Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Johannes D. Clausen"'
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
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:
Anne-Marie Lund Winther, Alexandre Marchand, Peter Joakim Holm, Claus Olesen, Marc le Maire, Bente Vilsen, Jens Peter Andersen, Philippe Champeil, Poul Nissen, Bertrand Arnou, Jesper V. Møller, Johannes D. Clausen, Christine Jaxel, Cédric Montigny
Publikováno v:
Aarhus University
In recent years crystal structures of the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA1a), stabilized in various conformations with nucleotide and phosphate analogs, have been obtained. However, structural analysis of mutant forms would also be valuab
Publikováno v:
Anthonisen, A N, Clausen, J D & Andersen, J P 2006, ' Mutational analysis of the conserved TGES loop of sarcoplasmic reticulum Ca 2+-ATPase. ', Journal of Biological Chemistry, vol. 281, pp. 31572-31582 .
Aarhus University
Aarhus University
Crystal structures have shown that the conserved TGES loop of the Ca2+-ATPase is isolated in the Ca2E1 state but becomes inserted in the catalytic site in E2 states. Here, we have examined the kinetics of the partial reaction steps of the transport c
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:
Clausen, J D, McIntosh, D B, Woolley, D G & Andersen, J P 2011, ' Modulatory ATP binding affinity in intermediate states of E2P dephosphorylation of sarcoplasmic reticulum Ca2+-ATPase ', Journal of Biological Chemistry, vol. 286, no. 13, pp. 11792-11802 .
Aarhus University
Aarhus University
The mechanism of ATP modulation of E2P dephosphorylation of sarcoplasmic reticulum Ca(2+)-ATPase wild type and mutant forms was examined in nucleotide binding studies of states analogous to the various intermediates of the dephosphorylation reaction,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5322cc71c31d7a9e03b3a1e74d4588b
https://pure.au.dk/portal/da/publications/modulatory-atp-binding-affinity-in-intermediate-states-of-e2p-dephosphorylation-of-sarcoplasmic-reticulum-ca2atpase(a95e7a6a-2cad-4924-ac9e-47680fbfa12c).html
https://pure.au.dk/portal/da/publications/modulatory-atp-binding-affinity-in-intermediate-states-of-e2p-dephosphorylation-of-sarcoplasmic-reticulum-ca2atpase(a95e7a6a-2cad-4924-ac9e-47680fbfa12c).html
Autor:
Bente Vilsen, David B. McIntosh, Johannes D. Clausen, David H. MacLennan, Jens Peter Andersen, David G. Woolley
Publikováno v:
The Journal of Biological Chemistry
32515-32523
32515-32523
Residues in conserved motifs (625)TGD, (676)FARXXPXXK, and (701)TGDGVND in domain P of sarcoplasmic reticulum Ca(2+)-ATPase, as well as in motifs (601)DPPR and (359)NQR(/K)MSV in the hinge segments connecting domains N and P, were examined by mutagen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6815355f0643bf917a418bd98a786d79
http://hdl.handle.net/11427/35009
http://hdl.handle.net/11427/35009