16 results on '"Hermsen, Harm P.H."'
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2. The carbonyl group of glutamic acid-795 is essential for gastric H (super)+,K (super)+ -ATPase activity
3. Constitutive activation of gastric H+,K+‐ATPase by a single mutation
4. K+-independent Gastric H+,K+-ATPase Activity: DISSOCIATION OF K+-INDEPENDENT DEPHOSPHORYLATION AND PREFERENCE FOR THE E1 CONFORMATION BY COMBINED MUTAGENESIS OF TRANSMEMBRANE GLUTAMATE RESIDUES
5. The K + affinity of gastric H +,K +-ATPase is affected by both lipid composition and the β-subunit
6. The β-Subunits of Na+,K+-ATPase and Gastric H+,K+-ATPase Have a High Preference for Their Own α-Subunit and Affect the K+ Affinity of These Enzymes
7. Mutagenesis of glutamate 820 of the gastric H +,K +-ATPase α-subunit to aspartate decreases the apparent ATP affinity
8. The K+ affinity of gastric H+,K+-ATPase is affected by both lipid composition and the β-subunit
9. Mutagenesis of glutamate 820 of the gastric H+,K+-ATPase α-subunit to aspartate decreases the apparent ATP affinity
10. Mutational analysis of the putative devazepide binding site of the CCKA receptor
11. High-affinity ouabain binding by a chimeric gastric H+, K+-ATPase containing transmembrane...
12. Mutation of aspartate 804 of Na[sup +],K[sup +]-ATPase modifies the cation binding pocket and...
13. The carbonyl group of glutamic acid-795 is essential for gastric H+,K+-ATPase activity.
14. Mutational analysis of the putative devazepide binding site of the CCK A receptor
15. Teh negatively charged glutamic acid 820 of the gastric H+,K+-ATPase α-subunit plays an essential role in K+ binding and transition of the E2 form.
16. Functional expression of Na+,K+-ATPase and their hybrids in insect cells.
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