ArticleThe Journal of clinical investigation1997
Characterization of mutant myosins of Dictyostelium discoideum equivalent to human familial hypertrophic cardiomyopathy mutants. Molecular force level of mutant myosins may have a prognostic implication.
Article in The Journal of clinical investigation, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 1 of them a synthesis that pooled it.
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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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Who cites it
29 citing papers in PubMed, 1 synthesis or guideline pooled it, 74 citations in OpenAlex.
- Comparative analysis of functional assay evidence use by ClinGen Variant Curation Expert Panels.Genome medicine · 2019Pooled it
- Sarcomeric gene variants among Indians with hypertrophic cardiomyopathy: A scoping review.The Indian journal of medical research · 2023Article
- Virus-free transfection, transient expression, and purification of human cardiac myosin in mammalian muscle cells for biochemical and biophysical assays.Scientific reports · 2023Article
- Electrostatic interactions in the force-generating region of the human cardiac myosin modulate ADP dissociation from actomyosin.Biochemical and biophysical research communications · 2019Article
- Hypertrophic cardiomyopathy R403Q mutation in rabbit β-myosin reduces contractile function at the molecular and myofibrillar levels.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- The Molecular Mechanisms of Mutations in Actin and Myosin that Cause Inherited Myopathy.International journal of molecular sciences · 2018Review
- Contractility parameters of human β-cardiac myosin with the hypertrophic cardiomyopathy mutation R403Q show loss of motor function.Science advances · 2015Article
- The hypertrophic cardiomyopathy myosin mutation R453C alters ATP binding and hydrolysis of human cardiac β-myosin.The Journal of biological chemistry · 2014Article
- Muscle dysfunction in hypertrophic cardiomyopathy: what is needed to move to translation?Journal of muscle research and cell motility · 2014Review
- Cell-intrinsic functional effects of the α-cardiac myosin Arg-403-Gln mutation in familial hypertrophic cardiomyopathy.Biophysical journal · 2012Article
- How do mutations in contractile proteins cause the primary familial cardiomyopathies?Journal of cardiovascular translational research · 2011Review
- Normal passive viscoelasticity but abnormal myofibrillar force generation in human hypertrophic cardiomyopathy.Journal of molecular and cellular cardiology · 2010Article
- Hypertrophic cardiomyopathy: from genetics to treatment.European journal of clinical investigation · 2010Review
- Article
- Mechanical and energetic consequences of HCM-causing mutations.Journal of cardiovascular translational research · 2009Review
- Experimental therapies in hypertrophic cardiomyopathy.Journal of cardiovascular translational research · 2009Review
- Cardiomyopathy mutations reveal variable region of myosin converter as major element of cross-bridge compliance.Biophysical journal · 2009Article
- The myosin C-loop is an allosteric actin contact sensor in actomyosin.Biochemistry · 2009Article
- Functional effects of the hypertrophic cardiomyopathy R403Q mutation are different in an alpha- or beta-myosin heavy chain backbone.The Journal of biological chemistry · 2008Article
- Myosin dynamics on the millisecond time scale.Biophysical chemistry · 2007Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent studies have revealed that familial hypertrophic cardiomyopathy (FHC) is caused by missence mutations in myosin heavy chain or other sarcomeric proteins. To investigate the functional impact of FHC mutations in myosin heavy chain, mutants of Dictyostelium discoideum myosin II equivalent to human FHC mutations were generated by site-directed mutagenesis, and their motor function was characterized at the molecular level. These mutants, i.e., R397Q, F506C, G575R, A699R, K703Q, and K703W are respectively equivalent to R403Q, F513C, G584R, G716R, R719Q, and R719W FHC mutants. We measured the force generated by these myosin mutants as well as the sliding velocity and the actin-activated ATPase activity. These measurements showed that the A699R, K703Q, and K703W myosins exhibited unexpectedly weak affinity with actin and the lowest level of force, though their ATPase activity remained rather high. F506C mutant which has been reported to have benign prognosis exhibited the least impairment of the motile and enzymatic activities. The motor functions of R397Q and G575R myosins were classified as intermediate. These results suggest that the force level of mutant myosin molecule may be one of the key factors for pathogenesis which affect the prognosis of human FHC.
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