Now showing items 1-2 of 2

    • The ATPase activity of molecular chaperone HSP60 is inhibited by immunosuppressant mizoribine 

      Tanabe, Masako; Ishida, Ryuichi; Izuhara, Fumiko; Komatsuda, Atsushi; Wakui, Hideki; Sawada, Kenichi; Otaka, Michiro; Nakamura, Nobuhiro; Itoh, Hideaki (Scientific Research Publishing, 2012-04)
      The molecular chaperone HSP60 is a chaperonin homolog of GroEL. We had previously shown that the immunosuppressant mizoribine is bound directly to HSP60 and inhibited its chaperone activity. However, the inhibitory mechanisms ...
    • Cytosolic chaperonin CCT possesses GTPase activity 

      Noguchi, Susumu; Toyoshima, Kazuyoshi; Yamamoto, Soh; Miyazaki, Toshio; Otaka, Michiro; Watanabe, Sumio; Imai, Katsunori; Senoo, Haruki; Kobayashi, Ryoji; Jikei, Mitsutoshi; Kawata, Yasushi; Kubota, Hiroshi; Itoh, Hideaki (Scientific Research Publishing, 2011-10)
      Cytosolic chaperonin CCT (also known as TRiC) is a hetero-oligomeric cage-like molecular chaperone that assists in protein folding by ATPase cycle-dependent conformational changes. However, role of the nucleo-tide binding ...