ArticleJournal of molecular evolution1993
The evolutionary relationship of avian and mammalian myosin heavy-chain genes.
Article in Journal of molecular evolution, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 37 citations in OpenAlex.
- The genome of the diploid anuran Xenopus tropicalis contains a novel array of sarcoplasmic myosin heavy chain genes expressed in larval muscle and larynx.Development genes and evolution · 2008Article
- Reversible Ca2+-induced fast-to-slow transition in primary skeletal muscle culture cells at the mRNA level.The Journal of physiology · 2000Article
- Four novel myosin heavy chain transcripts define a molecular basis for muscle fibre types in Rana pipiens.The Journal of physiology · 1998Article
- Strong evolutionary conservation of broadly expressed protein isoforms in the troponin I gene family and other vertebrate gene families.Journal of molecular evolution · 1996Article
- Concerted evolution of mammalian cardiac myosin heavy chain genes.Journal of molecular evolution · 1995Article
- Development and postnatal regulation of adult myoblasts.Microscopy research and technique · 1995Review
- Ceruloplasmin gene defect associated with epilepsy in EL mice.Nature genetics · 1994Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Sequence comparisons of avian and mammalian skeletal and cardiac myosin heavy-chain isoforms are used to examine the evolutionary relationships of sarcomeric myosin multigene families. Mammalian fast-myosin heavy-chain isoforms from different species, with comparable developmental expression, are more similar to each other than they are to other fast isoforms within the same genome. In contrast, the developmentally regulated chicken fast isoforms are more similar to each other than they are to myosin heavy-chain isoforms in other species. Extensive regions of nucleotide identity among the chicken fast myosin heavy chains and in the mouse and rat alpha- and beta-cardiac myosin heavy-chain sequences suggest that gene-conversion-like mechanisms have played a major role in the concerted evolution of these gene families. We also conclude that the chicken fast myosin heavy-chain multigene family has undergone recent expansion subsequent to the divergence of birds and mammals and that both the developmental regulation and the specialization of myosin isoforms have likely developed independently in birds and mammals.
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