Evidence map›Paper›PMID 31859248›Full record

ArticleCell chemical biology2020

Photocrosslinking Activity-Based Probes for Ubiquitin RING E3 Ligases.

Sunil Mathur, Adam J Fletcher, Emma Branigan, Ronald T Hay, Satpal Virdee

Abstract read
In one paragraph

Article in Cell chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
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

26 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. E2 variants for probing E3 ubiquitin ligase activities.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. Internal Ubiquitin Electrophiles for Covalent Trapping and Inhibition of Deubiquitinases.Chembiochem : a European journal of chemical biology · 2025
    Article
  8. Review
  9. Covalent inhibition ofiScience · 2025
    Article
  10. Chemical Tools for Probing the Ub/Ubl Conjugation Cascades.Chembiochem : a European journal of chemical biology · 2025
    Review
  11. Review
  12. Reading and Writing the Ubiquitin Code Using Genetic Code Expansion.Chembiochem : a European journal of chemical biology · 2024
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Site-specific ubiquitination: Deconstructing the degradation tag.Current opinion in structural biology · 2022
    Review
  18. Review
  19. Review
  20. Review
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.

Sunil MathurMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Scotland, UK.
Adam J FletcherMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Scotland, UK.
Emma BraniganDivision of Gene Regulation and Expression, University of Dundee, Scotland, UK.
Ronald T HayDivision of Gene Regulation and Expression, University of Dundee, Scotland, UK.
Satpal VirdeeMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Scotland, UK. Electronic address: s.s.virdee@dundee.ac.uk.

Funding

Biotechnology and Biological Sciences Research Council BB/P003982/1Medical Research Council MC_UU_00018/7Medical Research Council MC_UU_12016/8Wellcome TrustWellcome Trust 098391/Z/12/Z
6 · The paper itself

Abstract

Activity-based protein profiling is an invaluable technique for studying enzyme biology and facilitating the development of therapeutics. Ubiquitin E3 ligases (E3s) are one of the largest enzyme families and regulate a host of (patho)physiological processes. The largest subtype are the RING E3s of which there are >600 members. RING E3s have adaptor-like activity that can be subject to diverse regulatory mechanisms and have become attractive drug targets. Activity-based probes (ABPs) for measuring RING E3 activity do not exist. Here we re-engineer ubiquitin-charged E2 conjugating enzymes to produce photocrosslinking ABPs. We demonstrate activity-dependent profiling of two divergent cancer-associated RING E3s, RNF4 and c-Cbl, in response to their native activation signals. We also demonstrate profiling of endogenous RING E3 ligase activation in response to epidermal growth factor (EGF) stimulation. These photocrosslinking ABPs should advance E3 ligase research and the development of selective modulators against this important class of enzymes.

Indexed as

BenzophenonesCross-Linking ReagentsHumansModels, MolecularMolecular ConformationPhenylalaninePhotochemical ProcessesUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligases4-benzoylphenylalanineBenzophenonesCross-Linking ReagentsPhenylalanineUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligasesactivity-based probescancerdrug discoveryE3 ligasesphotocrosslinkingPROTACprotein degradationproteomicsRING E3ubiquitin

Identifiers

PMID31859248
PMCPMC6963778

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Registered trials

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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.