ArticleJournal of muscle research and cell motility1988
Identification and distribution of some developmental isoforms of myosin heavy chains in avian muscle fibres.
Article in Journal of muscle research and cell motility, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Evidence for differential post-translational modifications of slow myosin heavy chain during murine skeletal muscle development.Journal of muscle research and cell motility · 2000Article
- Both avian and mammalian embryonic myoblasts are intrinsically heterogeneous.Journal of muscle research and cell motility · 1998Article
- Evidence for distinct fast and slow myogenic cell lineages in human foetal skeletal muscle.Journal of muscle research and cell motility · 1998Article
- The chicken muscle thick filament: temperature and the relaxed cross-bridge arrangement.Journal of muscle research and cell motility · 1995Article
- Familial fetal akinesia deformation sequence with a skeletal muscle maturation defect.Acta neuropathologica · 1995Article
- Mammalian myoblasts become fast or slow myocytes within the somitic myotome.Journal of muscle research and cell motility · 1994Article
- Article
- Heterogeneity and distribution of fast myosin heavy chains in some adult vertebrate skeletal muscles.Histochemistry · 1992Article
- Characterization of myosin isoforms in satellite cell cultures from adult rat diaphragm, soleus and tibialis anterior muscles.Differentiation; research in biological diversity · 1990Article
- Expression of an alpha cardiac-like myosin heavy chain in muscle spindle fibres.Histochemistry · 1990Article
- Influence of neonatal motor denervation on expression of myosin heavy chain isoforms in rat muscle spindles.Histochemistry · 1990Article
- Expression of myosin heavy chain isoforms in developing rat muscle spindles.Histochemistry · 1990Article
- Diversity in expression of myosin heavy chain isoforms and M-band proteins in rat muscle spindles.Histochemistry · 1989Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two monoclonal antibodies that react with all the slow skeletal myosin heavy chains in the mammalian skeletal muscles appeared to react with only SM1 myosin heavy chain in the post-hatch muscles of chicken. Further studies on the developing chicken showed one of these two antibodies to react with an additional myosin heavy chain in the early embryonic skeletal muscle as well as with the cardiac muscle. It is concluded that this antibody identified a slow muscle-like embryonic isoform of myosin heavy chain during earlier stages of development. While this embryonic isoform was more abundant during early development, the synthesis of SM1 myosin heavy chain was restricted to only presumptive slow muscle cells.
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