Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Jan B. Koenderink"'
Autor:
Gijs Schaftenaar, Herman G.P. Swarts, Peter H.G.M. Willems, Jan B. Koenderink, Elmar Krieger, Jan Joep H.H.M. De Pont, Li Yan Qiu
Publikováno v:
Journal of Biological Chemistry, 280, 32349-32355
Journal of Biological Chemistry, 280, 37, pp. 32349-32355
Journal of Biological Chemistry, 280, 37, pp. 32349-55
Journal of Biological Chemistry, 280, 32349-55
Journal of Biological Chemistry, 280, 37, pp. 32349-32355
Journal of Biological Chemistry, 280, 37, pp. 32349-55
Journal of Biological Chemistry, 280, 32349-55
Contains fulltext : 32914.pdf (Publisher’s version ) (Open Access) Contains fulltext : 189403.pdf (Publisher’s version ) (Open Access) Although cardiac glycosides have been used as drugs for more than 2 centuries and their primary target, the sod
Autor:
Jan Joep H.H.M. De Pont, Peter H.G.M. Willems, H.P.H. Hermsen, Jan B. Koenderink, Herman G.P. Swarts
Publikováno v:
Journal of Biological Chemistry. 276:36909-36916
Several mutations of residues Glu(795) and Glu(820) present in M5 and M6 of the catalytic subunit of gastric H(+),K(+)-ATPase have resulted in a K(+)-independent, SCH 28080-sensitive ATPase activity, caused by a high spontaneous dephosphorylation rat
Publikováno v:
Mechanisms and Consequences of Proton Transport ISBN: 9781461353300
The Na,K-ATPase and gastric H,K-ATPase belong to the class of P-type ATPases, which use the energy from ATP for active transport of ions. Although both X,K-ATPases share many similarities, they have different ion specificities (Na+ vs. H+) and differ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c2788aa76ff1ca74f78b25cdb41a3493
https://doi.org/10.1007/978-1-4615-0971-4_7
https://doi.org/10.1007/978-1-4615-0971-4_7
Autor:
Peter H.G.M. Willems, H.P.H. Hermsen, J.J.H.H.M. De Pont, Herman G.P. Swarts, Jan B. Koenderink
Na + ,K + -ATPase and gastric H + ,K + -ATPase are two related enzymes that are responsible for active cation transport. Na + ,K + -ATPase activity is inhibited specifically by ouabain, whereas H + ,K + -ATPase is insensitive to this drug. Because it
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bd126f985a47d1fb0c3fea66e23d973
https://europepmc.org/articles/PMC17179/
https://europepmc.org/articles/PMC17179/
Publikováno v:
Journal of Biological Chemistry, 274, 11604-11610
Journal of Biological Chemistry, 274, pp. 11604-11610
Journal of Biological Chemistry, 274, pp. 11604-11610
The alpha- and beta-subunits of Na+,K+-ATPase and H+,K+-ATPase were expressed in Sf9 cells in different combinations. Immunoprecipitation of the alpha-subunits resulted in coprecipitation of the accompanying beta-subunit independent of the type of be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e06065520c42da55ce96a20ac9f656f
http://hdl.handle.net/2066/216410
http://hdl.handle.net/2066/216410
Publikováno v:
Biochemical Journal, 331, 465-472
Biochemical Journal, 331, pp. 465-472
Biochemical Journal, 331, pp. 465-472
To investigate the role of Glu820, located in transmembrane domain M6 of the alpha-subunit of gastric H+,K+-ATPase, a number of mutants was prepared and expressed in Sf9 cells using a baculovirus encoding for both H+,K+-ATPase subunits. The wild-type
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0133aab4e98cf711b9572c52e1f7ef85
http://hdl.handle.net/2066/265376
http://hdl.handle.net/2066/265376
Publikováno v:
Biochimica et Biophysica Acta. Biomembranes, 1768, 3, pp. 580-9
Biochimica et Biophysica Acta. Biomembranes, 1768, 580-9
Biochimica et Biophysica Acta. Biomembranes, 1768, 580-9
Contains fulltext : 51463.pdf (Publisher’s version ) (Closed access) The primary sequence of non-gastric H,K-ATPase differs much more between species than that of Na,K-ATPase or gastric H,K-ATPase. To investigate whether this causes species-depende