The conformation of myosin during the steady state of ATP hydrolysis: Studies with myosin spin labeled at the S1 thiol groups
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference9 articles.
1. Transient state phosphate production in the hydrolysis of nucleoside triphosphates by myosin
2. Myosin-product complex and its effect on the steady-state rate of nucleoside triphosphate hydrolysis
3. Effect of nucleotides and pyrophosphate on spin labels bound to S1 thiol groups of myosin
4. Interaction of spin-labeled myosin with substrate
5. Interaction of Heavy Meromyosin with Substrate
Cited by 93 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. Transient detection of spin-labeled myosin subfragment 1 conformational states during ATP hydrolysis;Biochemistry;1993-07
2. Effect of actin on the tryptic digestion of myosin subfragment 1 in the weakly attached state;European Journal of Biochemistry;1992-12
3. Nucleotide-induced changes in the interaction of myosin subfragment 1 with actin: detection by antibodies against the N-terminal segment of actin;Biochemistry;1991-10-01
4. Temperature-induced changes in the flexibility of the loop between SH1 (Cys-707) and SH3 (Cys-522) in myosin subfragment 1 detected by cross-linking;Archives of Biochemistry and Biophysics;1991-10
5. Transmission of ADP.vanadate-induced conformational changes to three peptide segments of myosin subfragment-1.;Journal of Biological Chemistry;1990-11
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