ArticleJournal of muscle research and cell motility1991
Fish myosin alkali light chains originate from two different genes.
Article in Journal of muscle research and cell motility, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed, 22 citations in OpenAlex.
- Myosin light chain of shark fast skeletal muscle exhibits intrinsic urea-resistibility.Scientific reports · 2023Article
- Identification and analysis of muscle-related protein isoforms expressed in the white muscle of the mandarin fish (Siniperca chuatsi).Marine biotechnology (New York, N.Y.) · 2011Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
We have determined the amino acid sequences of mullet white skeletal muscle myosin alkali light chains, LC1 and LC3. These are the first available fish myosin sequences. There are 29 differences between the mullet LC1 and LC3 sequences, spread throughout all regions of their polypeptide chains, leading us to conclude that fish myosin alkali light chains originate from two different genes. This finding is in sharp contrast to all previous studies on vertebrate fast skeletal muscle myosins, which showed that in birds and mammals LC1 and LC3 are produced from a single gene by alternative RNA transcription and splicing, yielding proteins which differ only in their N-terminal segments.
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