ArticleStructure (London, England : 1993)2010
Pi release from myosin: a simulation analysis of possible pathways.
Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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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
29 citing papers in PubMed.
- The Twisting and Untwisting of Actin and Tropomyosin Filaments Are Involved in the Molecular Mechanisms of Muscle Contraction, and Their Disruption Can Result in Muscle Disorders.International journal of molecular sciences · 2025Review
- The order of things: phosphate release or the power stroke, which does actomyosin do first?Frontiers in physiology · 2025Review
- Homologous mutations in human β, embryonic, and perinatal muscle myosins have divergent effects on molecular power generation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Phosphate rebinding induces force reversal via slow backward cycling of cross-bridges.Frontiers in physiology · 2024Article
- Molecular mechanisms of inorganic-phosphate release from the core and barbed end of actin filaments.Nature structural & molecular biology · 2023Article
- A mutation in switch I alters the load-dependent kinetics of myosin Va.Nature communications · 2023Article
- Multistep orthophosphate release tunes actomyosin energy transduction.Nature communications · 2022Article
- Cryo-EM structure of the autoinhibited state of myosin-2.Science advances · 2021Article
- A reverse stroke characterizes the force generation of cardiac myofilaments, leading to an understanding of heart function.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structural basis for power stroke vs. Brownian ratchet mechanisms of motor proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Overview of the mechanism of cytoskeletal motors based on structure.Biophysical reviews · 2018Review
- Allosteric modulation of cardiac myosin dynamics by omecamtiv mecarbil.PLoS computational biology · 2017Article
- Molecular mechanisms underlying deoxy-ADP.Pi activation of pre-powerstroke myosin.Protein science : a publication of the Protein Society · 2017Article
- Temperature effect on the chemomechanical regulation of substeps within the power stroke of a single Myosin II.Scientific reports · 2016Article
- A gating mechanism for Pi release governs the mRNA unwinding by eIF4AI during translation initiation.Nucleic acids research · 2015Article
- How actin initiates the motor activity of Myosin.Developmental cell · 2015Article
- Structural dynamics of myosin 5 during processive motion revealed by interferometric scattering microscopy.eLife · 2015Article
- Trapping the ATP binding state leads to a detailed understanding of the F1-ATPase mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- A new mechanokinetic model for muscle contraction, where force and movement are triggered by phosphate release.Journal of muscle research and cell motility · 2014Article
- Phosphate release coupled to rotary motion of F1-ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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3 authors.
Funding
Abstract
The release of phosphate (Pi) is an important element in actomyosin function and has been shown to be accelerated by the binding of myosin to actin. To provide information about the structural elements important for Pi release, possible escape pathways from various isolated myosin II structures have been determined by molecular dynamics simulations designed for studying such slow processes. The residues forming the pathways were identified and their role was evaluated by mutant simulations. Pi release is slow in the pre-powerstroke structure, an important element in preventing the powerstroke prior to actin binding, and is much more rapid for Pi modeled into the post-rigor and rigor-like structures. The previously proposed backdoor route is dominant in the pre-powerstroke and post-rigor states, whereas a different path is most important in the rigor-like state. This finding suggests a mechanism for the actin-activated acceleration of Pi release.
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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.