The Effect of the Arg91Gly and Glu139del Mutations in β-Tropomyosin Associated with Congenital Myopathy of Human Skeletal Muscles on Actin–Myosin Interaction
Author:
Publisher
Pleiades Publishing Ltd
Subject
Cell Biology
Link
http://link.springer.com/content/pdf/10.1134/S1990519X18030112.pdf
Reference36 articles.
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3. Borovikov, Y.S., Karpicheva, O.E., Avrova, S.V., Robinson, P., and Redwood, C.S., The effect of the dilated cardiomyopathy-causing mutation Glu54Lys of alpha-tropomyosin on actin-myosin interactions during the ATPase cycle, Arch. Biochem. Biophys., 2009, vol. 489, pp. 20–24.
4. Borovikov, Y.S., Avrova, S.V., Rysev, N.A., Sirenko, V.V., Simonyan, A.O., Chernev, A.A., Karpicheva, O.E., Piers, A., and Redwood, C.S., Aberrant movement of β-tropomyosin associated with congenital myopathy causes defective response of myosin heads and actin during the ATPase cycle, Arch. Biochem. Biophys., 2015, vol. 577–578, pp. 11–23.
5. Borovikov, Y.S., Rysev, N.A., Avrova, S.V., Karpicheva, O.E., Borys, D., and Moraczewska, J., Molecular mechanisms of deregulation of the thin filament associated with the R167H and K168E substitutions in tropomyosin Tpm 1, Arch. Biochem. Biophys., 2017, vol. 614, pp. 28–40.
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