Affinity of nucleotides for the active site of detergent-solubilized sarcoplasmic reticulum CaATPase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference20 articles.
1. Properties of a delipidated, detergent-activated calcium(2+)-activated ATPase
2. Detergent-solubilized sarcoplasmic reticulum ATPase. Hydrodynamic and catalytic properties.
3. Purification of the CaATPase of sarcoplasmic reticulum by affinity chromatography.
4. Phospholipid orientation in sacroplasmic membranes: Spin-label ESR and proton NMR studies
5. Preparation and properties of 2′(or 3′)-O-(2,4,6-trinitrophenyl) adenosine 5′-triphosphate, an analog of adenosine triphosphate
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1. The mechanism of inhibition of the sarco/endoplasmic reticulum Ca2+ ATPase by paxilline;Archives of Biochemistry and Biophysics;2002-10
2. The inhibition of the sarcoplasmic/endoplasmic reticulum Ca2+-ATPase by macrocyclic lactones and cyclosporin A;Biochemical Journal;2002-08-15
3. Inhibition of SERCA Ca2+pumps by 2-aminoethoxydiphenyl borate (2-APB);European Journal of Biochemistry;2002-07-17
4. The Mechanism of Inhibition of the Ca2+-ATPase by Mastoparan;Journal of Biological Chemistry;1999-05
5. Substrate Specificity for Catalysis of Phosphoryl Transfer by the Calcium ATPase of Sarcoplasmic reticulum;Archives of Biochemistry and Biophysics;1994-08
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