Poorly Understood Aspects of Striated Muscle Contraction.
Muscle contraction results from cyclic interactions between the contractile proteins myosin and actin, driven by the turnover of adenosine triphosphate (ATP). Despite intense studies, several molecular events in the contraction process are poorly understood, including the relationship between force-...
| Publicado en: | BioMed Research International Vol. 2015; pp. 1 - 29 |
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| Autores principales: | , , |
| Formato: | equations & formulas pictorial review tables/charts Journal Article |
| Publicado: |
Wiley-Blackwell
4/16/2015
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| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=ccm&AN=109273966&site=ehost-live header: @attributes: shortDbName: ccm uiTerm: 109273966 longDbName: CINAHL Complete uiTag: AN controlInfo: bkinfo: dissinfo: jinfo: jid: 23146133 FT2T jtl: BioMed Research International issn: 23146133 maglogo: N pubinfo: dt: 4/16/2015 vid: 2015 pid: 480 pub: Wiley-Blackwell place: Malden, Massachusetts artinfo: ui: 109273966 109273966 109273966 10.1155/2015/245154 109273966 ppf: 1 ppct: 28 formats: fmt: @attributes: type: P tig: atl: Poorly Understood Aspects of Striated Muscle Contraction. aug: au: Månsson, Alf Rassier, Dilson Tsiavaliaris, Georgios affil: Department of Chemistry Biomedical Sciences, Linnaeus University, 39182 Kalmar, Sweden sug: subj: Muscle Contraction Physiology Proteins Metabolism Adenosine Triphosphate Metabolism ab: Muscle contraction results from cyclic interactions between the contractile proteins myosin and actin, driven by the turnover of adenosine triphosphate (ATP). Despite intense studies, several molecular events in the contraction process are poorly understood, including the relationship between force-generation and phosphate-release in the ATP-turnover. Different aspects of the force-generating transition are reflected in the changes in tension development by muscle cells, myofibrils and single molecules upon changes in temperature, altered phosphate concentration, or length perturbations. It has been notoriously difficult to explain all these events within a given theoretical framework and to unequivocally correlate observed events with the atomic structures of the myosin motor. Other incompletely understood issues include the role of the two heads of myosin II and structural changes in the actin filaments as well as the importance of the three-dimensional order. We here review these issues in relation to controversies regarding basic physiological properties of striated muscle. We also briefly consider actomyosin mutation effects in cardiac and skeletal muscle function and the possibility to treat these defects by drugs. pubtype: Academic Journal doctype: equations & formulas pictorial review tables/charts Journal Article ougenre: Article language: English refInfo: holdings: @attributes: islocal: N |
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