Evidence map›Paper›PMID 22586102›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Repair complexes of FEN1 endonuclease, DNA, and Rad9-Hus1-Rad1 are distinguished from their PCNA counterparts by functionally important stability.

Jordi Querol-Audí, Chunli Yan, Xiaojun Xu, Susan E Tsutakawa, Miaw-Sheue Tsai, John A Tainer, Priscilla K Cooper, Eva Nogales, Ivaylo Ivanov

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

36 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Role of FEN1 S187 phosphorylation in counteracting oxygen-induced stress and regulating postnatal heart development.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2017
    Article
  20. Article
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

9 authors at 5 institutions in 1 country.

Jordi Querol-AudíDepartment of Molecular and Cell Biology, California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720, USA.
Chunli Yan
Xiaojun Xu
Susan E Tsutakawa
Miaw-Sheue Tsai
John A Tainer
Priscilla K Cooper
Eva Nogales
Ivaylo Ivanov
Georgia State University · USLawrence Berkeley National Laboratory · USHoward Hughes Medical Institute · USQB3 · USScripps 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
FEN1 STRUCTURES AND HUMAN GENOME STABILITYR01CA081967 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI TAINER, JOHN A. · 1999 to 2013
$4.2M
Howard Hughes Medical InstituteNCI NIH HHS P01 CA092584NCI NIH HHS R01 CA081967
6 · The paper itself

Abstract

Processivity clamps such as proliferating cell nuclear antigen (PCNA) and the checkpoint sliding clamp Rad9/Rad1/Hus1 (9-1-1) act as versatile scaffolds in the coordinated recruitment of proteins involved in DNA replication, cell-cycle control, and DNA repair. Association and handoff of DNA-editing enzymes, such as flap endonuclease 1 (FEN1), with sliding clamps are key processes in biology, which are incompletely understood from a mechanistic point of view. We have used an integrative computational and experimental approach to define the assemblies of FEN1 with double-flap DNA substrates and either proliferating cell nuclear antigen or the checkpoint sliding clamp 9-1-1. Fully atomistic models of these two ternary complexes were developed and refined through extensive molecular dynamics simulations to expose their conformational dynamics. Clustering analysis revealed the most dominant conformations accessible to the complexes. The cluster centroids were subsequently used in conjunction with single-particle electron microscopy data to obtain a 3D EM reconstruction of the human 9-1-1/FEN1/DNA assembly at 18-Å resolution. Comparing the structures of the complexes revealed key differences in the orientation and interactions of FEN1 and double-flap DNA with the two clamps that are consistent with their respective functions in providing inherent flexibility for lagging strand DNA replication or inherent stability for DNA repair.

Indexed as

DNA RepairAmino Acid SequenceBase SequenceBinding SitesCell Cycle ProteinsDNAElectrophoresis, Polyacrylamide GelExonucleasesFlap EndonucleasesHumansMicroscopy, ElectronModels, MolecularMolecular Dynamics SimulationMolecular Sequence DataMultiprotein ComplexesNucleic Acid ConformationCell Cycle ProteinsDNAExonucleasesFEN1 protein, humanFlap EndonucleasesHUS1 protein, humanMultiprotein ComplexesProliferating Cell Nuclear AntigenRad1 protein, humanrad9 protein

Identifiers

PMID22586102
PMCPMC3365210
OpenAlexW2150909836

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.