ArticleInternational journal of molecular sciences2008
Myosin assembly, maintenance and degradation in muscle: Role of the chaperone UNC-45 in myosin thick filament dynamics.
Article in International journal of molecular sciences, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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.
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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
21 citing papers in PubMed, 35 citations in OpenAlex.
- Novel Genetic Variants Associated with Primary Myocardial Fibrosis in Sudden Cardiac Death Victims.Journal of cardiovascular translational research · 2024Article
- UNC-45 assisted myosin folding depends on a conserved FXNature communications · 2024Article
- The myosin chaperone UNC-45 has an important role in maintaining the structure and function of muscle sarcomeres during adult aging.Molecular biology of the cell · 2024Article
- Expression of Smyd1b_tv1 by Alternative Splicing in Cardiac Muscle is Critical for Sarcomere Organization in Cardiomyocytes and Heart Function.Molecular and cellular biology · 2024Article
- Revealing Pathways Associated with Feed Efficiency and Meat Quality Traits in Slow-Growing Chickens.Animals : an open access journal from MDPI · 2021Article
- Mutational Analysis of the Structure and Function of the Chaperoning Domain of UNC-45B.Biophysical journal · 2020Article
- Article
- Genomic consequences of dietary diversification and parallel evolution due to nectarivory in leaf-nosed bats.GigaScience · 2020Article
- A feline orthologue of the human MYH7 c.5647G>A (p.(Glu1883Lys)) variant causes hypertrophic cardiomyopathy in a Domestic Shorthair cat.European journal of human genetics : EJHG · 2019Article
- An AP-MS- and BioID-compatible MAC-tag enables comprehensive mapping of protein interactions and subcellular localizations.Nature communications · 2018Article
- Loss of function of myosin chaperones triggers Hsf1-mediated transcriptional response in skeletal muscle cells.Genome biology · 2015Article
- UNC-45B chaperone: the role of its domains in the interaction with the myosin motor domain.Biophysical journal · 2014Article
- Tracking unfolding and refolding reactions of single proteins using atomic force microscopy methods.Methods (San Diego, Calif.) · 2013Article
- Article
- Dual function of the UNC-45b chaperone with myosin and GATA4 in cardiac development.Journal of cell science · 2012Article
- Tracking UNC-45 chaperone-myosin interaction with a titin mechanical reporter.Biophysical journal · 2012Article
- Drosophila UNC-45 accumulates in embryonic blastoderm and in muscles, and is essential for muscle myosin stability.Journal of cell science · 2011Article
- Dividing the spoils of growth and the cell cycle: The fission yeast as a model for the study of cytokinesis.Cytoskeleton (Hoboken, N.J.) · 2011Review
- A novel conserved isoform of the ubiquitin ligase UFD2a/UBE4B is expressed exclusively in mature striated muscle cells.PloS one · 2011Article
- Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Myofibrillogenesis in striated muscle cells requires a precise ordered pathway to assemble different proteins into a linear array of sarcomeres. The sarcomere relies on interdigitated thick and thin filaments to ensure muscle contraction, as well as properly folded and catalytically active myosin head. Achieving this organization requires a series of protein folding and assembly steps. The folding of the myosin head domain requires chaperone activity to attain its functional conformation. Folded or unfolded myosin can spontaneously assemble into short myosin filaments, but further assembly requires the short and incomplete myosin filaments to assemble into the developing thick filament. These longer filaments are then incorporated into the developing sarcomere of the muscle. Both myosin folding and assembly require factors to coordinate the formation of the thick filament in the sarcomere and these factors include chaperone molecules. Myosin folding and sarcomeric assembly requires association of classical chaperones as well as folding cofactors such as UNC-45. Recent research has suggested that UNC-45 is required beyond initial myosin head folding and may be directly or indirectly involved in different stages of myosin thick filament assembly, maintenance and degradation.
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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.