Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Johannes D. Clausen"'
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:
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