Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Johannes D. Clausen"'
Autor:
Virginie Monceau, Regis Bobe, Judith K. Gwathmey, Elisabeth Corvazier, Jocelyne Enouf, Aly Raies, Jens Peter Andersen, Johannes D. Clausen, Roger J. Hajjar, Raymonde Bredoux, Leonard Dode, Chiraz Chaabane, Saoussen Dally, Frederica Del Monte, Mohammed Fanchaouy, Pascal Gélébart
Publikováno v:
Aarhus University
We recently documented the expression of a novel human mRNA variant encoding a yet uncharacterized SERCA [SR (sarcoplasmic reticulum)/ER (endoplasmic reticulum) Ca2+-ATPase] protein, SERCA2c [Gélébart, Martin, Enouf and Papp (2003) Biochem. Biophys
Autor:
Regis Bobe, Raymonde Bredoux, Jocelyne Enouf, Jens Peter Andersen, Tünde Kovács, Johannes D. Clausen, Leonard Dode, Elisabeth Corvazier
Publikováno v:
Journal of Biological Chemistry. 279:24297-24306
Understanding of Ca(2+) signaling requires the knowledge of proteins involved in this process. Among these proteins are sarco/endoplasmic reticulum Ca(2+)-ATPases (SERCAs) that pump Ca(2+) into the endoplasmic reticulum (ER). Recently, the human SERC
Autor:
Johannes D. Clausen, David H. MacLennan, David G. Woolley, Jens Peter Andersen, David B. McIntosh, Bente Vilsen
Publikováno v:
Annals of the New York Academy of Sciences. 986:101-105
ATP-binding residues in the N and P domains of sarcoplasmic reticulum Ca-ATPase have been investigated using mutagenesis in combination with a binding assay based on the photolabeling of Lys(492) with [g-(32)P] 2',3'-O-(2,4,6 trinitrophenyl)-8-azido-
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:
David G. Woolley, Johannes D. Clausen, David B. McIntosh, Bente Vilsen, Jens Peter Andersen, Anne Nyholm Anthonisen
Publikováno v:
Aarhus University
Mutants with alteration to Asn(706) of the highly conserved (701)TGDGVND(707) motif in domain P of sarcoplasmic reticulum Ca(2+)-ATPase were analyzed for changes in transport cycle kinetics and binding of the inhibitors vanadate, BeF, AlF, and MgF. T
Publikováno v:
The Journal of biological chemistry. 279(52)
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:
Proceedings of the National Academy of Sciences of the United States of America. 101(9)
The recently determined crystal structures of the sarcoplasmic reticulum Ca(2+)-ATPase show that in the E(1)Ca(2) form, domain A is almost isolated from the other cytoplasmic domains, P and N, whereas in E(2), domain A has approached domains P and N,
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
Publikováno v:
Annals of the New York Academy of Sciences. 986
Publikováno v:
Annals of the New York Academy of Sciences. 986
Rapid kinetic measurements were used to study the rate of Ca(2+) dissociation from the high-affinity Ca(2+) sites of the dephosphoenzyme (i.e., from the E(1)Ca(2) form toward the cytoplasmic side) as well as the rate of Ca(2+) binding with associated