Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Vladimir V. Sirenko"'
Autor:
Olga E. Karpicheva, Stanislava V. Avrova, Andrey L. Bogdanov, Vladimir V. Sirenko, Charles S. Redwood, Yurii S. Borovikov
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 6, p 5829 (2023)
The substitution for Arg168His (R168H) in γ-tropomyosin (TPM3 gene, Tpm3.12 isoform) is associated with congenital muscle fiber type disproportion (CFTD) and muscle weakness. It is still unclear what molecular mechanisms underlie the muscle dysfunct
Externí odkaz:
https://doaj.org/article/677174c2a3e24f48bf86aef537c260e8
Autor:
Yurii S. Borovikov, Daria D. Andreeva, Stanislava V. Avrova, Vladimir V. Sirenko, Armen O. Simonyan, Charles S. Redwood, Olga E. Karpicheva
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 12, p 6318 (2021)
Point mutations in the genes encoding the skeletal muscle isoforms of tropomyosin can cause a range of muscle diseases. The amino acid substitution of Arg for Pro residue in the 90th position (R90P) in γ-tropomyosin (Tpm3.12) is associated with cong
Externí odkaz:
https://doaj.org/article/46352c04188c4fb495e5adebd78a1b1e
Autor:
Yurii S. Borovikov, Armen O. Simonyan, Stanislava V. Avrova, Vladimir V. Sirenko, Charles S. Redwood, Olga E. Karpicheva
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 12, p 4421 (2020)
Substitution of Ala for Glu residue in position 173 of γ-tropomyosin (Tpm3.12) is associated with muscle weakness. Here we observe that this mutation increases myofilament Ca2+-sensitivity and inhibits in vitro actin-activated ATPase activity of myo
Externí odkaz:
https://doaj.org/article/bf9509d4a292488d85302c5bdf92eedf
Autor:
Yurii S. Borovikov, Olga E. Karpicheva, Armen O. Simonyan, Stanislava V. Avrova, Elena A. Rogozovets, Vladimir V. Sirenko, Charles S. Redwood
Publikováno v:
International Journal of Molecular Sciences, Vol 19, Iss 12, p 3975 (2018)
Point mutations in genes encoding isoforms of skeletal muscle tropomyosin may cause nemaline myopathy, cap myopathy (Cap), congenital fiber-type disproportion (CFTD), and distal arthrogryposis. The molecular mechanisms of muscle dysfunction in these
Externí odkaz:
https://doaj.org/article/63308bccc81a48ecb3d809a5b2fbe966
Autor:
Stanislava V. Avrova, Vladimir V. Sirenko, Olga E. Karpicheva, Yurii S. Borovikov, Charles Redwood, Armen O. Simonyan
Publikováno v:
Biochemical and Biophysical Research Communications. 523:258-262
Ghost muscle fibres reconstituted with myosin heads labeled with the fluorescent probe 1,5-IAEDANS were used for analysis of muscle fibre dysfunction associated with the R133W mutation in β-tropomyosin (Tpm2.2). By using polarized microscopy, we sho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a0b285e67cd493deae360e9c8e56b82
https://doi.org/10.1016/j.bbrc.2019.12.061
https://doi.org/10.1016/j.bbrc.2019.12.061
Autor:
Vladimir V. Sirenko, Olga E. Karpicheva, Stanislava V. Avrova, Charles Redwood, Armen O. Simonyan, Daria D. Andreeva, Yurii S. Borovikov
Publikováno v:
International Journal of Molecular Sciences
Volume 22
Issue 12
International Journal of Molecular Sciences, Vol 22, Iss 6318, p 6318 (2021)
Volume 22
Issue 12
International Journal of Molecular Sciences, Vol 22, Iss 6318, p 6318 (2021)
Point mutations in the genes encoding the skeletal muscle isoforms of tropomyosin can cause a range of muscle diseases. The amino acid substitution of Arg for Pro residue in the 90th position (R90P) in γ-tropomyosin (Tpm3.12) is associated with cong
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcf31b3fc73deac77bcbc0a1af185c8a
http://europepmc.org/articles/PMC8231546
http://europepmc.org/articles/PMC8231546
Autor:
Armen O. Simonyan, Stanislava V. Avrova, Yurii S. Borovikov, Vladimir V. Sirenko, Olga E. Karpicheva, Charles Redwood
Publikováno v:
Biochemical and Biophysical Research Communications. 515:372-377
Substitution of Ala for Thr residue in 155th position in γ-tropomyosin (Tpm3.12) is associated with muscle weakness. To understand the mechanisms of this defect, we studied the Ca2+-sensitivity of thin filaments in solution and multistep changes in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e228b715a36811e239315ab031a63c36
https://doi.org/10.1016/j.bbrc.2019.05.146
https://doi.org/10.1016/j.bbrc.2019.05.146
Autor:
Vladimir V. Sirenko, Olga E. Karpicheva, Stanislava V. Avrova, Armen O. Simonyan, Yurii S. Borovikov, Charles Redwood
Publikováno v:
International Journal of Molecular Sciences
Volume 21
Issue 12
International Journal of Molecular Sciences, Vol 21, Iss 4421, p 4421 (2020)
Volume 21
Issue 12
International Journal of Molecular Sciences, Vol 21, Iss 4421, p 4421 (2020)
Substitution of Ala for Glu residue in position 173 of &gamma
tropomyosin (Tpm3.12) is associated with muscle weakness. Here we observe that this mutation increases myofilament Ca2+-sensitivity and inhibits in vitro actin-activated ATPase activi
tropomyosin (Tpm3.12) is associated with muscle weakness. Here we observe that this mutation increases myofilament Ca2+-sensitivity and inhibits in vitro actin-activated ATPase activi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ecb8a0679e9fd3dfb0169fe846e3d81
Autor:
Charles Redwood, Stanislava V. Avrova, Nikita A. Rysev, Vladimir V. Sirenko, Olga E. Karpicheva, Yurii S. Borovikov, Armen O. Simonyan
Publikováno v:
Biochemical and Biophysical Research Communications. 502:209-214
The E41K mutation in TPM2 gene encoding muscle regulatory protein beta-tropomyosin is associated with nemaline myopathy and cap disease. The mutation results in a reduced Ca2+-sensitivity of the thin filaments and in muscle weakness. To elucidate the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2df56d00063cb0cdf1b1bdfbf5b32110
https://doi.org/10.1016/j.bbrc.2018.05.145
https://doi.org/10.1016/j.bbrc.2018.05.145
Autor:
Armen O. Simonyan, Nikita A. Rysev, Vladimir V. Sirenko, Olga E. Karpicheva, Yu. S. Borovikov, Charles Redwood
Publikováno v:
Cell and Tissue Biology. 12:238-246
The structural changes in proteins of the contractile apparatus of muscle fiber and the violation of their function due to point mutations in these proteins can be a cause of many hereditary diseases of human muscular tissue. Some such diseases are c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::318ed41cf4cd1e79e965ee5aa85464a1
https://doi.org/10.1134/s1990519x18030112
https://doi.org/10.1134/s1990519x18030112