Transient kinetics of the interaction of 1,N6-ethenoadenosine 5'-triphosphate with myosin subfragment 1 under normal and cryoenzymic conditions: a comparison with adenosine 5'-triphosphate
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00413a047
Reference35 articles.
1. Regulation and Kinetics of the Actin-Myosin-ATP Interaction
2. The reversibility of adenosine triphosphate cleavage by myosin
3. The characterization of myosin–product complexes and of product-release steps during the magnesium ion-dependent adenosine triphosphatase reaction
4. Transient Kinetic Studies of the Mg++-dependent ATPase of Myosin and Its Proteolytic Subfragments
5. Cryobaroenzymic studies as a tool for investigating activated complexes: creatine kinase.ADP.Mg.nitrate.creatine as a model.
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1. Are there two different binding sites for ATP on the myosin head, or only one that switches between two conformers?;Journal of Muscle Research and Cell Motility;2017-04
2. Fluorescent analogs of NAADP with calcium mobilizing activity;Biochimica et Biophysica Acta (BBA) - General Subjects;1998-09
3. Half-stoichiometric trinitrophenylation of myosin subfragment 1 in the presence of pyrophosphate or adenosine diphosphate.;Journal of Biological Chemistry;1993-04
4. Effect of 2,3-butanedione monoxime on myosin and myofibrillar ATPases. An example of an uncompetitive inhibitor;Biochemistry;1992-12-08
5. Kinetics of the interaction of 2'(3')-O-(N-methylanthraniloyl)-ATP with myosin subfragment 1 and actomyosin subfragment 1: Characterization of two acto.cntdot.S1.cntdot.ADP complexes;Biochemistry;1991-01-15
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