Spudich, J.A., and Watt, S. (1971). Regulation of skeletal muscle contraction. I. Biochemical Studies of the Interaction of the Tropomyosin-Troponin Complex with Actin and the Proteolytic Fragments of Myosin. J. Biol. Chem. 246: 4866-4871. (full pdf text)
Biochemical experiments establishing that tropomyosin-troponin exerts its Ca2+ regulatory effect by interacting with actin. Also, widely quoted for purification of actin to homogeneity.
Spudich, J.A., Huxley, H.E., and Finch, J. (1972). Regulation of Skeletal Muscle Contraction. II. Structural Studies of the Interaction of the Tropomyosin-Troponin Complex with Actin. J. Mol. Biol. 72: 619-632. (full pdf text)
3D-reconstructions from electron micrographs reveal the location of tropomyosin-troponin in the grooves of the actin filament, and the first proposal of the steric blocking mechanism of the regulatory mechanism.
Sheetz, M.P., and Spudich, J.A. (1983). Movement of Myosin-Coated Fluorescent Beads on Actin Cables In Vitro. Nature 303: 31-35. (full pdf text)
First quantitative in vitro motility assay for molecular motor movement.
Spudich, J.A., Kron, S.J., and Sheetz, M.P. (1985). Movement of Myosin-Coated Beads on Oriented Filaments Reconstituted from Purified Actin. Nature 315: 584-586. (full pdf text)
First quantitative in vitro motility assay demonstrating with purified proteins that myosin moves along actin filaments, and at velocities comparable to those of muscle contraction.
Kron, J., and Spudich, J.A. (1986). Fluorescent Actin Filaments Move on Myosin Fixed to a Glass Surface. Proc. Natl. Acad. Sci. USA 83: 6272-6276. (full pdf text)
The form of the in vitro motility assay in wide use today.
Toyoshima, Y.Y., Kron, S.J., McNally, E.M., Niebling, K.R., Toyoshima, C., and Spudich, J.A. (1987). Myosin Subfragment-1 Is Sufficient to Move Actin Filaments In Vitro. Nature 328: 536-539. (full pdf text)
Demonstration that the Subfragment-1 head of myosin is the motor domain.
De Lozanne, A., and Spudich, J.A. (1987). Disruption of the DictyosteliumMyosin Heavy Chain Gene by Homologous Recombination. Science 236 :1086-1091. (full pdf text)
Demonstration of homologous recombination in Dictyostelium. Knockout of the single copy myosin II heavy chain gene providing genetic proof of its requirement for cytokinesis and cell polarization.
Finer, J.T., Simmons, R.M., and Spudich, J.A. (1994). Single Myosin Molecule Mechanics: Piconewton Forces and Nanometre Steps. Nature 368: 113-119. (full pdf text)
Single molecule analysis using laser traps, and demonstration of piconewton forces and step sizes of ~10 nm.
Uyeda, T.Q.P., Abramson, P.D., and Spudich, J.A. (1996). The Neck Region of the Myosin Motor Domain Acts as a Lever Arm to Generate Movement. Proc. Natl. Acad. Sci. USA 93:4459-4464. (full pdf text)
Strong evidence for the lever arm hypothesis.
Ruppel, K.M., and Spudich, J.A. (1996). Structure-Function Studies of the Myosin Motor Domain: Importance of the 50-kDa Cleft. Mol. Biol. Cell 7: 1123-1136. (full pdf text)
A broad scale mutagenesis effort that delineated the roles of specific residues and domains involved in the motor function.
Shih, W.M., Gryczynski, Z., Lakowicz, J.R. and Spudich, J.A. (2000). A FRET-Based Sensor Reveals Large ATP Hydrolysis-Induced Conformational Changes and Three Distinct States of the Molecular Motor Myosin. Cell 102: 683-694. (full pdf text)
Dynamic studies establishing a large lever arm rotation for myosin II.
Rief, M., Rock, R.S., Mehta, A.D., Mooseker, M.S., Cheney, R.E. and Spudich, J.A. (2000). Myosin-V Stepping Kinetics: A Molecular Model for Processivity. Proc. Natl. Acad. Sci. USA 97: 9482-9486. (full pdf text)
Strong evidence of tight coupling of ATP hydrolysis with mechanical movement of a myosin motor.
Altman, D., Sweeney, H.L., and Spudich, J.A. (2004). The Mechanism of Myosin VI Translocation and Its Load-Induced Anchoring. Cell 116: 737-749. (full pdf text)
Demonstration of the importance of tension sensing by molecular motors.
Churchman, L.S., Ökten, Z., Rock, R.S., Dawson, J.F., and Spudich, J.A. (2005). Single Molecule High-resolution Colocalization of Cy3 and Cy5 Attached to Macromolecules Measures Intramolecular Distances through Time. Proc. Natl. Acad. Sci. USA 102: 1419-1423. (full pdf text)
The development and utilization of SHREC (Single molecule High-REsolution Colocalization of two fluorescent probes) for molecules in motion.
Bryant, Z., Altman, D. and Spudich, J.A. (2007). The Power Stroke of Myosin VI and the Basis of Reverse Directionality. Proc. Natl. Acad. Sci. USA 104: 772-777. (full pdf text)
Demonstration that the myosin VI motor, viewed as the biggest challenge to the lever arm hypothesis, indeed involves a lever arm stroke, through an angle of ~180°.