Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Marc le Maire"'
Autor:
Maxwell M G, Geurts, Johannes D, Clausen, Bertrand, Arnou, Cédric, Montigny, Guillaume, Lenoir, Robin A, Corey, Christine, Jaxel, Jesper V, Møller, Poul, Nissen, Jens Peter, Andersen, Marc, le Maire, Maike, Bublitz
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance We present a crystal structure, functional data, and molecular dynamics (MD) simulations of the sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) mutant E340A. The mutation slows Ca2+-binding kinetics, and the structural differences betwe
Autor:
Anne-Marie Lund Winther, Alexandre Marchand, Peter Joakim Holm, Claus Olesen, Marc le Maire, Bente Vilsen, Jens Peter Andersen, Philippe Champeil, Poul Nissen, Bertrand Arnou, Jesper V. Møller, Johannes D. Clausen, Christine Jaxel, Cédric Montigny
Publikováno v:
Aarhus University
In recent years crystal structures of the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA1a), stabilized in various conformations with nucleotide and phosphate analogs, have been obtained. However, structural analysis of mutant forms would also be valuab
Autor:
Philippe Champeil, Jesper V. Møller, Martin Picard, Pierre Falson, Guillaume Lenoir, Marc le Maire
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2004, 279 (31), pp.32125-32133. ⟨10.1074/jbc.M402934200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2004, 279, pp.32125-32133
Journal of Biological Chemistry, 2004, 279 (31), pp.32125-32133. ⟨10.1074/jbc.M402934200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2004, 279 (31), pp.32125-32133. ⟨10.1074/jbc.M402934200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2004, 279, pp.32125-32133
Journal of Biological Chemistry, 2004, 279 (31), pp.32125-32133. ⟨10.1074/jbc.M402934200⟩
International audience; Wild-type (WT) and the double mutant D813A,D818A (ADA) of the L6-7 loop of SERCA1a were expressed in yeast, purified, and reconstituted into lipids. This allowed us to functionally study these ATPases by both kinetic and spect
Autor:
Marc le Maire, Pierre Falson, Thierry Menguy, Stéphane Deschamps, Jesper V. Møller, Laurence Bouneau, Fabienne Corre, Philippe Champeil
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1998, 273, pp.20134-20143
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1998, 273, pp.20134-20143
International audience; During active cation transport, sarcoplasmic reticulum Ca2+-ATPase, like other P-type ATPases, undergoes major conformational changes, some of which are dependent on Ca2+ binding to high affinity transport sites. We here repor
Autor:
Johannes D, Clausen, Maike, Bublitz, Bertrand, Arnou, Cédric, Montigny, Christine, Jaxel, Jesper Vuust, Møller, Poul, Nissen, Jens Peter, Andersen, Marc, le Maire
Publikováno v:
The EMBO journal. 32(24)
The sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA) couples ATP hydrolysis to transport of Ca(2+). This directed energy transfer requires cross-talk between the two Ca(2+) sites and the phosphorylation site over 50 Å distance. We have addressed t
Autor:
Marie Laure Durand, Philippe Champeil, Hubert Turc, Adrienne Gomez de Gracia, B Juul, Jesper Vuust M, Marc le Maire, Luc Denoroy
Publikováno v:
Journal of Biological Chemistry. 270:20123-20134
The present study was undertaken to investigate the Ca2+ binding properties of sarcoplasmic reticulum Ca(2+)-ATPase after removal of the cytoplasmic regions by treatment with proteinase K. One of the proteolysis cleavage sites (at the end of M6) was
Autor:
Marc le Maire, Philippe Champeil, Manuel Garrigos, A Viel, Sten Lund, Stéphane Deschamps, Jesper V. Møller
Publikováno v:
Europe PubMed Central
When high affinity Ca2+-binding proteins like calmodulin, or proteins with a high Ca2+-binding capacity like calsequestrin, underwent sodium dodecyl sulfate-gel electrophoresis in Laemmli systems, their electrophoretic migration rates were much highe
Autor:
Manuel Garrigos, Philippe Champeil, Martin Picard, Carole Gauron, Jean-Luc Popot, Tassadite Dahmane, Fabrice Giusti, Marc le Maire
Publikováno v:
Biochemistry
Biochemistry, American Chemical Society, 2006, 45, pp.1861-1869
Biochemistry, American Chemical Society, 2006, 45 (6), pp.1861-1869. ⟨10.1021/bi051954a⟩
HAL
Biochemistry, 2006, 45 (6), pp.1861-1869. ⟨10.1021/bi051954a⟩
Biochemistry, 2006, 45, pp.1861-1869
Biochemistry, American Chemical Society, 2006, 45, pp.1861-1869
Biochemistry, American Chemical Society, 2006, 45 (6), pp.1861-1869. ⟨10.1021/bi051954a⟩
HAL
Biochemistry, 2006, 45 (6), pp.1861-1869. ⟨10.1021/bi051954a⟩
Biochemistry, 2006, 45, pp.1861-1869
Amphipols are amphipathic polymers designed to replace or supplement detergents in membrane protein solution studies. Previous work has suggested both advantages and disadvantages to the use of a polyacrylate-based amphipol, A8-35, for studying the s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33c65867c8814c128da6b28b4f50c6e7
https://hal.archives-ouvertes.fr/hal-00095825
https://hal.archives-ouvertes.fr/hal-00095825
Autor:
Philippe Champeil, Pierre Falson, Martin Picard, Marc le Maire, Guillaume Lenoir, Christine Jaxel
Publikováno v:
Biochemistry
Biochemistry, American Chemical Society, 2006, 45, pp.5261-5270
Biochemistry, American Chemical Society, 2006, 45, pp.5261-5270
International audience; By analyzing, after expression in yeast and purification, the intrinsic fluorescence properties of point mutants of rabbit Ca(2+)-ATPase (SERCA1a) with alterations to amino acid residues in Ca(2+)-binding site I (E(771)), site
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::529b5e76b42db58c521cc8f3bcf9a390
https://hal.archives-ouvertes.fr/hal-00314156
https://hal.archives-ouvertes.fr/hal-00314156
Autor:
Martin Picard, Philippe Champeil, Pierre Le Maréchal, Pierre Falson, Carole Gauron, Guillaume Lenoir, Jesper V. Møller, Marc le Maire, Cédric Montigny
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2004, 279 (10), pp.9156-9166. ⟨10.1074/jbc.M311411200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2004, 279, pp.9156-9166
Journal of Biological Chemistry, 2004, 279 (10), pp.9156-9166. ⟨10.1074/jbc.M311411200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2004, 279 (10), pp.9156-9166. ⟨10.1074/jbc.M311411200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2004, 279, pp.9156-9166
Journal of Biological Chemistry, 2004, 279 (10), pp.9156-9166. ⟨10.1074/jbc.M311411200⟩
International audience; By measuring the phosphorylation levels of individual proteolytic fragments of SERCA1a separated by electrophoresis after their phosphorylation, we were able to study the catalytic properties of a p95C-p14N complex arising fro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89986bd690e3f86392ef5f738e3067c3
https://hal.archives-ouvertes.fr/hal-02544391
https://hal.archives-ouvertes.fr/hal-02544391