Evidence map›Paper›PMID 30429481›Full record

ArticleNature communications2018

An E2-ubiquitin thioester-driven approach to identify substrates modified with ubiquitin and ubiquitin-like molecules.

Gábor Bakos, Lu Yu, Igor A Gak, Theodoros I Roumeliotis, Dimitris Liakopoulos, Jyoti S Choudhary, Jörg Mansfeld

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
1.9field-weighted citation impact, top 14% 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

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 39 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Tracking E2-specific substrates.Nature chemical biology · 2025
    Article
  4. Journal of medicinal chemistry · 2025
    Article
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  6. Review
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  10. Review
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  15. Article
  16. Tools for Decoding Ubiquitin Signaling in DNA Repair.Frontiers in cell and developmental biology · 2021
    Review
  17. Review
  18. Article
  19. Review
  20. Article
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 3 institutions in 3 countries.

Gábor BakosCell Cycle, Biotechnology Center, Technische Universität Dresden, 01307, Dresden, Germany.
Lu YuFunctional Proteomics Group, The Institute of Cancer Research, London, SW3 6JB, UK.
Igor A GakCell Cycle, Biotechnology Center, Technische Universität Dresden, 01307, Dresden, Germany.
Theodoros I RoumeliotisFunctional Proteomics Group, The Institute of Cancer Research, London, SW3 6JB, UK.
Dimitris LiakopoulosCentre de Recherche en Biologie cellulaire de Montpellier (CRBM), CNRS UMR 5237, 34293, Montpellier Cedex 05, France.
Jyoti S ChoudharyFunctional Proteomics Group, The Institute of Cancer Research, London, SW3 6JB, UK.
Jörg MansfeldCell Cycle, Biotechnology Center, Technische Universität Dresden, 01307, Dresden, Germany. joerg.mansfeld@tu-dresden.de.ORCID http://orcid.org/0000-0002-0562-8206
Institute of Cancer Research · GBTechnische Universität Dresden · DECentre National de la Recherche Scientifique · FR

Funding

Wellcome Trust
6 · The paper itself

Abstract

Covalent modifications of proteins with ubiquitin and ubiquitin-like molecules are instrumental to many biological processes. However, identifying the E3 ligase responsible for these modifications remains a major bottleneck in ubiquitin research. Here, we present an E2-thioester-driven identification (E2~dID) method for the targeted identification of substrates of specific E2 and E3 enzyme pairs. E2~dID exploits the central position of E2-conjugating enzymes in the ubiquitination cascade and provides in vitro generated biotinylated E2~ubiquitin thioester conjugates as the sole source for ubiquitination in extracts. This enables purification and mass spectrometry-based identification of modified proteins under stringent conditions independently of the biological source of the extract. We demonstrate the sensitivity and specificity of E2-dID by identifying and validating substrates of APC/C in human cells. Finally, we perform E2~dID with SUMO in S. cerevisiae, showing that this approach can be easily adapted to other ubiquitin-like modifiers and experimental models.

Indexed as

Anaphase-Promoting Complex-CyclosomeCell LineHeLa CellsHumansSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSUMO-1 ProteinUbiquitinUbiquitin-Activating EnzymesUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesUbiquitinsAnaphase-Promoting Complex-CyclosomeSaccharomyces cerevisiae ProteinsSUMO-1 ProteinUbiquitinUbiquitin-Activating EnzymesUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesUbiquitins

Identifiers

PMID30429481
PMCPMC6235928
OpenAlexW2897066230

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.