ArticleRSC advances2021
Discovery of fragments inducing conformational effects in dynamic proteins using a second-harmonic generation biosensor.
Article in RSC advances, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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Who cites it
4 citing papers in PubMed, 11 citations in OpenAlex.
- Ligand-induced conformations and dynamic allosteric motions of IDO1 affecting the recruitment of a protein signaling partner.Communications chemistry · 2025Article
- Target Engagement Assays in Early Drug Discovery.Journal of medicinal chemistry · 2025Review
- Ligand-induced conformational changes in protein molecules detected by sum-frequency generation.Biophysical journal · 2024Article
- Identification of fragments targeting SMYD3 using highly sensitive kinetic and multiplexed biosensor-based screening.RSC medicinal chemistry · 2024Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biophysical screening of compound libraries for the identification of ligands that interact with a protein is efficient, but does typically not reveal if (or how) ligands may interfere with its functional properties. For this a biochemical/functional assay is required. But for proteins whose function is dependent on a conformational change, such assays are typically complex or have low throughput. Here we have explored a high-throughput second-harmonic generation (SHG) biosensor to detect fragments that induce conformational changes upon binding to a protein in real time and identify dynamic regions. Multiwell plate format SHG assays were developed for wild-type and six engineered single-cysteine mutants of acetyl choline binding protein (AChBP), a homologue to ligand gated ion channels (LGICs). They were conjugated with second harmonic-active labels
Identifiers
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Registered trials
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