Избранные публикации за 5 лет

1. Borovikov YS, Karpicheva OE, Simonyan AO, Avrova SV, Rogozovets EA, Sirenko VV, Redwood CS. 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. Int. J. Mol. Sci. 2018; 19(12):3975;
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6321504/pdf/ijms-19–03975.pdf.
doi: 10.3390/ijms19123975. (IF 2,928. Q2. Web of Science, Scopus, РИНЦ).

2. Simonyan AO, Sirenko VV, Karpicheva OE, Robaszkiewicz K, Śliwinska M, Moraczewska J, Krutetskaya ZI, Borovikov YS. 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. Arch. Biochem. Biophys. 2018; 644:17–28;
https://www.sciencedirect.com/science/article/abs/pii/S0003986117304149?via%3Dihub,
doi: 10.1016/j.abb.2018.03.002. (IF 3,559. Q1. Web of Science, Scopus, РИНЦ).

3. Avrova SV, Karpicheva OE, Rysev NA, Simonyan AO, Sirenko VV, Redwood CS, Borovikov YS. 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. Biochem Biophys Res Commun. 2018; 502(2):209–214;
https://www.sciencedirect.com/science/article/pii/S0006291X18312142?via%3Dihub,
doi: 10.1016/j.bbrc.2018.05.145. (IF 2,705, Q2. Web of Science, Scopus, РИНЦ).

4. Borovikov YS, Rysev NA, Karpicheva OE, Sirenko VV, Avrova SV, Piers A, Redwood CS. Molecular mechanisms of dysfunction of muscle fibres associated with Glu139 deletion in TPM2 gene. Sci Rep. 2017; 7(1): 16797;
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5711931/pdf/41598_2017_Article_17076.pdf,
doi: 10.1038/s41598-017–17076‑9. (IF 4.011, Q1 Web of Science, Scopus, РИНЦ).

5. Karpicheva OE, Sirenko VV, Rysev NA, Simonyan AO, Borys D, Moraczewska J, Borovikov YS. Deviations in conformational rearrangements of thin filaments and myosin caused by the Ala155Thr substitution in hydrophobic core of tropomyosin. Biochim Biophys Acta. 2017; 1865(12):1790–1799;
https://www.sciencedirect.com/science/article/abs/pii/S1570963917302169?via%3Dihub, doi:10.1016/j.bbapap.2017.09.008. (IF 2,540. Q2. Web of Science, Scopus, РИНЦ).

6. Borovikov YS, Simonyan AO, Karpicheva OE, Avrova SV, Rysev NA, Sirenko VV, Piers A, Redwood CS. The reason for a high Ca2+-sensitivity associated with Arg91Gly substitution in TPM2 gene is the abnormal behavior and high flexibility of tropomyosin during the ATPase cycle. Biochem Biophys Res Commun. 2017; 494(3–4): 681–686.
https://www.sciencedirect.com/science/article/pii/S0006291X17321496?via%3Dihub.
doi: 10.1016/j.bbrc.2017.10.161. (IF 2,705. Q2. Web of Science, Scopus, РИНЦ).

7. Borovikov YS, Rysev NA, Avrova SV, Karpicheva OE, Borys D, Moraczewska J. Molecular mechanisms of deregulation of the thin filament associated with the R167H and K168E substitutions in tropomyosin Tpm1.1. Arch Biochem Biophys 2017; 614:28–40;
https://www.sciencedirect.com/science/article/abs/pii/S0003986116305574?via%3Dihub,
doi: 10.1016/j.abb.2016.12.004. (IF 3,559. Q1. Web of Science, Scopus, РИНЦ).

8. Karpicheva OE, Simonyan AO, Kuleva NV, Redwood CS, Borovikov YS. Myopathy-causing Q147P TPM2 mutation shifts tropomyosin strands further towards the open position and increases the proportion of strong-binding cross-bridges during the ATPase cycle. Biochim Biophys Acta. 2016; 1864(3):260–267;
https://www.ncbi.nlm.nih.gov/pubmed/26708479,
doi: 10.1016/j.bbapap.2015.12.004. (IF 2,540. Q2. Web of Science, Scopus, РИНЦ).

9. Borovikov YS, Avrova SV, Rysev NA, Sirenko VV, Simonyan AO, Chernev AA, Karpicheva OE, Piers A, Redwood CS. 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; 577–578: 11–23;
https://www.ncbi.nlm.nih.gov/pubmed/25978979,
doi: 10.1016/j.abb.2015.05.002. (IF 3,559. Q2. Web of Science, Scopus, РИНЦ).

10. Borovikov YS, Karpicheva OE, Avrova SV, Simonyan AO, Sirenko VV, Redwood CS. The molecular mechanism of muscle dysfunction associated with the R133W mutation in Tpm2.2. Biochemical and Biophysical Research Communications. 2019; 523(1):258–262;
https://doi.org/10.1016/j.bbrc.2019.12.061,
doi: 10.1016/j.bbrc.2019.12.061. (IF 2,705. Q2. Web of Science, Scopus, РИНЦ).