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Unphosphorylated calponin enhances the binding force of unphosphorylated myosin to actin
BACKGROUND: Smooth muscle has the distinctive ability to maintain force for long periods of time and at low energy costs. While it is generally agreed that this property, called the latch-state, is due to the dephosphorylation of myosin while attached to actin, dephosphorylated-detached myosin can a...
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| Autores principales: | , , , , , , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
2013
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3740034/ https://ncbi.nlm.nih.gov/pubmed/23747303 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bbagen.2013.05.042 |
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