Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Daria S. Yampolskaya"'
Autor:
Victoria V. Nefedova, Daria S. Yampolskaya, Sergey Y. Kleymenov, Natalia A. Chebotareva, Alexander M. Matyushenko, Dmitrii I. Levitsky
Publikováno v:
Biochemistry (Moscow). 88:610-620
Autor:
Daria S, Yampolskaya, Galina V, Kopylova, Daniil V, Shchepkin, Sergey Y, Bershitsky, Alexander M, Matyushenko, Dmitrii I, Levitsky
Publikováno v:
Biochemistry (Moscow). 87:1260-1267
Abstract The effects of cardiomyopathic mutations E56G, M149V, and E177G in the MYL3 gene encoding essential light chain of human ventricular myosin (ELCv), on the functional properties of cardiac myosin and its isolated head (myosin subfragment 1, S
Autor:
Galina V. Kopylova, Anastasia M. Kochurova, Daria S. Yampolskaya, Victoria V. Nefedova, Andrey K. Tsaturyan, Natalia A. Koubassova, Sergey Y. Kleymenov, Dmitrii I. Levitsky, Sergey Y. Bershitsky, Alexander M. Matyushenko, Daniil V. Shchepkin
Publikováno v:
International Journal of Molecular Sciences; Volume 24; Issue 9; Pages: 8340
In the myocardium, the TPM1 gene expresses two isoforms of tropomyosin (Tpm), alpha (αTpm; Tpm 1.1) and kappa (κTpm; Tpm 1.2). κTpm is the result of alternative splicing of the TPM1 gene. We studied the structural features of κTpm and its regulat
Autor:
Daria S, Yampolskaya, Galina V, Kopylova, Daniil V, Shchepkin, Salavat R, Nabiev, Larisa V, Nikitina, Jonathan, Walklate, Rustam H, Ziganshin, Sergey Y, Bershitsky, Michael A, Geeves, Alexander M, Matyushenko, Dmitrii I, Levitsky
Publikováno v:
Biophysical Chemistry. 292:106936
The work aimed to investigate how the phosphorylation of the myosin essential light chain of fast skeletal myosin (LC1) affects the functional properties of the myosin molecule. Using mass-spectrometry, we revealed phosphorylated peptides of LC1 in m
Autor:
Daria S. Yampolskaya, L.V. Nikitina, Dmitrii I. Levitsky, S. R. Nabiev, Vera A. Borzova, Alexander M. Matyushenko, Sergey Yu. Kleymenov, Victoria V. Nefedova, Marina A. Marchenko
Publikováno v:
Archives of biochemistry and biophysics. 710
Tropomyosin (Tpm) is an actin-associated protein and key regulator of actin filament structure and dynamics in muscle and non-muscle cells where it participates in many vital processes. Human non-muscle cells produce many Tpm isoforms; however, littl
Autor:
Dmitrii I. Levitsky, Alexander M. Matyushenko, Daria S. Yampolskaya, Natalia A. Koubassova, D. V. Shchepkin, Victoria V. Nefedova, Galina V. Kopylova, Marina A. Marchenko, Andrey K. Tsaturyan, Sergey Y. Bershitsky
Publikováno v:
International Journal of Molecular Sciences
Volume 21
Issue 22
International Journal of Molecular Sciences, Vol 21, Iss 8720, p 8720 (2020)
Volume 21
Issue 22
International Journal of Molecular Sciences, Vol 21, Iss 8720, p 8720 (2020)
Tropomyosin (Tpm) is one of the major actin-binding proteins that play a crucial role in the regulation of muscle contraction. The flexibility of the Tpm molecule is believed to be vital for its functioning, although its role and significance are und