Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Gerard Castro"'
Autor:
Agata Szuba, Fouzia Bano, Gerard Castro-Linares, Francois Iv, Manos Mavrakis, Ralf P Richter, Aurélie Bertin, Gijsje H Koenderink
Publikováno v:
eLife, Vol 10 (2021)
Septins are conserved cytoskeletal proteins that regulate cell cortex mechanics. The mechanisms of their interactions with the plasma membrane remain poorly understood. Here, we show by cell-free reconstitution that binding to flat lipid membranes re
Externí odkaz:
https://doaj.org/article/3826cc62710c47248207cb9c6cf3745b
Autor:
Carla Silva Martins, Cyntia Taveneau, Gerard Castro-Linares, Mikhail Baibakov, Nicolas Buzhinsky, Mar Eroles, Violeta Milanović, Shizue Omi, Jean-Denis Pedelacq, Francois Iv, Léa Bouillard, Alexander Llewellyn, Maxime Gomes, Mayssa Belhabib, Mira Kuzmić, Pascal Verdier-Pinard, Stacey Lee, Ali Badache, Sanjay Kumar, Cristel Chandre, Sophie Brasselet, Felix Rico, Olivier Rossier, Gijsje H. Koenderink, Jerome Wenger, Stéphanie Cabantous, Manos Mavrakis
Publikováno v:
Journal of Cell Biology
Journal of Cell Biology, 2023, 222 (3), pp.e202203016. ⟨10.1083/jcb.202203016⟩
Journal of Cell Biology, 2022, 222 (3), pp.e202203016. ⟨10.1083/jcb.202203016⟩
The Journal of cell biology, vol 222, iss 3
Journal of Cell Biology, 2023, 222 (3), pp.e202203016. ⟨10.1083/jcb.202203016⟩
Journal of Cell Biology, 2022, 222 (3), pp.e202203016. ⟨10.1083/jcb.202203016⟩
The Journal of cell biology, vol 222, iss 3
International audience; Septins are cytoskeletal proteins conserved from algae and protists to mammals. A unique feature of septins is their presence as heteromeric complexes that polymerize into filaments in solution and on lipid membranes. Although
Autor:
Magda Rodrigues, Maxime Gomes, Jindřiška Leischner Fialová, Ali Badache, Alex Llewellyn, Francois, Danièle Salaün, Pascal Verdier-Pinard, Gijsje H. Koenderink, Yuxiang Liu, Mayssa Belhabib, Taro Tachibana, Gerard Castro Linares, Manos Mavrakis, Keisuke Asano, Mira Kuzmić, Daniel Isnardon
Publikováno v:
Journal of Cell Science, 135(1)
Septins, a family of GTP-binding proteins that assemble into higher order structures, interface with the membrane, actin filaments and microtubules, and are thus important regulators of cytoarchitecture. Septin 9 (SEPT9), which is frequently overexpr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::639d91a5b73db06478cbf478f31d39d4
http://resolver.tudelft.nl/uuid:cf35b74b-42ba-472c-978a-bef6b274d3a9
http://resolver.tudelft.nl/uuid:cf35b74b-42ba-472c-978a-bef6b274d3a9
Autor:
Gijsje H. Koenderink, Manos Mavrakis, Aurélie Bertin, Carla Silva Martins, Francois Iv, Jeffrey den Haan, Gerard Castro-Linares
Publikováno v:
Journal of Visualized Experiments, 2022(184)
Journal of visualized experiments : JoVE
Journal of visualized experiments : JoVE, JoVE, 2022, ⟨10.3791/63871⟩
Journal of visualized experiments : JoVE, 2022, 184, ⟨10.3791/63871⟩
Journal of visualized experiments : JoVE
Journal of visualized experiments : JoVE, JoVE, 2022, ⟨10.3791/63871⟩
Journal of visualized experiments : JoVE, 2022, 184, ⟨10.3791/63871⟩
International audience; Septins are a family of conserved eukaryotic GTP-binding proteins that can form cytoskeletal filaments and higher-order structures from hetero-oligomeric complexes. They interact with other cytoskeletal components and the cell
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fc42ad77b54865e1c8a5e5284a7c8bd
http://resolver.tudelft.nl/uuid:45884386-e383-4207-a835-027c6f5a1ebb
http://resolver.tudelft.nl/uuid:45884386-e383-4207-a835-027c6f5a1ebb
Akademický článek
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Autor:
Kuzmić, Mira, Linares, Gerard Castro, Fialovÿ, Jindřiška Leischner, Iv, François, Salaün, Danièle, Llewellyn, Alex, Gomes, Maxime, Belhabib, Mayssa, Yuxiang Liu, Asano, Keisuke, Rodrigues, Magda, Isnardon, Daniel, Tachibana, Taro, Koenderink, Gijsje H., Badache, Ali, Mavrakis, Manos, Verdier-Pinard, Pascal
Publikováno v:
Journal of Cell Science; Jan2023, Vol. 136 Issue 2, p1-18, 18p
Autor:
Laurie Ramond, Carla Silva Martins, Stéphanie Cabantous, Gerard Castro-Linares, Jérôme Wenger, Francois, Aurélie Bertin, Feng-Ching Tsai, Cyntia Taveneau, Renaud Vincentelli, Koyomi Nakazawa, Luc Camoin, Stéphane Audebert, Alex Llewellyn, Aurélie Di Cicco, Manos Mavrakis, Pascale Barbier, Mayssa Belhabib, Pascal Verdier-Pinard, Gijsje H. Koenderink
Publikováno v:
Journal of Cell Science
Journal of Cell Science, Company of Biologists, 2021, 134 (15), pp.jcs258484. ⟨10.1242/jcs.258484⟩
Journal of Cell Science, 2021, 134 (15), pp.jcs258484. ⟨10.1242/jcs.258484⟩
Journal of Cell Science, 134(15)
Journal of Cell Science, Company of Biologists, 2021, 134 (15), pp.jcs258484. ⟨10.1242/jcs.258484⟩
Journal of Cell Science, 2021, 134 (15), pp.jcs258484. ⟨10.1242/jcs.258484⟩
Journal of Cell Science, 134(15)
Septin GTP-binding proteins contribute essential biological functions that range from the establishment of cell polarity to animal tissue morphogenesis. Human septins in cells form hetero-octameric septin complexes containing the ubiquitously express
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3470c9090885fb43ab13209ff605666b
https://hal.archives-ouvertes.fr/hal-03119193
https://hal.archives-ouvertes.fr/hal-03119193
Publikováno v:
Biomedical Instrumentation & Technology. 53:444-451
Autor:
Pascal Verdier-Pinard, Gijsje H. Koenderink, Alex Llewellyn, Maxime Gomes, Keisuke Asano, Danièle Salaün, Taro Tachibana, Jindřiška Leischner Fialová, Yuxiang Liu, Gerard Castro Linares, Mira Kuzmić, Manos Mavrakis, Ali Badache, Francois, Mayssa Belhabib
Publikováno v:
Journal of Cell Science
Journal of Cell Science, Company of Biologists, In press, ⟨10.1101/2021.04.06.438596⟩
Journal of Cell Science, Company of Biologists, In press, ⟨10.1101/2021.04.06.438596⟩
Septins, a family of GTP-binding proteins assembling into higher order structures, interface with the membrane, actin filaments and microtubules, which positions them as important regulators of cytoarchitecture. Septin 9 (Sept9), which is frequently
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::388e18221a63183826708b01cf24c0a7
https://doi.org/10.1101/2021.04.06.438596
https://doi.org/10.1101/2021.04.06.438596