Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Serge M. Gisler"'
Publikováno v:
American Journal of Physiology-Renal Physiology. 313:F1018-F1025
The intrarenal autocrine-paracrine dopamine (DA) system mediates a significant fraction of the natriuresis in response to a salt load. DA inhibits a number of Na+transporters to effect sodium excretion, including the proximal tubule Na+/H+exchanger-3
The type IIa Na(+)/P(i) cotransporter (NaPi-IIa) plays a key role in the reabsorption of inorganic phosphate (P(i)) in the renal proximal tubule. The rat NaPi-IIa isoform is a protein of 637 residues for which different algorithms predict 8-12 transm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11d8d991da7e442b0bb5c195d6ef1a08
http://doc.rero.ch/record/320295/files/232_2006_Article_33.pdf
http://doc.rero.ch/record/320295/files/232_2006_Article_33.pdf
Publikováno v:
American journal of physiology. Renal physiology. 313(4)
The intrarenal autocrine-paracrine dopamine (DA) system mediates a significant fraction of the natriuresis in response to a salt load. DA inhibits a number of Na+ transporters to effect sodium excretion, including the proximal tubule Na+/H+ exchanger
Autor:
Heinrich Betz, Orson W. Moe, Gregory A. O'Sullivan, Sonja C. Reining, Serge M. Gisler, Heini Murer, Jürg Biber, Daniel Guido Fuster, Nati Hernando
Publikováno v:
American Journal of Physiology-Renal Physiology. 296:F1118-F1128
Renal reabsorption of inorganic phosphate (Pi) is mainly mediated by the Na+-dependent Pi-cotransporter NaPi-IIa that is expressed in the brush-border membrane (BBM) of renal proximal tubules. Regulation and apical expression of NaPi-IIa are known to
Autor:
Mia Bertic, Randy A. Hall, Serge M. Gisler, Tamara Radanovic, Daniel Guido Fuster, Orson W. Moe, Saranya Kittanakom, Jürg Biber, Heini Murer, Igor Stagljar, Victoria Wong, Daniel Markovich
Publikováno v:
Molecular & Cellular Proteomics. 7:1362-1377
PDZ-binding motifs are found in the C-terminal tails of numerous integral membrane proteins where they mediate specific protein-protein interactions by binding to PDZ-containing proteins. Conventional yeast two-hybrid screens have been used to probe
Autor:
Orson W. Moe, Serge M. Gisler, Paola Capuano, Sandra Pribanic, Carsten A. Wagner, Nati Hernando, Jürg Biber, Heini Murer, Nadine Déliot
Publikováno v:
The Journal of Physiology. 567:21-26
Regulation of renal proximal tubular reabsorption of phosphate (Pi) is one of the critical steps in Pi homeostasis. Experimental evidence suggests that this regulation is achieved mainly by controlling the apical expression of the Na+-dependent Pi co
Publikováno v:
Journal of Membrane Biology. 203:111-118
IntroductionEssentially all cellular functions rely on the correctspatial organization of proteins. In epithelial cells,this is manifested by a separation of the plasmamembrane into an apical and a basolateral area,which is required for vectorial tra
Publikováno v:
American Journal of Physiology-Renal Physiology. 287:F871-F875
In adults, the extent of renal reabsorption of Pi and consequently the extent of urinary excretion of phosphate are to a large extent determined by the abundance of the Na-Pi cotransporter NaPi-IIa (SLC34A1). Localization of this cotransporter is res
Autor:
Stephan J. Reshkin, Lorenzo Guerra, Heini Murer, Valeria Casavola, Rosa Angela Cardone, Serge M. Gisler, Anna Bagorda, Teresa Fanelli, Francesca Di Sole, Corinna Hemle-Kolb
Publikováno v:
Journal of Biological Chemistry. 277:21480-21488
Although Cystic fibrosis transmembrane conductance regulator (CFTR) has been shown to regulate the activity of NHE3, the potential reciprocal interaction of NHE3 to modulate the protein kinase A (PKA)-dependent regulation of CFTR in epithelial cells
Autor:
Hans-Joachim Schönfeld, Erika Sandmeier, Ezra V. Pierpaoli, Serge M. Gisler, Philipp Christen, Antonio Baici
Publikováno v:
Journal of Molecular Biology. 269:757-768
The molecular chaperone DnaK, the Hsp70 homolog of Escherichia coli, acts in concert with the co-chaperones DnaJ and GrpE. The aim of this study was to identify the particular phase of the peptide binding-release cycle of the DnaK/DnaJ/GrpE system th