ArticleNature communications2021
The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 33 citations in OpenAlex.
- Article
- Antimalarial cytoskeletal targeting with broad apicomplexan activity.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Dynamics of the β-cardiac myosin auto-inhibited state explain cardiomyopathy pathogenesis.Nature communications · 2026Article
- Article
- Integrated structural model of the palladin-actin complex using XL-MS, docking, NMR, and SAXS.Protein science : a publication of the Protein Society · 2025Article
- Coupling between the lever arm and active site via an N-terminal extension tunes force sensitivity in the myosin-1 family.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- High-resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- High resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory.bioRxiv : the preprint server for biology · 2025Article
- Biochemical characterization of cardiac α-actin mutations A21V and D26N implicated in hypertrophic cardiomyopathy.Cytoskeleton (Hoboken, N.J.) · 2024Article
- Super-relaxed myosins contribute to respiratory muscle hibernation in mechanically ventilated patients.Science translational medicine · 2024Article
- Article
- Mechanism of small molecule inhibition of Plasmodium falciparum myosin A informs antimalarial drug design.Nature communications · 2023Article
- Cryo-EM structure of the folded-back state of human β-cardiac myosin.Nature communications · 2023Article
- Cryo-EM structure of the folded-back state of human β-cardiac myosin.bioRxiv : the preprint server for biology · 2023Article
- Acetylation of fission yeast tropomyosin does not promote differential association with cognate formins.Cytoskeleton (Hoboken, N.J.) · 2023Article
- Helical ultrastructure of the metalloprotease meprin α in complex with a small molecule inhibitor.Nature communications · 2022Article
- High-resolution structures of malaria parasite actomyosin and actin filaments.PLoS pathogens · 2022Article
- Discovery of ultrafast myosin, its amino acid sequence, and structural features.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
- Review
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
Abstract
Plasmodium falciparum, the causative agent of malaria, moves by an atypical process called gliding motility. Actomyosin interactions are central to gliding motility. However, the details of these interactions remained elusive until now. Here, we report an atomic structure of the divergent Plasmodium falciparum actomyosin system determined by electron cryomicroscopy at the end of the powerstroke (Rigor state). The structure provides insights into the detailed interactions that are required for the parasite to produce the force and motion required for infectivity. Remarkably, the footprint of the myosin motor on filamentous actin is conserved with respect to higher eukaryotes, despite important variability in the Plasmodium falciparum myosin and actin elements that make up the interface. Comparison with other actomyosin complexes reveals a conserved core interface common to all actomyosin complexes, with an ancillary interface involved in defining the spatial positioning of the motor on actin filaments.
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Registered trials
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 OpenQuestion graph.