ArticleBiophysical journal1993
Characterization of a caldesmon fragment that competes with myosin-ATP binding to actin.
Article in Biophysical journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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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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
7 citing papers in PubMed, 16 citations in OpenAlex.
- Myosin II is involved in the production of constitutive transport vesicles from the TGN.The Journal of cell biology · 1997Article
- Inhibition of cross-bridge binding to actin by caldesmon fragments in skinned skeletal muscle fibers.Biophysical journal · 1997Article
- Radial equilibrium lengths of actomyosin cross-bridges in muscle.Biophysical journal · 1996Article
- The effects of caldesmon extraction on mechanical properties of skinned smooth muscle fibre preparations.Pflugers Archiv : European journal of physiology · 1996Article
- Flexation of caldesmon: effect of conformation on the properties of caldesmon.Journal of muscle research and cell motility · 1995Article
- Alignment of caldesmon on the actin-tropomyosin filaments.The Biochemical journal · 1995Article
- Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The protein caldesmon inhibits actin-activated ATP hydrolysis of myosin and inhibits the binding of myosin.ATP to actin. A fragment isolated from a chymotryptic digest of caldesmon contains features of the intact molecule that make it useful as a selective inhibitor of the binding of myosin.ATP complexes to actin without having the complexity of binding to myosin. The COOH-terminal 20 kDa region of caldesmon binds to actin with one-sixth the affinity of caldesmon with a stoichiometry of binding of one fragment per two actin monomers. This contrasts with the 1:6-9 stoichiometry of intact caldesmon. The binding of the 20 kDa fragments to actin is totally reversed by Ca(2+)-calmodulin and, like intact caldesmon, the 20 kDa fragments are competitive with the binding of myosin subfragments to actin. This competition with myosin binding is largely responsible for the inhibition of ATP hydrolysis, although both the fragments and intact caldesmon also reverse the potentiation of ATPase activity caused by tropomyosin. These polypeptides are useful both in defining the function of caldesmon and in studying the role of weakly bound cross-bridges in muscle.
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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.