ArticleNano letters2018
Nanothermometry Reveals Calcium-Induced Remodeling of Myosin.
Article in Nano letters, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- (Invited) Influence of NdChemistry, an Asian journal · 2025Article
- Quantum dot-based thermometry uncovers decreased myosin efficiency in an experimental intensive care unit model.Frontiers in physiology · 2024Article
- Differences in pork myosin solubility and structure with various chloride salts and their property of pork gel.Journal of animal science and technology · 2023Article
- Muscle Mechanics and Thick Filament Activation: An Emerging Two-Way Interaction for the Vertebrate Striated Muscle Fine Regulation.International journal of molecular sciences · 2023Review
- CaProtein science : a publication of the Protein Society · 2022Article
- Secondary Structure of the Novel Myosin Binding Domain WYR and Implications within Myosin Structure.Biology · 2021Article
- Probing the subcellular nanostructure of engineered human cardiomyocytes in 3D tissue.Microsystems & nanoengineering · 2021Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Ions greatly influence protein structure-function and are critical to health and disease. A 10, 000-fold higher calcium in the sarcoplasmic reticulum (SR) of muscle suggests elevated calcium levels near active calcium channels at the SR membrane and the impact of localized high calcium on the structure-function of the motor protein myosin. In the current study, combined quantum dot (QD)-based nanothermometry and circular dichroism (CD) spectroscopy enabled detection of previously unknown enthalpy changes and associated structural remodeling of myosin, impacting its function following exposure to elevated calcium. Cadmium telluride QDs adhere to myosin, function as thermal sensors, and reveal that exposure of myosin to calcium is exothermic, resulting in lowering of enthalpy, a decrease in alpha helical content measured using CD spectroscopy, and the consequent increase in motor efficiency. Isolated muscle fibers subjected to elevated levels of calcium further demonstrate fiber lengthening and decreased motility of actin filaments on myosin-functionalized substrates. Our results, in addition to providing new insights into our understanding of muscle structure-function, establish a novel approach to understand the enthalpy of protein-ion interactions and the accompanying structural changes that may occur within the protein molecule.
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Registered trials
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