Phosphorylated Ca2+-ATPase Stable Enough for Structural Studies
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference12 articles.
1. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
2. Pumping ions
3. Dynamic interconversions of phosphorylated and n0n-phosphorylated intermediates of the Ca-ATPase from sarcoplasmic reticulum followed in a flourescein-labeled enzyme
4. A Remarkably Stable Phosphorylated Form of Ca2+-ATPase Prepared from Ca2+-loaded and Fluorescein Isothiocyanate-labeled Sarcoplasmic Reticulum Vesicles
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1. 1,2-Dichlorobenzene affects the formation of the phosphoenzyme stage during the catalytic cycle of the Ca2+-ATPase from sarcoplasmic reticulum;BMC Biochemistry;2016-03-11
2. Nucleotide Activation of the Ca-ATPase;Journal of Biological Chemistry;2012-11
3. Structural Studies of a Stabilized Phosphoenzyme Intermediate of Ca2+-ATPase;Journal of Biological Chemistry;2005-05
4. Structure and Function of the Calcium Pump;Annual Review of Biophysics and Biomolecular Structure;2003-06
5. Projection Map of Covalently Phosphorylated Ca-ATPase from Tubular Crystals;Annals of the New York Academy of Sciences;2003-04
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