Evidence map›Paper›PMID 24813613›Full record

ArticleCell2014

Enhanced protein degradation by branched ubiquitin chains.

Hermann-Josef Meyer, Michael Rape

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 290 papers.

0numbers the graph read from it
0cells of the map it votes in
290citing papers in PubMed
18.8field-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

290 citing papers in PubMed, 479 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Function and regulation of the mitochondrial stress response.Nature structural & molecular biology · 2026
    Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Computational Pipelines for Protein Ubiquitylation Analysis and Prediction.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  18. Article
  19. Targeting ubiquitination in disease and therapy.Signal transduction and targeted therapy · 2025
    Review
  20. Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Hermann-Josef MeyerDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA.
Michael RapeHoward Hughes Medical Institute, University of California, Berkeley, Berkeley, CA 94720, USA; Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA. Electronic address: mrape@berkeley.edu.
University of California, Berkeley · US

Funding

Dissecting Mechanisms of Ubiquitination and Deubiquitination in Cell Cycle ControR01GM083064 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI RAPE, MICHAEL P · 2008 to 2016
$2.2M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM083064
6 · The paper itself

Abstract

Posttranslational modification of cell-cycle regulators with ubiquitin chains is essential for eukaryotic cell division. Such chains can be connected through seven lysine residues or the amino terminus of ubiquitin, thereby allowing the assembly of eight homogenous and multiple mixed or branched conjugates. Although functions of homogenous chain types have been described, physiological roles of branched structures are unknown. Here, we report that the anaphase-promoting complex (APC/C) efficiently synthesizes branched conjugates that contain multiple blocks of K11-linked chains. Compared to homogenous chains, the branched conjugates assembled by the APC/C strongly enhance substrate recognition by the proteasome, thereby driving degradation of cell-cycle regulators during early mitosis. Our work, therefore, identifies an enzyme and substrates for modification with branched ubiquitin chains and points to an important role of these conjugates in providing an improved signal for proteasomal degradation.

Indexed as

ProteolysisAnaphase-Promoting Complex-CyclosomeHeLa CellsHumansNIMA-Related KinasesProteasome Endopeptidase ComplexProtein Serine-Threonine KinasesUbiquitin-Conjugating EnzymesAnaphase-Promoting Complex-CyclosomeNEK2 protein, humanNIMA-Related KinasesProteasome Endopeptidase ComplexProtein Serine-Threonine KinasesUbe2S protein, humanUbiquitin-Conjugating Enzymes

Identifiers

PMID24813613
PMCPMC4028144
OpenAlexW1986429623

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.