Journal of Molecular Biology
ArticleIdentification and characterization of Drosophila melanogaster paramyosin☆
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Cited by (44)
Parasitization by Scleroderma guani influences protein expression in Tenebrio molitor pupae
2014, Journal of Insect PhysiologyCitation Excerpt :These two proteins are candidates for future hypotheses about their roles in manipulating host development by parasitization (Pennacchio and Strand, 2006). Paramyosin, a major structural component of thick filaments in invertebrates (Vinós et al., 1991), was up-regulated following parasitization. Expression of several other cytoskeleton proteins including actin, actin depolymerisation, tropomyosin and tubulin were up-regulated after parasitization (Nguyen et al., 2008; Zhu et al., 2010).
From action potential to contraction: Neural control and excitation-contraction coupling in larval muscles of Drosophila
2009, Comparative Biochemistry and Physiology - A Molecular and Integrative PhysiologyPassive stiffness in Drosophila indirect flight muscle reduced by disrupting paramyosin phosphorylation, but not by embryonic myosin S2 hinge substitution
2006, Biophysical JournalCitation Excerpt :Paramyosin, a major structural protein of invertebrate thick filaments, is a rod-like molecule with a central α-helical region and two nonhelical terminal domains (30,31). In vivo phosphorylation of paramyosin has been reported in Drosophila(32) as well as in other species (33,34). In Drosophila IFM, paramyosin, despite its low concentration, is uniformly distributed along the core of the thick filament (35,36).
Expression of thick filament proteins during ontogenesis of the mussel Mytilus trossulus (Mollusca: Bivalvia)
2006, Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
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This work was supported by funds from the CSIC, DGICYT and FIS.