Zobrazeno 1 - 10
of 57
pro vyhledávání: '"Joanna Moraczewska"'
Autor:
Katarzyna Robaszkiewicz, Małgorzata Siatkowska, Renske I. Wadman, Erik-Jan Kamsteeg, Zhiyong Chen, Ashirwad Merve, Matthew Parton, Enrico Bugiardini, Charlotte de Bie, Joanna Moraczewska
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 22, p 16147 (2023)
A novel variant of unknown significance c.8A > G (p.Glu3Gly) in TPM3 was detected in two unrelated families. TPM3 encodes the transcript variant Tpm3.12 (NM_152263.4), the tropomyosin isoform specifically expressed in slow skeletal muscle fibers. The
Externí odkaz:
https://doaj.org/article/deff2e4f2b5f4386a039e032b45df582
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 22, p 16457 (2023)
Uniform actin filament length is required for synchronized contraction of skeletal muscle. In myopathies linked to mutations in tropomyosin (Tpm) genes, irregular thin filaments are a common feature, which may result from defects in length maintenanc
Externí odkaz:
https://doaj.org/article/5a23e8371f0e4881b8fc4f303d3070b4
Autor:
Balaganesh Kuruba, Marta Kaczmarek, Małgorzata Kęsik-Brodacka, Magdalena Fojutowska, Małgorzata Śliwinska, Alla S. Kostyukova, Joanna Moraczewska
Publikováno v:
Molecules, Vol 26, Iss 22, p 6980 (2021)
Tropomyosin (Tpm) is an actin-binding coiled-coil protein. In muscle, it regulates contractions in a troponin/Ca2+-dependent manner and controls the thin filament lengths at the pointed end. Due to its size and periodic structure, it is difficult to
Externí odkaz:
https://doaj.org/article/ffa9559956aa48ffac03a76114657829
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 8, 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
Externí odkaz:
https://doaj.org/article/974f136b50494f5c90b15469b072bc4c
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 12, 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
Externí odkaz:
https://doaj.org/article/0c8dc0a4cb414d1e8c2d942f3c1cbebc
Publikováno v:
PeerJ, Vol 1, p e181 (2013)
Tropomyosins are actin-binding regulatory proteins which overlap end-to-end along the filament. High resolution structures of the overlap regions were determined for muscle and non-muscle tropomyosins in the absence of actin. Conformations of the jun
Externí odkaz:
https://doaj.org/article/1450c9a60ea24be394956d2a9e421bf9
Autor:
Joanna Moraczewska, Paul Trevorrow
Publikováno v:
Cytoskeleton.
Autor:
Joanna Moraczewska, Małgorzata Śliwinska, Balaganesh Kuruba, Magdalena Fojutowska, Marta Kaczmarek, Alla S. Kostyukova, Małgorzata Kęsik-Brodacka
Publikováno v:
Molecules
Volume 26
Issue 22
Molecules, Vol 26, Iss 6980, p 6980 (2021)
Volume 26
Issue 22
Molecules, Vol 26, Iss 6980, p 6980 (2021)
Tropomyosin (Tpm) is an actin-binding coiled-coil protein. In muscle, it regulates contractions in a troponin/Ca2+-dependent manner and controls the thin filament lengths at the pointed end. Due to its size and periodic structure, it is difficult to
Publikováno v:
Cell calcium. 99
S100A6 is a Ca
Autor:
Joanna Moraczewska
Publikováno v:
Journal of Muscle Research and Cell Motility
Tropomyosin is the major regulator of the thin filament. In striated muscle its function is to bind troponin complex and control the access of myosin heads to actin in a Ca2+-dependent manner. It also participates in the maintenance of thin filament