ArticleJournal of muscle research and cell motility1993
In vitro production of enzymatically active myosin heavy chain.
Article in Journal of muscle research and cell motility, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
2 citing papers in PubMed.
- Virus-free transfection, transient expression, and purification of human cardiac myosin in mammalian muscle cells for biochemical and biophysical assays.Scientific reports · 2023Article
- Segregated assembly of muscle myosin expressed in nonmuscle cells.Molecular biology of the cell · 1993Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In order to initiate studies on the structural and functional relationships of the myosin heavy chain, we constructed a full-length complementary DNA encoding the isoform that is found in the fast white muscle of the embryonic chicken. The complementary DNA contained 108 basepairs of its 3'-untranslated region and was preceded by a leader sequence derived from the alfalfa mosaic virus. Similarly, a complementary DNA encoding 963 amino acids which encompass the subfragment-1 of myosin and part of the subfragment-2 was also constructed. Each was inserted into the expression vector pMT2 and transiently transfected into COS-1 cells. Both constructs directed the expression of the respective proteins, each of which was immunogenic. The full-length and subfragment-1 proteins interacted with actin and demonstrated high levels of a K(+)-activated, EDTA-resistant ATPase activity, which is characteristic of myosin.
Indexed as
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.