Evidence map›Paper›PMID 28298557›Full record

ReviewThe Biochemical journal2017

Chemical approaches to targeted protein degradation through modulation of the ubiquitin-proteasome pathway.

Ian Collins, Hannah Wang, John J Caldwell, Raj Chopra

Open access · hybridAbstract readReview
In one paragraph

Review in The Biochemical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
10.0field-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

59 citing papers in PubMed, 137 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. The Role of CELMoD Agents in Multiple Myeloma.OncoTargets and therapy · 2025
    Review
  5. Identification and Development of BRD9 Chemical Probes.Pharmaceuticals (Basel, Switzerland) · 2024
    Review
  6. Article
  7. Review
  8. Article
  9. Determination of Ligand-Binding Affinity (Journal of medicinal chemistry · 2023
    Article
  10. Review
  11. Review
  12. Article
  13. Synthesis and biological evaluation of niclosamide PROTACs.Bioorganic & medicinal chemistry letters · 2022
    Article
  14. Article
  15. Review
  16. Reductive site-selective atypicalScience advances · 2022
    Article
  17. Review
  18. Article
  19. Article
  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

4 authors at 1 institution in 1 country.

Ian CollinsCancer Research UK Cancer Therapeutics Unit, The Institute of Cancer Research, London SM2 5NG, U.K.
Hannah WangCancer Research UK Cancer Therapeutics Unit, The Institute of Cancer Research, London SM2 5NG, U.K.
John J CaldwellCancer Research UK Cancer Therapeutics Unit, The Institute of Cancer Research, London SM2 5NG, U.K.
Raj ChopraCancer Research UK Cancer Therapeutics Unit, The Institute of Cancer Research, London SM2 5NG, U.K. raj.chopra@icr.ac.uk.
Institute of Cancer Research · GB

Funding

Cancer Research UK 22897
6 · The paper itself

Abstract

Manipulation of the ubiquitin-proteasome system to achieve targeted degradation of proteins within cells using chemical tools and drugs has the potential to transform pharmacological and therapeutic approaches in cancer and other diseases. An increased understanding of the molecular mechanism of thalidomide and its analogues following their clinical use has unlocked small-molecule modulation of the substrate specificity of the E3 ligase cereblon (CRBN), which in turn has resulted in the advancement of new immunomodulatory drugs (IMiDs) into the clinic. The degradation of multiple context-specific proteins by these pleiotropic small molecules provides a means to uncover new cell biology and to generate future drug molecules against currently undruggable targets. In parallel, the development of larger bifunctional molecules that bring together highly specific protein targets in complexes with CRBN, von Hippel-Lindau, or other E3 ligases to promote ubiquitin-dependent degradation has progressed to generate selective chemical compounds with potent effects in cells and

Indexed as

Adaptor Proteins, Signal TransducingDrug DiscoveryDrugs, InvestigationalGene ExpressionHumansImmunologic FactorsMolecular Targeted TherapyPeptide HydrolasesProteasome Endopeptidase ComplexProteasome InhibitorsProteolysisSmall Molecule LibrariesSubstrate SpecificityThalidomideUbiquitinUbiquitinationAdaptor Proteins, Signal TransducingCRBN protein, humanDrugs, InvestigationalImmunologic FactorsPeptide HydrolasesProteasome Endopeptidase ComplexProteasome InhibitorsSmall Molecule LibrariesThalidomideUbiquitinUbiquitin-Protein LigasesVHL protein, humanVon Hippel-Lindau Tumor Suppressor Proteinchemical biologychemical toolsubiquitin ligasesubiquitin–proteasome system

Identifiers

PMID28298557
PMCPMC5350610
OpenAlexW2595729735

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.