Key result
Review outlines methodological framework to study aminoacyl-tRNA synthetase phosphorylation and noncanonical cellular activities.
Why the study?
Phosphorylation of phospholamban induces a conformational change that affects its regulatory function on cardiac Ca-ATPase, but the structural details remain unclear.
Comparison
Phosphorylated phospholamban vs non-phosphorylated phospholamban and mutants
Design
Spectroscopic experiments including intrinsic fluorescence and CD under SDS-PAGE and lipid bilayer conditions
Authors
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Phosphorylation alters phospholamban protomer conformation without secondary structure change; extends consensus on SERCA regulation but leaves clinical translation open.
Key points are not available for this paper at this time.
Li et al. (1998) reported a review. This paper outlines a comprehensive methodological framework for investigating the phosphorylation of aminoacyl-tRNA synthetases and their noncanonical cellular activities.
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