State of aggregation of the (Ca2+ + Mg2+)-ATPase studied using chemical cross-linking
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference33 articles.
1. State of aggregation of the (Ca2+ + Mg2+)-ATPase studied using saturation-transfer electron spin resonance
2. Three-dimensional reconstruction of negatively stained crystals of the Ca2+-ATPase from muscle sarcoplasmic reticulum
3. The structure of the Ca2+ ATPase as revealed by electron microscopy and image processing of ordered arrays
4. Dimer ribbons in the three-dimensional structure of sarcoplasmic reticulum
5. The application of chemical crosslinking for studies on cell membranes and the identification of surface reporters
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1. Cross-linking of C-terminal Residues of Phospholamban to the Ca2+ Pump of Cardiac Sarcoplasmic Reticulum to Probe Spatial and Functional Interactions within the Transmembrane Domain;Journal of Biological Chemistry;2006-05
2. Evidence that the effects of phospholipids on the activity of the Ca2+-ATPase do not involve aggregation;Biochemical Journal;1995-05-15
3. Molecular mechanism of calcium-ATPase activation by halothane in sarcoplasmic reticulum;Biochemistry;1993-07
4. Chemical crosslinking and enzyme kinetics provide no evidence for a regulatory role for the 53 kDa glycoprotein of sarcoplasmic reticulum in calcium transport;Biochimica et Biophysica Acta (BBA) - Biomembranes;1991-04
5. Antibodies against the 53 kDa glycoprotein inhibit the rotational dynamics of both the 53 kDa glycoprotein and the Ca2+-ATPase in the sarcoplasmic reticulum membrane;Biochimica et Biophysica Acta (BBA) - Biomembranes;1991-04
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