Evidence map›Paper›PMID 12574115›Full record

ArticleThe EMBO journal2003

Doc1 mediates the activity of the anaphase-promoting complex by contributing to substrate recognition.

Lori A Passmore, Elizabeth A McCormack, Shannon W N Au, Angela Paul, Keith R Willison, J Wade Harper, David Barford

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

101 citing papers in PubMed, 205 citations in OpenAlex.

  1. Article
  2. Cryo-EM structures of apo-APC/C and APC/CNature communications · 2024
    Article
  3. Article
  4. Article
  5. The Anaphase-Promoting Complex/Cyclosome Is a Cellular Ageing Regulator.International journal of molecular sciences · 2022
    Review
  6. Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. The substrate specificity of eukaryotic cytosolic chaperonin CCT.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  17. Article
  18. Article
  19. Article
  20. Review

41 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

7 authors at 1 institution in 1 country.

Lori A PassmoreSection of Structural Biology and Cancer Research UK Centre for Cell and Molecular Biology, Institute of Cancer Research, 237 Fulham Road, London SW3 6JB, UK.
Elizabeth A McCormack
Shannon W N Au
Angela Paul
Keith R Willison
J Wade Harper
David Barford
Institute of Structural and Molecular Biology · GB

Funding

Ubiquitin Mediated Proteolysis and Cell Cycle ControlR01AG011085 · NIA · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI JEFFREY W HARPER · 1993 to 2026
$10.9M
NIA NIH HHS AG11085NIA NIH HHS R01 AG011085
6 · The paper itself

Abstract

The anaphase-promoting complex (APC) is a multisubunit E3 ubiquitin ligase that targets specific cell cycle-related proteins for degradation, regulating progression from metaphase to anaphase and exit from mitosis. The APC is regulated by binding of the coactivator proteins Cdc20p and Cdh1p, and by phosphorylation. We have developed a purification strategy that allowed us to purify the budding yeast APC to near homogeneity and identify two novel APC-associated proteins, Swm1p and Mnd2p. Using an in vitro ubiquitylation system and a native gel binding assay, we have characterized the properties of wild-type and mutant APC. We show that both the D and KEN boxes contribute to substrate recognition and that coactivator is required for substrate binding. APC lacking Apc9p or Doc1p/Apc10 have impaired E3 ligase activities. However, whereas Apc9p is required for structural stability and the incorporation of Cdc27p into the APC complex, Doc1p/Apc10 plays a specific role in substrate recognition by APC-coactivator complexes. These results imply that Doc1p/Apc10 may play a role to regulate the binding of specific substrates, similar to that of the coactivators.

Indexed as

Ubiquitin-Protein Ligase ComplexesAnaphase-Promoting Complex-CyclosomeApc10 Subunit, Anaphase-Promoting Complex-CyclosomeCell CycleCell Cycle ProteinsLigasesProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityUbiquitinUbiquitin-Protein LigasesAnaphase-Promoting Complex-CyclosomeApc10 Subunit, Anaphase-Promoting Complex-CyclosomeCell Cycle ProteinsDOC1 protein, S cerevisiaeLigasesMND2 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSWM1 protein, S cerevisiaeUbiquitinUbiquitin-Protein Ligase ComplexesUbiquitin-Protein Ligases

Identifiers

PMID12574115
PMCPMC145444
OpenAlexW2131035051

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.