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Changing face of contractile activation in striated muscle at physiological temperature
Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences. Linnaeus University, Linnaeus Knowledge Environments, Advanced Materials.ORCID iD: 0000-0002-5889-7792
2023 (English)In: The Journal of General Physiology, ISSN 0022-1295, E-ISSN 1540-7748, Vol. 155, no 12, article id e202313494Article in journal, Editorial material (Other academic) Published
Abstract [en]

Calcium binding to troponin, with subsequent displacement of its linked tropomyosin molecule on the thin filament surface, cooperates with myosin binding to actin in the contractile regulation of striated muscle. The intertwined role of these systems is studied in the present issue of JGP by Ishii et al. (https://doi.org/10.1085/jgp.202313414). A particularly interesting feature of the paper, except for studying both skeletal and cardiac muscle proteins, is that the experiments unlike most other similar studies are performed at physiological temperature (35-40(degrees)C).

Place, publisher, year, edition, pages
Rockefeller University Press, 2023. Vol. 155, no 12, article id e202313494
National Category
Biochemistry Molecular Biology Physiology and Anatomy
Research subject
Chemistry, Biochemistry
Identifiers
URN: urn:nbn:se:lnu:diva-125904DOI: 10.1085/jgp.202313494ISI: 001101157800001PubMedID: 37934475OAI: oai:DiVA.org:lnu-125904DiVA, id: diva2:1817845
Available from: 2023-12-07 Created: 2023-12-07 Last updated: 2025-03-19Bibliographically approved

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Månsson, Alf

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  • ieee
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  • de-DE
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