Evidence map›Paper›PMID 22118811›Full record

ReviewTrends in biochemical sciences2012

Unpairing and gating: sequence-independent substrate recognition by FEN superfamily nucleases.

Jane A Grasby, L David Finger, Susan E Tsutakawa, John M Atack, John A Tainer

Abstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

44 citing papers in PubMed, 72 citations in OpenAlex.

  1. DNA polymerase I: structure, activity, and function in bacterial DNA replication and repair.Critical reviews in biochemistry and molecular biology · 2026
    Review
  2. Article
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  5. A four-point molecular handover during Okazaki maturation.Nature structural & molecular biology · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
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  14. Review
  15. Human XPG nuclease structure, assembly, and activities with insights for neurodegeneration and cancer from pathogenic mutations.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Article
  17. 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

5 authors at 2 institutions in 2 countries.

Jane A GrasbyCentre for Chemical Biology, Department of Chemistry, Krebs Institute, University of Sheffield, Sheffield S3 7HF, UK. j.a.grasby@sheffield.ac.uk
L David Finger
Susan E Tsutakawa
John M Atack
John A Tainer
University of Sheffield · GBLawrence Berkeley National Laboratory · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
FEN1 STRUCTURES AND HUMAN GENOME STABILITYR01CA081967 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI TAINER, JOHN A. · 1999 to 2013
$4.2M
Biotechnology and Biological Sciences Research Council BB/F014732/1Biotechnology and Biological Sciences Research Council BBF0147321NCI NIH HHS P01 CA092584NCI NIH HHS P01CA092584NCI NIH HHS R01 CA081967NCI NIH HHS R01CA081967
6 · The paper itself

Abstract

Structure-specific 5'-nucleases form a superfamily of evolutionarily conserved phosphodiesterases that catalyse a precise incision of a diverse range of DNA and RNA substrates in a sequence-independent manner. Superfamily members, such as flap endonucleases, exonuclease 1, DNA repair protein XPG, endonuclease GEN1 and the 5'-3'-exoribonucleases, play key roles in many cellular processes such as DNA replication and repair, recombination, transcription, RNA turnover and RNA interference. In this review, we discuss recent results that highlight the conserved architectures and active sites of the structure-specific 5'-nucleases. Despite substrate diversity, a common gating mechanism for sequence-independent substrate recognition and incision emerges, whereby double nucleotide unpairing of substrates is required to access the active site.

Indexed as

Amino Acid SequenceAnimalsCatalytic DomainDNADNA RepairEndonucleasesExodeoxyribonucleasesFlap EndonucleasesHumansMolecular Sequence DataProtein ConformationRNA InterferenceSubstrate SpecificityDNAEndonucleasesexodeoxyribonuclease IExodeoxyribonucleasesFlap Endonucleases

Identifiers

PMID22118811
PMCPMC3341984
OpenAlexW1998495506

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.