Lower Activation Energy for Sliding of F-Actin on a Less Thermostable Isoform of Carp Myosin
Author:
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,General Medicine
Link
http://academic.oup.com/jb/article-pdf/120/4/788/2439642/120-4-788.pdf
Cited by 23 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. Possible cold-adaptation for the fungal kinesin in compensation for thermal stability acquired by single amino acid substitution;The Journal of Biochemistry;2018-12-05
2. Thermal activation energy for bidirectional movement of actin along bipolar tracks of myosin filaments;Biochemical and Biophysical Research Communications;2010-05
3. Three embryonic myosin heavy chain genes encoding different motor domain structures from common carp show distinct expression patterns in cranial muscles;Marine Genomics;2010-03
4. Linking functional molecular variation with environmental gradients: Myosin gene diversity in a crustacean broadly distributed across variable thermal environments;Gene;2009-05
5. cDNA cloning and characterization of temperature-acclimation-associated light meromyosins from grass carp fast skeletal muscle;Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology;2008-02
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