ArticleThe Biochemical journal1995
Interaction of calponin with actin and its functional implications.
Article in The Biochemical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 52 citations in OpenAlex.
- The unique biology of catch muscles: insights into structure, function, and robotics innovations.Frontiers in bioengineering and biotechnology · 2025Review
- Acid pH Strategy Adaptation throughJournal of fungi (Basel, Switzerland) · 2021Article
- TwoThe Journal of biological chemistry · 2020Article
- Unphosphorylated calponin enhances the binding force of unphosphorylated myosin to actin.Biochimica et biophysica acta · 2013Article
- Functional proteomic analysis of long-term growth factor stimulation and receptor tyrosine kinase coactivation in Swiss 3T3 fibroblasts.Molecular & cellular proteomics : MCP · 2012Article
- Tianma modulates blood vessel tonicity.The open biochemistry journal · 2012Article
- Effects of basic calponin on the flexural mechanics and stability of F-actin.Cytoskeleton (Hoboken, N.J.) · 2012Article
- 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
- The Saccharomyces cerevisiae calponin/transgelin homolog Scp1 functions with fimbrin to regulate stability and organization of the actin cytoskeleton.Molecular biology of the cell · 2003Article
- Calponin interaction with alpha-actinin-actin: evidence for a structural role for calponin.Biophysical journal · 1999Article
- Troponin I and troponin T interact with troponin C to produce different Ca2+-dependent effects on actin-tropomyosin filament motility.The Biochemical journal · 1997Article
- Correlation between calponin and myosin subfragment 1 binding to F-actin and ATPase inhibition.The Biochemical journal · 1997Article
- Inhibition by calponin of isometric force in demembranated vascular smooth muscle strips: the critical role of serine-175.The Biochemical journal · 1996Article
- A simple method for automatic tracking of actin filaments in the motility assay.Journal of muscle research and cell motility · 1996Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Titration of F-actin with calponin causes the formation of two types of complexes. One, at saturation, contains a lower ratio of calponin to actin (0.5:1) and is insoluble at physiological ionic strength. The another is soluble, with a higher ratio of calponin to actin (1:1). Electron microscopy revealed that the former complex consists of paracrystalline bundles of actin filaments, whereas the latter consists of separate filaments. Ca(2+)-calmodulin causes dissociation of bundles with simultaneous increase in the number of separate calponin-containing filaments. Further increase in the calmodulin concentration results in full release of calponin from actin filaments. In motility assays, calponin, when added together with ATP to actin filaments complexed with immobilized myosin, evoked a decrease in both the number and velocity of moving actin filaments. Addition of calponin to actin filaments before their binding to myosin resulted in a formation of actin filament bundles which were dissociated by ATP.
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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.