Evidence map›Paper›PMID 32123106›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

bioPROTACs as versatile modulators of intracellular therapeutic targets including proliferating cell nuclear antigen (PCNA).

Shuhui Lim, Regina Khoo, Khong Ming Peh, Jinkai Teo, Shih Chieh Chang, Simon Ng, Greg L Beilhartz, Roman A Melnyk, Charles W Johannes, Christopher J Brown and 3 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing 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

93 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. De Novo-Designed Bifunctional Proteins for Targeted Protein Degradation.Journal of the American Chemical Society · 2026
    Article
  7. Reductive Methylation: An Alternative to Lysine → Arginine Mutagenesis.Journal of peptide science : an official publication of the European Peptide Society · 2026
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Emerging biologic modalities for targeted protein degradation.The Journal of biological chemistry · 2026
    Review
  17. Article
  18. Article
  19. Review
  20. Article

33 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

13 authors.

Shuhui LimQuantitative Biosciences, MSD International, Singapore 138665.
Regina KhooQuantitative Biosciences, MSD International, Singapore 138665.
Khong Ming PehQuantitative Biosciences, MSD International, Singapore 138665.
Jinkai TeoPacific Translational Biomarkers, MSD International, Singapore 138665.
Shih Chieh ChangQuantitative Biosciences, MSD International, Singapore 138665.
Simon NgQuantitative Biosciences, MSD International, Singapore 138665.
Greg L BeilhartzMolecular Medicine, Hospital for Sick Children, Toronto, ON, Canada M5G 0A4.
Roman A MelnykMolecular Medicine, Hospital for Sick Children, Toronto, ON, Canada M5G 0A4.
Charles W Johannesp53Lab, Agency for Science, Technology and Research (A*STAR), Singapore 138648.
Christopher J Brownp53Lab, Agency for Science, Technology and Research (A*STAR), Singapore 138648.
David P Lanep53Lab, Agency for Science, Technology and Research (A*STAR), Singapore 138648.
Brian HenryQuantitative Biosciences, MSD International, Singapore 138665.
Anthony W PartridgeQuantitative Biosciences, MSD International, Singapore 138665; anthony_partridge@merck.com.ORCID 0000-0001-8568-2079

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Targeted degradation approaches such as proteolysis targeting chimeras (PROTACs) offer new ways to address disease through tackling challenging targets and with greater potency, efficacy, and specificity over traditional approaches. However, identification of high-affinity ligands to serve as PROTAC starting points remains challenging. As a complementary approach, we describe a class of molecules termed biological PROTACs (bioPROTACs)-engineered intracellular proteins consisting of a target-binding domain directly fused to an E3 ubiquitin ligase. Using GFP-tagged proteins as model substrates, we show that there is considerable flexibility in both the choice of substrate binders (binding positions, scaffold-class) and the E3 ligases. We then identified a highly effective bioPROTAC against an oncology target, proliferating cell nuclear antigen (PCNA) to elicit rapid and robust PCNA degradation and associated effects on DNA synthesis and cell cycle progression. Overall, bioPROTACs are powerful tools for interrogating degradation approaches, target biology, and potentially for making therapeutic impacts.

Indexed as

ProteolysisBinding SitesHEK293 CellsHumansMolecular Targeted TherapyProliferating Cell Nuclear AntigenProtein BindingProtein EngineeringRecombinant ProteinsUbiquitin-Protein LigasesProliferating Cell Nuclear AntigenRecombinant ProteinsUbiquitin-Protein LigasesbioPROTACPCNAtargeted degradation

Identifiers

PMID32123106
PMCPMC7084165

What OpenQuestion holds

Textmetadata
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.