Zobrazeno 1 - 10
of 87
pro vyhledávání: '"Dmitrii I. Levitsky"'
Autor:
Victoria V. Nefedova, Sergey Y. Kleymenov, Irina V. Safenkova, Dmitrii I. Levitsky, Alexander M. Matyushenko
Publikováno v:
Biomolecules, Vol 14, Iss 1, p 85 (2024)
Neurofilaments are neuron-specific proteins that belong to the intermediate filament (IFs) protein family, with the neurofilament light chain protein (NFL) being the most abundant. The IFs structure typically includes a central coiled-coil rod domain
Externí odkaz:
https://doaj.org/article/75f5457c99a04118980c5d18599a76f3
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d185e042d55328931c0be1ecd8f7ae22
https://doi.org/10.1134/s0006297923050048
https://doi.org/10.1134/s0006297923050048
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b83a38708441057fe77b67f855ad824d
https://doi.org/10.1134/s0006297922110050
https://doi.org/10.1134/s0006297922110050
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a73973d1e9b4c11f7068478c0bbfce5
Autor:
Andrey K. Tsaturyan, Elena V. Zaklyazminskaya, Margarita E. Polyak, Galina V. Kopylova, Daniil V. Shchepkin, Anastasia M. Kochurova, Anastasiia D. Gonchar, Sergey Y. Kleymenov, Natalia A. Koubasova, Sergey Y. Bershitsky, Alexander M. Matyushenko, Dmitrii I. Levitsky
Publikováno v:
International Journal of Molecular Sciences; Volume 24; Issue 1; Pages: 18
Hypertrophic cardiomyopathy (HCM), caused by mutations in thin filament proteins, manifests as moderate cardiac hypertrophy and is associated with sudden cardiac death (SCD). We identified a new de novo variant, c.656A>T (p.D219V), in the TPM1 gene e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afe4d2e3cb8bb53b1fdeba5b061fffac
Autor:
Dmitrii I. Levitsky, Valentina Y. Berg, Galina V. Kopylova, Alexander M. Matyushenko, Sergey Y. Bershitsky, D. V. Shchepkin
Publikováno v:
Journal of Muscle Research and Cell Motility. 42:343-353
Phosphorylation of α-tropomyosin (Tpm1.1), a predominant Tpm isoform in the myocardium, is one of the regulatory mechanisms of the heart contractility. The Tpm 1.1 molecule has one site of phosphorylation, Ser283. The degree of the Tpm phosphorylati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::30b04e0f531bb74fcbd82b5c8658934d
https://doi.org/10.1007/s10974-020-09593-4
https://doi.org/10.1007/s10974-020-09593-4
Autor:
Sergey Yu. Kleymenov, Victoria V. Nefedova, Dmitrii I. Levitsky, Andrey K. Tsaturyan, Natalia A. Koubassova, Alexander M. Matyushenko, Vera A. Borzova
Publikováno v:
International Journal of Biological Macromolecules. 166:424-434
We applied various methods to investigate how mutations S283D and S61D that mimic phosphorylation of tropomyosin (Tpm) affect structural and functional properties of cardiac Tpm carrying cardiomyopathy-associated mutations in different parts of its m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1fc1b6c169f7035030af30b09cdd9ad7
https://doi.org/10.1016/j.ijbiomac.2020.10.201
https://doi.org/10.1016/j.ijbiomac.2020.10.201
Autor:
Victoria V. Nefedova, Galina V. Kopylova, Daniil V. Shchepkin, Anastasia M. Kochurova, Olga I. Kechko, Vera A. Borzova, Natalia S. Ryabkova, Ivan A. Katrukha, Vladimir A. Mitkevich, Sergey Y. Bershitsky, Dmitrii I. Levitsky, Alexander M. Matyushenko
Publikováno v:
International Journal of Molecular Sciences; Volume 23; Issue 24; Pages: 15723
Tropomyosin (Tpm) mutations cause inherited cardiac diseases such as hypertrophic and dilated cardiomyopathies. We applied various approaches to investigate the role of cardiac troponin (Tn) and especially the troponin T (TnT) in the pathogenic effec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05b365e0addc1992fad217ed2a945193
https://doi.org/10.3390/ijms232415723
https://doi.org/10.3390/ijms232415723
Autor:
Daria S Logvinova, Denis I Markov, Olga P Nikolaeva, Nikolai N Sluchanko, Dmitry S Ushakov, Dmitrii I Levitsky
Publikováno v:
PLoS ONE, Vol 10, Iss 9, p e0137517 (2015)
Myosin head (myosin subfragment 1, S1) consists of two major structural domains, the motor (or catalytic) domain and the regulatory domain. Functioning of the myosin head as a molecular motor is believed to involve a rotation of the regulatory domain
Externí odkaz:
https://doaj.org/article/71546a5e73e740959df65ee1e34c650b
Autor:
D. V. Shchepkin, Alexander M. Matyushenko, Natalia A. Koubassova, Galina V. Kopylova, Sergey Y. Bershitsky, Andrey K. Tsaturyan, Dmitrii I. Levitsky
Publikováno v:
Journal of Muscle Research and Cell Motility. 41:55-70
Tropomyosin is a dimer coiled-coil actin-binding protein. Adjacent tropomyosin molecules connect each other ‘head-to-tail’ via an overlap junction and form a continuous strand that winds around an actin filament and controls the actin–myosin in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9acc3b750a8d03828c8efaded238fcd
https://doi.org/10.1007/s10974-019-09552-8
https://doi.org/10.1007/s10974-019-09552-8