Relaxed tarantula skeletal muscle has two ATP energy-saving mechanisms
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Title
Relaxed tarantula skeletal muscle has two ATP energy-saving mechanisms
Authors
Keywords
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Journal
JOURNAL OF GENERAL PHYSIOLOGY
Volume 153, Issue 3, Pages -
Publisher
Rockefeller University Press
Online
2021-01-24
DOI
10.1085/jgp.202012780
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- Conserved Intramolecular Interactions Maintain Myosin Interacting-Heads Motifs Explaining Tarantula Muscle Super-Relaxed State Structural Basis
- (2016) Lorenzo Alamo et al. JOURNAL OF MOLECULAR BIOLOGY
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- The Hydrophobic Temperature Dependence of Amino Acids Directly Calculated from Protein Structures
- (2015) Erik van Dijk et al. PLoS Computational Biology
- Different Head Environments in Tarantula Thick Filaments Support a Cooperative Activation Process
- (2013) Guidenn Sulbarán et al. BIOPHYSICAL JOURNAL
- A Molecular Model of Phosphorylation-Based Activation and Potentiation of Tarantula Muscle Thick Filaments
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- Myosin ATP turnover rate is a mechanism involved in thermogenesis in resting skeletal muscle fibers
- (2009) M. A. Stewart et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Three-Dimensional Reconstruction of Tarantula Myosin Filaments Suggests How Phosphorylation May Regulate Myosin Activity
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