ArticleJournal of muscle research and cell motility1993
Identification of functioning regulatory sites and a new myosin binding site in the C-terminal 288 amino acids of caldesmon expressed from a human clone.
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 12 papers.
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Who cites it
12 citing papers in PubMed, 29 citations in OpenAlex.
- Article
- Correlation between proteome changes and synchrony of cardiac electrical excitation under 3-day «dry immersion» conditions.Frontiers in physiology · 2023Article
- Phenotypic and proteomic characteristics of human dental pulp derived mesenchymal stem cells from a natal, an exfoliated deciduous, and an impacted third molar tooth.Stem cells international · 2014Article
- Caldesmon and the regulation of cytoskeletal functions.Advances in experimental medicine and biology · 2008Review
- Smooth muscle myosin filament assembly under control of a kinase-related protein (KRP) and caldesmon.Journal of muscle research and cell motility · 2002Article
- Characterization of the functional properties of smooth muscle caldesmon domain 4a: evidence for an independent inhibitory actin-tropomyosin binding domain.The Biochemical journal · 1998Article
- Location and functional characterization of myosin contact sites in smooth muscle caldesmon.The Biochemical journal · 1997Article
- Both N-terminal myosin-binding and C-terminal actin-binding sites on smooth muscle caldesmon are required for caldesmon-mediated inhibition of actin filament velocity.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Location of smooth-muscle myosin and tropomyosin binding sites in the C-terminal 288 residues of human caldesmon.The Biochemical journal · 1995Article
- Alignment of caldesmon on the actin-tropomyosin filaments.The Biochemical journal · 1995Article
- Mode of caldesmon binding to smooth muscle thin filament: possible projection of the amino-terminal of caldesmon from native thin filament.Biophysical journal · 1995Article
- Phosphorylation of aorta caldesmon by endogenous proteolytic fragments of protein kinase C.Journal of muscle research and cell motility · 1994Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
A partial clone of caldesmon, coding for the C-terminal 288 amino acids, was isolated from a human fetal liver cDNA library and sequenced. Expression of the clone in Escherichia coli produced a peptide called H1 (M(r) 32,549), which inhibited tropomyosin-enhanced actomyosin Mg(2+)-ATPase activity by 90% with half maximal inhibition at 0.03-0.04 mol H1 per mol actin. The inhibition could be reversed by Ca(2+)-calmodulin. H1 bound actin, Ca(2+)-calmodulin and tropomyosin and smooth muscle myosin with high affinities. This latter finding shows the presence of a second myosin-binding site in caldesmon. This was confirmed in thrombic digests of native sheep aorta and chicken gizzard caldesmon.
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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.