The DOI matches its Crossref record; 26 of the 27 references it cites were found in a registry or an index.
Fast and slow myosin within single skeletal muscle fibres of adult rabbits
Abstract
There is good evidence for the coexistence of different myosin types both in developing muscles and in Purkinje cells from adult chicken hearts. In skeletal muscle fibres of adult animals, however, coexistence of fast (FM) and slow (SM) myosin has only been demonstrated after long-term electrical stimulation. The term 'promiscuity' has recently been coined to describe the coexistence of different myosin isoenzymes within a single fibre. Using novel, refined immunological methods we demonstrate here the presence of both FM and SM within single fibres of the musculus tibialis anterior of adult rabbits. Essentially identical results were also obtained with other muscles. Our findings imply that the genes coding for FM and SM can be expressed simultaneously within the same cell throughout an animal's entire life, and not only during development or after artificial electrical stimulation.
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“The gastrocnemii and TA muscles consist of 'fast-twitch' fibers primarily [49], that are usually innervated by axons with higher conduction velocities [50].”
From Directed stimulation with interfascicular interfaces for peripheral nerve stimulation (2021) · cites this paper as [49]
Citations
Cites
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Research works printed but not linked: 1
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Immunochemical analysis of myosin heavy chain during avian myogenesis in vivo and in vitro.
Bader, D. M., Masaki, Τ., & Fischman, D. A. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.95.3.763 · Cited by 919
Cellular and molecular diversities of mammalian skeletal muscle fibers
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The adaptive response of skeletal muscle to increased use
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Invited review: Neural control of phenotypic expression in mammalian muscle fibers
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Mammalian Skeletal Muscle Fiber Type Transitions
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Metadata
- Authors
- Lutz, H., Weber, H., Billeter, R., & Jenny, E.
- Affiliations
- University of Zurich (CH)
- ORCID
- Billeter, R.
- Venue
- Nature
- Published
- 1979-09
- Volume
- 281
- Issue
- 5727
- Pages
- 142-144
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2069007869
- Cited by
- 84
- References
- 27
- Citations by year
- 2024: 1 · 2021: 2 · 2017: 3 · 2013: 1
- FWCI
- 5.15
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Meat and Animal Product Quality
- Keywords
- fast myosin, slow myosin, myosin isoenzymes, skeletal muscle fibers, tibialis anterior, adult muscle, rabbits
- MeSH terms
- Animals, Immunologic Techniques, Isoenzymes, Kinetics, Muscle Contraction, Muscles, Myosins, Rabbits, Muscle Development
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