Zobrazeno 1 - 10
of 138
pro vyhledávání: '"Marc le Maire"'
Autor:
Cédric Montigny, Dong Liang Huang, Veronica Beswick, Thomas Barbot, Christine Jaxel, Marc le Maire, Ji-Shen Zheng, Nadège Jamin
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
Abstract Sarcolipin (SLN), a single-spanning membrane protein, is a regulator of the sarco-endoplasmic reticulum Ca2+-ATPase (SERCA1a). Chemically synthesized SLN, palmitoylated or not (pSLN or SLN), and recombinant wild-type rabbit SERCA1a expressed
Externí odkaz:
https://doaj.org/article/3eb36468a91b4c0ca6076ee2a771897a
Autor:
Anaïs Lamy, Ewerton Macarini-Bruzaferro, Thibaud Dieudonné, Alex Perálvarez-Marín, Guillaume Lenoir, Cédric Montigny, Marc le Maire, José Luis Vázquez-Ibar
Publikováno v:
Emerging Microbes and Infections, Vol 10, Iss 1, Pp 132-147 (2021)
Gene targeting approaches have demonstrated the essential role for the malaria parasite of membrane transport proteins involved in lipid transport and in the maintenance of membrane lipid asymmetry, representing emerging oportunites for therapeutical
Externí odkaz:
https://doaj.org/article/32ef37ed354c4f258e41774b1f2a0777
Autor:
Philippe Champeil, Béatrice de Foresta, Martin Picard, Carole Gauron, Dominique Georgin, Marc le Maire, Jesper V Møller, Guillaume Lenoir, Cédric Montigny
Publikováno v:
PLoS ONE, Vol 14, Iss 10, p e0222932 (2019)
The present study mainly consists of a re-evaluation of the rate at which C12E8, a typical non-ionic detergent used for membrane studies, is able to dissociate from biological membranes, with sarcoplasmic reticulum membrane vesicles being used as an
Externí odkaz:
https://doaj.org/article/4aa83949c10942028c6720c14d91f2f1
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:
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://doaj.org/article/bf204653007148e3ac35407cb29a2cfe
Autor:
Hassina Azouaoui, Cédric Montigny, Miriam-Rose Ash, Frank Fijalkowski, Aurore Jacquot, Christina Grønberg, Rosa L López-Marqués, Michael G Palmgren, Manuel Garrigos, Marc le Maire, Paulette Decottignies, Pontus Gourdon, Poul Nissen, Philippe Champeil, Guillaume Lenoir
Publikováno v:
PLoS ONE, Vol 9, Iss 11, p e112176 (2014)
P-type ATPases from the P4 subfamily (P4-ATPases) are energy-dependent transporters, which are thought to establish lipid asymmetry in eukaryotic cell membranes. Together with their Cdc50 accessory subunits, P4-ATPases couple ATP hydrolysis to lipid
Externí odkaz:
https://doaj.org/article/c31bf3d6336a4e34909681868cf0c53a
Publikováno v:
PLoS ONE, Vol 8, Iss 8, p e71842 (2013)
Methods for recombinant production of eukaryotic membrane proteins, yielding sufficient quantity and quality of protein for structural biology, remain a challenge. We describe here, expression and purification optimisation of the human SERCA2a cardia
Externí odkaz:
https://doaj.org/article/dc81a285bde44c2d8dc9baba33242bee
Autor:
Jesper V. Møller, Maxwell M. G. Geurts, Poul Nissen, Marc le Maire, Johannes D. Clausen, Maike Bublitz, Jens Peter Andersen, Robin A. Corey, Guillaume Lenoir, Cédric Montigny, Bertrand Arnou, Christine Jaxel
Publikováno v:
Geurts, M M G, Clausen, J D, Arnou, B, Montigny, C, Lenoir, G, Corey, R A, Jaxel, C, Møller, J V, Nissen, P, Andersen, J P, Le Maire, M & Bublitz, M 2020, ' The SERCA residue Glu340 mediates interdomain communication that guides Ca 2+ transport ', Proceedings of the National Academy of Sciences of the United States of America, vol. 117, no. 49, pp. 31114-31122 . https://doi.org/10.1073/pnas.2014896117
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2020, 117 (49), pp.31114-31122. ⟨10.1073/pnas.2014896117⟩
Proceedings of the National Academy of Sciences of the United States of America, 2020, 117 (49), pp.31114-31122. ⟨10.1073/pnas.2014896117⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2020, ⟨10.1073/pnas.2014896117⟩
Proceedings of the National Academy of Sciences of the United States of America, 2020, ⟨10.1073/pnas.2014896117⟩
'Proceedings of the National Academy of Sciences of the USA ', vol: 117, pages: 31114-31122 (2020)
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2020, 117 (49), pp.31114-31122. ⟨10.1073/pnas.2014896117⟩
Proceedings of the National Academy of Sciences of the United States of America, 2020, 117 (49), pp.31114-31122. ⟨10.1073/pnas.2014896117⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2020, ⟨10.1073/pnas.2014896117⟩
Proceedings of the National Academy of Sciences of the United States of America, 2020, ⟨10.1073/pnas.2014896117⟩
'Proceedings of the National Academy of Sciences of the USA ', vol: 117, pages: 31114-31122 (2020)
International audience; The sarco(endo)plasmic reticulum Ca 2+ -ATPase (SERCA) is a P-type ATPase that transports Ca 2+ from the cytosol into the sarco(endo)plasmic reticulum (SR/ER) lumen, driven by ATP. This primary transport activity depends on ti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3867a5f502b30265725229f2fb4e35be
https://pure.au.dk/portal/da/publications/the-serca-residue-glu340-mediates-interdomain-communication-that-guides-ca2transport(5358e6d5-d66c-4063-8a5e-6952008d820f).html
https://pure.au.dk/portal/da/publications/the-serca-residue-glu340-mediates-interdomain-communication-that-guides-ca2transport(5358e6d5-d66c-4063-8a5e-6952008d820f).html
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:
Johannes D. Clausen, Jesper V. Moeller, Maxwell M. G. Geurts, Maike Bublitz, Jens Peter Andersen, Christine Jaxel, Poul Nissen, Guillaume Lenoir, Robin A. Corey, Marc le Maire, Bertrand Arnou, Cédric Montigny
The sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) is a P-type ATPase that transports Ca2+from the cytosol into the SR/ER lumen, driven by ATP. This primary transport activity depends on tight coupling between movements of the transmembrane helices
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2f4fb1043ba8382d36ca7792feccef0e
https://doi.org/10.1101/2020.06.22.165365
https://doi.org/10.1101/2020.06.22.165365
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