Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Nikita A, Rysev"'
Autor:
Anna P. Sokolenko, Fedor V. Moiseyenko, Aglaya G. Iyevleva, Alexandr O. Ivantsov, Georgiy D. Dolmatov, Ksenia V. Shelekhova, Elizaveta V. Gulo, Anastasya X. Topal, Elizaveta V. Artemieva, Nuriniso H. Abduloeva, Nikita A. Rysev, Daria A. Barsova, Natalia V. Levchenko, Nikita M. Volkov, Vitaliy V. Egorenkov, Vladimir M. Moiseyenko, Evgeny N. Imyanitov
Publikováno v:
International Journal of Molecular Sciences; Volume 24; Issue 3; Pages: 1870
Neoadjuvant chemotherapy (NACT) for breast cancer (BC) often results in pathologic complete response (pCR), i.e., the complete elimination of visible cancer cells. It is unclear whether the use of ultrasensitive genetic methods may still detect resid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd67cf2ee7392c706f8da4b994ca5076
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 7590, p 7590 (2020)
International Journal of Molecular Sciences
Volume 21
Issue 20
International Journal of Molecular Sciences
Volume 21
Issue 20
We have used the technique of polarized microfluorimetry to obtain new insight into the pathogenesis of skeletal muscle disease caused by the Gln147Pro substitution in &beta
tropomyosin (Tpm2.2). The spatial rearrangements of actin, myosin and t
tropomyosin (Tpm2.2). The spatial rearrangements of actin, myosin and t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8cd6b7738d8a7ec5b6c6e13144c872a6
https://www.mdpi.com/1422-0067/21/20/7590
https://www.mdpi.com/1422-0067/21/20/7590
Autor:
Olga E, Karpicheva, Armen O, Simonyan, Nikita A, Rysev, Charles S, Redwood, Yurii S, Borovikov
Publikováno v:
International Journal of Molecular Sciences
We have used the technique of polarized microfluorimetry to obtain new insight into the pathogenesis of skeletal muscle disease caused by the Gln147Pro substitution in β-tropomyosin (Tpm2.2). The spatial rearrangements of actin, myosin and tropomyos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e0fe044e21d801edc7f9b6e716f83665
https://pubmed.ncbi.nlm.nih.gov/33066566
https://pubmed.ncbi.nlm.nih.gov/33066566
Autor:
Nikita A. Rysev, S.V. Avrova, Olga E. Karpicheva, Dmitrii I. Levitsky, Yu. S. Borovikov, I. A. Nevzorov
Publikováno v:
Cell and Tissue Biology. 12:510-516
It is known that the regulation of muscle contraction is carried out by tropomyosin and calcium-sensitive protein troponin, which form thin filament with the F-actin. The noncanonical glycine residue at position 126 of the central part of the skeleta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ee08747452ed5a0ca2d090616e13e32d
https://doi.org/10.1134/s1990519x1806010x
https://doi.org/10.1134/s1990519x1806010x
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
Autor:
S.V. Avrova, Dmitrii I. Levitsky, Yu. S. Borovikov, Olga E. Karpicheva, I. A. Nevzorov, Nikita A. Rysev
Publikováno v:
Tsitologiya. 60:639-644
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f2bcd82d09d723926fd464eff8229d6b
https://doi.org/10.31116/tsitol.2018.08.08
https://doi.org/10.31116/tsitol.2018.08.08
Autor:
Joanna Moraczewska, Nikita A. Rysev, Armen O. Simonyan, Danuta Borys, Vladimir V. Sirenko, Olga E. Karpicheva, Yurii S. Borovikov
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1865:1790-1799
Effects of the Ala155Thr substitution in hydrophobic core of tropomyosin Tpm1.1 on conformational rearrangements of the components of the contractile system (Tpm1.1, actin and myosin heads) were studied by polarized fluorimetry technique at different
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c084a2bc70595882f292c2d75e6e2687
https://doi.org/10.1016/j.bbapap.2017.09.008
https://doi.org/10.1016/j.bbapap.2017.09.008
Autor:
Adam Piers, Nikita A. Rysev, Vladimir V. Sirenko, Yurii S. Borovikov, Olga E. Karpicheva, Stanislava V. Avrova, Charles Redwood
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
Scientific Reports
Scientific Reports
Deletion of Glu139 in β-tropomyosin caused by a point mutation in TPM2 gene is associated with cap myopathy characterized by high myofilament Ca2+-sensitivity and muscle weakness. To reveal the mechanism of these disorders at molecular level, mobili
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f6f395b9a298ecc008ea1b6c927b68e
http://link.springer.com/article/10.1038/s41598-017-17076-9
http://link.springer.com/article/10.1038/s41598-017-17076-9
Autor:
Joanna Moraczewska, Olga E. Karpicheva, Stanislava V. Avrova, Nikita A. Rysev, Yurii S. Borovikov, Danuta Borys
Publikováno v:
Archives of Biochemistry and Biophysics. 614:28-40
Point mutations R167H and K168E in tropomyosin Tpm1.1 (TM) disturb Ca2+-dependent regulation of the actomyosin ATPase. To understand mechanisms of this defect we studied multistep changes in mobility and spatial arrangement of tropomyosin, actin and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24e9cf8421b569a7ac05409bdaeaf9bc
https://doi.org/10.1016/j.abb.2016.12.004
https://doi.org/10.1016/j.abb.2016.12.004