ArticleAnalytical chemistry2026
Native Mass Spectrometry Analysis of Cullin-RING Ubiquitin E3 Ligase Complexes in the Context of Targeted Protein Degradation.
Article in Analytical chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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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.
The trial behind it
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Who cites it
2 citing papers in PubMed.
- Methods to Study the Molecular Mechanism and Drive the Design of Protein Degraders.Chemical reviews · 2026Review
- Interface Architecture of a VHL-PROTAC Complex with and without Cullin-2.Journal of the American Chemical Society · 2026Article
Corrections and comments
- Update of
Authors and funding
5 authors.
Funding
Abstract
The binding of PROTACs to their partner ubiquitin E3 ligase (E3) and a protein of interest (POI) is critical for PROTAC development and validation. Characterization of PROTAC complexes by cryo-electron microscopy and X-ray crystallography is not always feasible, especially where species may be transient and protein structures may not resolve due to flexible domains or intrinsically disordered regions or where the air-water interface poses risks such as dissociation. More routine biophysical methods with broader applicability to varied samples are essential to support the rapidly expanding targeted protein degradation field. The majority of PROTACs in development and in the clinic act through a Cullin-RING E3 ligase (CRL), of which the pentameric von Hippel-Lindau (VHL) Cullin 2 RING E3 complex (CRL2
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Registered trials
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