ArticleThe Journal of biological chemistry1992
Localization and characterization of a 7.3-kDa region of caldesmon which reversibly inhibits actomyosin ATPase activity.
Article in The Journal of biological chemistry, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
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Who cites it
12 citing papers in PubMed, 28 citations in OpenAlex.
- Calponin (CaP) as a latch-bridge protein--a new concept in regulation of contractility in smooth muscles.Journal of muscle research and cell motility · 2004Review
- Characterization of the functional properties of smooth muscle caldesmon domain 4a: evidence for an independent inhibitory actin-tropomyosin binding domain.The Biochemical journal · 1998Article
- Inhibition of cross-bridge binding to actin by caldesmon fragments in skinned skeletal muscle fibers.Biophysical journal · 1997Article
- The size and shape of caldesmon and its fragments in solution studied by dynamic light scattering and hydrodynamic model calculations.Biophysical journal · 1997Article
- Multiple-sited interaction of caldesmon with Ca(2+)-calmodulin.The Biochemical journal · 1996Article
- Flexation of caldesmon: effect of conformation on the properties of caldesmon.Journal of muscle research and cell motility · 1995Article
- Article
- Kinetics of binding of caldesmon to actin.The Journal of biological chemistry · 1995Article
- Overexpression, purification, and characterization of full-length and mutant caldesmons using a baculovirus expression system.Journal of muscle research and cell motility · 1994Article
- Characterization of a caldesmon fragment that competes with myosin-ATP binding to actin.Biophysical journal · 1993Article
- Reversal of caldesmon binding to myosin with calcium-calmodulin or by phosphorylating caldesmon.The Journal of biological chemistry · 1993Article
- Caldesmon and a 20-kDa actin-binding fragment of caldesmon inhibit tension development in skinned gizzard muscle fiber bundles.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Cleavage of caldesmon with chymotrypsin yields a series of fragments which bind both calmodulin and actin and inhibit the binding of myosin subfragments to actin and the subsequent stimulation of ATPase activity. Several of these fragments have been purified by cation exchange chromatography and their amino-terminal sequences determined. The smallest fragment has a molecular mass of about 7.3 kDa and extends from Leu597 to Phe665. This polypeptide inhibits the actin-activated ATPase of myosin S-1; this inhibition is augmented by smooth muscle tropomyosin and relieved by Ca(2+)-calmodulin. The binding of the 7.3-kDa fragment to actin is competitive with the binding of S-1 to actin. Thus, this polypeptide has several of the important features characteristic of intact caldesmon. However, although an intact caldesmon molecule covers between six and nine actin monomers, the 7.3-kDa fragment binds to actin in a 1:1 complex. Comparison of this fragment with others suggests that a small region of caldesmon is responsible for at least part of the interaction with both calmodulin and actin.
Indexed as
Identifiers
1386604PMC1262679W1566196370What OpenQuestion holds
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.