Superinhibitory Phospholamban Mutants Compete with Ca2+ for Binding to SERCA2a by Stabilizing a Unique Nucleotide-dependent Conformational State
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference49 articles.
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2. Phospholamban: a crucial regulator of cardiac contractility
3. Phospholamban Inhibitory Function Is Activated by Depolymerization
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5. Mutation and Phosphorylation Change the Oligomeric Structure of Phospholamban in Lipid Bilayers
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1. Structural basis for allosteric control of the SERCA-Phospholamban membrane complex by Ca2+ and phosphorylation;eLife;2021-05-12
2. A Temporal Examination of Cytoplasmic Ca2 + Levels, Sarcoplasmic Reticulum Ca2 + Levels, and Ca2 + -Handling-Related Proteins in Different Skeletal Muscles of Hibernating Daurian Ground Squirrels;Frontiers in Physiology;2020-10-21
3. Structural Basis for Allosteric Control of the SERCA-Phospholamban Membrane Complex by Ca2+and cAMP-dependent Phosphorylation;2020-08-28
4. Protein docking and steered molecular dynamics suggest alternative phospholamban-binding sites on the SERCA calcium transporter;Journal of Biological Chemistry;2020-08
5. Protein Docking and Steered Molecular Dynamics Reveal Alternative Regulatory Sites on the SERCA Calcium Transporter;2019-12-20
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