Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Nicanor González-Morales"'
Autor:
Lucas A B Fisher, Belén Carriquí-Madroñal, Tiara Mulder, Sven Huelsmann, Frieder Schöck, Nicanor González-Morales
Publikováno v:
PLoS Genetics, Vol 20, Iss 6, p e1011101 (2024)
Filamins are mechanosensitive actin crosslinking proteins that organize the actin cytoskeleton in a variety of shapes and tissues. In muscles, filamin crosslinks actin filaments from opposing sarcomeres, the smallest contractile units of muscles. Thi
Externí odkaz:
https://doaj.org/article/f8fa05e11c324186be81365d948c7edc
Publikováno v:
Bio-Protocol, Vol 10, Iss 7 (2020)
Protein-protein interactions in Drosophila myofibrils are essential for their function and formation. Bimolecular Fluorescence Complementation (BiFC) is an effective method for studying protein interactions and localization. BiFC relies on the recons
Externí odkaz:
https://doaj.org/article/71262d003e4b4e32872c3910afbf79f0
Commentary: Nanoscopy reveals the layered organization of the sarcomeric H-zone and I-band complexes
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 8 (2020)
Externí odkaz:
https://doaj.org/article/3a239d41773b4f019c50d2fcbe84c83c
Publikováno v:
PLoS ONE, Vol 15, Iss 7, p e0232137 (2020)
In sarcomeres, α-actinin crosslinks thin filaments and anchors them at the Z-disc. Drosophila melanogaster Zasp52 also localizes at Z-discs and interacts with α-actinin via its extended PDZ domain, thereby contributing to myofibril assembly and mai
Externí odkaz:
https://doaj.org/article/43b9f076fc8446c585af1af9db7d9557
Autor:
Nicanor González-Morales, Yu Shu Xiao, Matthew Aaron Schilling, Océane Marescal, Kuo An Liao, Frieder Schöck
Publikováno v:
eLife, Vol 8 (2019)
Myofibrils are huge cytoskeletal assemblies embedded in the cytosol of muscle cells. They consist of arrays of sarcomeres, the smallest contractile unit of muscles. Within a muscle type, myofibril diameter is highly invariant and contributes to its p
Externí odkaz:
https://doaj.org/article/f9789045067d4b7998edb7eacd398ff8
Publikováno v:
Bio-Protocol, Vol 7, Iss 22 (2017)
Sarcomeres, the smallest contractile unit of muscles, are arguably the most impressive actomyosin structure. Yet a complete understanding of sarcomere formation and maintenance is missing. The Drosophila indirect flight muscle (IFM) has proven to be
Externí odkaz:
https://doaj.org/article/b486bff150874cb4a8ca15ddd38cdc04
Publikováno v:
PLoS Genetics, Vol 13, Iss 7, p e1006880 (2017)
Many proteins contribute to the contractile properties of muscles, most notably myosin thick filaments, which are anchored at the M-line, and actin thin filaments, which are anchored at the Z-discs that border each sarcomere. In humans, mutations in
Externí odkaz:
https://doaj.org/article/505c3aeff28442a5b857daee2e6a81a3
Publikováno v:
PLoS Genetics, Vol 12, Iss 10, p e1006400 (2016)
Z-discs are organizing centers that establish and maintain myofibril structure and function. Important Z-disc proteins are α-actinin, which cross-links actin thin filaments at the Z-disc and Zasp PDZ domain proteins, which directly interact with α-
Externí odkaz:
https://doaj.org/article/683eb6bca6bc4adb81f914723fe3f5e9
Autor:
Nicanor González-Morales, Miguel Ángel Mendoza-Ortíz, Liisa M Blowes, Fanis Missirlis, Juan R Riesgo-Escovar
Publikováno v:
PLoS ONE, Vol 10, Iss 7, p e0133499 (2015)
In Drosophila melanogaster, iron is stored in the cellular endomembrane system inside a protein cage formed by 24 ferritin subunits of two types (Fer1HCH and Fer2LCH) in a 1:1 stoichiometry. In larvae, ferritin accumulates in the midgut, hemolymph, g
Externí odkaz:
https://doaj.org/article/6eff797c5fbc4e0f9b6ef7e605dcb005
Publikováno v:
Journal of Cell Science. 135
Myofibrils are the intracellular structures formed by actin and myosin filaments. They are paracrystalline contractile cables with unusually well-defined dimensions. The sliding of actin past myosin filaments powers contractions, and the entire syste
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b526d277b3630c9251841d892e370c5b
https://doi.org/10.1242/jcs.260179
https://doi.org/10.1242/jcs.260179