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Autor:
Joanna Moraczewska, Paul Trevorrow
Publikováno v:
Cytoskeleton.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0cd85e9830d1db6ab4f937237c69b0bb
https://doi.org/10.1002/cm.21746
https://doi.org/10.1002/cm.21746
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
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::075157c49fa2aa5ae34e796e3706d88b
https://pubmed.ncbi.nlm.nih.gov/34834072
https://pubmed.ncbi.nlm.nih.gov/34834072
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8dd9e67365221a77c91b55d0140f0620
http://europepmc.org/articles/PMC7109180
http://europepmc.org/articles/PMC7109180
Publikováno v:
Cell calcium. 99
S100A6 is a Ca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::61d3ce0f06ea04ce6bca4ef505ff8c5d
https://pubmed.ncbi.nlm.nih.gov/34464867
https://pubmed.ncbi.nlm.nih.gov/34464867
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5dc6180c950e4634e62672fb97ddf32
http://europepmc.org/articles/PMC8070786
http://europepmc.org/articles/PMC8070786
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
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64b117f3743f711229963fcd9fafca5d
https://doi.org/10.1038/s41598-020-69752-y
https://doi.org/10.1038/s41598-020-69752-y
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a47fa13b4f4c29d200e5bfb1bc496394