Evidence map›Paper›PMID 22520345›Full record

ArticleBMC biology2012

Clamp loader ATPases and the evolution of DNA replication machinery.

Brian A Kelch, Debora L Makino, Mike O'Donnell, John Kuriyan

Open access · goldAbstract read
In one paragraph

Article in BMC biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

63 citing papers in PubMed, 106 citations in OpenAlex.

  1. Article
  2. Mechanistic diversity of clamp loading at small DNA gaps.The Journal of biological chemistry · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. ThebioRxiv : the preprint server for biology · 2026
    Article
  7. Article
  8. Review
  9. Structure of the human CTF18-RFC clamp loader bound to PCNA.bioRxiv : the preprint server for biology · 2025
    Article
  10. Article
  11. SNARE disassembly requires Sec18/NSF side loading.Nature structural & molecular biology · 2025
    Article
  12. Article
  13. SNARE disassembly requires Sec18/NSF side-loading.bioRxiv : the preprint server for biology · 2025
    Article
  14. Review
  15. Article
  16. Cryo-EM reveals a nearly complete PCNA loading process and unique features of the human alternative clamp loader CTF18-RFC.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. Differences in clamp loader mechanism between bacteria and eukaryotes.bioRxiv : the preprint server for biology · 2023
    Article

3 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

4 authors at 4 institutions in 2 countries.

Brian A KelchDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA. bkelch@berkeley.edu
Debora L Makino
Mike O'Donnell
John Kuriyan
Howard Hughes Medical Institute · USLawrence Berkeley National Laboratory · USQB3 · USUniversity of California, Berkeley · US

Funding

BIOCHEMICAL MECHANISM OF DNA POLYMERASE III HOLOENZYMER01GM038839 · NIGMS · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI O'DONNELL, MICHAEL E · 1988 to 2014
$2.9M
BIOCHEMICAL MECHANISM OF DNA POLYMERASE III HOLOENZYMER37GM038839 · NIGMS · ROCKEFELLER UNIVERSITY · PI O'DONNELL, MICHAEL E · 1997 to 2006
$2.2M
NIGMS NIH HHS GM38839NIGMS NIH HHS GM45547
6 · The paper itself

Abstract

Clamp loaders are pentameric ATPases of the AAA+ family that operate to ensure processive DNA replication. They do so by loading onto DNA the ring-shaped sliding clamps that tether the polymerase to the DNA. Structural and biochemical analysis of clamp loaders has shown how, despite differences in composition across different branches of life, all clamp loaders undergo the same concerted conformational transformations, which generate a binding surface for the open clamp and an internal spiral chamber into which the DNA at the replication fork can slide, triggering ATP hydrolysis, release of the clamp loader, and closure of the clamp round the DNA. We review here the current understanding of the clamp loader mechanism and discuss the implications of the differences between clamp loaders from the different branches of life.

Indexed as

DNA ReplicationEvolution, MolecularAdenosine TriphosphatasesBacteriaBacteriophage T4EukaryotaHydrolysisModels, MolecularPhylogenyProtein Structure, TertiaryAdenosine Triphosphatases

Identifiers

PMID22520345
PMCPMC3331839
OpenAlexW2052065853

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.