Zobrazeno 1 - 10
of 65
pro vyhledávání: '"Marc le Maire"'
Autor:
Claire Montpellier, Gilles Duverlie, Marc le Maire, Cédric Montigny, Yann Ciczora, François-Loïc Cosset, Jean Dubuisson, Birke Andrea Tews, Pierre Falson, Laura Riva, Eve-Isabelle Pécheur, Antoine Loquet, Birke Bartosch, Khaled Alsaleh, François Penin
Publikováno v:
Journal of Virology
Journal of Virology, 2015, pp.10333-46. ⟨10.1128/JVI.00991-15⟩
Journal of Virology, American Society for Microbiology, 2015, pp.10333-46. ⟨10.1128/JVI.00991-15⟩
Journal of Virology, American Society for Microbiology, 2015, pp.10333-46. 〈10.1128/JVI.00991-15〉
Journal of Virology, 2015, pp.10333-46. ⟨10.1128/JVI.00991-15⟩
Journal of Virology, American Society for Microbiology, 2015, pp.10333-46. ⟨10.1128/JVI.00991-15⟩
Journal of Virology, American Society for Microbiology, 2015, pp.10333-46. 〈10.1128/JVI.00991-15〉
In hepatitis C virus (HCV)-infected cells, the envelope glycoproteins E1 and E2 assemble as a heterodimer. To investigate potential changes in the oligomerization of virion-associated envelope proteins, we performed SDS-PAGE under reducing conditions
Autor:
Cédric Montigny, Thibaud Dieudonné, Stéphane Orlowski, José Luis Vázquez-Ibar, Carole Gauron, Dominique Georgin, Sten Lund, Marc le Maire, Jesper V Møller, Philippe Champeil, Guillaume Lenoir
Publikováno v:
Montigny, C, Dieudonné, T, Orlowski, S, Vázquez-Ibar, J L, Gauron, C, Georgin, D, Lund, S, le Maire, M, Møller, J V, Champeil, P & Lenoir, G 2017, ' Slow Phospholipid Exchange between a Detergent-Solubilized Membrane Protein and Lipid-Detergent Mixed Micelles Brominated Phospholipids as Tools to Follow Its Kinetics ', P L o S One, vol. 12, no. 1, pp. e0170481 . https://doi.org/10.1371/journal.pone.0170481
PLoS ONE
PLoS ONE, 2017, 12 (1), pp.e0170481. ⟨10.1371/journal.pone.0170481⟩
PLoS ONE, Public Library of Science, 2017, 12 (1), pp.e0170481. ⟨10.1371/journal.pone.0170481⟩
PLoS ONE, Vol 12, Iss 1, p e0170481 (2017)
PLoS ONE
PLoS ONE, 2017, 12 (1), pp.e0170481. ⟨10.1371/journal.pone.0170481⟩
PLoS ONE, Public Library of Science, 2017, 12 (1), pp.e0170481. ⟨10.1371/journal.pone.0170481⟩
PLoS ONE, Vol 12, Iss 1, p e0170481 (2017)
Membrane proteins are largely dependent for their function on the phospholipids present in their immediate environment, and when they are solubilized by detergent for further study, residual phospholipids are critical, too. Here, brominated phosphati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::8e4b931923f41409563aa208c19c63e8
https://pure.au.dk/portal/da/publications/slow-phospholipid-exchange-between-a-detergentsolubilized-membrane-protein-and-lipiddetergent-mixed-micelles-brominated-phospholipids-as-tools-to-follow-its-kinetics(190cc4fa-0846-4d5d-a513-f65c40e84abf).html
https://pure.au.dk/portal/da/publications/slow-phospholipid-exchange-between-a-detergentsolubilized-membrane-protein-and-lipiddetergent-mixed-micelles-brominated-phospholipids-as-tools-to-follow-its-kinetics(190cc4fa-0846-4d5d-a513-f65c40e84abf).html
Autor:
Catherine Berrier, Alexandre Ghazi, Marc le Maire, Solenne Chardonnet, Alexandre Pozza, Christine Jaxel, Agnes de Lacroix de Lavalette, Agnes Mesneau
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2013, 288 (38), pp.27307-14. ⟨10.1074/jbc.M113.478321⟩
Journal of Biological Chemistry, 2013, 288 (38), pp.27307-14. ⟨10.1074/jbc.M113.478321⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2013, 288 (38), pp.27307-14. ⟨10.1074/jbc.M113.478321⟩
Journal of Biological Chemistry, 2013, 288 (38), pp.27307-14. ⟨10.1074/jbc.M113.478321⟩
International audience; Mechanosensitive channels are detected in all cells and are speculated to play a key role in many functions including osmoregulation, growth, hearing, balance, and touch. In prokaryotic cells, a direct gating of mechanosensiti
Autor:
John Bondo Hansen, Anne-Marie Lund Winther, Isabelle Florent, Christine Jaxel, Paul Machillot, Marc le Maire, Morten J. Buch-Pedersen, Stéphanie David-Bosne
Publikováno v:
David-Bosne, S, Florent, I, Winther, A-M L, Hansen, J B, Buch-Pedersen, M J, Machillot, P, le Maire, M & Jaxel, C 2013, ' Antimalarial screening via large-scale purification of Plasmodium falciparum Ca2+-ATPase 6 and in vitro studies ', F E B S Journal, vol. 280, no. 21, pp. 5419-29 . https://doi.org/10.1111/febs.12244
FEBS Journal
FEBS Journal, 2013, 280 (21), pp.5419-5429. ⟨10.1111/febs.12244⟩
FEBS Journal
FEBS Journal, 2013, 280 (21), pp.5419-5429. ⟨10.1111/febs.12244⟩
International audience; The most severe form of human malaria is caused by the parasite Plasmo-dium falciparum. Despite the current need, there is no effective vaccine and parasites are becoming resistant to most of the antimalarials available. There
Publikováno v:
FEBS Journal. 280:5398-5407
Recombinant Ca(2+)-ATPase was expressed in Saccharomyces cerevisiae with a biotin-acceptor domain linked to its C-terminus by a thrombin cleavage site. We obtained 200 μg of ~ 70% pure recombinant sarcoendoplasmic reticulum Ca(2+)-ATPase isoform 1a
Autor:
Jesper V. Møller, Marc le Maire, Simon Babin, Stéphane Orlowski, Sten Lund, Philippe Champeil, Guillaume Lenoir, Cédric Montigny
Publikováno v:
Analytical Biochemistry
Analytical Biochemistry, Elsevier Masson, 2016, 511, pp.31-35
Champeil, P, Orlowski, S, Babin, S, Lund, S, le Maire, M, Møller, J, Lenoir, G & Montigny, C 2016, ' A robust method to screen detergents for membrane protein stabilization, revisited ', Analytical Biochemistry, vol. 511, pp. 31-5 . https://doi.org/10.1016/j.ab.2016.07.017
Analytical Biochemistry, 2016, 511, pp.31-35
Analytical Biochemistry, Elsevier Masson, 2016, 511, pp.31-35
Champeil, P, Orlowski, S, Babin, S, Lund, S, le Maire, M, Møller, J, Lenoir, G & Montigny, C 2016, ' A robust method to screen detergents for membrane protein stabilization, revisited ', Analytical Biochemistry, vol. 511, pp. 31-5 . https://doi.org/10.1016/j.ab.2016.07.017
Analytical Biochemistry, 2016, 511, pp.31-35
International audience; This report is a follow up of our previous paper (Lund, Orlowski, de Foresta, Champeil, le Maire and Møller (1989), J Biol Chem 264:4907–4915) showing that solubilization in detergent of a membrane protein may interfere wit
Autor:
Cédric Montigny, Thomas Barbot, Veronica Beswick, Paulette Decottignies, Nadège Jamin, Christine Jaxel, Marc le Maire
Publikováno v:
Regulation of Ca2+-ATPases,V-ATPases and F-ATPases
Chakraborti, Sajal; Dhalla, Naranjan S. Regulation of Ca2+-ATPases,V-ATPases and F-ATPases, 14, Springer International Publishing, pp.153-186, 2016, Advances in Biochemistry in Health and Disease, 978-3-319-24778-6
Regulation of Ca2+-ATPases,V-ATPases and F-ATPases ISBN: 9783319247786
Chakraborti, Sajal; Dhalla, Naranjan S. Regulation of Ca2+-ATPases,V-ATPases and F-ATPases, 14, Springer International Publishing, pp.153-186, 2015, Advances in Biochemistry in Health and Disease, 978-3-319-24778-6
Chakraborti, Sajal; Dhalla, Naranjan S. Regulation of Ca2+-ATPases,V-ATPases and F-ATPases, 14, Springer International Publishing, pp.153-186, 2016, Advances in Biochemistry in Health and Disease, 978-3-319-24778-6
Regulation of Ca2+-ATPases,V-ATPases and F-ATPases ISBN: 9783319247786
Chakraborti, Sajal; Dhalla, Naranjan S. Regulation of Ca2+-ATPases,V-ATPases and F-ATPases, 14, Springer International Publishing, pp.153-186, 2015, Advances in Biochemistry in Health and Disease, 978-3-319-24778-6
International audience; Sarcolipin (SLN), a transmembrane peptide from sarcoplasmic reticulum, is one of the major proteins involved in the muscle contraction/relaxation process. A number of enzymological studies have underlined its regulatory role i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5183081836811683f6a8199ec2ef6494
https://hal.archives-ouvertes.fr/hal-02393614
https://hal.archives-ouvertes.fr/hal-02393614
Autor:
Marc le Maire, Claus Olesen, Jesper V. Møller, Yonathan Sonntag, S. Brøgger Christensen, Anne-Marie Lund Winther, Poul Nissen, Carl-Erik Olsen, Huizhen Liu, Helmer Soehoel
Publikováno v:
Winther, A-M L, Liu, H, Sonntag, Y, Olesen, C E, le Maire, M, Søhoel, H, Olsen, C E, Christensen, S B, Nissen, P & Møller, J V 2010, ' Critical roles of hydrophobicity and orientation of side chains for inactivation of sarcoplasmic reticulum Ca2+-ATPase with thapsigargin and thapsigargin analogs. ', Journal of Biological Chemistry, vol. 285, no. 37, pp. 28883-92 .
Aarhus University
Aarhus University
Thapsigargin (Tg), a specific inhibitor of sarco/endoplasmic Ca(2+)-ATPases (SERCA), binds with high affinity to the E2 conformation of these ATPases. SERCA inhibition leads to elevated calcium levels in the cytoplasm, which in turn induces apoptosis
Autor:
Gilles Mourier, Spencer Brown, Emmanuelle Girard, Carole Fruchart-Gaillard, Catherine Marquer, Olivier Grandjean, Marc le Maire, Denis Servent
Publikováno v:
Biology of the Cell. 102:409-420
Background information. The idea that GPCRs (G-protein-coupled receptors) may exist as homo- or hetero-oligomers, although still controversial, is now widely accepted. Nevertheless, the functional roles of oligomerization are still unclear and gainin
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