Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Anne-Elisabeth Molza"'
Autor:
Anne-Elisabeth Molza, Yvonne Westermaier, Magali Moutte, Pierre Ducrot, Claudia Danilowicz, Veronica Godoy-Carter, Mara Prentiss, Charles H. Robert, Marc Baaden, Chantal Prévost
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Recent advances in structural biophysics and integrative modelling methods now allow us to decipher the structures of large macromolecular assemblies. Understanding the dynamics and mechanisms involved in their biological function requires rigorous i
Externí odkaz:
https://doaj.org/article/cbb8e3ac6752421ebb24cb7700b5bdd9
Publikováno v:
Journal of Chemical Theory and Computation
Journal of Chemical Theory and Computation, American Chemical Society, 2021, 17 (7), pp.4499-4511. ⟨10.1021/acs.jctc.1c00140⟩
Journal of Chemical Theory and Computation, American Chemical Society, 2021, 17 (7), pp.4499-4511. ⟨10.1021/acs.jctc.1c00140⟩
International audience; Poly(ornithine-co-citrulline)s are ureido-based polymers which were shown to exhibit tunable upper critical solution temperature (UCST) behavior, a property that can be exploited to develop thermoresponsive nanoparticles for c
Autor:
Anne-Elisabeth Molza, Yvonne Westermaier, Magali Moutte, Pierre Ducrot, Claudia Danilowicz, Veronica Godoy-Carter, Mara Prentiss, Charles H. Robert, Marc Baaden, Chantal Prévost
Publikováno v:
Frontiers in molecular biosciences. 9
Recent advances in structural biophysics and integrative modelling methods now allow us to decipher the structures of large macromolecular assemblies. Understanding the dynamics and mechanisms involved in their biological function requires rigorous i
Autor:
Mirjam Czjzek, Jean-François Hubert, E. Le Rumeur, Marc Baaden, Olivier Delalande, Nicolas Ferey, Alex Tek, Benoist Laurent, Anne-Elisabeth Molza
Publikováno v:
Faraday Discussions
Faraday Discussions, 2014, 169, pp.45-62. ⟨10.1039/C3FD00134B⟩
Faraday Discussions, Royal Society of Chemistry, 2014, 169, pp.45-62. ⟨10.1039/C3FD00134B⟩
Faraday Discussions, 2014, 169, pp.45-62. ⟨10.1039/C3FD00134B⟩
Faraday Discussions, Royal Society of Chemistry, 2014, 169, pp.45-62. ⟨10.1039/C3FD00134B⟩
International audience; At present, our molecular knowledge of dystrophin, the protein encoded by the DMD gene and mutated in myopathy patients, remains limited. To get around the absence of its atomic structure, we have developed an innovative inter
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:
Aurélie Nicolas, Anne-Elisabeth Molza, Elisabeth Le Rumeur, Olivier Delalande, Yoann Laurin, Emmanuel Giudice
Publikováno v:
Biochemistry
Biochemistry, 2013, 52 (44), pp.7777-84. ⟨10.1021/bi400794p⟩
Biochemistry, American Chemical Society, 2013, 52 (44), pp.7777-84. ⟨10.1021/bi400794p⟩
Biochemistry, 2013, 52 (44), pp.7777-84. ⟨10.1021/bi400794p⟩
Biochemistry, American Chemical Society, 2013, 52 (44), pp.7777-84. ⟨10.1021/bi400794p⟩
International audience; Dystrophin is a large skeletal muscle protein located at the internal face of the plasma membrane and interacting with membrane phospholipids and a number of cytosolic proteins. Binding of neuronal nitric oxide synthase (nNOS)
Autor:
Reynald Gillet, Emmanuel Giudice, Annie Cavalier, Anne-Elisabeth Molza, Daniel Thomas, Nicolas Cougot
Publikováno v:
RNA Biology
RNA Biology, Taylor & Francis, 2013, 10 (2), pp.314-20. ⟨10.4161/rna.23342⟩
RNA Biology, 2013, 10 (2), pp.314-20. ⟨10.4161/rna.23342⟩
RNA Biology, Taylor & Francis, 2013, 10 (2), pp.314-20. ⟨10.4161/rna.23342⟩
RNA Biology, 2013, 10 (2), pp.314-20. ⟨10.4161/rna.23342⟩
International audience; A finely tuned balance of translation, storage and decay of mRNAs (mRNAs) is important for the regulation of gene expression. In eukaryotic cells, this takes place in dynamic cytoplasmic RNA-protein granules termed Processing
Autor:
Nick Menhart, Olivier Delalande, Elisabeth Le Rumeur, Jean-François Hubert, Khushdeep Mangat, Anne-Elisabeth Molza
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2015, 290 (49), pp.29531-29541. ⟨10.1074/jbc.M115.680660⟩
Journal of Biological Chemistry, 2015, 290 (49), pp.29531-29541. ⟨10.1074/jbc.M115.680660⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2015, 290 (49), pp.29531-29541. ⟨10.1074/jbc.M115.680660⟩
Journal of Biological Chemistry, 2015, 290 (49), pp.29531-29541. ⟨10.1074/jbc.M115.680660⟩
International audience; Duchenne muscular dystrophy is a lethal genetic defect that is associated with the absence of dystrophin protein. Lack of dystrophin protein completely abolishes muscular nitric oxide synthase (NOS) function as a regulator of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c37a519b8dcfe4c085a468b232f8bc64
https://hal-univ-rennes1.archives-ouvertes.fr/hal-01214011
https://hal-univ-rennes1.archives-ouvertes.fr/hal-01214011
Autor:
Jérémy Delesques, Annie Cavalier, Anne-Elisabeth Molza, Jean-Paul Rolland, Emmanuel Giudice, Reynald Gillet, Gwennola Ermel, Carlos Blanco, Daniel Thomas, Nicolas Cougot
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, 2013, 426 (2), pp.377-388. ⟨10.1016/j.jmb.2013.09.035⟩
Journal of Molecular Biology, Elsevier, 2013, 426 (2), pp.377-388. ⟨10.1016/j.jmb.2013.09.035⟩
Journal of Molecular Biology, 2013, 426 (2), pp.377-388. ⟨10.1016/j.jmb.2013.09.035⟩
Journal of Molecular Biology, Elsevier, 2013, 426 (2), pp.377-388. ⟨10.1016/j.jmb.2013.09.035⟩
International audience; During protein synthesis, many translating ribosomes are bound together with an mRNA molecule to form polysomes (or polyribosomes). While the spatial organization of bacterial polysomes has been well studied in vitro, little i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b77ec6f9329b57f6dd860ff24c125452
https://univ-rennes.hal.science/hal-00874756
https://univ-rennes.hal.science/hal-00874756