Zobrazeno 1 - 10
of 71
pro vyhledávání: '"Claus Olesen"'
Autor:
Kamel El Omari, Nada Mohamad, Kiran Bountra, Ramona Duman, Maria Romano, Katja Schlegel, Hok-Sau Kwong, Vitaliy Mykhaylyk, Claus Olesen, Jesper Vuust Moller, Maike Bublitz, Konstantinos Beis, Armin Wagner
Publikováno v:
IUCrJ, Vol 7, Iss 6, Pp 1092-1101 (2020)
The structure determination of soluble and membrane proteins can be hindered by the crystallographic phase problem, especially in the absence of a suitable homologous structure. Experimental phasing is the method of choice for novel structures; howev
Externí odkaz:
https://doaj.org/article/97406e4f17cc4e1cac866e06b368fa63
Autor:
Maike Bublitz, Karol Nass, Nikolaj D. Drachmann, Anders J. Markvardsen, Matthias J. Gutmann, Thomas R. M. Barends, Daniel Mattle, Robert L. Shoeman, R. Bruce Doak, Sébastien Boutet, Marc Messerschmidt, Marvin M. Seibert, Garth J. Williams, Lutz Foucar, Linda Reinhard, Oleg Sitsel, Jonas L. Gregersen, Johannes D. Clausen, Thomas Boesen, Kamil Gotfryd, Kai-Tuo Wang, Claus Olesen, Jesper V. Møller, Poul Nissen, Ilme Schlichting
Publikováno v:
IUCrJ, Vol 2, Iss 4, Pp 409-420 (2015)
Membrane proteins are key players in biological systems, mediating signalling events and the specific transport of e.g. ions and metabolites. Consequently, membrane proteins are targeted by a large number of currently approved drugs. Understanding th
Externí odkaz:
https://doaj.org/article/0eb55fd648bc4163964e04aef172633f
Autor:
Hok-Sau Kwong, Maike Bublitz, Claus Olesen, Vitaliy Mykhaylyk, Armin Wagner, Jesper V. Møller, Konstantinos Beis, Nada Mohamad, R. Duman, Kiran Bountra, Katja Schlegel, Maria Romano, Kamel El Omari
Publikováno v:
El Omari, K, Mohamad, N, Bountra, K, Duman, R, Romano, M, Schlegel, K, Kwong, H S, Mykhaylyk, V, Olesen, C, Moller, J V, Bublitz, M, Beis, K & Wagner, A 2020, ' Experimental phasing with vanadium and application to nucleotide-binding membrane proteins ', IUCrJ, vol. 7, pp. 1092-1101 . https://doi.org/10.1107/S2052252520012312
IUCrJ
IUCrJ, Vol 7, Iss 6, Pp 1092-1101 (2020)
IUCrJ
IUCrJ, Vol 7, Iss 6, Pp 1092-1101 (2020)
Crystal structure determination of membrane proteins can be challenging. Here, the use of vanadium phasing as an alternative experimental phasing method is described.
The structure determination of soluble and membrane proteins can be hindered b
The structure determination of soluble and membrane proteins can be hindered b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a28328d9c9902e5aac0e2af9ca97c9b7
https://pure.au.dk/portal/da/publications/experimental-phasing-with-vanadium-and-application-to-nucleotidebinding-membrane-proteins(dcfd4d87-3c0b-48c7-bd03-b434a797e37e).html
https://pure.au.dk/portal/da/publications/experimental-phasing-with-vanadium-and-application-to-nucleotidebinding-membrane-proteins(dcfd4d87-3c0b-48c7-bd03-b434a797e37e).html
Autor:
Thomas Boesen, Poul Nissen, Jesper V. Moeller, Line Cecilie Hansen, Temitope I. Ayeotan, Magnus Kjaergaard, Claus Olesen
The histidine-rich Ca2+-binding protein (HRC) stimulates the sarco-endoplasmic reticulum Ca2+-ATPase (SERCA) to increase Ca2+-uptake into the lumen. HRC also binds the triadin scaffold in a Ca2+-dependent manner, and HRC tunes both the uptake and rel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d2dc0742bdee9a2db6617fcea962fe67
https://doi.org/10.1101/2020.09.17.302869
https://doi.org/10.1101/2020.09.17.302869
Autor:
Maike Bublitz, William Dalby-Brown, Franco Aversa, Paolo Sportoletti, Anne-Marie Lund Winther, Marilena Baglione, Giorgia Rastelli, Chiara Rompietti, Rocchina Vilella, Donatella Stilli, Caterina Loiacono, Federica Rizzi, Samuel Kitara, Luca Pagliaro, Giovanni Roti, Andrea Gherli, Claus Olesen, Anna Montanaro, Roberta La Starza, Monia Savi, Matteo Marchesini, Leonardo Bocchi, Cristina Mecucci, Laura Patrizi, Sabine Heit, Claudia Sorrentino, Jesper V. Møller, Kimberly Stegmaier
Publikováno v:
Cell Chem Biol
Marchesini, M, Gherli, A, Montanaro, A, Patrizi, L, Sorrentino, C, Pagliaro, L, Rompietti, C, Kitara, S, Heit, S, Olesen, C E, Møller, J V, Savi, M, Bocchi, L, Vilella, R, Rizzi, F, Baglione, M, Rastelli, G, Loiacono, C, La Starza, R, Mecucci, C, Stegmaier, K, Aversa, F, Stilli, D, Lund Winther, A M, Sportoletti, P, Bublitz, M, Dalby-Brown, W & Roti, G 2020, ' Blockade of Oncogenic NOTCH1 with the SERCA Inhibitor CAD204520 in T Cell Acute Lymphoblastic Leukemia ', Cell Chemical Biology, vol. 27, no. 6, pp. 678-697.e13 . https://doi.org/10.1016/j.chembiol.2020.04.002
Marchesini, M, Gherli, A, Montanaro, A, Patrizi, L, Sorrentino, C, Pagliaro, L, Rompietti, C, Kitara, S, Heit, S, Olesen, C E, Møller, J V, Savi, M, Bocchi, L, Vilella, R, Rizzi, F, Baglione, M, Rastelli, G, Loiacono, C, La Starza, R, Mecucci, C, Stegmaier, K, Aversa, F, Stilli, D, Lund Winther, A M, Sportoletti, P, Bublitz, M, Dalby-Brown, W & Roti, G 2020, ' Blockade of Oncogenic NOTCH1 with the SERCA Inhibitor CAD204520 in T Cell Acute Lymphoblastic Leukemia ', Cell Chemical Biology, vol. 27, no. 6, pp. 678-697.e13 . https://doi.org/10.1016/j.chembiol.2020.04.002
The identification of SERCA (sarco/endoplasmic reticulum calcium ATPase) as a target for modulating gain-of-function NOTCH1 mutations in Notch-dependent cancers has spurred the development of this compound class for cancer therapeutics. Despite the i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86e63576c860546d9cf10c8571266edb
https://doi.org/10.1016/j.chembiol.2020.04.002
https://doi.org/10.1016/j.chembiol.2020.04.002
Autor:
Matteo Levantino, Martin Nors Pedersen, Chenge Li, Magnus Andersson, Mattias Eklund, Michael Wulff, Andreas Barth, Aljona Sitsel, Annette Duelli, Poul Nissen, Claus Olesen, Harsha Ravishankar
Publikováno v:
Ravishankar, H, Pedersen, M N, Eklund, M, Sitsel, A, Li, C, Duelli, A, Levantino, M, Wulff, M, Barth, A, Olesen, C, Nissen, P & Andersson, M 2020, ' Tracking Ca 2+ ATPase intermediates in real time by x-ray solution scattering ', Science Advances, vol. 6, no. 12, eaaz0981 . https://doi.org/10.1126/sciadv.aaz0981
'Science Advances ', vol: 6, pages: aaz0981-1-aaz0981-11 (2020)
'Science Advances ', vol: 6, pages: aaz0981-1-aaz0981-11 (2020)
Sarco/endoplasmic reticulum Ca2+ ATPase (SERCA) transporters regulate calcium signaling by active calcium ion reuptake to internal stores. Structural transitions associated with transport have been characterized by x-ray crystallography, but critical
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd20dc81064942645b3b496ce9815625
http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-169875
http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-169875
Autor:
Søren Brøgger Christensen, Helle A. Praetorius, Jesper V. Møller, Pankaj Sehgal, Paula Szalai, Nikolai Engedal, Poul Nissen, Claus Olesen
Publikováno v:
Sehgal, P, Szalai, P, Olesen, C, Praetorius, H A, Nissen, P, Christensen, S B, Engedal, N & Møller, J V 2017, ' Inhibition of the sarco/endoplasmic reticulum (ER) Ca2+-ATPase by thapsigargin analogs induces cell death via ER Ca2+ depletion and the unfolded protein response ', Journal of Biological Chemistry, vol. 292, pp. 19656-19673 . https://doi.org/10.1074/jbc.M117.796920
Calcium (Ca2+) is a fundamental regulator of cell signaling and function. Thapsigargin (Tg) blocks the sarco/endoplasmic reticulum (ER) Ca2+-ATPase (SERCA), disrupts Ca2+ homeostasis, and causes cell death. However, the exact mechanisms whereby SERCA
Autor:
Harsha, Ravishankar, Martin Nors, Pedersen, Mattias, Eklund, Aljona, Sitsel, Chenge, Li, Annette, Duelli, Matteo, Levantino, Michael, Wulff, Andreas, Barth, Claus, Olesen, Poul, Nissen, Magnus, Andersson
Publikováno v:
Science Advances
We characterize thus-far elusive domain rearrangements of a calcium-transporting ATPase in the native membrane.
Sarco/endoplasmic reticulum Ca2+ ATPase (SERCA) transporters regulate calcium signaling by active calcium ion reuptake to internal st
Sarco/endoplasmic reticulum Ca2+ ATPase (SERCA) transporters regulate calcium signaling by active calcium ion reuptake to internal st
Autor:
Poul Nissen, Claus Olesen, Andreas Barth, Annette Duelli, Michael Wulff, Chenge Li, Martin Nors Pedersen, Matteo Levantino, Alya Sitsel, Harsha Ravishankar, Magnus Andersson
Publikováno v:
Biophysical Journal. 118:26a
Autor:
Peter Vangheluwe, Ilse Vandecaetsbeek, Poul Nissen, Rita Derua, Claus Olesen, Susanne Smaardijk, Nikolaj D. Drachmann, Marc De Maeyer, Aljona Sitsel, Jacob Andersen, Joren De Raeymaecker, Etienne Waelkens, Jialin Chen
Publikováno v:
Sitsel, A, De Raeymaecker, J, Drachmann, N D, Derua, R, Smaardijk, S, Andersen, J L, Vandecaetsbeek, I, Chen, J, De Maeyer, M, Waelkens, E, Olesen, C, Vangheluwe, P & Nissen, P 2019, ' Structures of the heart specific SERCA2a Ca 2+-ATPase ', EMBO Journal, vol. 38, no. 5, e100020 . https://doi.org/10.15252/embj.2018100020
The sarcoplasmic/endoplasmic reticulum Ca 2+ -ATPase 2a (SERCA2a) performs active reuptake of cytoplasmic Ca 2+ and is a major regulator of cardiac muscle contractility. Dysfunction or dysregulation of SERCA2a is associated with heart failure, while
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1375fe87026caee8963f972e32144ac8
https://doi.org/10.1101/344911
https://doi.org/10.1101/344911