H Okazawa

Summary

Affiliation: University of Tokyo
Country: Japan

Publications

  1. ncbi PQBP-1 (Np/PQ): a polyglutamine tract-binding and nuclear inclusion-forming protein
    H Okazawa
    Department of Neurology, University of Tokyo, Tokyo, Japan
    Brain Res Bull 56:273-80. 2001
  2. ncbi PQBP-1, a novel polyglutamine tract-binding protein, inhibits transcription activation by Brn-2 and affects cell survival
    M Waragai
    Group of Molecular Neurobiology, Department of Neurology, Graduate School of Medicine, University of Tokyo, Japan
    Hum Mol Genet 8:977-87. 1999
  3. ncbi PQBP-1/Npw38, a nuclear protein binding to the polyglutamine tract, interacts with U5-15kD/dim1p via the carboxyl-terminal domain
    M Waragai
    Department of Neurology, Graduate School of Medicine, University of Tokyo, 7 3 1, Hongo, Bunkyo ku, Tokyo, 113 8655, Japan
    Biochem Biophys Res Commun 273:592-5. 2000
  4. ncbi Polar amino acid-rich sequences bind to polyglutamine tracts
    I Imafuku
    Department of Neurology, Graduate School of Medicine, University of Tokyo, Japan
    Biochem Biophys Res Commun 253:16-20. 1998

Collaborators

Detail Information

Publications4

  1. ncbi PQBP-1 (Np/PQ): a polyglutamine tract-binding and nuclear inclusion-forming protein
    H Okazawa
    Department of Neurology, University of Tokyo, Tokyo, Japan
    Brain Res Bull 56:273-80. 2001
    ..In this review, we discuss the structure and function of the PQBP-1 protein, the relevance of its aggregation and possible roles in normal and disease processes...
  2. ncbi PQBP-1, a novel polyglutamine tract-binding protein, inhibits transcription activation by Brn-2 and affects cell survival
    M Waragai
    Group of Molecular Neurobiology, Department of Neurology, Graduate School of Medicine, University of Tokyo, Japan
    Hum Mol Genet 8:977-87. 1999
    ..These results suggest that PQBP-1 mediates important cellular functions under physiological and pathological conditions via its interaction with polyglutamine tracts...
  3. ncbi PQBP-1/Npw38, a nuclear protein binding to the polyglutamine tract, interacts with U5-15kD/dim1p via the carboxyl-terminal domain
    M Waragai
    Department of Neurology, Graduate School of Medicine, University of Tokyo, 7 3 1, Hongo, Bunkyo ku, Tokyo, 113 8655, Japan
    Biochem Biophys Res Commun 273:592-5. 2000
    ..This finding suggests physiological functions of PQBP-1 in splicing, cell cycle, and ubiquitination, through which we can speculate the pathological roles of PQBP-1 in triplet repeat diseases...
  4. ncbi Polar amino acid-rich sequences bind to polyglutamine tracts
    I Imafuku
    Department of Neurology, Graduate School of Medicine, University of Tokyo, Japan
    Biochem Biophys Res Commun 253:16-20. 1998
    ..Three of these clones could form polar helical structures. These observations suggest that polar amino acid-rich sequences are essential for binding to the polyglutamine tract...