Evidence map›Paper›PMID 39297173›Full record

ReviewiScience2024

Molecular glue-mediated targeted protein degradation: A novel strategy in small-molecule drug development.

Xueqiang Tan, Zuyi Huang, Hairun Pei, Zongchao Jia, Jimin Zheng

Abstract readReview
In one paragraph

Review in iScience, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. E3 Ubiquitin Ligases in MASH-Associated Liver Fibrosis: Mechanisms and Therapeutic Opportunities.Liver international : official journal of the International Association for the Study of the Liver · 2026
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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.

Xueqiang TanDepartment of Chemistry, Beijing Normal University, Beijing 100875, China.
Zuyi HuangDepartment of Chemistry, Beijing Normal University, Beijing 100875, China.
Hairun PeiBeijing Advanced Innovation Centre for Food Nutrition and Human Health, Beijing Technology & Business University, Beijing 100048, China.
Zongchao JiaDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, ON K7L 3N6, Canada.
Jimin ZhengDepartment of Chemistry, Beijing Normal University, Beijing 100875, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small-molecule drugs are effective and thus most widely used. However, their applications are limited by their reliance on active high-affinity binding sites, restricting their target options. A breakthrough approach involves molecular glues, a novel class of small-molecule compounds capable of inducing protein-protein interactions (PPIs). This opens avenues to target conventionally undruggable proteins, overcoming limitations seen in conventional small-molecule drugs. Molecular glues play a key role in targeted protein degradation (TPD) techniques, including ubiquitin-proteasome system-based approaches such as proteolysis targeting chimeras (PROTACs) and molecular glue degraders and recently emergent lysosome system-based techniques like molecular degraders of extracellular proteins through the asialoglycoprotein receptors (MoDE-As) and macroautophagy degradation targeting chimeras (MADTACs). These techniques enable an innovative targeted degradation strategy for prolonged inhibition of pathology-associated proteins. This review provides an overview of them, emphasizing the clinical potential of molecular glues and guiding the development of molecular-glue-mediated TPD techniques.

Indexed as

Applied chemistryBiochemistryBiological sciencesChemistryNatural sciences

Identifiers

PMID39297173
PMCPMC11409024

What OpenQuestion holds

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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.