464 Unity Hall
Walcott, S. and D. M. Warshaw, Modeling myosin Va liposome transport through actin filament networks reveals a percolation threshold that modulates transport properties. Molecular Biology of the Cell. 33(2): ar18.
Jarvis, K. J., K. M. Bell, A. K. Loya, D. M. Swank and S. Walcott, Force-velocity and tension transient measurements from Drosophila jump muscle reveal the necessity of both weakly-bound cross-bridges and series elasticity in models of muscle contraction. Archives of Biochemistry and Biophysics. 701: 108809.
Newhard, C. S., S. Walcott, and D. M. Swank, The load-dependence of muscle's force-velocity curve is modulated by alternative myosin converter domains. American Journal of Physiology (Cell Physiology). 316(6): C844-C861.
Lombardo, A.T., S. R. Nelson, G. G. Kennedy, K. M. Trybus, S. Walcott, and D. M. Warshaw, Myosin Va transport of liposomes in three-dimensional actin networks is modulated by actin filament density, position, and polarity. Proceedings of the National Academy of Sciences. 116(17): 8326-8335.
Jarvis, K., M. A. Woodward, E. P. Debold and S. Walcott, Acidosis affects muscle contraction by slowing the rates myosin attaches to and detaches from actin. Journal of Muscle Research and Cell Motililty. 39(3): 135-147.