Kinetic Analysis of Drosophila Muscle Myosin Isoforms Suggests a Novel Mode of Mechanochemical Coupling
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference49 articles.
1. Molecular diversity of myofibrillar proteins: gene regulation and functional significance
2. Kinetic differences at the single molecule level account for the functional diversity of rabbit cardiac myosin isoforms
3. Alternative Exon-encoded Regions of Drosophila Myosin Heavy Chain Modulate ATPase Rates and Actin Sliding Velocity
4. The converter domain modulates kinetic properties ofDrosophila myosin
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1. Myosin dilated cardiomyopathy mutation S532P disrupts actomyosin interactions, leading to altered muscle kinetics, reduced locomotion, and cardiac dilation in Drosophila;Molecular Biology of the Cell;2021-08-19
2. Alternative N-terminal regions of Drosophila myosin heavy chain II regulate communication of the purine binding loop with the essential light chain;Journal of Biological Chemistry;2020-10
3. The load dependence of muscle’s force-velocity curve is modulated by alternative myosin converter domains;American Journal of Physiology-Cell Physiology;2019-06-01
4. Five Alternative Myosin Converter Domains Influence Muscle Power, Stretch Activation, and Kinetics;Biophysical Journal;2018-03
5. Myosin storage myopathy mutations yield defective myosin filament assembly in vitro and disrupted myofibrillar structure and function in vivo;Human Molecular Genetics;2017-09-14
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