for DNA repair, which is also essential to life. How DNA repair enzymes maintain genome fidelity is one of the DNA double helix secrets missed by James Watson and Francis Crick, that is only now being illuminated though structural biology and mutational analyses. Structures reveal motifs for repair nucleases and mechanisms whereby these enzymes follow the old carpenter adage: measure twice, cut once. Furthermore, to measure twice these nucleases act as molecular level transformers that typically reshape the DNA and sometimes themselves to achieve extraordinary specificity and efficiency.

Indexed as

Nucleic Acid ConformationProtein ConformationDeoxyribonuclease IV (Phage T4-Induced)Deoxyribonuclease (Pyrimidine Dimer)DNA-(Apurinic or Apyrimidinic Site) LyaseDNA-Binding ProteinsDNA DamageDNA RepairEndodeoxyribonucleasesFlap EndonucleasesHumansMultienzyme ComplexesNuclear ProteinsPhosphoric Diester HydrolasesTranscription FactorsAPEX1 protein, humanDeoxyribonuclease IV (Phage T4-Induced)Deoxyribonuclease (Pyrimidine Dimer)DNA-(Apurinic or Apyrimidinic Site) LyaseDNA-Binding ProteinsEndodeoxyribonucleasesFEN1 protein, humanFlap EndonucleasesMultienzyme ComplexesNuclear ProteinsPhosphoric Diester HydrolasesTDP2 protein, humanTranscription FactorsUV endonucleasevsr endonucleaseAPE1Base excision repairCrystallographyDNADNA repairDNaseDouble strand break repairEndoIVEndonucleasesEndoVEnzyme–DNA complexExo1ExonucleaseFEN1Genome maintenanceMagnesiumManganeseMetalsMismatch repairMre11NfiNfoNucleasesNucleotide incision repairRNARNaseStructure-specific nucleaseTDP2TelomereUVDEVsrZinc

Identifiers

PMID24754999
PMCPMC4051888
OpenAlexW2082749639

What OpenQuestion holds

Textmetadata
LicenceTDM
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.