Toshiro Oda

Summary

Affiliation: Japan Synchrotron Radiation Research Institute
Country: Japan

Publications

  1. doi request reprint The nature of the globular- to fibrous-actin transition
    Toshiro Oda
    X ray Structural Analysis Research Team, RIKEN SPring 8 Center, RIKEN Harima Institute, 1 1 1, Kouto, Sayo, Hyogo 679 5148, Japan
    Nature 457:441-5. 2009
  2. ncbi request reprint Dolastatin 11 connects two long-pitch strands in F-actin to stabilize microfilaments
    Toshiro Oda
    Department of Biophysics, Max Planck Institute for Medical Research, Jahnstr 29, Heidelberg, D 69120, Germany
    J Mol Biol 328:319-24. 2003
  3. doi request reprint Multiple Conformations of F-actin
    Toshiro Oda
    X ray Structural Analysis Team, RIKEN SPring 8 Center, RIKEN Harima Institute 1 1 1 Kouto, Sayo gun, Hogo, Japan
    Structure 18:761-7. 2010
  4. ncbi request reprint Modeling of the F-actin structure
    Toshiro Oda
    RIKEN Harima Institute, RIKEN SPring 8 Center, 1 1 1 Kouto, Sayo, Hyogo 679 5148, Japan
    Adv Exp Med Biol 592:385-401. 2007
  5. pmc Position and orientation of phalloidin in F-actin determined by X-ray fiber diffraction analysis
    Toshiro Oda
    Max Planck Institute for Medical Research, Department of Biophysics, Heidelberg, Germany
    Biophys J 88:2727-36. 2005
  6. doi request reprint Protofilament formation of ParM mutants
    David Popp
    ERATO Actin Filament Dynamics Project, Japan Science and Technology Corporation, c o RIKEN Harima Institute at Spring 8, 1 1 1 Kouto, Sayo, Hyogo 679 5148, Japan
    J Mol Biol 388:209-17. 2009
  7. pmc Molecular structure of the ParM polymer and the mechanism leading to its nucleotide-driven dynamic instability
    David Popp
    ERATO Actin Filament Dynamics Project, RIKEN Harima Institute, Japan Science and Technology Corporation, Sayo, Hyogo, Japan
    EMBO J 27:570-9. 2008
  8. doi request reprint Polymeric structures and dynamic properties of the bacterial actin AlfA
    David Popp
    ERATO Actin Filament Dynamics Project, Japan Science and Technology Corporation, c o RIKEN Harima Institute at Spring 8, 1 1 1 Kouto, Sayo, Hyogo 679 5148, Japan
    J Mol Biol 397:1031-41. 2010
  9. pmc Dual roles of Gln137 of actin revealed by recombinant human cardiac muscle alpha-actin mutants
    Mitsusada Iwasa
    ERATO Actin Filament Dynamics Project, Japan Science and Technology Agency, c o RIKEN SPring 8 Center, Sayo, Hyogo, Japan
    J Biol Chem 283:21045-53. 2008
  10. pmc Role of the actin Ala-108-Pro-112 loop in actin polymerization and ATPase activities
    Mitsusada Iwasa
    ERATO Actin Filament Dynamics Project, Japan Science and Technology Agency, c o RIKEN SPring 8 Center, Kouto 1 1, Sayo, Hyogo 679 5148, Japan
    J Biol Chem 287:43270-6. 2012

Detail Information

Publications14

  1. doi request reprint The nature of the globular- to fibrous-actin transition
    Toshiro Oda
    X ray Structural Analysis Research Team, RIKEN SPring 8 Center, RIKEN Harima Institute, 1 1 1, Kouto, Sayo, Hyogo 679 5148, Japan
    Nature 457:441-5. 2009
    ..The flat form is essential for the formation of stable, helical F-actin. Our F-actin structure model provides the basis for understanding actin polymerization as well as its molecular interactions with actin-binding proteins...
  2. ncbi request reprint Dolastatin 11 connects two long-pitch strands in F-actin to stabilize microfilaments
    Toshiro Oda
    Department of Biophysics, Max Planck Institute for Medical Research, Jahnstr 29, Heidelberg, D 69120, Germany
    J Mol Biol 328:319-24. 2003
    ..The result suggests that the connection between the two long-pitch F-actin strands might be a key for the control of F-actin stabilization...
  3. doi request reprint Multiple Conformations of F-actin
    Toshiro Oda
    X ray Structural Analysis Team, RIKEN SPring 8 Center, RIKEN Harima Institute 1 1 1 Kouto, Sayo gun, Hogo, Japan
    Structure 18:761-7. 2010
    ..Recently, we published a refined model for F-actin. In this review, based on this model, we discuss the origin, mechanism, and possible physiological significance of the multiple conformations of F-actin...
  4. ncbi request reprint Modeling of the F-actin structure
    Toshiro Oda
    RIKEN Harima Institute, RIKEN SPring 8 Center, 1 1 1 Kouto, Sayo, Hyogo 679 5148, Japan
    Adv Exp Med Biol 592:385-401. 2007
  5. pmc Position and orientation of phalloidin in F-actin determined by X-ray fiber diffraction analysis
    Toshiro Oda
    Max Planck Institute for Medical Research, Department of Biophysics, Heidelberg, Germany
    Biophys J 88:2727-36. 2005
    ..The method of analysis developed in this study is applicable for the determination of binding positions of other drugs, such as jasplakinolide and dolastatin 11...
  6. doi request reprint Protofilament formation of ParM mutants
    David Popp
    ERATO Actin Filament Dynamics Project, Japan Science and Technology Corporation, c o RIKEN Harima Institute at Spring 8, 1 1 1 Kouto, Sayo, Hyogo 679 5148, Japan
    J Mol Biol 388:209-17. 2009
    ..ParM is the first example of a helical actin homolog that can be induced to form protofilaments...
  7. pmc Molecular structure of the ParM polymer and the mechanism leading to its nucleotide-driven dynamic instability
    David Popp
    ERATO Actin Filament Dynamics Project, RIKEN Harima Institute, Japan Science and Technology Corporation, Sayo, Hyogo, Japan
    EMBO J 27:570-9. 2008
    ....
  8. doi request reprint Polymeric structures and dynamic properties of the bacterial actin AlfA
    David Popp
    ERATO Actin Filament Dynamics Project, Japan Science and Technology Corporation, c o RIKEN Harima Institute at Spring 8, 1 1 1 Kouto, Sayo, Hyogo 679 5148, Japan
    J Mol Biol 397:1031-41. 2010
    ..These results emphasize that actin-like polymerizing machineries have diverged to produce a variety of filament geometries with diverse properties that are tailored for specific biological processes...
  9. pmc Dual roles of Gln137 of actin revealed by recombinant human cardiac muscle alpha-actin mutants
    Mitsusada Iwasa
    ERATO Actin Filament Dynamics Project, Japan Science and Technology Agency, c o RIKEN SPring 8 Center, Sayo, Hyogo, Japan
    J Biol Chem 283:21045-53. 2008
    ..These results suggest that Gln(137) plays dual roles in actin polymerization, in both the conformational transition of the actin molecule and the mechanism of ATP hydrolysis...
  10. pmc Role of the actin Ala-108-Pro-112 loop in actin polymerization and ATPase activities
    Mitsusada Iwasa
    ERATO Actin Filament Dynamics Project, Japan Science and Technology Agency, c o RIKEN SPring 8 Center, Kouto 1 1, Sayo, Hyogo 679 5148, Japan
    J Biol Chem 287:43270-6. 2012
    ..The rigidity of the loop, which mediates neither too strong nor too weak interactions between subdomains 1 and 3, might play crucial roles in actin polymerization...
  11. doi request reprint Cooperative and non-cooperative conformational changes of F-actin induced by cofilin
    Tomoki Aihara
    Structural Analysis Research Team, RIKEN SPring 8 Center, RIKEN, Sayo, Hyogo, Japan
    Biochem Biophys Res Commun 435:229-33. 2013
    ..The two processes of local and global changes do not necessarily proceed in sequence...
  12. ncbi request reprint From the crystal structure of troponin to the mechanism of calcium regulation of muscle contraction
    Yuichiro Maeda
    ERATO Actin Filament Dynamics Project, c o RIKEN Harima Institute SPring 8 Center, Sayo, Hyogo, Japan
    Adv Exp Med Biol 592:37-46. 2007
  13. pmc Differences in internal dynamics of actin under different structural states detected by neutron scattering
    Satoru Fujiwara
    Quantum Beam Science Directorate, Japan Atomic Energy Agency, Tokai mura, Naka gun, Ibaraki 319 1195, Japan
    Biophys J 94:4880-9. 2008
    ..Based on structural data, the assignment of the differences observed in the two samples to dynamics of specific loop regions involved in the polymerization of G-actin into F-actin is proposed...
  14. doi request reprint Total synthesis of chondramide C and its binding mode to F-actin
    Herbert Waldmann
    Max Planck Institut fur molekulare Physiologie, Abteilung Chemische Biologie, Otto Hahn Strasse 11, 44227 Dortmund, Germany
    Angew Chem Int Ed Engl 47:6473-7. 2008