Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Johannes D. Clausen"'
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:
William Dalby-Brown, Anne-Marie Lund Winther, Johannes D. Clausen, Thomas David Pallin, Anne Louise Mortensen, Karen O'Hanlon Cohrt, Maike Bublitz, John Bondo Hansen, Anja T. Fuglsang, Lasse Kjellerup, Sandra Gordon
Publikováno v:
PLoS ONE
Bublitz, M, Kjellerup, L, Cohrt, K OH, Gordon, S, Mortensen, A L, Clausen, J D, Pallin, T D, Hansen, J B, Fuglsang, A T, Dalby-Brown, W & Winther, A-M L 2018, ' Tetrahydrocarbazoles are a novel class of potent P-type ATPase inhibitors with antifungal activity ', PLOS ONE, vol. 13, no. 1, e0188620 . https://doi.org/10.1371/journal.pone.0188620
PLoS ONE, Vol 13, Iss 1, p e0188620 (2018)
Bublitz, M, Kjellerup, L, Cohrt, K OH, Gordon, S, Mortensen, A L, Clausen, J D, Pallin, T D, Hansen, J B, Fuglsang, A T, Dalby-Brown, W & Winther, A-M L 2018, ' Tetrahydrocarbazoles are a novel class of potent P-type ATPase inhibitors with antifungal activity ', PLOS ONE, vol. 13, no. 1, e0188620 . https://doi.org/10.1371/journal.pone.0188620
PLoS ONE, Vol 13, Iss 1, p e0188620 (2018)
We have identified a series of tetrahydrocarbazoles as novel P-type ATPase inhibitors. Using a set of rationally designed analogues, we have analyzed their structure-activity relationship using functional assays, crystallographic data and computation
Autor:
Jesper V. Møller, Kamil Gotfryd, Oleg Sitsel, Daniel Mattle, Poul Nissen, Nikolaj D. Drachmann, Garth J. Williams, Maike Bublitz, Matthias J. Gutmann, M. Marvin Seibert, Lutz Foucar, Thomas R. M. Barends, Sébastien Boutet, Marc Messerschmidt, Ilme Schlichting, Karol Nass, Anders J. Markvardsen, Johannes D. Clausen, Claus Olesen, Jonas Lindholt Gregersen, Kaituo Wang, R. Bruce Doak, Thomas Boesen, Robert L. Shoeman, Linda Reinhard
Publikováno v:
Bublitz, M, Nass, K, Drachmann, N D, Markvardsen, A J, Gutmann, M J, Barends, T R M, Mattle, D, Shoeman, R L, Doak, R B, Boutet, S, Messerschmidt, M, Seibert, M M, Williams, G J, Foucar, L, Reinhard, L, Sitsel, O, Gregersen, J L, Clausen, J D, Boesen, T, Gotfryd, K, Wang, K-T, Olesen, C, Møller, J V, Nissen, P & Schlichting, I 2015, ' Structural studies of P-type ATPase-ligand complexes using an X-ray free-electron laser ', IUCrJ, vol. 2, no. Pt 4, pp. 409-420 . https://doi.org/10.1107/S2052252515008969
IUCrJ
IUCrJ, Vol 2, Iss 4, Pp 409-420 (2015)
IUCrJ
IUCrJ, Vol 2, Iss 4, Pp 409-420 (2015)
The structure determination of P-type ATPase–ligand complexes from microcrystals by serial femtosecond crystallography using a free-electron laser is described. The feasibility of the method for ligand screening is demonstrated, and SFX data qualit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d303314bc35636a6e5c090a57fe0aac
https://pure.au.dk/portal/da/publications/structural-studies-of-ptype-atpaseligand-complexes-using-an-xray-freeelectron-laser(1918c96e-fcba-4d3e-8a74-13d447ba2bf5).html
https://pure.au.dk/portal/da/publications/structural-studies-of-ptype-atpaseligand-complexes-using-an-xray-freeelectron-laser(1918c96e-fcba-4d3e-8a74-13d447ba2bf5).html
Publikováno v:
Journal of Biological Chemistry. 279:54426-54437
Point mutants with alterations to amino acid residues Thr(247), Pro(248), Glu(340), Asp(813), Arg(819), and Arg(822) of sarcoplasmic reticulum Ca(2+)-ATPase were analyzed by transient kinetic measurements. In the Ca(2+)-ATPase crystal structures, mos
Publikováno v:
Journal of Biological Chemistry. 278:20245-20258
Nine single mutations were introduced to amino acid residues Thr441, Glu442, Lys515, Arg560, Cys561, and Leu562 located in the nucleotide-binding domain of sarcoplasmic reticulum Ca2+-ATPase, and the functional consequences were studied in a direct n
Publikováno v:
Aarhus University
The roles of Ser(72), Glu(90), and Lys(297) at the luminal ends of transmembrane helices M1, M2, and M4 of sarcoplasmic reticulum Ca(2+)-ATPase were examined by transient and steady-state kinetic analysis of mutants. The dependence on the luminal Ca(
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bbfdb74efef050944c1d86c44f2130a6
https://pure.au.dk/portal/en/publications/glutamate-90-at-the-luminal-ion-gate-of-sarcoplasmic-reticulum-ca2atpase-is-critical-for-ca2-binding-on-both-sides-of-the-membrane(8e566a90-828a-11df-8c1a-000ea68e967b).html
https://pure.au.dk/portal/en/publications/glutamate-90-at-the-luminal-ion-gate-of-sarcoplasmic-reticulum-ca2atpase-is-critical-for-ca2-binding-on-both-sides-of-the-membrane(8e566a90-828a-11df-8c1a-000ea68e967b).html