The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
The in vitro motility activity of β-cardiac myosin depends on the nature of the β-myosin heavy chain gene mutation in hypertrophic cardiomyopathy
Abstract
Several mutations in the beta-myosin heavy chain gene cause hypertrophic cardiomyopathy. This study investigates (1) the in vitro velocities of translocation of fluorescently-labelled actin by beta-myosin purified from soleus muscle of 30 hypertrophic cardiomyopathy patients with seven distinct beta-myosin heavy chain gene mutations: Thr124Ile, Tyr162Cys, Gly256Glu, Arg403Gln, Val606Met, Arg870His, and Leu908Val mutations; and (2) motility activity of beta-myosin purified from cardiac and soleus muscle biopsies in the same patients. The velocity of translocation of actin by beta-myosin purified from soleus or cardiac muscle of 22 normal controls was 0.48 +/- 0.09 micron s-1. By comparison, the motility activity was reduced in all 30 patients with beta-myosin heavy chain gene mutations (range, 0.112 +/- 0.041 to 0.292 +/- 0.066 micron s-1. Notably, the Tyr162Cys and Arg403Gln mutations demonstrated significantly lower actin sliding velocities: 0.123 +/- 0.044, and 0.112 +/- 0.041 micron s-1, respectively. beta-myosin purified from soleus muscle from four patients with the Arg403Gln mutation had a similar actomyosin motility activity compared to beta-myosin purified from their cardiac biopsies (0.127 +/- 0.045 micron s-1 versus 0.119 +/- 0.068 micron s-1, respectively). Since these seven mutations lie in several distinct functional domains, it is likely that the mechanisms of their inhibitions of motility are different.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Such an increased energetic cost of contraction with the Arg403Gln mutation in the intact mouse heart3 is thought to be consistent with several molecular studies suggesting a decrease in actomyosin motility20,21 that effectively puts an energetic “drag” on the wild-type myosin during shortening3,19,22.”
From iRhythm ZIO: The Diagnostic Yield of a 14-day Continuous Ambulatory ECG Monitor (Turakhia et al., diagnostic yield of extended ambulatory ECG monitoring) (2013) · cites this paper as [20]
Citations
Cites
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011
Three-dimensional structure of myosin subfragment-1: a molecular motor
Rayment, I., Rypniewski, W. R., Schmidt‐Bäse, K., Smith, R., Tomchick, D. R., Benning, M. M., Winkelmann, D. A., Wesenberg, G. E., & Holden, H. M. (1993) · Science · doi:10.1126/science.8316857 · Cited by 2,054
Structure of the actin-myosin complex and its implications for muscle contraction
Rayment, I., Holden, H. M., Whittaker, M., Yohn, C. B., Lorenz, M., Holmes, K. C., & Milligan, R. A. (1993) · Science · doi:10.1126/science.8316858 · Cited by 1,815
Geisterfer-Lowrance, A. A. T., Kass, S., Tanigawa, G., Vosberg, H.-P., McKenna, W., Seidman, C. E., & Seidman, J. G. (1990) · Cell · doi:10.1016/0092-8674(90)90274-i · Cited by 1,380
Mutations in the Genes for Cardiac Troponin T and α-Tropomyosin in Hypertrophic Cardiomyopathy
Watkins, H. C., McKenna, W. J., Thierfelder, L., Suk, H. J., Anan, R., O'Donoghue, A., Spirito, P., Matsumori, A., Moravec, C. S., Seidman, J. G., et al. (1995) · New England Journal of Medicine · doi:10.1056/nejm199504203321603 · Cited by 935
Watkins, H. C., Rosenzweig, A., Hwang, D., Levi, T., McKenna, W. J., Seidman, C. E., & Seidman, J. G. (1992) · New England Journal of Medicine · doi:10.1056/nejm199204233261703 · Cited by 742
Force measurements by micromanipulation of a single actin filament by glass needles
Kishino, A., & Yanagida, T. (1988) · Nature · doi:10.1038/334074a0 · Cited by 682
Predicting coiled coils by use of pairwise residue correlations.
Berger, B., Wilson, D. B., Wolf, E., Tonchev, T., Milla, M. E., & Kim, P. S. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.18.8259 · Cited by 622
Fisher, A. J., Smith, C. A., Thoden, J. B., Smith, R., Sutoh, K., Holden, H. M., & Rayment, I. (1995) · Biochemistry · doi:10.1021/bi00028a004 · Cited by 593
Watkins, H. C., Conner, D. A., Thierfelder, L., Jarcho, J. A., MacRae, C. A., McKenna, W. J., Maron, B. J., Seidman, J. G., & Seidman, C. E. (1995) · Nature Genetics · doi:10.1038/ng1295-434 · Cited by 589
Research works printed but not linked: 1
- FANANAPAZIR, L., MCAREAVEY, D. & EPSTEIN, N. D. (1994) Hypertrophic cardiomyopathy. In Electrophysiology, From Cell to Bedside (edited by ZIPES, D. & JALIFE, J. ) pp. 769–79. Philadelphia: W. B. Saunders Co.
Cited by
Sorted by citations
The Genetic Basis for Cardiomyopathy
Seidman, J. G., & Seidman, C. E. (2001) · Cell · doi:10.1016/s0092-8674(01)00242-2 · Cited by 1,050
Structural Mechanism of Muscle Contraction
Geeves, M. A., & Holmes, K. C. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.687 · Cited by 781
Striated Muscle Cytoarchitecture: An Intricate Web of Form and Function
Clark, K. A., McElhinny, A., Beckerle, M. C., & Gregorio, C. C. (2002) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.18.012502.105840 · Cited by 705
Myosin heavy chain isoform expression in the failing and nonfailing human heart
Miyata, S., Minobe, W., Bristow, M. R., & Leinwand, L. A. (2000) · Circulation Research · doi:10.1161/01.res.86.4.386 · Cited by 538
The Molecular Genetic Basis for Hypertrophic Cardiomyopathy
Marian, A. J., & Roberts, R. (2001) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.2001.1340 · Cited by 438
Metadata
- Authors
- CUDA, G., FANANAPAZIR, L., EPSTEIN, N. D., & SELLERS, J. R.
- Affiliations
- National Institutes of Health (US)
- Venue
- Journal of Muscle Research & Cell Motility
- Published
- 1997-05
- Volume
- 18
- Issue
- 3
- Pages
- 275-283
- ISSN
- 0142-4319 (ISSN-L)
- 1573-2657
- OpenAlex
- W383489959
- Cited by
- 137
- References
- 39
- Citations by year
- 2025: 1 · 2024: 2 · 2023: 1 · 2022: 3 · 2021: 6 · 2020: 2 · 2019: 6 · 2018: 2 · 2017: 5 · 2016: 2 · 2015: 3 · 2014: 2 · 2013: 6 · 2012: 2
- FWCI
- 7.04
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Journal of Muscle Research and Cell Motility (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac electrophysiology and arrhythmias
- Keywords
- hypertrophic cardiomyopathy, beta-myosin heavy chain, myosin mutations, actomyosin motility, soleus muscle, myocardium, cardiac contractility
- MeSH terms
- Actins, Cardiomyopathy, Hypertrophic, Humans, Models, Biological, Myocardium, Myosins, Muscle, Skeletal, Myosin Heavy Chains
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
