Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Frédéric Wissler"'
Autor:
Frédéric Wissler, Sophie Quintin, Harald Hutter, Frédéric Landmann, Satis Sookhareea, Marie Diogon, Nicolas Vitale, Yasuko Nagamatsu, Michel Labouesse
Publikováno v:
Development (Cambridge, England)
Development (Cambridge, England), Company of Biologists, 2007, 134 (13), pp.2469-79. ⟨10.1242/dev.005074⟩
Development (Cambridge, England), Company of Biologists, 2007, 134 (13), pp.2469-79. ⟨10.1242/dev.005074⟩
Embryonic morphogenesis involves the coordinate behaviour of multiple cells and requires the accurate balance of forces acting within different cells through the application of appropriate brakes and throttles. In C. elegans, embryonic elongation is
Autor:
Sophie Quintin, Michel Labouesse, Christelle Gally, Frédéric Landmann, Hala Zahreddine, Frédéric Wissler
Publikováno v:
Development (Cambridge, England)
Development (Cambridge, England), Company of Biologists, 2009, 136 (18), pp.3109-19. ⟨10.1242/dev.039412⟩
Development (Cambridge, England), 2009, 136 (18), pp.3109-19. ⟨10.1242/dev.039412⟩
Development (Cambridge, England), Company of Biologists, 2009, 136 (18), pp.3109-19. ⟨10.1242/dev.039412⟩
Development (Cambridge, England), 2009, 136 (18), pp.3109-19. ⟨10.1242/dev.039412⟩
International audience; Myosin II plays a central role in epithelial morphogenesis; however, its role has mainly been examined in processes involving a single cell type. Here we analyze the structure, spatial requirement and regulation of myosin II d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd53e137971ba2f883f133c72f6fbfd8
https://www.hal.inserm.fr/inserm-00420802
https://www.hal.inserm.fr/inserm-00420802
Autor:
Michel Labouesse, Hala Zahreddine, Frédéric Wissler, Sophie Quintin, Frédéric Landmann, Christelle Gally
Publikováno v:
Mechanisms of Development. 126
Autor:
Michel Labouesse, Frédéric Wissler
Publikováno v:
Nature Cell Biology
Nature Cell Biology, Nature Publishing Group, 2007, 9 (9), pp.1027-9. ⟨10.1038/ncb0907-1027⟩
Nature Cell Biology, Nature Publishing Group, 2007, 9 (9), pp.1027-9. ⟨10.1038/ncb0907-1027⟩
The evolutionarily conserved PAR3–PAR6–aPKC–Cdc42 complex has a well-established role in cell polarity. The exact job of PAR proteins in polarity is not known, but the finding that they affect endocytosis casts new light on their function.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::280725e51882a80cec9558108e47096f
https://hal.archives-ouvertes.fr/hal-00188986
https://hal.archives-ouvertes.fr/hal-00188986