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Eight amino acids form the ATP recognition site of Na(+)/K(+)-ATPase.
Kubala M, Teisinger J, Ettrich R, Hofbauerová K, Kopecký V Jr, Baumruk V, Krumscheid R, Plásek J, Schoner W, Amler E. Kubala M, et al. Among authors: plasek j. Biochemistry. 2003 Jun 3;42(21):6446-52. doi: 10.1021/bi034162u. Biochemistry. 2003. PMID: 12767226
The hydrogen bonds between Arg423 and Glu472 and other key residues, Asp443, Ser477, and Pro489, are responsible for the formation and a different positioning of TNP-ATP and ATP within the nucleotide-binding site of Na(+)/K(+)-ATPase.
Lánský Z, Kubala M, Ettrich R, Kutý M, Plásek J, Teisinger J, Schoner W, Amler E. Lánský Z, et al. Among authors: plasek j. Biochemistry. 2004 Jul 6;43(26):8303-11. doi: 10.1021/bi0496485. Biochemistry. 2004. PMID: 15222743
Early changes in membrane potential of Saccharomyces cerevisiae induced by varying extracellular K(+), Na (+) or H (+) concentrations.
Plášek J, Gášková D, Ludwig J, Höfer M. Plášek J, et al. J Bioenerg Biomembr. 2013 Dec;45(6):561-8. doi: 10.1007/s10863-013-9528-6. Epub 2013 Sep 20. J Bioenerg Biomembr. 2013. PMID: 24052423
Recently we introduced a fluorescent probe technique that makes possible to convert changes of equilibrium fluorescence spectra of 3,3'-dipropylthiadicarbocyanine, diS-C3(3), measured in yeast cell suspensions under defined conditions into underlying membrane potential difference …
Recently we introduced a fluorescent probe technique that makes possible to convert changes of equilibrium fluorescence spectra of 3,3'-dipr …
103 results