Evidence map›Paper›PMID 41735327›Full record

ArticleNature communications2026

Heterobifunctional proteomimetic polymers for targeted degradation of MYC and KRAS.

Max M Wang, Mihai I Truica, Brayley S Gattis, Julia Oktawiec, Vinay Sagar, Ananya A Basu, Paul A Bertin, Xiaoyu Zhang, Sarki A Abdulkadir, Nathan C Gianneschi

Abstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Emerging biologic modalities for targeted protein degradation.The Journal of biological chemistry · 2026
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Max M Wang *Department of Chemistry, Northwestern University, Evanston, IL, USA.
Mihai I Truica *Department of Urology, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.ORCID 0000-0002-0866-1407
Brayley S GattisDepartment of Chemistry, Northwestern University, Evanston, IL, USA.
Julia OktawiecDepartment of Chemistry, Northwestern University, Evanston, IL, USA.
Vinay SagarDepartment of Urology, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.
Ananya A BasuDepartment of Chemistry, Northwestern University, Evanston, IL, USA.ORCID 0000-0002-1427-5326
Paul A BertinGrove Biopharma, Inc., Chicago, IL, USA.
Xiaoyu ZhangDepartment of Chemistry, Northwestern University, Evanston, IL, USA.ORCID 0000-0002-0951-9664
Sarki A AbdulkadirDepartment of Urology, Northwestern University Feinberg School of Medicine, Chicago, IL, USA. sarki.abdulkadir@northwestern.edu.ORCID 0000-0003-2963-2899
Nathan C GianneschiDepartment of Chemistry, Northwestern University, Evanston, IL, USA. nathan.gianneschi@northwestern.edu.ORCID 0000-0001-9945-5475

Funding

National Science Foundation (NSF) 0960140National Science Foundation (NSF) NSF-GRFP No. DGE-1842165U.S. Department of Health & Human Services | National Institutes of Health (NIH) 5F30CA250196U.S. Department of Health & Human Services | National Institutes of Health (NIH) 5F30CA257519U.S. Department of Health & Human Services | NIH | National Cancer Institute (NCI) NCI CCSG P30 CA060553
6 · The paper itself

Abstract

Targeted protein degradation (TPD) has enabled modulation of previously undruggable proteins. However, existing small-molecule approaches require arduous optimization and are largely confined to targets bearing ligandable pockets. To address these challenges, we introduce the HYbrid DegRAding Copolymer (HYDRAC), a polymeric platform that integrates target‑binding peptides with peptide-based or small‑molecule degrons to orchestrate selective degradation of disease‑relevant proteins. HYDRACs are amenable to scalable synthetic methods, exhibit broad structural tunability, and support multivalent payload conjugation. This intrinsic modularity enables incorporation of a diverse repertoire of target‑binding motifs and E3‑ligase recruiters. These include von Hippel-Lindau protein (VHL), Kelch-like ECH-associated protein 1 (KEAP1), and Cereblon (CRBN). We deploy HYDRACs against two historically intractable targets, Myelocytomatosis proto-oncogene (MYC) and Kirsten rat sarcoma viral oncogene homolog (KRAS), achieving potent degradation in vitro and durable tumor suppression in murine models. Notably, HYDRACs bearing consensus RAS-binding motifs effectuate degradation of KRAS across multiple alleles, suggesting pan‑KRAS potential. We envision HYDRACs as a generalizable paradigm that substantially expands the TPD armamentarium.

Indexed as

PolymersProto-Oncogene Proteins c-mycProto-Oncogene Proteins p21(ras)AnimalsCell Line, TumorDegronsHumansMicePeptidesProteolysisProteolysis Targeting ChimeraProto-Oncogene MasVon Hippel-Lindau Tumor Suppressor ProteinKRAS protein, humanMAS1 protein, humanMYC protein, humanPeptidesPolymersProteolysis Targeting ChimeraProto-Oncogene MasProto-Oncogene Proteins c-mycProto-Oncogene Proteins p21(ras)Von Hippel-Lindau Tumor Suppressor Protein

Identifiers

PMID41735327
PMCPMC12932639

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Registered trials

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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.