ArticleJournal of molecular and cellular cardiology2010
Mutations at the same amino acid in myosin that cause either skeletal or cardiac myopathy have distinct molecular phenotypes.
Article in Journal of molecular and cellular cardiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 33 citations in OpenAlex.
- A song of heads and tails: myosin II conformational regulation and filament dynamics shape force generation in non-muscle cells.Biophysical reviews · 2026Review
- Article
- A Laing distal myopathy-associated proline substitution in the β-myosin rod perturbs myosin cross-bridging activity.The Journal of clinical investigation · 2024Article
- [Phenotype and genotype characteristics of children with cardiomyopathy associated withZhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics · 2023Article
- Changes in beef protein digestibility in anHeliyon · 2023Article
- CCDC66 frameshift variant associated with a new form of early-onset progressive retinal atrophy in Portuguese Water Dogs.Scientific reports · 2020Article
- A1603P and K1617del, Mutations in β-Cardiac Myosin Heavy Chain that Cause Laing Early-Onset Distal Myopathy, Affect Secondary Structure and Filament Formation In Vitro and In Vivo.Journal of molecular biology · 2018Article
- Myosin storage myopathy mutations yield defective myosin filament assembly in vitro and disrupted myofibrillar structure and function in vivo.Human molecular genetics · 2017Article
- Article
- Pathophysiological concepts in the congenital myopathies: blurring the boundaries, sharpening the focus.Brain : a journal of neurology · 2015Review
- Novel mutations widen the phenotypic spectrum of slow skeletal/β-cardiac myosin (MYH7) distal myopathy.Human mutation · 2014Article
- Cardiomyopathy mutations in the tail of β-cardiac myosin modify the coiled-coil structure and affect integration into thick filaments in muscle sarcomeres in adult cardiomyocytes.The Journal of biological chemistry · 2013Article
- Hormone replacement therapy improves contractile function and myonuclear organization of single muscle fibres from postmenopausal monozygotic female twin pairs.The Journal of physiology · 2013Article
- Myosinopathies: pathology and mechanisms.Acta neuropathologica · 2013Review
- A de novo germline mutation in MYH7 causes a progressive dominant myopathy in pigs.BMC genetics · 2012Article
- Effects of pathogenic proline mutations on myosin assembly.Journal of molecular biology · 2012Article
- Almanac 2011: cardiomyopathies. The national society journals present selected research that has driven recent advances in clinical cardiology.Acta informatica medica : AIM : journal of the Society for Medical Informatics of Bosnia & Herzegovina : casopis Drustva za medicinsku informatiku BiH · 2011Article
- A mutation in the beta-myosin rod associated with hypertrophic cardiomyopathy has an unexpected molecular phenotype.Biochemical and biophysical research communications · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
To date, more than 230 disease-causing mutations have been linked to the slow/cardiac muscle myosin gene, beta-MyHC (MYH7). Most of these mutations are located in the globular head region of the protein and result in cardiomyopathies. Recently, however, a number of novel disease-causing mutations have been described in the long, alpha-helical, coiled coil tail region of the beta-MyHC protein. Mutations in this region are of particular interest because they are associated with a multitude of human diseases, including both cardiac and skeletal myopathies. Here, we attempt to dissect the mechanism(s) by which mutations in the rod region of beta-MyHC can cause a variety of diseases by analyzing two mutations at a single amino acid (R1500P and R1500W) which cause two distinct diseases (Laing-type early-onset distal myopathy and dilated cardiomyopathy, respectively). For diseases linked to the R1500 residue, we find that each mutation displays distinct structural, thermodynamic, and functional properties. Both R1500P and R1500W cause a decrease in thermodynamic stability, although the R1500W phenotype is more severe. Both mutations also affect filament assembly, with R1500P causing an additional decrease in filament stability. In addition to furthering our understanding of the mechanism of pathogenesis for each of these diseases, these data also suggest how the variance in molecular phenotype may be associated with the variance in clinical phenotype present with mutations in the beta-MyHC rod.
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