{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,26]],"date-time":"2026-03-26T23:14:30Z","timestamp":1774566870423,"version":"3.50.1"},"reference-count":39,"publisher":"Oxford University Press (OUP)","issue":"2","license":[{"start":{"date-parts":[[2002,1,1]],"date-time":"2002-01-01T00:00:00Z","timestamp":1009843200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2002,1,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>It has recently been suggested that dystrophin deficiency in mdx diaphragm muscle is associated with quantitative changes in the myosin molecular motor. In vitro motility assays were used to study the kinetics of actomyosin interactions between purified actin filaments and myosin molecules. Monomeric myosin was obtained from the diaphragm and limb (semitendinosus) muscles of 9-mo-old male mdx (mdx) and age-matched control mice. The sliding velocity (vo, \u03bc m\/s) of fluorescent-labeled actin filaments moving over a myosin-coated surface (40 \u03bc g\/ml) was measured. In diaphragm, vo was significantly slower in mdx than in control mice (1.2 \u00b1 0.1 \u03bc m s\u2212 \u00a01 versus 1.9 \u00b1 0.1 \u03bc m s\u2212 \u00a01, p &amp;lt; 0.001). Conversely, there was no significant difference in vo between control and mdx semitendinous muscles (2.4 \u00b1 0.1 \u03bc m s\u2212 \u00a01 versus 2.5 \u00b1 0.1 \u03bc m s\u2212 \u00a01). As compared with control mice, mdx diaphragm exhibited a shift from IIX-MHC to IIA-MHC (p &amp;lt; 0.001) and a reduction in IIB-MHC (p &amp;lt; 0.01). Semitendinous muscle from control and mdx mice contained almost exclusively type IIB MHC. Our results are in good agreement with the proposal that myosin is altered in dystrophic mouse diaphragm.<\/jats:p>","DOI":"10.1164\/ajrccm.165.2.2105088","type":"journal-article","created":{"date-parts":[[2013,4,4]],"date-time":"2013-04-04T14:57:53Z","timestamp":1365087473000},"page":"250-253","source":"Crossref","is-referenced-by-count":25,"title":["Velocity of Actomyosin Sliding\n                    <i>in Vitro<\/i>\n                    Is Reduced in Dystrophic Mouse Diaphragm"],"prefix":"10.1093","volume":"165","author":[{"given":"Catherine","family":"Coirault","sequence":"first","affiliation":[{"name":"INSERM\u2013UMR 7639, LOA-Ensta-Ecole Polytechnique, Batterie de l'Yvette, Palaiseau Cedex, France; and Service d'Explorations Fonctionnelles Cardiovasculaires et Respiratoires, Centre Hospitalier et Universitaire de Bic\u00eatre, Assistance Publique-H\u00f4pitaux de Paris, Le Kremlin-Bic\u00eatre, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Francine","family":"Lambert","sequence":"additional","affiliation":[{"name":"INSERM\u2013UMR 7639, LOA-Ensta-Ecole Polytechnique, Batterie de l'Yvette, Palaiseau Cedex, France; and Service d'Explorations Fonctionnelles Cardiovasculaires et Respiratoires, Centre Hospitalier et Universitaire de Bic\u00eatre, Assistance Publique-H\u00f4pitaux de Paris, Le Kremlin-Bic\u00eatre, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jean-Claude","family":"Pourny","sequence":"additional","affiliation":[{"name":"INSERM\u2013UMR 7639, LOA-Ensta-Ecole Polytechnique, Batterie de l'Yvette, Palaiseau Cedex, France; and Service d'Explorations Fonctionnelles Cardiovasculaires et Respiratoires, Centre Hospitalier et Universitaire de Bic\u00eatre, Assistance Publique-H\u00f4pitaux de Paris, Le Kremlin-Bic\u00eatre, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yves","family":"Lecarpentier","sequence":"additional","affiliation":[{"name":"INSERM\u2013UMR 7639, LOA-Ensta-Ecole Polytechnique, Batterie de l'Yvette, Palaiseau Cedex, France; and Service d'Explorations Fonctionnelles Cardiovasculaires et Respiratoires, Centre Hospitalier et Universitaire de Bic\u00eatre, Assistance Publique-H\u00f4pitaux de Paris, Le Kremlin-Bic\u00eatre, France"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2002,1,15]]},"reference":[{"key":"2026031623125588800_B1","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1126\/science.3659917","article-title":"Conservation of the Duchenne muscular dystrophy gene in mice and humans.","volume":"238","author":"Hoffman","year":"1987","journal-title":"Science"},{"key":"2026031623125588800_B2","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1038\/333466a0","article-title":"The Duchenne muscular dystrophy gene product is localized in sarcolemma of human skeletal muscle.","volume":"333","author":"Zubryzcka-Gaarn","year":"1998","journal-title":"Nature"},{"key":"2026031623125588800_B3"},{"key":"2026031623125588800_B4","doi-asserted-by":"crossref","first-page":"3710","DOI":"10.1073\/pnas.90.8.3710","article-title":"Dystrophin protects the sarcolemma from stresses developed during muscle contraction.","volume":"90","author":"Petrof","year":"1993","journal-title":"Proc Natl Acad Sci USA"},{"key":"2026031623125588800_B5","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1038\/344670a0","article-title":"Calcium entry through stretch-inactivated ion channel in mdx myotubes.","volume":"344","author":"Franco","year":"1990","journal-title":"Nature"},{"key":"2026031623125588800_B6","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1007\/BF00232023","article-title":"Proteolysis results in altered leak channel kinetics and elevated free calcium in mdx muscle.","volume":"133","author":"Turner","year":"1993","journal-title":"J Membrane Biol"},{"key":"2026031623125588800_B7","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1126\/science.2173137","article-title":"Increased activity of calcium leak channels in myotubes of Duchenne human and mdx mouse origin.","volume":"250","author":"Fong","year":"1990","journal-title":"Science"},{"key":"2026031623125588800_B8","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1002\/mus.880010407","article-title":"Muscular dystrophy and activation of proteinases.","volume":"1","author":"Kar","year":"1978","journal-title":"Muscle Nerve"},{"key":"2026031623125588800_B9","doi-asserted-by":"crossref","first-page":"10909","DOI":"10.1074\/jbc.270.18.10909","article-title":"Calpains are activated in necrotic fibers from mdx dystrophic mice.","volume":"270","author":"Spencer","year":"1995","journal-title":"J Biol Chem"},{"key":"2026031623125588800_B10","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1038\/335735a0","article-title":"Increased protein degradation results from elevated free calcium levels found in muscle from mdx mice.","volume":"335","author":"Turner","year":"1988","journal-title":"Nature"},{"key":"2026031623125588800_B11","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/0960-8966(95)00001-4","article-title":"How does dystrophin deficiency lead to muscle degeneration? 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