Evidence map›Paper›PMID 42797522›Full record

ReviewPharmaceuticals (Basel, Switzerland)2026

Hydrophobic Tag Protein Degraders: An Emerging Therapeutic Strategy for Cancer.

Tania Aguilera-Pineda, Siddhartha Kumar, Gargi Ghosal, Amarnath Natarajan, Adam R Karpf

Abstract readReview
In one paragraph

Review in Pharmaceuticals (Basel, Switzerland), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Tania Aguilera-PinedaEppley Institute for Research in Cancer, University of Nebraska Medical Center, Omaha, NE 68198, USA.
Siddhartha KumarDivision of Pharmaceutical Sciences, James L. Winkle College of Pharmacy, Department of Internal Medicine, College of Medicine, University of Cincinnati, Cincinnati, OH 45229, USA.ORCID 0000-0002-6794-2794
Gargi GhosalThe Fred & Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE 68198, USA.ORCID 0000-0001-8399-5354
Amarnath NatarajanDivision of Pharmaceutical Sciences, James L. Winkle College of Pharmacy, Department of Internal Medicine, College of Medicine, University of Cincinnati, Cincinnati, OH 45229, USA.ORCID 0000-0001-5067-0203
Adam R KarpfEppley Institute for Research in Cancer, University of Nebraska Medical Center, Omaha, NE 68198, USA.ORCID 0000-0002-0866-0666

Funding

UNMC/EPPLEY CANCER CENTER SUPPORT GRANTP30CA036727 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI James Eudy · 1985 to 2026
$55.0M
Targeting RHNO1 in Ovarian CancerR21CA273399 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI KARPF, ADAM R. · 2023 to 2024
$384k
NCI NIH HHS P30 CA036727NCI NIH HHS R21 CA273399
6 · The paper itself

Abstract

Hydrophobic tag degraders (HyTDs) are a promising strategy for achieving targeted protein degradation (TPD). HyTDs are composed of a hydrophobic moiety conjugated via a linker to a ligand that binds to the protein of interest (POI). Binding induces a surface-exposed hydrophobic patch that mimics a misfolded protein, triggering degradation through the cell's diverse quality-control networks, including the ubiquitin-proteasome system (UPS), ubiquitin-independent proteasome degradation (UbInPD), the autophagy-lysosome pathway (ALP), and the unfolded protein response (UPR). This distinct multi-pathway mechanism distinguishes HyTDs from traditional TPD strategies such as PROTACs and molecular glue degraders (MGDs), which rely on a narrow pool of specific E3 ligases. The effectiveness of HyTDs is influenced by the chemical properties of the hydrophobic moiety, the linker, and the ligand's binding kinetics to the POI. To date, several relevant cancer targets, including the androgen receptor (AR), AKT serine/threonine kinase 3 (Akt3), and enhancer of zeste homolog 2 (EZH2), have been successfully targeted using HyTDs. Gaining deeper mechanistic insight into the nature of HyT degradation will be essential to further the potential of HyTDs as powerful tools in cancer research and therapeutics.

Indexed as

cancer therapyhydrophobic tag degradersHyTD designmechanism of actiontarget protein degradation

Identifiers

PMID42797522
PMCPMC13609999

What Socratic 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 Socratic graph.