ArticleJournal of biomedicine & biotechnology2010
Isolation of nebulin from rabbit skeletal muscle and its interaction with actin.
Article in Journal of biomedicine & biotechnology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 16 citations in OpenAlex.
- Comprehensive phenotypic characterization of an allelic series of zebrafish models of NEB-related nemaline myopathy.Human molecular genetics · 2024Article
- Molecular Mechanisms of the Deregulation of Muscle Contraction Induced by the R90P Mutation in Tpm3.12 and the Weakening of This Effect by BDM and W7.International journal of molecular sciences · 2021Article
- Nebulin: big protein with big responsibilities.Journal of muscle research and cell motility · 2020Review
- Nebulin, a multi-functional giant.The Journal of experimental biology · 2016Review
- Nebulin interactions with actin and tropomyosin are altered by disease-causing mutations.Skeletal muscle · 2014Article
- Titin isoform size is not correlated with thin filament length in rat skeletal muscle.Frontiers in physiology · 2014Article
- Tropomodulins: pointed-end capping proteins that regulate actin filament architecture in diverse cell types.Cytoskeleton (Hoboken, N.J.) · 2012Review
- Nebulin, a major player in muscle health and disease.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011Review
- The Nebulin family: an actin support group.Trends in cell biology · 2011Review
- Tropomodulin capping of actin filaments in striated muscle development and physiology.Journal of biomedicine & biotechnology · 2011Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nebulin is about 800 kDa filamentous protein that binds the entire thin filament of vertebrate skeletal muscle sarcomeres. Nebulin cannot be isolated from muscle except in a completely denatured form by direct solubilization of myofibrils with SDS because nebulin is hardly soluble under salt conditions. In the present study, nebulin was solubilized by a salt solution containing 1 M urea and purified by DEAE-Toyopearl column chromatography via 4 M urea elution. Rotary-shadowed images of nebulin showed entangled knit-like particles, about 20 nm in diameter. The purified nebulin bound to actin filaments to form loose bundles. Nebulin was confirmed to bind actin, alpha-actinin, beta-actinin, and tropomodulin, but not troponin or tropomyosin. The data shows that full-length nebulin can be also obtained in a functional and presumably native form, verified by data from experiments using recombinant subfragments.
Indexed as
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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.