- Limitations in linearized analyses of binding equilibria: binding of TNP-ATP to the H-4-H-5 loop of Na/K-ATPase2003 | Faculty of Mathematics and Physics, Central Library of Charles University
- Limitations in linearized analyses of binding equilibria: binding of TNP-ATP to the H4-H5 loop of Na/K-ATPase2003 | Second Faculty of Medicine
- The hydrogen bonds between Arg(423) and Glu(472) and other key residues, Asp(443), Ser(477), and Pro(489), are responsible for the formation and a different positioning of TNP-ATP and ATP within the nucleotide-binding site of Na+/K+-ATPase2004 | Second Faculty of Medicine
- The phosphatase activity of the isolated H-4-H-5 loop of Na+/K+ ATPase resides outside its ATP binding site2004 | Second Faculty of Medicine
- Phe475 and Glu446 but not Ser445 participate in ATP-binding to the alfa-subunit of NA/K-ATPase2002 | Faculty of Science
- The hydrogen bonds between Arg(423) and Glu(472) and other key residues, Asp(443), Ser(477), and Pro(489), are responsible for the formation and a different positioning of TNP-ATP and ATP within the nucleotide-binding site of Na+/K+-ATPase2004 | Faculty of Mathematics and Physics
- ATP binding site on the C-terminus of the vanilloid receptor2007 | Faculty of Science
- Fluorescence competition assay for the assessment of ATP binding to an isolated domain of Na+,K+-ATPase2004 | Second Faculty of Medicine
- Voltammetric Determination of Ecotoxic Nitro Compounds Using Polished Silver Amalgam Composite Electrode2012 | Faculty of Science
- Phe475 and Glu446 but not Ser445 participate in ATP-binding to the alfa-subunit of NA/K-ATPase2002 | Faculty of Mathematics and Physics, First Faculty of Medicine