Ю.С. Боровиков

1. Borovikov YS, Rysev NA, Chernev AA, Avrova SV, Karpicheva OE, Borys D, Śliwińska M, Moraczewska J. Abnormal movement of tropomyosin and response of myosin heads and actin during the ATPase cycle caused by the Arg167His, Arg167Gly and Lys168Glu mutations in TPM1 gene. Arch. Biochem. Biophys. 2016; 606: 157-166. http://www.ncbi.nlm.nih.gov/pubmed/27480605. doi: 10.1016/j.abb.2016.07.022. IF 3,043.

2. Sirenko VV, Dobrzhanskaya AV, Shelud'ko NS, Borovikov YS. Calponin-like protein from mussel smooth muscle is a competitive inhibitor of actomyosin ATPase. Biochemistry (Mosc). 2016; 81(1): 28-33. http://www.ncbi.nlm.nih.gov/pubmed/26885580. doi: 10.1134/S000629791601003X. IF 1,149.

3. 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. http://www.ncbi.nlm.nih.gov/pubmed/26708479. doi: 10.1016/j.bbapap.2015.12.004. IF 3,191.

4. 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. http://www.ncbi.nlm.nih.gov/pubmed/25978979. doi: 10.1016/j.abb.2015.05.002. IF 3,043.

5. Karpicheva OE, Redwood CS, Borovikov YS. The E117K mutation in beta-tropomyosin disturbs concerted conformational changes of actomyosin in muscle fibers. Arch. Biochem. Biophys. 2014; 549: 12-16. http://www.ncbi.nlm.nih.gov/pubmed/24657080. doi: 10.1016/j.abb.2014.03.007. IF 3,043.