Zobrazeno 1 - 10
of 45
pro vyhledávání: '"Johannes D. Clausen"'
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:
Maike Bublitz, Lasse Kjellerup, Karen O'Hanlon Cohrt, Sandra Gordon, Anne Louise Mortensen, Johannes D Clausen, Thomas David Pallin, John Bondo Hansen, Anja Thoe Fuglsang, William Dalby-Brown, Anne-Marie L Winther
Publikováno v:
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
Externí odkaz:
https://doaj.org/article/e2b6d98723684c38a8ade703a93f35c5
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
Elucidation of antimicrobial activity and mechanism of action by N-substituted carbazole derivatives
Autor:
Karen O'Hanlon Cohrt, Lasse Kjellerup, John Bondo Hansen, William Dalby-Brown, Anne-Marie Lund Winther, Johannes D. Clausen
Publikováno v:
Clausen, J D, Kjellerup, L, Cohrt, K OH, Hansen, J B, Dalby-Brown, W & Winther, A-M L 2017, ' Elucidation of antimicrobial activity and mechanism of action by N-substituted carbazole derivatives ', Bioorganic & Medicinal Chemistry Letters, vol. 27, no. 19, pp. 4564-4570 . https://doi.org/10.1016/j.bmcl.2017.08.067
Bioorganic & Medicinal Chemistry Letters
Bioorganic & Medicinal Chemistry Letters
Graphical abstract
Compounds belonging to a carbazole series have been identified as potent fungal plasma membrane proton adenosine triphophatase (H+-ATPase) inhibitors with a broad spectrum of antifungal activity. The carbazole compounds inhibi
Compounds belonging to a carbazole series have been identified as potent fungal plasma membrane proton adenosine triphophatase (H+-ATPase) inhibitors with a broad spectrum of antifungal activity. The carbazole compounds inhibi
Autor:
Laura Marín, Anne-Marie Lund Winther, Lasse Kjellerup, William Dalby-Brown, José Antonio Calera, Karen A. O'Hanlon Cohrt, Johannes D. Clausen
Publikováno v:
GREDOS. Repositorio Institucional de la Universidad de Salamanca
instname
Antimicrobial Agents and Chemotherapy
Digital.CSIC. Repositorio Institucional del CSIC
Cohrt, K A OH, Marín, L, Kjellerup, L, Clausen, J D, Dalby-Brown, W, Antonio Calera, J & Winther, A-M L 2018, ' Novel zinc-attenuating compounds as potent broad-spectrum antifungal agents with In Vitro and In Vivo efficacy ', Antimicrobial Agents and Chemotherapy, vol. 62, no. 5, e02024-17 . https://doi.org/10.1128/AAC.02024-17
instname
Antimicrobial Agents and Chemotherapy
Digital.CSIC. Repositorio Institucional del CSIC
Cohrt, K A OH, Marín, L, Kjellerup, L, Clausen, J D, Dalby-Brown, W, Antonio Calera, J & Winther, A-M L 2018, ' Novel zinc-attenuating compounds as potent broad-spectrum antifungal agents with In Vitro and In Vivo efficacy ', Antimicrobial Agents and Chemotherapy, vol. 62, no. 5, e02024-17 . https://doi.org/10.1128/AAC.02024-17
An increase in the incidence of rare but hard-to-treat invasive fungal pathogens as well as resistance to the currently available antifungal drugs calls for new broad-spectrum antifungals with a novel mechanism of action. Here we report the identific
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c177540d77100e16b977e5e30050db1
http://hdl.handle.net/10261/182769
http://hdl.handle.net/10261/182769
Publikováno v:
Clausen, J D, Holdensen, A N & Andersen, J P 2014, ' Critical Roles of Interdomain Interactions for Modulatory ATP Binding to Sarcoplasmic Reticulum Ca2+-ATPase ', Journal of Biological Chemistry . https://doi.org/10.1074/jbc.M114.571687
ATP has dual roles in the reaction cycle of sarcoplasmic reticulum Ca(2+)-ATPase. Upon binding to the Ca2E1 state, ATP phosphorylates the enzyme, and by binding to other conformational states in a non-phosphorylating modulatory mode ATP stimulates th
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, Marc le Maire, Bertrand Arnou, Cédric Montigny, Jens Peter Andersen, Maike Bublitz, Johannes D. Clausen, Christine Jaxel, Poul Nissen
Publikováno v:
The EMBO Journal. 32:3231-3243
The sarco(endo)plasmic reticulum Ca 2+ ‐ATPase (SERCA) couples ATP hydrolysis to transport of Ca 2+ . This directed energy transfer requires cross‐talk between the two Ca 2+ sites and the phosphorylation site over 50 A distance. We have addressed