ArticleChembiochem : a European journal of chemical biology2018
Dual Labeling of the CBP/p300 KIX Domain for
Article in Chembiochem : a European journal of chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Methods for the Investigation of Protein-Ligands Interactions.Advances in experimental medicine and biology · 2026Review
- Leveraging relaxation-optimizedNature chemistry · 2025Article
- Fluorine-Thiol Displacement Stapling on the Disordered αSynlett : accounts and rapid communications in synthetic organic chemistry · 2025Article
- Review
- Inhibition of CREB Binding and Function with a Dual-Targeting Ligand.Biochemistry · 2024Article
- Garcinolic Acid Distinguishes Between GACKIX Domains and Modulates Interaction Networks.Chembiochem : a European journal of chemical biology · 2023Article
- Review
- 2-Fluorotyrosine is a valuable but understudied amino acid for protein-observedJournal of biomolecular NMR · 2020Article
- SAR by (Protein-Observed)Accounts of chemical research · 2019Review
- Modulating the masters: chemical tools to dissect CBP and p300 function.Current opinion in chemical biology · 2018Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Protein-Observed Fluorine NMR (PrOF NMR) spectroscopy is an emerging technique for screening and characterizing small-molecule-protein interactions. The choice of which amino acid to label for PrOF NMR can be critical for analysis. Here we report the first use of a protein containing two different fluoroaromatic amino acids for NMR studies. Using the KIX domain of the CBP/p300 as a model system, we examine ligand binding of several small-molecule compounds elaborated from our previous fragment screen and identify a new ligand binding site distinct from those used by native transcription factors. This site was further supported by computational modeling (FTMap and Schrödinger) and
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Registered trials
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