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W Schoner

Showing results (61-70 of 125) with videos related to

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Progress in Clinical and Biological Research|January 1, 1988
The catalytic subunits cooperate in (Na+ + K+)-ATPase: demonstration with MgPO4 and MgATP complex analoguesG Scheiner-Bobis, E Buxbaum, W Schoner
Hoppe-Seyler'S Zeitschrift Fur Physiologische Chemie|August 1, 1977
Inactivation of pyruvate kinase type M2 from chicken liver by phosphorylation, catalyzed by a cAMP-independent protein kinaseE Eigenbrodt, M A Mostafa, W Schoner
Recent Advances in Studies on Cardiac Structure and Metabolism|January 1, 1975
Cardiac glycoside receptor in potassium depletionE Erdmann, H D Bolte, W Schoner
European Journal of Biochemistry|August 1, 1980
Demonstration of two different reactive sulfhydryl groups in the ATP-binding sites of Ca2+-ATPase of sarcoplasmic reticulum by disulfides of thioinosine triphosphatesR Patzelt-Wenczler, H Kreickmann, W Schoner
European Journal of Biochemistry|October 1, 1987
Demonstration of cooperating alpha subunits in working (Na+ + K+)-ATPase by the use of the MgATP complex analogue cobalt tetrammine ATPG Scheiner-Bobis, K Fahlbusch, W Schoner
European Journal of Biochemistry|February 1, 1982
Demonstration of a stable occluded form of Ca2+ by the use of the chromium complex of ATP in the Ca2+-ATPase of sarcoplasmic reticulumE H Serpersu, U Kirch, W Schoner
European Journal of Biochemistry|July 31, 1990
How do MgATP analogues differentially modify high-affinity and low-affinity ATP binding sites of Na+/K(+)-ATPase?E H Serpersu, S Bunk, W Schoner
European Journal of Biochemistry|July 15, 1989
Shift to the Na+ form of Na+/K+-transporting ATPase due to modification of the low-affinity ATP-binding site by Co(NH3)4ATPG Scheiner-Bobis, M Esmann, W Schoner
European Journal of Biochemistry|May 1, 1989
Characterization of a cysteine-containing peptide after affinity labelling of Ca2+-ATPase of sarcoplasmic reticulum with the disulfide of 3'(2')-O-biotinyl-thioinosine triphosphateR Kison, H E Meyer, W Schoner
European Journal of Biochemistry|May 13, 1998
Binding of the Co(NH3)4 derivative of (2')3'-O-[N-methyl-anthraniloyl]-ATP to the E2ATP site of Na+/K+-transporting ATPase lowers the conformational flexibility of its E1ATP siteW Schoner, W Mertens, M Helms, et al.
Pageof 13

Showing results (61-70 of 125) with videos related to

Sort By:
Pageof 13
Progress in Clinical and Biological Research|January 1, 1988
The catalytic subunits cooperate in (Na+ + K+)-ATPase: demonstration with MgPO4 and MgATP complex analoguesG Scheiner-Bobis, E Buxbaum, W Schoner
Hoppe-Seyler'S Zeitschrift Fur Physiologische Chemie|August 1, 1977
Inactivation of pyruvate kinase type M2 from chicken liver by phosphorylation, catalyzed by a cAMP-independent protein kinaseE Eigenbrodt, M A Mostafa, W Schoner
Recent Advances in Studies on Cardiac Structure and Metabolism|January 1, 1975
Cardiac glycoside receptor in potassium depletionE Erdmann, H D Bolte, W Schoner
European Journal of Biochemistry|August 1, 1980
Demonstration of two different reactive sulfhydryl groups in the ATP-binding sites of Ca2+-ATPase of sarcoplasmic reticulum by disulfides of thioinosine triphosphatesR Patzelt-Wenczler, H Kreickmann, W Schoner
European Journal of Biochemistry|October 1, 1987
Demonstration of cooperating alpha subunits in working (Na+ + K+)-ATPase by the use of the MgATP complex analogue cobalt tetrammine ATPG Scheiner-Bobis, K Fahlbusch, W Schoner
European Journal of Biochemistry|February 1, 1982
Demonstration of a stable occluded form of Ca2+ by the use of the chromium complex of ATP in the Ca2+-ATPase of sarcoplasmic reticulumE H Serpersu, U Kirch, W Schoner
European Journal of Biochemistry|July 31, 1990
How do MgATP analogues differentially modify high-affinity and low-affinity ATP binding sites of Na+/K(+)-ATPase?E H Serpersu, S Bunk, W Schoner
European Journal of Biochemistry|July 15, 1989
Shift to the Na+ form of Na+/K+-transporting ATPase due to modification of the low-affinity ATP-binding site by Co(NH3)4ATPG Scheiner-Bobis, M Esmann, W Schoner
European Journal of Biochemistry|May 1, 1989
Characterization of a cysteine-containing peptide after affinity labelling of Ca2+-ATPase of sarcoplasmic reticulum with the disulfide of 3'(2')-O-biotinyl-thioinosine triphosphateR Kison, H E Meyer, W Schoner
European Journal of Biochemistry|May 13, 1998
Binding of the Co(NH3)4 derivative of (2')3'-O-[N-methyl-anthraniloyl]-ATP to the E2ATP site of Na+/K+-transporting ATPase lowers the conformational flexibility of its E1ATP siteW Schoner, W Mertens, M Helms, et al.
Pageof 13