Publikace
- 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 | Matematicko-fyzikální fakulta
- Substrate evokes translocation of both domains in the mitochondrial processing peptidase alpha-subunit during which the C-terminus acts as a stabilizing element2004 | Matematicko-fyzikální fakulta, Ústřední knihovna
- Protein modeling combined with spectroscopic techniques: An attractive quick alternative to obtain structural information2004 | Matematicko-fyzikální fakulta
- Fluorescence competition assay for the assessment of ATP binding to an isolated domain of Na+,K+-ATPase2004 | Matematicko-fyzikální fakulta
- ATP-binding is stabilized by a stacking interaction within the binding site of Na+/K+-ATPase2003 | Matematicko-fyzikální fakulta, Ústřední knihovna
- Eight amino acids form the ATP recognition site of Na+/K+-ATPase2003 | Matematicko-fyzikální fakulta, Ústřední knihovna
- Limitations in linearized analyses of binding equilibria: binding of TNP-ATP to the H-4-H-5 loop of Na/K-ATPase2003 | Matematicko-fyzikální fakulta, Ústřední knihovna
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