Z
Zofia Ostrowska
Researcher at Kazimierz Wielki University in Bydgoszcz
Publications - 5
Citations - 114
Zofia Ostrowska is an academic researcher from Kazimierz Wielki University in Bydgoszcz. The author has contributed to research in topics: Actin & Tropomyosin. The author has an hindex of 5, co-authored 5 publications receiving 92 citations.
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Journal ArticleDOI
Cofilin - a protein controlling dynamics of actin filaments.
TL;DR: Cofilins are evolutionary conserved proteins present in all Eukaryotic cells, involved in development of cancer, neurodegenerative diseases, congenital myopathies and cardiomyopathies, and cofilin 2, which dominates in mature skeletal and cardiac muscles.
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Tropomyosin isoforms differentially modulate the regulation of actin filament polymerization and depolymerization by cofilins
TL;DR: The results reveal that isoform‐specific interactions with actin filament permit tropomyosins to discriminate between cofilin isoforms and to differentially regulate their activities.
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CacyBP/SIP as a novel modulator of the thin filament.
Ewelina Jurewicz,Zofia Ostrowska,Jolanta Jozwiak,Maria Jolanta Redowicz,Wieslawa Lesniak,Joanna Moraczewska,Anna Filipek +6 more
TL;DR: The results suggest that CacyBP/SIP, through its interaction with both actin and tropomyosin, regulates the organization and functional properties of the thin filament.
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Regulation of actin filament turnover by cofilin-1 and cytoplasmic tropomyosin isoforms.
TL;DR: The effects of actin dynamics regulation by four cytoskeletal tropomyosin isoforms and cofilin-1 were studied with the use of biochemical and fluorescent microscopy assays and it was concluded that the effects were executed through different actin affinities of tropomyOSinisoforms and cooperativities of tropomeosin and coFilin- 1 binding.
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Impaired tropomyosin-troponin interactions reduce activation of the actin thin filament.
TL;DR: It is demonstrated that the myopathy-causing mutations affected tropomyosin structure and led to changes in interactions between tropomyo-troponin and troponin, which impaired the transition of the thin filament from the inactive off to the active on state.