Evidence map›Paper›PMID 20929870›Full record

ReviewNucleic acids research2011

Functional regulation of FEN1 nuclease and its link to cancer.

Li Zheng, Jia Jia, L David Finger, Zhigang Guo, Cindy Zer, Binghui Shen

Open access · goldAbstract readReview
In one paragraph

Review in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed, 1 pooled it
5.3field-weighted citation impact, top 4% 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

111 citing papers in PubMed, 1 synthesis or guideline pooled it, 231 citations in OpenAlex.

  1. Pooled it
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  7. Biomolecular NMR assignments · 2025
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51 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

6 authors at 2 institutions in 3 countries.

Li ZhengInstitute of Cell Biology and Genetics, College of Life Sciences, Zhejiang University, Hangzhou, China.
Jia Jia
L David Finger
Zhigang Guo
Cindy Zer
Binghui Shen
City Of Hope National Medical Center · USZhejiang University · CN

Funding

Function Analysis of FEN-1 Nuclease in Genome StabilityR01CA073764 · NCI · CITY OF HOPE/BECKMAN RESEARCH INSTITUTE · PI BINGHUI SHEN · 2002 to 2026
$7.9M
Role of Nucleases in RNA Primer Removal and MutagenesisR01CA085344 · NCI · CITY OF HOPE/BECKMAN RESEARCH INSTITUTE · PI SHEN, BINGHUI · 1999 to 2024
$7.7M
FEN-1/WRN Complex in Prevention of Genetic DiseasesF32CA117236 · NCI · BECKMAN RESEARCH INSTITUTE/CITY OF HOPE · PI FINGER, L DAVID · 2006 to 2008
$151k
NCI NIH HHS F32CA117236NCI NIH HHS R01CA073764NCI NIH HHS R01CA085344
6 · The paper itself

Abstract

Flap endonuclease-1 (FEN1) is a member of the Rad2 structure-specific nuclease family. FEN1 possesses FEN, 5'-exonuclease and gap-endonuclease activities. The multiple nuclease activities of FEN1 allow it to participate in numerous DNA metabolic pathways, including Okazaki fragment maturation, stalled replication fork rescue, telomere maintenance, long-patch base excision repair and apoptotic DNA fragmentation. Here, we summarize the distinct roles of the different nuclease activities of FEN1 in these pathways. Recent biochemical and genetic studies indicate that FEN1 interacts with more than 30 proteins and undergoes post-translational modifications. We discuss how FEN1 is regulated via these mechanisms. Moreover, FEN1 interacts with five distinct groups of DNA metabolic proteins, allowing the nuclease to be recruited to a specific DNA metabolic complex, such as the DNA replication machinery for RNA primer removal or the DNA degradosome for apoptotic DNA fragmentation. Some FEN1 interaction partners also stimulate FEN1 nuclease activities to further ensure efficient action in processing of different DNA structures. Post-translational modifications, on the other hand, may be critical to regulate protein-protein interactions and cellular localizations of FEN1. Lastly, we also review the biological significance of FEN1 as a tumor suppressor, with an emphasis on studies of human mutations and mouse models.

Indexed as

AnimalsFlap EndonucleasesHumansMiceNeoplasmsFEN1 protein, humanFlap Endonucleases

Identifiers

PMID20929870
PMCPMC3035468
OpenAlexW1975775716

What OpenQuestion holds

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LicenceCC BY-NC
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.