Evidence map›Paper›PMID 41362117›Full record

ReviewDrug development research2025

Next-Generation Proteolysis-Targeting Chimeras in Precision Oncology: Multifunctional Designs, Emerging Modalities, and Translational Prospects in Targeted Protein Degradation.

Mohamed S Nafie, Mohamed K Diab, Asmaa S A Yassen, Amany M Elshamy, Mohamed R El Tohamy, Haytham O Tawfik, Sherif Ashraf Fahmy

Abstract readReview
In one paragraph

Review in Drug development research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

7 authors.

Mohamed S NafieDepartment of Chemistry, College of Sciences, University of Sharjah, Sharjah, United Arab Emirates.ORCID 0000-0003-4454-6390
Mohamed K DiabPest Physiology Department, Plant Protection Research Institute, Agricultural Research Center, Giza, Egypt.ORCID 0000-0001-7879-1357
Asmaa S A YassenDepartment of Medicinal Chemistry, Faculty of Pharmacy, Galala University, Egypt.
Amany M ElshamyMedical Laboratory Science Department, School of Allied Health Sciences, Badr University in Cairo (BUC), Badr City, Egypt.
Mohamed R El TohamyMedical Laboratory Science Department, School of Allied Health Sciences, Badr University in Cairo (BUC), Badr City, Egypt.
Haytham O TawfikDepartment of Pharmaceutical Chemistry, Faculty of Pharmacy, Tanta University, Tanta, Egypt.ORCID 0000-0001-6455-5716
Sherif Ashraf FahmyDepartment of Pharmacy, Institute of Pharmaceutics and Biopharmaceutics, Marburg University, Marburg, Germany.ORCID 0000-0003-3056-8281

Funding

Dr Mohamed S. Nafie appreciates the Seed Research Project No. (24021440154) funded by the Research and Graduate Studies at the University of Sharjah, United Arab Emirates. Dr. Sherif Ashraf Fahmy acknowledges the financial support and sponsorship received from the Alexander von Humboldt Foundation, Germany. Open Access funding was provided by the Open Access Publishing Fund of Marburg University to Dr. Sherif Ashraf Fahmy.
6 · The paper itself

Abstract

Proteolysis-targeting chimeras (PROTACs)-mediated protein degradation has been recently developed as a game-changing approach in oncology drug development. It represents a paradigm shift from traditional enzyme inhibition to selective protein degradation. PROTACs are different from regular small-molecule inhibitors because they are heterobifunctional compounds that use the ubiquitin-proteasome system to breakdown disease-causing oncogenic proteins. This review discusses the next generation of PROTAC platforms that innovate beyond traditional designs, such as dual-targeting PROTACS that present a novel mode of action, transcription factor-targeting PROTACs (TF-PROTACs), phosphorylation-dependent PROTACs (PhosphoTACs), and phosphorylation binding chimeras (PhosTACs). In kinase degradation, PROTACs have shown promise in addressing resistance mechanisms and carcinogenic drivers. Despite these advancements, issues with clinical pharmacokinetics, E3 ligase tissue selectivity, and subcellular localization persist. Additionally, the development of bio-responsive and spatially controlled PROTAC systems, such as photocaged and folate-caged PROTACs, was fully discussed, which achieves maximal precision in tumor selectivity. Furthermore, ARV-110 and ARV-471, as two representative PROTACs, have entered clinical trials, suggesting their potentially broader application. Accordingly, this review provides a critical overview of the design rationales, molecular mechanisms of action, therapeutic utilities, and synthetic issues associated with these innovative modalities, focusing on on their translational implication and pharmacokinetic limitations, as well as potential future clinical applications.

Indexed as

Antineoplastic AgentsNeoplasmsProteolysisAnimalsDrug DevelopmentHumansPrecision MedicineAntineoplastic Agentsclinical developmentdual‐target degradersfolate‐caged PROTACsphosphoTACsphotocaged PROTACsPROTACstargeted protein degradationTF‐PROTACsubiquitin‐proteasome system

Identifiers

PMID41362117
PMCPMC12686766

What Socratic holds

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LicenceCC BY
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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 Socratic graph.