Zobrazeno 1 - 10
of 65
pro vyhledávání: '"Elisabeth Le Rumeur"'
Autor:
Elisabeth Le Rumeur
Publikováno v:
Biomolecules & Biomedicine, Vol 15, Iss 3 (2015)
Mutations of the dystrophin DMD gene, essentially deletions of one or several exons, are the cause of two devastating and to date incurable diseases, Duchenne (DMD) and Becker (BMD) muscular dystrophies. Depending upon the preservation or not of the
Externí odkaz:
https://doaj.org/article/f6cd618f0bc248409a76229da24d68de
Publikováno v:
PLoS ONE, Vol 6, Iss 8, p e23819 (2011)
Dystrophin is a large protein involved in the rare genetic disease Duchenne muscular dystrophy (DMD). It functions as a mechanical linker between the cytoskeleton and the sarcolemma, and is able to resist shear stresses during muscle activity. In all
Externí odkaz:
https://doaj.org/article/dc015f86c1f740da8707f3c41916764e
Autor:
Olivier Delalande, Jean-François Hubert, Angélique Chéron, Dominique Mias-Lucquin, Elisabeth Le Rumeur
Publikováno v:
Protein Science. 28:561-570
Coiled-coil domain is a structural motif found in proteins crucial for achievement of central biological processes, such as cellular cohesion or neuro-transmission. The coiled-coil fold consists of alpha-helices bundle that can be repeated to form la
Autor:
Liza Mouret, Olivier Delalande, Marie-Sousai Appavou, Jean-François Hubert, Raphael Dos Santos Morais, Anne Martel, Sophie Combet, Elisabeth Le Rumeur, Arnaud Bondon, Javier Pérez
Publikováno v:
Langmuir
Langmuir, 2017, 33 (26), pp.6572-6580. ⟨10.1021/acs.langmuir.7b01369⟩
Langmuir, American Chemical Society, 2017, 33 (26), pp.6572-6580. ⟨10.1021/acs.langmuir.7b01369⟩
Langmuir, 2017, 33 (26), pp.6572-6580. ⟨10.1021/acs.langmuir.7b01369⟩
Langmuir, American Chemical Society, 2017, 33 (26), pp.6572-6580. ⟨10.1021/acs.langmuir.7b01369⟩
International audience; Obtaining structural information on integral or peripheral membrane proteins is currently arduous due to the difficulty of their solubilization, purification, and crystallization (for X-ray crystallography (XRC) application).
Autor:
Marie-Sousai Appavou, Olivier Delalande, Dominique Mias-Lucquin, Steve J. Winder, Javier Pérez, Thomas Chenuel, Angélique Chéron, Mélanie Lagarrigue, Elisabeth Le Rumeur, Raphael Dos Santos Morais, Anne L. Martel, Jean-François Hubert, Sophie Combet, Guillaume Alviset
Publikováno v:
Journal of Structural Biology
Journal of Structural Biology, Elsevier, 2020, 209 (1), pp.107411. ⟨10.1016/j.jsb.2019.107411⟩
Journal of Structural Biology, 2020, 209 (1), pp.107411. ⟨10.1016/j.jsb.2019.107411⟩
'Journal of Structural Biology ', vol: 209, pages: 107411-1-107411-12 (2020)
Journal of structural biology 209, 107411-(2020). doi:10.1016/j.jsb.2019.107411
Journal of Structural Biology, Elsevier, 2020, 209 (1), pp.107411. ⟨10.1016/j.jsb.2019.107411⟩
Journal of Structural Biology, 2020, 209 (1), pp.107411. ⟨10.1016/j.jsb.2019.107411⟩
'Journal of Structural Biology ', vol: 209, pages: 107411-1-107411-12 (2020)
Journal of structural biology 209, 107411-(2020). doi:10.1016/j.jsb.2019.107411
International audience; Dystrophin is a large intracellular protein that prevents sarcolemmal ruptures by providing a mechanical link between the intracellular actin cytoskeleton and the transmembrane dystroglycan complex. Dystrophin deficiency leads
Publikováno v:
Les Cahiers de Myologie. :15-24
Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions
Autor:
Olivier Delalande, Angélique Chéron, Céline Raguénès-Nicol, Mirjam Czjzek, Arnaud Bondon, Christophe Tascon, Jean-François Hubert, Nicolas Ferey, Elisabeth Le Rumeur, Emmanuel Giudice, Aurélie Nicolas, Émeline Pollet, Marc Baaden, Javier Pérez, Raphael Dos Santos Morais, Marine Guilbaud, Pierre Roblin, Anne-Elisabeth Molza
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, 2018, 293 (18), pp.6637-6646. ⟨10.1074/jbc.M117.809798⟩
BASE-Bielefeld Academic Search Engine
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2018, 293 (18), pp.6637-6646. ⟨10.1074/jbc.M117.809798⟩
Journal of Biological Chemistry 18 (293), 6637-6646. (2018)
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2018, 293 (18), pp.6637-6646. ⟨10.1074/jbc.m117.809798⟩
Journal of Biological Chemistry, 2018, 293 (18), pp.6637-6646. ⟨10.1074/jbc.M117.809798⟩
BASE-Bielefeld Academic Search Engine
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2018, 293 (18), pp.6637-6646. ⟨10.1074/jbc.M117.809798⟩
Journal of Biological Chemistry 18 (293), 6637-6646. (2018)
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2018, 293 (18), pp.6637-6646. ⟨10.1074/jbc.m117.809798⟩
International audience; Dystrophin, encoded by the DMD gene, is critical for maintaining plasma membrane integrity during muscle contraction events. Mutations in the DMD gene disrupting the reading frame prevent dystrophin production and result in se
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9ccc3e07c52f1fe9cdf14f6f392151d
https://univ-rennes.hal.science/hal-01795395v2/document
https://univ-rennes.hal.science/hal-01795395v2/document
Autor:
Mélanie Lagarrigue, Olivier Delalande, Thomas Chenuel, Raphael Dos Santos Morais, Sophie Combet, Elisabeth Le Rumeur, Jean-François Hubert, Anne-Elisabeth Molza, Dominique Mias-Lucquin, Angélique Chéron, Céline Raguénès-Nicol, Arnaud Bondon, Anne L. Martel, Marie-Sousai Appavou, Javier Pérez
Publikováno v:
Biophysical Journal
Biophysical Journal, Biophysical Society, 2018, 115 (7), pp.1231-1239. ⟨10.1016/j.bpj.2018.07.039⟩
Biophysical Journal, 2018, 115 (7), pp.1231-1239. ⟨10.1016/j.bpj.2018.07.039⟩
BASE-Bielefeld Academic Search Engine
Biophysical Journal, Biophysical Society, 2018, 115 (7), pp.1231-1239. ⟨10.1016/j.bpj.2018.07.039⟩
Biophysical Journal, 2018, 115 (7), pp.1231-1239. ⟨10.1016/j.bpj.2018.07.039⟩
BASE-Bielefeld Academic Search Engine
International audience; Scaffolding proteins play important roles in supporting the plasma membrane (sarcolemma) of muscle cells. Among them, dystrophin strengthens the sarcolemma through protein-lipid interactions, and its absence due to gene mutati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53e5f81f06011530b53f3c5717f6bb69
https://hal-univ-rennes1.archives-ouvertes.fr/hal-01880131
https://hal-univ-rennes1.archives-ouvertes.fr/hal-01880131
Autor:
Diane M. Dunn, John W. Day, Craig M. McDonald, Michael T. Howard, Elisabeth Le Rumeur, Andrew R. Findlay, Katherine D. Mathews, Richard S. Finkel, Nicolas Wein, Kevin M. Flanigan, Julaine Florence, Yuuki Kaminoh, Wendy King, Robert B. Weiss, Laura E. Taylor, Aurélie Nicolas, Jerry R. Mendell, Kathryn J. Swoboda, Alan Pestronk
Publikováno v:
Annals of Neurology. 77:668-674
Objective Exon-skipping therapies aim to convert Duchenne muscular dystrophy (DMD) into less severe Becker muscular dystrophy (BMD) by altering pre-mRNA splicing to restore an open reading frame, allowing translation of an internally deleted and part
Autor:
Olivier, Delalande, Aleksander, Czogalla, Jean-François, Hubert, Aleksander, Sikorski, Elisabeth, Le Rumeur
Publikováno v:
Sub-cellular biochemistry. 82
Dystrophin and Spectrin are two proteins essential for the organization of the cytoskeleton and for the stabilization of membrane cells. The comparison of these two sister proteins, and with the dystrophin homologue utrophin, enables us to emphasise