1998
DOI: 10.1002/(sici)1097-4598(199803)21:3<309::aid-mus4>3.0.co;2-e
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Effects of denervation and muscle inactivity on the organization of F-actin

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Cited by 7 publications
(3 citation statements)
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“…2002). Furthermore, a study investigating actin filament organization in different models of muscle decreased use reported significantly greater disruption of actin filament organization in the rat soleus after 4 days of denervation than after tenotomy or immobilization, despite similar changes in contractile structure organization among the three models (Szczepanowska et al. 1998).…”
Section: Discussionmentioning
confidence: 99%
“…2002). Furthermore, a study investigating actin filament organization in different models of muscle decreased use reported significantly greater disruption of actin filament organization in the rat soleus after 4 days of denervation than after tenotomy or immobilization, despite similar changes in contractile structure organization among the three models (Szczepanowska et al. 1998).…”
Section: Discussionmentioning
confidence: 99%
“…In soleus muscle, denervation was found to induce not only a decrease in -actin mRNA (Babij and Booth, 1988), but also changes in F-actin conformation; a decrease of the flexibility of the C-terminus of the actin polypeptide might explain differences in the actinmyosin interaction between the normal and the denervated muscle. The changes are induced by the lack of connection with motoneurons rather than by the muscle inactivity (Szczepanowska et al, 1998).…”
Section: Variations In Actin Expressionmentioning
confidence: 97%
“…Fluorescently labeled C374 shows that the peptide chain around the C‐terminus is flexible (Ikkai, Wahl, & Auchet, 1979; Miki, Wahl, & Auchet, 1982), and this inherent flexibility is central to C‐terminal functions (Szczepanowska, Borovikov, & Jakubiec‐Puka, 1998). Structural reconstructions suggest that the C‐terminus rearranges during polymerization to interact with the D‐loop of the neighboring protomer (Chou & Pollard, 2019; Orlova & Egelman, 1992).…”
Section: Actin's C‐terminusmentioning
confidence: 99%