Evidence map›Paper›PMID 27509861›Full record

ArticleNature2016

Molecular basis of APC/C regulation by the spindle assembly checkpoint.

Claudio Alfieri, Leifu Chang, Ziguo Zhang, Jing Yang, Sarah Maslen, Mark Skehel, David Barford

Abstract read
In one paragraph

Article in Nature, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
140citing papers in PubMed, 1 pooled it
16.1field-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

140 citing papers in PubMed, 1 synthesis or guideline pooled it, 258 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. When the Clock Is Ticking: The Role of Mitotic Duration in Cell Fate Determination.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  12. Article
  13. Article
  14. Linear ubiquitination of p31Cell & bioscience · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. The Use of APC/C Antagonists to Promote Mitotic Catastrophe in Cancer Cells.Methods in molecular biology (Clifton, N.J.) · 2025
    Article

80 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Claudio Alfieri *MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Leifu Chang *MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Ziguo ZhangMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Jing YangMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Sarah MaslenMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Mark SkehelMRC 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 A14109Cancer Research UK C576/A14109Medical Research Council MC_UP_1201/6Medical Research Council MRC_UP_1201/6
6 · The paper itself

Abstract

In the dividing eukaryotic cell, the spindle assembly checkpoint (SAC) ensures that each daughter cell inherits an identical set of chromosomes. The SAC coordinates the correct attachment of sister chromatid kinetochores to the mitotic spindle with activation of the anaphase-promoting complex (APC/C), the E3 ubiquitin ligase responsible for initiating chromosome separation. In response to unattached kinetochores, the SAC generates the mitotic checkpoint complex (MCC), which inhibits the APC/C and delays chromosome segregation. By cryo-electron microscopy, here we determine the near-atomic resolution structure of a human APC/C–MCC complex (APC/C(MCC)). Degron-like sequences of the MCC subunit BubR1 block degron recognition sites on Cdc20, the APC/C coactivator subunit responsible for substrate interactions. BubR1 also obstructs binding of the initiating E2 enzyme UbcH10 to repress APC/C ubiquitination activity. Conformational variability of the complex enables UbcH10 association, and structural analysis shows how the Cdc20 subunit intrinsic to the MCC (Cdc20(MCC)) is ubiquitinated, a process that results in APC/C reactivation when the SAC is silenced.

Indexed as

Cryoelectron MicroscopyAnaphase-Promoting Complex-CyclosomeBiocatalysisCdc20 ProteinsCell Cycle ProteinsChromosome SegregationHumansKinetochoresModels, MolecularM Phase Cell Cycle CheckpointsProtein BindingProtein ConformationProtein Serine-Threonine KinasesProtein SubunitsSpindle ApparatusStructure-Activity RelationshipANAPC15 protein, humanAnaphase-Promoting Complex-CyclosomeBUB1 protein, humanCDC20 protein, humanCdc20 ProteinsCell Cycle ProteinsProtein Serine-Threonine KinasesProtein SubunitsUBE2C protein, humanUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligases

Identifiers

PMID27509861
PMCPMC5019344
OpenAlexW2489412446

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.