Roles of Long-range Electrostatic Domain Interactions and K+ in Phosphoenzyme Transition of Ca2+-ATPase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference38 articles.
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3. Structural changes in the calcium pump accompanying the dissociation of calcium;Toyoshima;Nature,2002
4. Distinct natures of beryllium fluoride-bound, aluminum fluoride-bound, and magnesium fluoride-bound stable analogues of an ADP-insensitive phosphoenzyme intermediate of sarcoplasmic reticulum Ca2+-ATPase;Danko;J. Biol. Chem,2004
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1. Electrostatic interactions between single arginine and phospholipids modulate physiological properties of sarcoplasmic reticulum Ca2+-ATPase;Scientific Reports;2022-07-16
2. Long-Range Modulations of Electric Fields in Proteins;The Journal of Physical Chemistry B;2018-08-15
3. Nanodisc-based kinetic assays reveal distinct effects of phospholipid headgroups on the phosphoenzyme transition of sarcoplasmic reticulum Ca2+-ATPase;Journal of Biological Chemistry;2017-12
4. Phosphorylation-Dependent Effects on the Structural Flexibility of Phosphoglucosamine Mutase from Bacillus anthracis;ACS Omega;2017-11-29
5. Phosphorylation/Dephosphorylation Assays;P-Type ATPases;2016
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