Electric birefringence study of the solution structure of chymotrypsin-cleaved Acanthamoeba myosin II.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference33 articles.
1. Acanthamoeba myosin II.
2. Isolation of a non-muscle myosin heavy chain gene from Acanthamoeba.
3. Complete nucleotide sequence and deduced polypeptide sequence of a nonmuscle myosin heavy chain gene from Acanthamoeba: evidence of a hinge in the rodlike tail.
4. Characterization of a second myosin from Acanthamoeba castellanii
5. Filament formation and actin-activated ATPase activity are abolished by proteolytic removal of a small peptide from the tip of the tail of the heavy chain of Acanthamoeba myosin II.
Cited by 14 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. Phenylglyoxal Reveals Phosphorylation-Dependent Difference in the Conformation of Acanthamoeba Myosin II Active Site;Archives of Biochemistry and Biophysics;2000-12
2. Flexibility of Acanthamoeba Myosin Rod Minifilaments;Biochemistry;1999-05-11
3. Nucleotides Increase the Internal Flexibility of Filaments of Dephosphorylated Acanthamoeba Myosin II;Journal of Biological Chemistry;1996-05
4. Effects of phosphorylation and nucleotides on the conformation of myosin II from Acanthamoeba castellanii.;Journal of Biological Chemistry;1994-05
5. A structural difference between filaments of phosphorylated and dephosphorylated Acanthamoeba myosin II revealed by electric birefringence.;Journal of Biological Chemistry;1993-03
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