Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Cytoplasmic Vesicles/metabolism"'
Autor:
Vincent Olieric, Valentina Cecatiello, Silvia Monzani, Julien Colombani, Valentina Palmerini, Ditte S. Andersen, Sara Mari, Rihab Loudhaief, Marina Mapelli, Quentin Laurichesse, Sebastiano Pasqualato
Publikováno v:
Nature Communications
Palmerini, V, Monzani, S, Laurichesse, Q, Loudhaief, R, Mari, S, Cecatiello, V, Olieric, V, Pasqualato, S, Colombani, J, Andersen, D S & Mapelli, M 2021, ' Drosophila TNFRs Grindelwald and Wengen bind Eiger with different affinities and promote distinct cellular functions ', Nature Communications, vol. 12, 2070 . https://doi.org/10.1038/s41467-021-22080-9
'Nature Communications ', vol: 12, pages: 2070-1-2070-12 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Palmerini, V, Monzani, S, Laurichesse, Q, Loudhaief, R, Mari, S, Cecatiello, V, Olieric, V, Pasqualato, S, Colombani, J, Andersen, D S & Mapelli, M 2021, ' Drosophila TNFRs Grindelwald and Wengen bind Eiger with different affinities and promote distinct cellular functions ', Nature Communications, vol. 12, 2070 . https://doi.org/10.1038/s41467-021-22080-9
'Nature Communications ', vol: 12, pages: 2070-1-2070-12 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
The Drosophila tumour necrosis factor (TNF) ligand-receptor system consists of a unique ligand, Eiger (Egr), and two receptors, Grindelwald (Grnd) and Wengen (Wgn), and therefore provides a simple system for exploring the interplay between ligand and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52c287e7402c450fb99e08121a0e23be
https://doi.org/10.1038/s41467-021-22080-9
https://doi.org/10.1038/s41467-021-22080-9
Autor:
Ariane Dimitrov, Raja Bonifay, Cécile Bougeret, Hugo Bousquet, Gaëlle Bressanelli, Arnaud Echard, Vincent Fraisier, Bruno Goud, Olena Pylypenko, Sabine Bardin, Catherine Guillou, Anne Houdusse, Stéphanie Miserey-Lenkei
Publikováno v:
Nature Communications
Nature Communications, 2017, 8 (1), pp.1254. ⟨10.1038/s41467-017-01266-0⟩
Nature Communications, Vol 8, Iss 1, Pp 1-13 (2017)
Nature Communications, Nature Publishing Group, 2017, 8 (1), pp.1254. ⟨10.1038/s41467-017-01266-0⟩
'Nature Communications ', vol: 8, pages: 1254-1-1254-13 (2017)
Nature Communications, 2017, 8 (1), pp.1254. ⟨10.1038/s41467-017-01266-0⟩
Nature Communications, Vol 8, Iss 1, Pp 1-13 (2017)
Nature Communications, Nature Publishing Group, 2017, 8 (1), pp.1254. ⟨10.1038/s41467-017-01266-0⟩
'Nature Communications ', vol: 8, pages: 1254-1-1254-13 (2017)
The actin and microtubule cytoskeletons play important roles in Golgi structure and function, but how they are connected remain poorly known. In this study, we investigated whether RAB6 GTPase, a Golgi-associated RAB involved in the regulation of sev
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94563cceacba255a8dcff764307474b1
https://doi.org/10.1038/s41467-017-01266-0
https://doi.org/10.1038/s41467-017-01266-0
Publikováno v:
Drabek, K, van de Peppel, J, Eijken, M & van Leeuwen, J P T M 2011, ' GPM6B regulates osteoblast function and induction of mineralization by controlling cytoskeleton and matrix vesicle release ', Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research, vol. 26, no. 9, pp. 2045-51 . https://doi.org/10.1002/jbmr.435
Journal of Bone and Mineral Research, 26(9), 2045-2051. Wiley-Blackwell
Journal of Bone and Mineral Research, 26(9), 2045-2051. Wiley-Blackwell
Neuronal membrane glycoprotein gene (GPM6B) encodes a membrane glycoprotein that belongs to the proteolipid protein family. We identified GPM6B as a gene that is strongly upregulated during osteoblast differentiation. To investigate the role of GPM6B
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b50fca442a0b893998b8481f0c42064f
https://hdl.handle.net/1765/33944
https://hdl.handle.net/1765/33944
Publikováno v:
Traffic, Vol. 10, No 2 (2009) pp. 186-200
Previous biochemical work has revealed two parallel routes of exit from the endoplasmic reticulum (ER) in the yeast Saccharomyces cerevisiae, one seemingly specific for glycosyl-phosphatidylinositol (GPI)-anchored proteins. Using the coat protein II
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64ec2727cee58378696dd0ab81e75794
https://doi.org/10.1111/j.1600-0854.2008.00857.x
https://doi.org/10.1111/j.1600-0854.2008.00857.x
Autor:
Hagemeijer, Marne C, Verheije, Monique H, Ulasli, Mustafa, Shaltiël, Indra A, de Vries, Lisa A, Reggiori, Fulvio, Rottier, Peter J M, de Haan, Cornelis A M, LS Pathologie, LS Virologie
Publikováno v:
Hagemeijer, M C, Verheije, M H, Ulasli, M, Shaltiël, I A, de Vries, L A, Reggiori, F, Rottier, P J M & de Haan, C A M 2010, ' Dynamics of coronavirus replication-transcription complexes ', Journal of Virology, vol. 84, no. 4, pp. 2134-49 . https://doi.org/10.1128/JVI.01716-09
Journal of Virology
Journal of Virology, 84(4), 2134. American Society for Microbiology
Journal of Virology
Journal of Virology, 84(4), 2134. American Society for Microbiology
Coronaviruses induce in infected cells the formation of double-membrane vesicles (DMVs) in which the replication-transcription complexes (RTCs) are anchored. To study the dynamics of these coronavirus replicative structures, we generated recombinant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05a952b462fe912c7a61b65ccd69f054
https://dspace.library.uu.nl/handle/1874/315376
https://dspace.library.uu.nl/handle/1874/315376
Autor:
Sookja K. Chung, Sidney Tam, Samuel C. K. Chung, Amy K. M. Lam, Billy K. C. Chow, Jessica Y. S. Chu
Aquaporin 2 (AQP2) is responsible for regulating the concentration of urine in the collecting tubules of the kidney under the control of vasopressin (Vp). Studies using Vp-deficient Brattleboro rats, however, indicated the existence of substantial Vp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::503c55c8bb99fff21d4e0a8b3905ce14
http://hdl.handle.net/10722/67894
http://hdl.handle.net/10722/67894
Autor:
Andreas T. Grasskamp, Martin Kollmar, Janine Tittel, Margaret A. Titus, Petra Schwille, Eugen Kerkhoff, Florian Chardon, Bruno Goud, Thomas Weidemann, Gilles Malherbe, Olena Pylypenko, Annette Samol-Wolf, Bruno Baron, Patrick England, Carina Ida Luise Michel, Sabine Weiss, Alistair N. Hume, Anne Houdusse, Tobias Welz
Publikováno v:
eLife
eLife, 2016, 5, pp.e17523. ⟨10.7554/eLife.17523⟩
eLife, eLife Sciences Publication, 2016, 5, pp.e17523. ⟨10.7554/eLife.17523⟩
eLife, Vol 5 (2016)
eLife, eLife Sciences Publication, 2016, 5, ⟨10.7554/eLife.17523⟩
eLife, 2016, 5, pp.e17523. ⟨10.7554/eLife.17523⟩
eLife, eLife Sciences Publication, 2016, 5, pp.e17523. ⟨10.7554/eLife.17523⟩
eLife, Vol 5 (2016)
eLife, eLife Sciences Publication, 2016, 5, ⟨10.7554/eLife.17523⟩
There is growing evidence for a coupling of actin assembly and myosin motor activity in cells. However, mechanisms for recruitment of actin nucleators and motors on specific membrane compartments remain unclear. Here we report how Spir actin nucleato
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b75111f3d4af95e8ee9b72d320b7cc30