ArticleThe Journal of biological chemistry2018
High-throughput screen, using time-resolved FRET, yields actin-binding compounds that modulate actin-myosin structure and function.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 24 citations in OpenAlex.
- Modulation of striated-muscle contractility by a high-affinity myosin-targeting peptide.Biophysical journal · 2025Article
- Detection speed optimization of the OI-RD microscope for ultra-high throughput screening.Biomedical optics express · 2023Article
- Synergistic FRET assays for drug discovery targeting RyR2 channels.Journal of molecular and cellular cardiology · 2022Article
- Actin-binding compounds, previously discovered by FRET-based high-throughput screening, differentially affect skeletal and cardiac muscle.The Journal of biological chemistry · 2020Article
- Strategies for targeting the cardiac sarcomere: avenues for novel drug discovery.Expert opinion on drug discovery · 2020Review
- Actin-Myosin Interaction: Structure, Function and Drug Discovery.International journal of molecular sciences · 2018Review
- Getting site-specific with actomyosin inhibitors.The Journal of biological chemistry · 2018Article
- Novel drug discovery platform for spinocerebellar ataxia, using fluorescence technology targeting β-III-spectrin.The Journal of biological chemistryArticle
- Mechanistic analysis of actin-binding compounds that affect the kinetics of cardiac myosin-actin interaction.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
We have used a novel time-resolved FRET (TR-FRET) assay to detect small-molecule modulators of actin-myosin structure and function. Actin-myosin interactions play crucial roles in the generation of cellular force and movement. Numerous mutations and post-translational modifications of actin or myosin disrupt muscle function and cause life-threatening syndromes. Here, we used a FRET biosensor to identify modulators that bind to the actin-myosin interface and alter the structural dynamics of this complex. We attached a fluorescent donor to actin at Cys-374 and a nonfluorescent acceptor to a peptide containing the 12 N-terminal amino acids of the long isoform of skeletal muscle myosin's essential light chain. The binding site on actin of this acceptor-labeled peptide (ANT) overlaps with that of myosin, as indicated by (
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Registered trials
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