M Ohba

Summary

Affiliation: Mitsubishi Kagaku Institute of Life Sciences
Country: Japan

Publications

  1. ncbi Modulation of intracellular protein degradation by SSB1-SIS1 chaperon system in yeast S. cerevisiae
    M Ohba
    Mitsubishi Kasei Institute of Life Sciences, Machida shi, Tokyo, Japan
    FEBS Lett 409:307-11. 1997
  2. ncbi A 70-kDa heat shock cognate protein suppresses the defects caused by a proteasome mutation in Saccharomyces cerevisiae
    M Ohba
    Mitsubishi Kasei Institute of Life Sciences, Tokyo, Japan
    FEBS Lett 351:263-6. 1994
  3. ncbi CDNA cloning of p112, the largest regulatory subunit of the human 26s proteasome, and functional analysis of its yeast homologue, sen3p
    K Yokota
    Department of Urology, School of Medicine, Tokushima, Japan
    Mol Biol Cell 7:853-70. 1996

Collaborators

  • Katsunori Tanaka
  • K Yokota
  • C A Slaughter
  • M Yamasaki
  • Y Shimizu
  • G N DeMartino
  • H Akioka
  • C Noda
  • T Fujiwara
  • C Tsurumi
  • E Takahashi
  • A Toh-e
  • M Fujimuro
  • S Kagawa
  • H Yokosawa

Detail Information

Publications3

  1. ncbi Modulation of intracellular protein degradation by SSB1-SIS1 chaperon system in yeast S. cerevisiae
    M Ohba
    Mitsubishi Kasei Institute of Life Sciences, Machida shi, Tokyo, Japan
    FEBS Lett 409:307-11. 1997
    ..Thus SSB1, with its partner DnaJ, SIS1, modulates the efficiency of protein turnover through its chaperon activity...
  2. ncbi A 70-kDa heat shock cognate protein suppresses the defects caused by a proteasome mutation in Saccharomyces cerevisiae
    M Ohba
    Mitsubishi Kasei Institute of Life Sciences, Tokyo, Japan
    FEBS Lett 351:263-6. 1994
    ..Thus, the SSB1 protein, one of the chaperons of the yeast, facilitated intracellular protein degradation...
  3. ncbi CDNA cloning of p112, the largest regulatory subunit of the human 26s proteasome, and functional analysis of its yeast homologue, sen3p
    K Yokota
    Department of Urology, School of Medicine, Tokushima, Japan
    Mol Biol Cell 7:853-70. 1996
    ....