Trinitrophenylation of smooth muscle myosin
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference32 articles.
1. MYOSIN
2. On the Active Site of Myosin A-Adenosine Triphosphatase
3. Effect of trinitrophenylation on myosin ATPase
4. The sequence of the NH2-terminal 204-residue fragment of the heavy chain of rabbit skeletal muscle myosin.
5. Localization of the reactive trinitrophenylated lysyl residue of myosin ATPase site in the NH2 -terminal (27 k domain) of S1 heavy chain
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1. Role of ATP in the Binding of Caldesmon to Smooth Muscle Myosin;Biochemistry;1995-05-16
2. Reaction of thiol groups of gizzard myosin heavy chains with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole;Archives of Biochemistry and Biophysics;1990-08
3. Myosin and Contractile Activity in Smooth Muscle;Calcium Protein Signaling;1989
4. The regulatory light chain is required for folding of smooth muscle myosin.;Journal of Biological Chemistry;1988-11
5. Pathway for the communication between the ATPase and actin sites in myosin;Journal of Muscle Research and Cell Motility;1988-06
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