Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Katarzyna Robaszkiewicz"'
Publikováno v:
Cell calcium. 99
S100A6 is a Ca
Publikováno v:
International Journal of Molecular Sciences
Volume 22
Issue 8
International Journal of Molecular Sciences, Vol 22, Iss 4036, p 4036 (2021)
Volume 22
Issue 8
International Journal of Molecular Sciences, Vol 22, Iss 4036, p 4036 (2021)
Tropomyosin is a two-chain coiled coil protein, which together with the troponin complex controls interactions of actin with myosin in a Ca2+-dependent manner. In fast skeletal muscle, the contractile actin filaments are regulated by tropomyosin isof
Publikováno v:
Scientific Reports, Vol 10, Iss 1, Pp 1-12 (2020)
Scientific Reports
Scientific Reports
S100A6 is a low molecular weight Ca2+-binding protein belonging to the S100 family. Many reports indicate that in the cell S100A6 has an influence on the organization of actin filaments, but so far no direct interaction between S100A6 and actin has b
Publikováno v:
International Journal of Molecular Sciences
Volume 21
Issue 12
International Journal of Molecular Sciences, Vol 21, Iss 4285, p 4285 (2020)
Volume 21
Issue 12
International Journal of Molecular Sciences, Vol 21, Iss 4285, p 4285 (2020)
In striated muscle the extent of the overlap between actin and myosin filaments contributes to the development of force. In slow twitch muscle fibers actin filaments are longer than in fast twitch fibers, but the mechanism which determines this diffe
Autor:
Katarzyna Robaszkiewicz, Vladimir V. Sirenko, Olga E. Karpicheva, Joanna Moraczewska, Zoya I. Krutetskaya, Armen O. Simonyan, Yurii S. Borovikov, Małgorzata Śliwinska
Publikováno v:
Archives of Biochemistry and Biophysics. 644:17-28
Using the polarized photometry technique we have studied the effects of two amino acid replacements, E240K and R244G, in tropomyosin (Tpm1.1) on the position of Tpm1.1 on troponin-free actin filaments and the spatial arrangement of actin monomers and
Publikováno v:
Cell Calcium. 99:102457
S100A6 is a Ca2+-binding protein belonging to the S100 family. Many reports indicate that S100A6 is involved in actin filament organization, however the mechanism of S100A6 action in this process is not fully understood. By screening S100A6 binding p
Autor:
Marta Czajkowska, Katarzyna Robaszkiewicz, Alla S. Kostyukova, Wenjun Zheng, Thu Ly, Han Wen, Joanna Moraczewska, Małgorzata Śliwinska
Publikováno v:
FEBS J
Tropomyosin binds along actin filaments and regulates myosin binding to control muscle contraction. Tropomodulin binds to the pointed end of a filament and regulates actin dynamics, which maintains the length of a thin filament. To define the structu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b7275b8201053d799567b45d012da56
https://europepmc.org/articles/PMC7202179/
https://europepmc.org/articles/PMC7202179/
Autor:
Katarzyna Robaszkiewicz, Joanna Moraczewska, Wenjun Zheng, Marta Czajkowska, Małgorzata Śliwinska
Publikováno v:
Biochimica et biophysica acta. Proteins and proteomics. 1866(4)
Tropomyosin polymerizes along actin filaments and together with troponin regulates muscle contraction in a Ca-dependent manner. Actin-binding periods are homologous residues, which repeat along tropomyosin sequence, form tropomyosin-actin interface a
Publikováno v:
Biochimica et biophysica acta. Proteins and proteomics. 1865(1)
Tropomyosin and cofilin are actin-binding proteins which control dynamics of actin assembly and disassembly. Tropomyosin isoforms can either inhibit or enhance cofilin activity, but the mechanism of this diverse regulation is not well understood. In
Publikováno v:
Postępy Higieny i Medycyny Doświadczalnej, Vol 65, Iss 846636, Pp 347-356 (2011)
Postępy Higieny i Medycyny Doświadczalnej, Vol 65, Pp 347-356 (2011)
Postępy Higieny i Medycyny Doświadczalnej, Vol 65, Pp 347-356 (2011)
Wrodzone miopatie są heterogenną pod względem klinicznym i genetycznym grupą chorób układu mięśniowego, charakteryzującą się strukturalnymi zaburzeniami w obrębie włókien mięśniowych oraz osłabieniem i deformacją różnych partii mi