ArticleJournal of muscle research and cell motility1989
Comparative study of invertebrate actins: antigenic cross-reactivity versus sequence variability.
Article in Journal of muscle research and cell motility, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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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
4 citing papers in PubMed, 9 citations in OpenAlex.
- Molecular Characterization of a Novel Shell Matrix Protein With PDZ Domain FromFrontiers in physiology · 2020Article
- Interaction of skeletal-muscle myosin subfragment-1 with the actin-(338-348) peptide.The Biochemical journal · 1994Article
- Characterization and fine-structural localization of actin- and fibronectin-like proteins in planaria (Dugesia lugubris s.l.).Cell and tissue research · 1992Article
- Characterization of an actin-myosin head interface in the 40-113 region of actin using specific antibodies as probes.The Biochemical journal · 1990Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The immunological similarities or differences between various actins from muscles of invertebrates were investigated. We elicited antibodies to actin purified from the adductor muscle of the mollusc, Pecten maximus. The antiserum comprised a major population that was specific for the N-terminal extremity of this isoform. This antibody population was used together with other antibodies specific for various domains on the surface of skeletal muscle actin to compare seven actins from invertebrate muscles. The N-terminal extremity showed close homologies between invertebrates (except for Crustacea) but differences were observed with vertebrate skeletal and cytoplasmic actins. In contrast, sequence 18-28, which constitutes part of the myosin interaction domain, appears to be conserved in all actins studied. Other regions (sequences 40-113, 168-226 and 285-375) presented a variable behaviour depending on the particular invertebrate species.
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Registered trials
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