Evidence map›Paper›PMID 21828267›Full record

ReviewGenes & development2011

Mechanism of CRL4(Cdt2), a PCNA-dependent E3 ubiquitin ligase.

Courtney G Havens, Johannes C Walter

Open access · diamondAbstract readReview
In one paragraph

Review in Genes & development, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 150 papers.

0numbers the graph read from it
0cells of the map it votes in
150citing 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

150 citing papers in PubMed, 225 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Degrons: defining the rules of protein degradation.Nature reviews. Molecular cell biology · 2025
    Review
  9. Article
  10. Article
  11. CDK5 targets p21Molecular medicine reports · 2025
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Epithelial CRL4Digestive diseases and sciences · 2024
    Article
  19. Article
  20. Review

90 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 at 1 institution in 1 country.

Courtney G HavensDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Johannes C Walter
Harvard University · US

Funding

The mechanism of vertebrate DNA replication terminationR01GM080676 · NIGMS · HARVARD MEDICAL SCHOOL · PI WALTER, JOHANNES · 2007 to 2019
$3.7M
NIGMS NIH HHS GM80676NIGMS NIH HHS R01 GM080676
6 · The paper itself

Abstract

Eukaryotic cell cycle transitions are driven by E3 ubiquitin ligases that catalyze the ubiquitylation and destruction of specific protein targets. For example, the anaphase-promoting complex/cyclosome (APC/C) promotes the exit from mitosis via destruction of securin and mitotic cyclins, whereas CRL1(Skp2) allows entry into S phase by targeting the destruction of the cyclin-dependent kinase (CDK) inhibitor p27. Recently, an E3 ubiquitin ligase called CRL4(Cdt2) has been characterized, which couples proteolysis to DNA synthesis via an unusual mechanism that involves display of substrate degrons on the DNA polymerase processivity factor PCNA. Through its destruction of Cdt1, p21, and Set8, CRL4(Cdt2) has emerged as a master regulator that prevents rereplication in S phase. In addition, it also targets other factors such as E2F and DNA polymerase η. In this review, we discuss our current understanding of the molecular mechanism of substrate recognition by CRL4(Cdt2) and how this E3 ligase helps to maintain genome integrity.

Indexed as

AnimalsCell Cycle ProteinsDNA RepairDNA ReplicationHumansNuclear ProteinsProliferating Cell Nuclear AntigenProtein Processing, Post-TranslationalUbiquitinationUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesXenopus ProteinsCell Cycle ProteinsDTL protein, humandtl protein, XenopusNuclear ProteinsProliferating Cell Nuclear AntigenUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesXenopus Proteins

Identifiers

PMID21828267
PMCPMC3182024
OpenAlexW2121291166

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.