Y
Yoko Y. Toyoshima
Researcher at University of Tokyo
Publications - 76
Citations - 5669
Yoko Y. Toyoshima is an academic researcher from University of Tokyo. The author has contributed to research in topics: Microtubule & Dynein. The author has an hindex of 39, co-authored 76 publications receiving 5380 citations. Previous affiliations of Yoko Y. Toyoshima include University of California, San Francisco & University of California, Los Angeles.
Papers
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Journal ArticleDOI
Myosin subfragment-1 is sufficient to move actin filaments in vitro.
Yoko Y. Toyoshima,Stephen J. Kron,Elizabeth M. McNally,Kenneth R. Niebling,Chikashi Toyoshima,James A. Spudich +5 more
TL;DR: That S1 is sufficient to cause sliding movement of actin filaments in vitro gives strong support to models of contraction that place the site of active movement in muscle within the myosin head.
Book ChapterDOI
Assays for actin sliding movement over myosin-coated surfaces.
TL;DR: This chapter is a compilation of techniques for purified in vitro motility assays for actin sliding movement over myosin, limited to studies using skeletal muscle proteins, but only slight modification of these protocols may be necessary for proteins derived from smooth muscle and nonmuscle sources.
Journal ArticleDOI
Overlapping hand-over-hand mechanism of single molecular motility of cytoplasmic dynein
TL;DR: The step size and force produced by single molecules of active cytoplasmic dynein are measured by using an optical trap and fluorescence imaging with a high temporal resolution and the velocity of dyneIn movement, 800 nm/s, is consistent with that reported in cells.
Journal ArticleDOI
Rotation and translocation of microtubules in vitro induced by dyneins from Tetrahymena cilia
Ronald D. Vale,Yoko Y. Toyoshima +1 more
TL;DR: A quantitative in vitro motility assay in which dynein adsorbed onto a glass surface induces linear translocation of purified bovine microtubules and shows that both 22S and 14S dyneins from Tetrahymena cilia induce movement but have distinct motile properties.
Journal ArticleDOI
Distinct functions of nucleotide-binding/hydrolysis sites in the four AAA modules of cytoplasmic dynein.
TL;DR: Results indicate that ATP binding and its hydrolysis only at the P1 site are essential for the motor activities of cytoplasmic dynein, and suggest that the other nucleotide-binding/hydrolysis sites regulate the motor Activities.