[11] Chemical modification of myosin by active-site trapping of metal-nucleotides with thiol crosslinking reagents
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Elsevier
Reference38 articles.
1. Reaction of 5,5'-dithiobis(2-nitrobenzoic acid) with myosin subfragment one: evidence for formation of a single protein disulfide with trapping of metal nucleotide at the active site
2. Magnesium nucleotide is stoichiometrically trapped at the active site of myosin and its active proteolytic fragments by thiol cross-linking reagents.
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1. Using Optical Tweezers to Study the Fine Details of Myosin ATPase Mechanochemical Cycle;Single Molecule Enzymology;2011
2. Equilibrium Binding of Proteins to F-Actin;Methods in Molecular Biology™;2007
3. Decavanadate Binding to a High Affinity Site near the Myosin Catalytic Centre Inhibits F-Actin-Stimulated Myosin ATPase Activity;Biochemistry;2004-04-14
4. Three-Dimensional Structural Analysis of Individual Myosin Heads Under Various Functional States;Advances in Experimental Medicine and Biology;2003
5. Crystallographic findings on the internally uncoupled and near-rigor states of myosin: Further insights into the mechanics of the motor;Proceedings of the National Academy of Sciences;2002-09-24
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