ArticleJournal of muscle research and cell motility2006
Smooth muscle alpha-actinin binds tightly to fesselin and attenuates its activity toward actin polymerization.
Article in Journal of muscle research and cell motility, 2006. 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.
The trial behind it
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, 14 citations in OpenAlex.
- Article
- Avian synaptopodin 2 (fesselin) stabilizes myosin filaments and actomyosin in the presence of ATP.Biochemistry · 2013Article
- Myopodin is an F-actin bundling protein with multiple independent actin-binding regions.Journal of muscle research and cell motility · 2013Article
- Synaptopodin family of natively unfolded, actin binding proteins: physical properties and potential biological functions.Biophysical reviews · 2010Review
- Localization of the actin-binding protein fesselin in chicken smooth muscle.Histochemistry and cell biology · 2009Article
- In vitro characterization of native mammalian smooth-muscle protein synaptopodin 2.Bioscience reports · 2008Article
- The actin binding protein, fesselin, is a member of the synaptopodin family.Biochemical and biophysical research communications · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Fesselin is an actin binding protein from smooth muscle that nucleates actin polymerization in a Ca(++)-calmodulin dependent manner, bundles actin and inhibits the actin-activated ATPase activity of myosin S1. We now report that fesselin binds to smooth muscle alpha-actinin. Binding was measured by blot overlay, affinity chromatography and sedimentation methods. Binding was moderate with an association constant of 1-4 x 10(7) M(-1) assuming a 1:1 association of fesselin with alpha-actinin. Fesselin binds to the central spectrin domain repeat region of alpha-actinin but not to the CH1-CH2 domain. Fesselin accelerates the polymerization of actin. This activity of fesselin was attenuated by alpha-actinin. These observations support the role of fesselin in organizing the cytoskeleton.
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What 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.