18O labeling on Ser45 but not on Ser35 supports the cooperative phosphorylation mechanism on tarantula thick filament activation
Author:
Funder
CPA
Howard Hughes Medical Institute
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference22 articles.
1. Atomic model of a myosin filament in the relaxed state;Woodhead;Nature,2005
2. Three-dimensional reconstruction of tarantula myosin filaments suggests how phosphorylation may regulate myosin activity;Alamo;J. Mol. Biol.,2008
3. A molecular model of phosphorylation-based activation and potentiation of tarantula muscle thick filaments;Brito;J. Mol. Biol.,2011
4. Different head environments in tarantula thick filaments support a cooperative activation process;Sulbarán;Biophys. J.,2013
5. Sequential myosin phosphorylation activates tarantula thick filament via a disorder-order transition;Espinoza-Fonseca;Mol. Biosyst.,2015
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1. Stable Isotope Phosphate Labelling of Diverse Metabolites is Enabled by a Family of 18 O‐Phosphoramidites**;Angewandte Chemie International Edition;2021-11-23
2. Stable Isotope Phosphate Labelling of Diverse Metabolites is Enabled by a Family of 18 O‐Phosphoramidites**;Angewandte Chemie;2021-11-23
3. Relaxed tarantula skeletal muscle has two ATP energy-saving mechanisms;Journal of General Physiology;2021-01-22
4. The myosin interacting-heads motif present in live tarantula muscle explains tetanic and posttetanic phosphorylation mechanisms;Proceedings of the National Academy of Sciences;2020-05-22
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