Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Nicolas Audugé"'
Autor:
Benoit Souquet, Ellen Freed, Alessandro Berto, Vedrana Andric, Nicolas Audugé, Bernardo Reina-San-Martin, Elizabeth Lacy, Valérie Doye
Publikováno v:
Cell Reports, Vol 23, Iss 8, Pp 2443-2454 (2018)
Summary: Nup133 belongs to the Y-complex, a key component of the nuclear pore complex (NPC) scaffold. Studies on a null mutation in mice previously revealed that Nup133 is essential for embryonic development but not for mouse embryonic stem cell (mES
Externí odkaz:
https://doaj.org/article/a2307bf7c7884691abc72400fd4b59b8
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, 2019, 47 (12), pp.6184-6194. ⟨10.1093/nar/gkz373⟩
Nucleic Acids Research, Oxford University Press, 2019, 47 (12), pp.6184-6194. ⟨10.1093/nar/gkz373⟩
Nucleic Acids Research, 2019, 47 (12), pp.6184-6194. ⟨10.1093/nar/gkz373⟩
Nucleic Acids Research, Oxford University Press, 2019, 47 (12), pp.6184-6194. ⟨10.1093/nar/gkz373⟩
Chromatin accessibility to protein factors is critical for genome activities. Dynamic changes in nucleosomal DNA compaction and higher order chromatin structures are expected to allow specific sites to be accessible to regulatory factors and the tran
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9364c2cf2f03f9af2a2ff52b493eab34
https://univ-rennes.hal.science/hal-02277997
https://univ-rennes.hal.science/hal-02277997
Vinculin head–tail interaction defines multiple early mechanisms for cell substrate rigidity sensing
Publikováno v:
Integr Biol (Camb)
Integr Biol (Camb), 2016, 8 (6), pp.693-703. ⟨10.1039/c5ib00307e⟩
Integr Biol (Camb), 2016, 8 (6), pp.693-703. ⟨10.1039/c5ib00307e⟩
Rigidity sensing is a critical determinant of cell fate and behavior but its molecular mechanisms are poorly understood. Focal adhesions (FAs) are complexes that anchor cells to the matrix. Among their components, vinculin undergoes an auto-inhibitor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fa3237f6811e1b97aa31b613eb81ed0
https://hal.archives-ouvertes.fr/hal-01401565
https://hal.archives-ouvertes.fr/hal-01401565
Publikováno v:
Biophysical Journal
Biophysical Journal, Biophysical Society, 2008, epub ahead of print. ⟨10.1529/biophysj.108.131276⟩
Biophysical Journal, Biophysical Society, 2008, epub ahead of print. ⟨10.1529/biophysj.108.131276⟩
International audience; Quantitative analysis in F?er Resonance Energy Transfer (FRET) experiments in live cells for protein interaction studies is still a challenging issue. In a two component system (FRET and no FRET donor species), fitting of Fluo
Autor:
Xavier Baudin, Marie-Claude Geoffroy, Valérie Doye, Kevin Van Bortle, Imène B. Bouhlel, Annabelle Alves, Stéphanie Morchoisne-Bolhy, Nicolas Audugé, Maureen A. Powers
Publikováno v:
Molecular Biology of the Cell
Molecular Biology of the Cell, American Society for Cell Biology, 2015, 26 (12), pp.2343-2356. ⟨10.1091/mbc.E15-02-0060⟩
Molecular Biology of the Cell, American Society for Cell Biology, 2015, 26 (12), pp.2343-56. ⟨10.1091/mbc.E15-02-0060⟩
Molecular Biology of the Cell, American Society for Cell Biology, 2015, 26 (12), pp.2343-2356. ⟨10.1091/mbc.E15-02-0060⟩
Molecular Biology of the Cell, American Society for Cell Biology, 2015, 26 (12), pp.2343-56. ⟨10.1091/mbc.E15-02-0060⟩
The Nup107-160 nuclear pore subcomplex (Y-complex) and the chromatin-binding nucleoporin Elys dynamically colocalize with Nup98 and the export factor CRM1 in nuclear GLFG bodies present in HeLa sublines. Thus, in addition to its structural role at th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b584b5f67b2dc54598c6184d0fbda515
https://hal-cnrs.archives-ouvertes.fr/hal-03083392
https://hal-cnrs.archives-ouvertes.fr/hal-03083392
Publikováno v:
Methods in Molecular Biology
Methods in Molecular Biology, Humana Press/Springer Imprint, 2014, 1076, pp.683-98. ⟨10.1007/978-1-62703-649-8_31⟩
Methods in Molecular Biology, 2014, 1076, pp.683-98. ⟨10.1007/978-1-62703-649-8_31⟩
Methods in Molecular Biology ISBN: 9781627036481
Methods in Molecular Biology (Clifton then Totova)
Methods in Molecular Biology (Clifton then Totova), Humana Press (Springer Imprint), 2014, 1076, pp.683-98. 〈10.1007/978-1-62703-649-8_31〉
Methods in Molecular Biology, Humana Press/Springer Imprint, 2014, 1076, pp.683-98. ⟨10.1007/978-1-62703-649-8_31⟩
Methods in Molecular Biology, 2014, 1076, pp.683-98. ⟨10.1007/978-1-62703-649-8_31⟩
Methods in Molecular Biology ISBN: 9781627036481
Methods in Molecular Biology (Clifton then Totova)
Methods in Molecular Biology (Clifton then Totova), Humana Press (Springer Imprint), 2014, 1076, pp.683-98. 〈10.1007/978-1-62703-649-8_31〉
International audience; Dual-color FCS is a powerful method to monitor protein-protein interactions in living cells. The main idea is based on the cross-correlation analysis of temporal fluorescence intensity fluctuations of two fluorescent proteins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6482d53c5e33f1aa2baf3f20c8e79242
https://hal.archives-ouvertes.fr/hal-00951087
https://hal.archives-ouvertes.fr/hal-00951087
Publikováno v:
Microscopy Research and Technique
Microscopy Research and Technique, Wiley, 2011, 74 (8), pp.788-93. ⟨10.1002/jemt.21015⟩
Microscopy Research and Technique, 2011, 74 (8), pp.788-93. ⟨10.1002/jemt.21015⟩
Microscopy Research and Technique, Wiley, 2011, 74 (8), pp.788-93. ⟨10.1002/jemt.21015⟩
Microscopy Research and Technique, 2011, 74 (8), pp.788-93. ⟨10.1002/jemt.21015⟩
International audience; Dual-color fluorescence correlation spectroscopy is an interesting method to quantify protein interaction in living cells. But, when performing these experiments, one must compensate for a known spectral bleed through artifact
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13ded7d78e7b5d47a305acf3de37c135
https://www.hal.inserm.fr/inserm-00604664
https://www.hal.inserm.fr/inserm-00604664
Publikováno v:
Imaging: A Laboratory Manual
Rafael Yuste (ed.). Imaging: A Laboratory Manual, CSH Press, 2011
Rafael Yuste (ed.). Imaging: A Laboratory Manual, CSH Press, 2011
Quantitative analysis in Förster resonance energy transfer (FRET) imaging studies of protein–protein interactions within live cells is still a challenging issue. Many cellular biology applications aim at the determination of the space and time var
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76caac05200586c5f86088d23e959b94
https://hal-univ-rennes1.archives-ouvertes.fr/hal-01121040
https://hal-univ-rennes1.archives-ouvertes.fr/hal-01121040
Autor:
Nicolas Audugé, Jean-Claude Mevel, Maïté Coppey-Moisan, Marc Tramier, Sergi Padilla-Parra, Hervé Lalucque
Publikováno v:
Biophysical Journal
Biophysical Journal, Biophysical Society, 2009, 97 (8), pp.2368-76. ⟨10.1016/j.bpj.2009.07.044⟩
Biophysical Journal, Biophysical Society, 2009, 97 (8), pp.2368-76. ⟨10.1016/j.bpj.2009.07.044⟩
International audience; The fluorescent-protein based fluorescence resonance energy transfer (FRET) approach is a powerful method for quantifying protein-protein interactions in living cells, especially when combined with fluorescence lifetime imagin