Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Guillaume, Lenoir"'
Autor:
Thibaud Dieudonné, Kahina Slimani, Poul Nissen, Charlott Stock, Michelle Juknaviciute Laursen, Cédric Montigny, Christine Jaxel, Thomas Günther Pomorski, Joseph A. Lyons, Sara Abad Herrera, Guillaume Lenoir, Maylis Lejeune
P-type ATPases from the P4 subfamily (P4-ATPases) are primary active transporters that maintain lipid asymmetry in eukaryotic cell membranes by flipping lipids from the exoplasmic to the cytosolic leaflet. Mutations in several human P4-ATPase genes a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::01f0dba3aae680201131f68c05594c27
https://doi.org/10.1101/2021.11.03.467174
https://doi.org/10.1101/2021.11.03.467174
Publikováno v:
Frontiers in Cell and Developmental Biology
Frontiers in Cell and Developmental Biology, Frontiers media, 2021, 9, ⟨10.3389/fcell.2021.737907⟩
Lenoir, G, D’Ambrosio, J M, Dieudonné, T & Čopič, A 2021, ' Transport Pathways That Contribute to the Cellular Distribution of Phosphatidylserine ', Frontiers in Cell and Developmental Biology, vol. 9, 737907 . https://doi.org/10.3389/fcell.2021.737907
Frontiers in Cell and Developmental Biology, 2021, 9, ⟨10.3389/fcell.2021.737907⟩
Frontiers in Cell and Developmental Biology, Vol 9 (2021)
Frontiers in Cell and Developmental Biology, Frontiers media, 2021, 9, ⟨10.3389/fcell.2021.737907⟩
Lenoir, G, D’Ambrosio, J M, Dieudonné, T & Čopič, A 2021, ' Transport Pathways That Contribute to the Cellular Distribution of Phosphatidylserine ', Frontiers in Cell and Developmental Biology, vol. 9, 737907 . https://doi.org/10.3389/fcell.2021.737907
Frontiers in Cell and Developmental Biology, 2021, 9, ⟨10.3389/fcell.2021.737907⟩
Frontiers in Cell and Developmental Biology, Vol 9 (2021)
Phosphatidylserine (PS) is a negatively charged phospholipid that displays a highly uneven distribution within cellular membranes, essential for establishment of cell polarity and other processes. In this review, we discuss how combined action of PS
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99e375837c8827a31363c73d7d8c552d
https://hal.archives-ouvertes.fr/hal-03450317/document
https://hal.archives-ouvertes.fr/hal-03450317/document
Autor:
Thomas Boesen, Cédric Montigny, Dovile Januliene, Joseph A. Lyons, Arne Möller, Poul Nissen, Milena Timcenko, Werner Kühlbrandt, Guillaume Lenoir, Thibaud Dieudonné, Jesper Lykkegaard Karlsen, Jakob Ulstrup, Miriam-Rose Ash
Publikováno v:
Timcenko, M, Lyons, J A, Januliene, D, Ulstrup, J J, Dieudonné, T, Montigny, C, Ash, M R, Karlsen, J L, Boesen, T, Kühlbrandt, W, Lenoir, G, Moeller, A & Nissen, P 2019, ' Structure and autoregulation of a P4-ATPase lipid flippase ', Nature, vol. 571, no. 7765, pp. 366-370 . https://doi.org/10.1038/s41586-019-1344-7
Nature
Nature, Nature Publishing Group, 2019, ⟨10.1038/s41586-019-1344-7⟩
Nature, 2019, ⟨10.1038/s41586-019-1344-7⟩
Nature
Nature, Nature Publishing Group, 2019, ⟨10.1038/s41586-019-1344-7⟩
Nature, 2019, ⟨10.1038/s41586-019-1344-7⟩
International audience; Type 4 P-type ATPases (P4-ATPases) are lipid flippases that drive the active transport of phospholipids from exoplasmic or luminal leaflets to cytosolic leaflets of eukaryotic membranes. The molecular architecture of P4-ATPase
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
Publikováno v:
Current Opinion in Chemical Biology. 11:654-661
Membrane lipid asymmetry influences a multitude of cellular functions, including membrane vesiculation, cell division, and lifespan. Most cells retain the bulk of aminophospholipids to the cytosolic membrane leaflet by means of ATP-fuelled flippases
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