Evidence map›Paper›PMID 34473924›Full record

ReviewBiochemistry2023

Ligandability of E3 Ligases for Targeted Protein Degradation Applications.

Bridget P Belcher, Carl C Ward, Daniel K Nomura

Open access · greenAbstract readReview
In one paragraph

Review in Biochemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
7.0field-weighted citation impact, top 2% 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

71 citing papers in PubMed, 127 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. RSC advances · 2026
    Article
  11. Article
  12. Article
  13. Review
  14. Emerging biologic modalities for targeted protein degradation.The Journal of biological chemistry · 2026
    Review
  15. Induced proximity-based therapeutic modalities.Nature reviews. Drug discovery · 2026
    Review
  16. Article
  17. Review
  18. Review
  19. Review
  20. Review

11 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

3 authors at 1 institution in 1 country.

Bridget P BelcherDepartment of Chemistry, University of California, Berkeley, Berkeley, California 94720 United States.
Carl C WardDepartment of Chemistry, University of California, Berkeley, Berkeley, California 94720 United States.
Daniel K NomuraDepartment of Chemistry, University of California, Berkeley, Berkeley, California 94720 United States.ORCID 0000-0003-1614-8360
Innovative Genomics Institute · US

Funding

Tackling Undruggable Cancer Targets using Chemoproteomic PlatformsR35CA263814 · NCI · UNIVERSITY OF CALIFORNIA BERKELEY · PI Daniel Nomura · 2022 to 2026
$4.6M
Harnessing E3 Ligases for Cancer TherapyR01CA240981 · NCI · UNIVERSITY OF CALIFORNIA BERKELEY · PI Daniel Nomura · 2019 to 2026
$4.3M
NCI NIH HHS R01 CA240981NCI NIH HHS R35 CA263814
6 · The paper itself

Abstract

Targeted protein degradation (TPD) using proteolysis targeting chimeras (PROTACs) and molecular glue degraders has arisen as a powerful therapeutic modality for eliminating disease-causing proteins from cells. PROTACs and molecular glue degraders employ heterobifunctional or monovalent small molecules, respectively, to chemically induce the proximity of target proteins with E3 ubiquitin ligases to ubiquitinate and degrade specific proteins via the proteasome. Whereas TPD is an attractive therapeutic strategy for expanding the druggable proteome, only a relatively small number of E3 ligases out of the >600 E3 ligases encoded by the human genome have been exploited by small molecules for TPD applications. Here we review the existing E3 ligases that have thus far been successfully exploited for TPD and discuss chemoproteomics-enabled covalent screening strategies for discovering new E3 ligase recruiters. We also provide a chemoproteomic map of reactive cysteines within hundreds of E3 ligases that may represent potential ligandable sites that can be pharmacologically interrogated to uncover additional E3 ligase recruiters.

Indexed as

ProteinsUbiquitin-Protein LigasesHumansProteasome Endopeptidase ComplexProteolysisUbiquitinationProteasome Endopeptidase ComplexProteinsUbiquitin-Protein Ligases

Identifiers

PMID34473924
PMCPMC8928483
OpenAlexW3197828497

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.