1. 2018
  2. Molecular mechanisms of muscle dysfunction resulting from the myopathy-causing E41K mutation in the TPM2 gene

    Avrova, S. V., Borovikov, Y. S., Karpicheva, O. E., Симонян, А. О., Sirenko, V. V., Rysev, N. A. & Redwood, C. S., 19 Dec 2018, In: Journal of Muscle Research and Cell Motility. p. 44 1 p., P12-17.

    Research output: Contribution to journalMeeting Abstractpeer-review

  3. The E173A substitution in gamma-tropomyosin disturbs the transition of contractile system to relaxation

    Симонян, А. О., Karpicheva, O. E., Sirenko, V. V., Redwood, C. S. & Borovikov, Y. S., 19 Dec 2018, In: Journal of Muscle Research and Cell Motility. p. 33 1 p., P7-12.

    Research output: Contribution to journalMeeting Abstractpeer-review

  4. The Primary Causes of Muscle Dysfunction Associated with the Point Mutations in Tpm3.12; Conformational Analysis of Mutant Proteins as a Tool for Classification of Myopathies

    Borovikov, Y. S., Karpicheva, O. E., Симонян, А. О., Avrova, S. V., Rogozovets, E. A., Sirenko, V. V. & Redwood, C. S., 10 Dec 2018, In: International Journal of Molecular Sciences. 19, 12, 30 p.

    Research output: Contribution to journalArticlepeer-review

  5. The reason for the low Ca2+-sensitivity of thin filaments associated with the Glu41Lys mutation in the TPM2 gene is “freezing” of tropomyosin near the outer domain of actin and inhibition of actin monomer switching off during the ATPase cycle

    Avrova, S. V., Karpicheva, O. E., Rysev, N. A., Симонян, А. О., Sirenko, V. V., Redwood, C. S. & Borovikov, Y. S., 12 Jul 2018, In: Biochemical and Biophysical Research Communications. 502, 2, p. 209-214 6 p.

    Research output: Contribution to journalArticlepeer-review

  6. The primary cause of muscle disfunction associated with substitutions E240K and R244G in tropomyosin is aberrant behavior of tropomyosin and response of actin and myosin during ATPase cycle

    Симонян, А. О., Sirenko, V. V., Karpicheva, O. E., Robaszkiewicz, K., Śliwinska, M., Moraczewska, J., Крутецкая, З. И. & Borovikov, Y. S., 15 Apr 2018, In: Archives of Biochemistry and Biophysics. 644, p. 17-28 12 p.

    Research output: Contribution to journalArticlepeer-review

  7. The effect of the Arg91Gly and Glu139del mutations in β-tropomyosin associated with congenital myopathy of human skeletal muscles on actin–myosin interaction

    Rysev, N. A., Karpicheva, O. E., Sirenko, V. V., Simonyan, A. O., Redwood, C. S. & Borovikov, Y. S., 2018, In: Cell and Tissue Biology. 12, 3, p. 238-246 9 p.

    Research output: Contribution to journalArticlepeer-review

  8. 2017
  9. Влияние мутаций Arg91Gly и Glu139del в бета-тропомиозине, связанных с наследственной миопатией скелетных мышц человека, на актин-миозиновое взаимодействие

    Рысев, Н. А., Карпичева, О. Е., Сиренко, В. В., Симонян, А. О., Рэдвуд, Ч. & Боровиков, Ю. С., Dec 2017, In: Цитология. 59, 12, p. 888-896 9 p.

    Research output: Contribution to journalArticlepeer-review

  10. Deviations in conformational rearrangements of thin filaments and myosin caused by the Ala155Thr substitution in hydrophobic core of tropomyosin

    Karpicheva, O. E., Sirenko, V. V., Rysev, N. A., Симонян, А. О., Borys, D., Moraczewska, J. & Borovikov, Y. S., 2017, In: BBA - Proteins and Proteomics. 1865, 12, p. 1790-1799 10 p.

    Research output: Contribution to journalArticlepeer-review

  11. Substitutions E240K and R244G in tropomyosin have similar effects on actin-myosin interaction during ATPase cycle

    Симонян, А. О., Sirenko, V. V., Robaszkiewicz, K., Boris, D., Moraczewska, J., Крутецкая, З. И. & Borovikov, Y. S., 2017, In: Journal of Muscle Research and Cell Motility. 38, 1, p. 94

    Research output: Contribution to journalMeeting Abstractpeer-review

  12. The effect of Ala155Thr substitution in tropomyosin on the modulation of actin- myosin interaction during simulated stages of ATPase cycle

    Симонян, А. О., Karpicheva, O. E., Chernev, A. A., Borovikov, Y. S. & Moraczewska, J., 2017, In: FEBS Journal. 284, S1, p. 28

    Research output: Contribution to journalMeeting Abstractpeer-review

ID: 168281