Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Maike, Bublitz"'
Publikováno v:
Drachmann, N D, Olesen, C, Møller, J V, Guo, Z, Bublitz, M & Nissen, P 2014, ' Comparing crystal structures of Ca 2+-ATPase in the presence of different lipids ', F E B S Journal, vol. 281, no. 18, pp. 4249-4262 . https://doi.org/10.1111/febs.12957
The activity of the sarco/endoplasmic reticulum Ca(2+) -ATPase (SERCA) depends strongly on the lipid composition of the surrounding membrane. Yet, structural information on SERCA-lipid interaction is still relatively scarce, and the influence of diff
Autor:
Anne-Marie Lund Winther, John Bondo Hansen, Jesper V. Møller, Poul Nissen, Maike Bublitz, Morten J. Buch-Pedersen, Jesper Lykkegaard Karlsen
Publikováno v:
Nature
Winther, A-M L, Bublitz, M, Karlsen, J L, Møller, J V, Hansen, J B, Nissen, P & Buch-Pedersen, M J 2013, ' The sarcolipin-bound calcium pump stabilizes calcium sites exposed to the cytoplasm ', Nature, vol. 495, no. 7440, pp. 265-269 . https://doi.org/10.1038/nature11900
Winther, A-M L, Bublitz, M, Karlsen, J L, Møller, J V, Hansen, J B, Nissen, P & Buch-Pedersen, M J 2013, ' The sarcolipin-bound calcium pump stabilizes calcium sites exposed to the cytoplasm ', Nature, vol. 495, no. 7440, pp. 265-269 . https://doi.org/10.1038/nature11900
The contraction and relaxation of muscle cells is controlled by the successive rise and fall of cytosolic Ca(2+), initiated by the release of Ca(2+) from the sarcoplasmic reticulum and terminated by re-sequestration of Ca(2+) into the sarcoplasmic re
Autor:
Johannes D. Clausen, Jens Peter Andersen, Maike Bublitz, Jesper V. Møller, Poul Nissen, Bertrand Arnou, Claus Olesen
Publikováno v:
Clausen, J D, Bublitz, M, Arnou, B J-P, Olesen, C, Andersen, J P, Møller, J V & Nissen, P 2016, ' Crystal Structure of the Vanadate-Inhibited Ca 2+-ATPase ', Structure, vol. 24, no. 4, pp. 617-623 . https://doi.org/10.1016/j.str.2016.02.018
Vanadate is the hallmark inhibitor of the P-type ATPase family; however, structural details of its inhibitory mechanism have remained unresolved. We have determined the crystal structure of sarcoplasmic reticulum Ca(2+)-ATPase with bound vanadate in
Autor:
Jesper V. Møller, Maike Bublitz, Karine Moncoq, Poul Nissen, J. Preben Morth, Claus Olesen, Mette Laursen, Howard S. Young
Publikováno v:
Journal of Biological Chemistry. 284:13513-13518
We have determined the structure of the sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) in an E2·Pi-like form stabilized as a complex with \documentclass[10pt]{article} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{ams
Autor:
Paulette Decottignies, Marc le Maire, Cédric Montigny, Jesper V. Møller, Pierre Le Maréchal, Pierre Capy, Claus Olesen, Poul Nissen, Maike Bublitz
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2014, 289 (49), pp.33850-61. ⟨10.1074/jbc.M114.590307⟩
Montigny, C, Decottignies, P, le Maréchal, P, Capy, P, Bublitz, M, Olesen, C, Møller, J V, le Maire, M & Nissen, P 2014, ' S-Palmitoylation and S-Oleoylation of Rabbit and Pig Sarcolipin ', Journal of Biological Chemistry, vol. 289, pp. 33850-33861 . https://doi.org/10.1074/jbc.M114.590307
Journal of Biological Chemistry, 2014, 289 (49), pp.33850-61. ⟨10.1074/jbc.M114.590307⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2014, 289 (49), pp.33850-61. ⟨10.1074/jbc.M114.590307⟩
Montigny, C, Decottignies, P, le Maréchal, P, Capy, P, Bublitz, M, Olesen, C, Møller, J V, le Maire, M & Nissen, P 2014, ' S-Palmitoylation and S-Oleoylation of Rabbit and Pig Sarcolipin ', Journal of Biological Chemistry, vol. 289, pp. 33850-33861 . https://doi.org/10.1074/jbc.M114.590307
Journal of Biological Chemistry, 2014, 289 (49), pp.33850-61. ⟨10.1074/jbc.M114.590307⟩
International audience; Sarcolipin (SLN) is a regulatory peptide present in sarcoplasmic reticulum (SR) from skeletal muscle of animals. We find that native rabbit SLN is modified by a fatty acid anchor on Cys-9 with a palmitic acid in about 60% and,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e559e276fe961f69bd7509f43b28ed9e
https://hal.archives-ouvertes.fr/hal-01179260
https://hal.archives-ouvertes.fr/hal-01179260
Autor:
Birgit Schiøtt, Lea Thøgersen, Maria Musgaard, Poul Nissen, Jesper V. Møller, J. Preben Morth, Claus Olesen, Maike Bublitz, Hanne Poulsen
Publikováno v:
Bublitz, M, Musgaard, M, Poulsen, H, Thøgersen, L, Olesen, C, Schiøtt, B, Morth, P, Møller, J V & Nissen, P 2013, ' Ion Pathways in the Sarcoplasmic Reticulum Ca 2+-ATPase ', Journal of Biological Chemistry, vol. 288, pp. 10759-10765 . https://doi.org/10.1074/jbc.R112.436550
The sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA) is a transmembrane ion transporter belonging to the P(II)-type ATPase family. It performs the vital task of re-sequestering cytoplasmic Ca(2+) to the sarco/endoplasmic reticulum store, thereby als