Evidence map›Paper›PMID 42133863›Full record

ReviewChemical reviews2026

Methods to Study the Molecular Mechanism and Drive the Design of Protein Degraders.

Charlotte Crowe, Alessio Ciulli

Abstract readReview
In one paragraph

Review in Chemical reviews, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

2 authors.

Charlotte CroweCentre for Targeted Protein Degradation, School of Life Sciences, University of Dundee, 1 James Lindsay Place, Dundee DD1 5JJ, U.K.ORCID 0000-0003-2068-8255
Alessio CiulliCentre for Targeted Protein Degradation, School of Life Sciences, University of Dundee, 1 James Lindsay Place, Dundee DD1 5JJ, U.K.ORCID 0000-0002-8654-1670

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small-molecule degraders eliminate disease-driving proteins by hijacking the ubiquitin-proteasome system. To achieve cellular activity, protein degraders must perform a series of consecutive steps involving cell permeability, binary target engagement, and formation of a ternary complex with the target protein and a ubiquitin E3 ligase, followed by protein ubiquitination, culminating with protein degradation. Monitoring each mechanistic step of a degraders' mode of action is important to confirm its

Indexed as

Drug DesignProteinsProteolysisSmall Molecule LibrariesAnimalsHumansProteasome Endopeptidase ComplexUbiquitinUbiquitinationUbiquitin-Protein LigasesProteasome Endopeptidase ComplexProteinsSmall Molecule LibrariesUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID42133863
PMCPMC13220276

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.