Evidence map›Paper›PMID 23451868›Full record

ReviewAnnual review of biochemistry2013

Flap endonuclease 1.

Lata Balakrishnan, Robert A Bambara

Abstract readReview
In one paragraph

Review in Annual review of biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 170 papers.

0numbers the graph read from it
0cells of the map it votes in
170citing papers in PubMed
–field-weighted citation impact
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

170 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. DNA polymerase I: structure, activity, and function in bacterial DNA replication and repair.Critical reviews in biochemistry and molecular biology · 2026
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Biomolecular NMR assignments · 2025
    Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review

110 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

2 authors.

Lata BalakrishnanDepartment of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, New York 14642, USA. lata_balakrishnan@urmc.rochester.edu
Robert A Bambara

Funding

ENZYMATIC MECHANISMS OF DNA SYNTHESISR01GM024441 · NIGMS · UNIVERSITY OF ROCHESTER · PI BAMBARA, ROBERT A · 1985 to 2011
$3.8M
Regulating Pathways and Fidelity of DNA Replication and Repair by AcetylationR00GM098328 · NIGMS · INDIANA UNIVERSITY INDIANAPOLIS · PI BALAKRISHNAN, LATA · 2014 to 2016
$746k
Regulating Pathways and Fidelity of DNA Replication and Repair by AcetylationK99GM098328 · NIGMS · UNIVERSITY OF ROCHESTER · PI BALAKRISHNAN, LATA · 2012 to 2013
$180k
NIGMS NIH HHS GM098328NIGMS NIH HHS GM24441NIGMS NIH HHS K99 GM098328NIGMS NIH HHS R00 GM098328NIGMS NIH HHS R01 GM024441
6 · The paper itself

Abstract

First discovered as a structure-specific endonuclease that evolved to cut at the base of single-stranded flaps, flap endonuclease (FEN1) is now recognized as a central component of cellular DNA metabolism. Substrate specificity allows FEN1 to process intermediates of Okazaki fragment maturation, long-patch base excision repair, telomere maintenance, and stalled replication fork rescue. For Okazaki fragments, the RNA primer is displaced into a 5' flap and then cleaved off. FEN1 binds to the flap base and then threads the 5' end of the flap through its helical arch and active site to create a configuration for cleavage. The threading requirement prevents this active nuclease from cutting the single-stranded template between Okazaki fragments. FEN1 efficiency and specificity are critical to the maintenance of genome fidelity. Overall, recent advances in our knowledge of FEN1 suggest that it was an ancient protein that has been fine-tuned over eons to coordinate many essential DNA transactions.

Indexed as

AnimalsDNADNA RepairDNA ReplicationFlap EndonucleasesHumansSubstrate SpecificityDNAFlap EndonucleasesOkazaki fragments

Identifiers

PMID23451868
PMCPMC3679248

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.