@article {573056,
	title = {A small-molecule inhibitor of skeletal muscle myosin II.},
	journal = {Nat Cell Biol},
	volume = {4},
	number = {1},
	year = {2002},
	month = {2002 Jan},
	pages = {83-8},
	abstract = {We screened a small-molecule library for inhibitors of rabbit muscle myosin II subfragment 1 (S1) actin-stimulated ATPase activity. The best inhibitor, N-benzyl-p-toluene sulphonamide (BTS), an aryl sulphonamide, inhibited the Ca2+-stimulated S1 ATPase, and reversibly blocked gliding motility. Although BTS does not compete for the nucleotide-binding site of myosin, it weakens myosin{\textquoteright}s interaction with F-actin. BTS reversibly suppressed force production in skinned skeletal muscle fibres from rabbit and frog skin at micromolar concentrations. BTS suppressed twitch production of intact frog fibres with minimum alteration of Ca2+ metabolism. BTS is remarkably specific, as it was much less effective in suppressing contraction in rat myocardial or rabbit slow-twitch muscle, and did not inhibit platelet myosin II. The isolation of BTS and the recently discovered Eg5 kinesin inhibitor, monastrol, suggests that motor proteins may be potential targets for therapeutic applications.},
	keywords = {Adenosine Triphosphatases, Animals, Calcium, Enzyme Inhibitors, In Vitro Techniques, Molecular Motor Proteins, Muscle Contraction, Muscle, Skeletal, Myosin Subfragments, Peptide Library, Rabbits, Ranidae, Rats, Skeletal Muscle Myosins, Sulfonamides, Toluene},
	issn = {1465-7392},
	doi = {10.1038/ncb734},
	author = {Cheung, A and Dantzig, J A and Hollingworth, S and Baylor, S M and Goldman, Y E and Mitchison, T. J. and Straight, A F}
}
