Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Elizabeth A. Jewell-Motz"'
Publikováno v:
Journal of Biological Chemistry. 275:28989-28993
The alpha(2A)-adrenergic receptor (AR) undergoes rapid agonist-promoted desensitization due to phosphorylation by G protein-coupled receptor kinases (GRKs) 2 and 3 at serines in the third intracellular loop of the receptor. In contrast, the alpha(2C)
Publikováno v:
Biochemistry. 37:15720-15725
One mechanism of long-term agonist-promoted desensitization of alpha2AR function is downregulation of the cellular levels of the alpha subunit of the inhibitory G protein, Gi. In transfected CHO cells expressing the human alpha2AAR, a 40.1 +/- 3.3% d
Autor:
Jerry B. Lingrel, Elizabeth A. Jewell-Motz, Lauren A. Millette, Carl L. Johnson, Katherine Tepperman, Earl T. Wallick
Publikováno v:
American Journal of Physiology-Cell Physiology. 273:C2065-C2079
A competition assay of86Rb+uptake in HeLa cells transfected with ouabain-resistant Na+-K+-ATPase mutants revealed a stimulation of86Rb+uptake at low external concentrations (1 mM) of competitor (K+). Of the models that were tested, those that require
Publikováno v:
Journal of Biological Chemistry. 271:18082-18087
The alpha2-adrenergic receptor (alpha2AR) subtype alpha2C10 undergoes rapid agonist-promoted desensitization which is due to phosphorylation of the receptor. One kinase that has been shown to phosphorylate alpha2C10 in an agonist-dependent manner is
Autor:
Gerald W. Dorn, Margaret G. Eason, Cheryl T. Theiss, Elizabeth A. Jewell-Motz, Stephen B. Liggett, Mark A. Williams, Mei Liang
Publikováno v:
Molecular pharmacology. 54(1)
We have investigated the potential for protein kinase C (PKC) to phosphorylate and desensitize the alpha2A-adrenergic receptor (alpha2AAR). In whole-cell phosphorylation studies, recombinantly expressed human alpha2AAR displayed an increase in phosph
Publikováno v:
Biochemistry. 34(37)
The alpha 2C2 adrenergic receptor contains a highly acidic stretch of amino acids (EDEAEEEEEEEEEEEE) within the third intracellular loop. To investigate the role of this region, we utilized site-directed mutagenesis to delete these 16 amino acids as
Autor:
William J. O'Brien, Patrick J. Schultheis, Jerry B. Lingrel, Elizabeth A. Jewell-Motz, J. Van Huysse
Publikováno v:
Renal physiology and biochemistry. 17(3-4)
Autor:
Patrick J. Schultheis, Jerry B. Lingrel, James W. Van Huysse, Elizabeth A. Jewell-Motz, William J. O'Brien
Publikováno v:
Molecular and Cellular Mechanisms of H+ Transport ISBN: 9783642793035
The Na, K-ATPase, which is found in the cells of all higher eukaryotes, utilizes ATP to transport Na+ and K+ across the cell membrane. For every three sodium ions transported out of the cell two potassium ions are transported in. The enzyme is compos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::efdbf8b94ce96d6a83afc3a4df1b7cc5
https://doi.org/10.1007/978-3-642-79301-1_20
https://doi.org/10.1007/978-3-642-79301-1_20
Autor:
Patrick J. Schultheis, G. Roger Askew, Elizabeth A. Jewell-Motz, Earl T. Wallick, Jerry B. Lingrel, James W. Van Huysse, William J. O'Brien
Publikováno v:
The Sodium Pump ISBN: 9783642725135
Na+/K+-ATPase is the receptor for cardiac glycosides, a class of drugs used to treat congestive heart failure and arrhythymias. Binding of these compounds to the enzyme is antagonized by K+ ions suggesting that the binding sites for these ligands may
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dfd2253f98f87e1c053e7a31a2c2d415
https://doi.org/10.1007/978-3-642-72511-1_48
https://doi.org/10.1007/978-3-642-72511-1_48
Publikováno v:
Biochemistry. 32(49)
Site-directed mutagenesis was used to examine the importance of five carboxyl-containing amino acids localized in the putative membrane-spanning regions of the Na,K-ATPase (i.e., E327, E778, D803, D807, and D925 of the rat alpha 2 isoform). The subst