Random myosin loss along thick-filaments increases myosin attachment time and the proportion of bound myosin heads to mitigate force decline in skeletal muscle-Reference-Cited by-同舟云学术

Random myosin loss along thick-filaments increases myosin attachment time and the proportion of bound myosin heads to mitigate force decline in skeletal muscle

Published:2014-06 Issue: Volume:552-553 Page:117-127
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Tanner Bertrand C.W.,McNabb Mark,Palmer Bradley M.,Toth Michael J.,Miller Mark S.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference45 articles.

1. Cancer cachexia is regulated by selective targeting of skeletal muscle gene products

2. Skeletal muscle unweighting: spaceflight and ground-based models

3. In VivoandIn VitroHeterogeneity of Segment Length Changes in the Semimembranosus Muscle of the Toad

4. Myosin filament 3D structure in mammalian cardiac muscle

5. Single Particle Analysis: A new approach to solving the 3D structure of myosin filaments

Cited by 7 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Design Principles and Benefits of Spatially Explicit Models of Myofilament Function;Methods in Molecular Biology;2023-12-02

2. Skeletal muscle single fiber force production declines early in juvenile male mice with chronic kidney disease;Physiological Reports;2023-04

3. The spatial distribution of thin filament activation influences force development and myosin activity in computational models of muscle contraction;Archives of Biochemistry and Biophysics;2021-05

4. Effects of cross-bridge compliance on the force-velocity relationship and muscle power output;PLOS ONE;2017-12-28

5. Increased Titin Compliance Reduced Length-Dependent Contraction and Slowed Cross-Bridge Kinetics in Skinned Myocardial Strips from Rbm20ΔRRM Mice;Frontiers in Physiology;2016-07-29