Evidence map›Paper›PMID 26083744›Full record

ArticleNature2015

Atomic structure of the APC/C and its mechanism of protein ubiquitination.

Leifu Chang, Ziguo Zhang, Jing Yang, Stephen H McLaughlin, David Barford

Abstract read
In one paragraph

Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 153 papers.

0numbers the graph read from it
0cells of the map it votes in
153citing papers in PubMed
14.0field-weighted citation impact, top 1% 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

153 citing papers in PubMed, 267 citations in OpenAlex.

  1. WEE1 opposes APC/CNature · 2026
    Article
  2. Review
  3. Article
  4. The mutational burden in os odontoideum patients.Orphanet journal of rare diseases · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. NSP7 Molecular Degrader Attenuates Coronaviral Infection Through the β-TrCP1/FBXO5 Axis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  10. Journal of medicinal chemistry · 2025
    Article
  11. Article
  12. Notch controls APC/CScience advances · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Chemical Tools for Probing the Ub/Ubl Conjugation Cascades.Chembiochem : a European journal of chemical biology · 2025
    Review
  18. Article
  19. Article
  20. Article

93 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

5 authors at 1 institution in 1 country.

Leifu Chang *MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Ziguo Zhang *MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Jing YangMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Stephen H McLaughlinMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
David BarfordMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
MRC Laboratory of Molecular Biology · GB

Funding

Cancer Research UK 14109Cancer Research UK A8022Medical Research Council MC_UP_1201/6
6 · The paper itself

Abstract

The anaphase-promoting complex (APC/C) is a multimeric RING E3 ubiquitin ligase that controls chromosome segregation and mitotic exit. Its regulation by coactivator subunits, phosphorylation, the mitotic checkpoint complex and interphase early mitotic inhibitor 1 (Emi1) ensures the correct order and timing of distinct cell-cycle transitions. Here we use cryo-electron microscopy to determine atomic structures of APC/C-coactivator complexes with either Emi1 or a UbcH10-ubiquitin conjugate. These structures define the architecture of all APC/C subunits, the position of the catalytic module and explain how Emi1 mediates inhibition of the two E2s UbcH10 and Ube2S. Definition of Cdh1 interactions with the APC/C indicates how they are antagonized by Cdh1 phosphorylation. The structure of the APC/C with UbcH10-ubiquitin reveals insights into the initiating ubiquitination reaction. Our results provide a quantitative framework for the design of future experiments to investigate APC/C functions in vivo.

Indexed as

UbiquitinationAnaphase-Promoting Complex-CyclosomeAntigens, CDApc10 Subunit, Anaphase-Promoting Complex-CyclosomeApc11 Subunit, Anaphase-Promoting Complex-CyclosomeApc1 Subunit, Anaphase-Promoting Complex-CyclosomeApc3 Subunit, Anaphase-Promoting Complex-CyclosomeApc8 Subunit, Anaphase-Promoting Complex-CyclosomeCadherinsCatalytic DomainCell Cycle ProteinsCryoelectron MicroscopyCytoskeletal ProteinsF-Box ProteinsHumansLysineANAPC10 protein, humanANAPC11 protein, humanANAPC1 protein, humanAnaphase-Promoting Complex-CyclosomeAntigens, CDApc10 Subunit, Anaphase-Promoting Complex-CyclosomeApc11 Subunit, Anaphase-Promoting Complex-CyclosomeApc1 Subunit, Anaphase-Promoting Complex-CyclosomeAPC2 protein, humanApc3 Subunit, Anaphase-Promoting Complex-CyclosomeApc8 Subunit, Anaphase-Promoting Complex-CyclosomeCadherinsCDC23 protein, humanCDC27 protein, humanCDH1 protein, humanCell Cycle ProteinsCytoskeletal ProteinsF-Box ProteinsFBXO5 protein, humanLysineProtein SubunitsUBE2C protein, humanUbe2S protein, humanUbiquitinUbiquitin-Conjugating Enzymes

Identifiers

PMID26083744
PMCPMC4608048
OpenAlexW1881319148

What OpenQuestion holds

Textmetadata
LicenceTDM
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.