ArticleThe Biochemical journal1997
Correlation between calponin and myosin subfragment 1 binding to F-actin and ATPase inhibition.
Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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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
1 citing paper in PubMed, 8 citations in OpenAlex.
- Cytoskeletal targeting of calponin in differentiated, contractile smooth muscle cells of the ferret.The Journal of physiology · 1998Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Calponin is a thin-filament-associated protein that has been implicated in the regulation of smooth-muscle contractility. It binds to F-actin and inhibits the MgATPase activity of actomyosin. In the present work we have examined the effect of recombinant chicken gizzard alpha-calponin (R alpha CaP) on the binding of rabbit skeletal-muscle myosin subfragment 1 (S1) to F-actin and on the inhibition of its actin-activated MgATPase. We have found that binding of one R alpha CaP molecule to every three to four actin monomers is sufficient for maximal inhibition of acto-S1 ATPase. At this R alpha CaP/actin ratio R alpha CaP does not interfere with S1 binding to F-actin. At higher concentrations, R alpha CaP displaces S1 from F-actin and a 1:1 R alpha CaP-actin monomer complex is formed. R alpha CaP is also able to displace troponin I from its complex with F-actin which may reflect the amino acid sequence similarity between R alpha CaP and troponin I in their actin-binding regions.
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