... the protein level and aggregation of polyQ-expanded huntingtin through the involvement of heat shock protein 90 (HSP90). Here, we present solution structures of the CS1, CS2 and UbL domains of USP19 and structural insights into their domain interactions. We found that the tandem CS domains fold back...

...Hitoshi Nakamoto; Yosuke Amaya; Taiwa Komatsu; Takehiro Suzuki; Naoshi Dohmae; Yusuke Nakamura; Ibrahim Jantan; Yoshihiko Miyata Hsp90 is an ATP-dependent molecular chaperone that assists folding and conformational maturation/maintenance of many proteins. It is a potential cancer drug target...

... with the RNA component of telomerase. The molecular chaperones heat shock protein 90 (Hsp90) and p23 maintain hTERT in a conformation that enables nuclear translocation. However, the regulatory role of chaperones in nuclear transport of hTERT remains unclear. In this work, we demonstrate that immunophilin...

...Chrisostomos Prodromou Heat shock protein 90 (Hsp90) is a molecular chaperone that is involved in the activation of disparate client proteins. This implicates Hsp90 in diverse biological processes that require a variety of co-ordinated regulatory mechanisms to control its activity. Perhaps the most...

... about the function of the putative GHKL (gyrase, Hsp90, histidine kinase, MutL)-type ATPase domain at its N-terminus. To formally assess the structure and function of Smchd1’s ATPase domain, we have generated recombinant proteins encompassing the predicted ATPase domain and the adjacent region. Here, we...

... and threonine residues in proteins [ 2 , 3 ], was identified as a component of GR-Hsp90 complexes [ 4 , 5 ] and shown to interact with Hsp90 and Hsp70 via its tetratricopeptide repeat (TPR) domain [ 6 , 7 ]. Three TPR-containing proteins, FK506 binding protein 51 (FKBP51), FKBP52 and Ppp5/PP5 are now known...

... of the G2019S mutation in the kinase domain. Hsp90 (heat-shock protein of 90 kDa) has an increased affinity for the G2385R variant compared with WT (wild-type) LRRK2, and inhibition of the chaperone binding combined with proteasome inhibition leads to association of mutant LRRK2 with high molecular mass native...

... by the proteasome; this process was accelerated for the S714P mutant. Accelerated degradation of the S714P mutant enzyme accounted for the diminished enzyme activity of this mutant. Hsp90 (heat-shock protein 90) associated with NOS2 and modulated degradation, but was not responsible for the accentuated degradation...

...Miki OKADA; Hideaki ITOH; Takashi HATAKEYAMA; Hiroshi TOKUMITSU; Ryoji KOBAYASHI Hsp90 (heat-shock protein 90) alone can act to prevent protein aggregation and promote refolding in vitro , but in vivo it operates as a part of a multichaperone complex, which includes Hsp70 and cohort proteins. Since...

... information on receptor structural requirements for ligand binding. For the assays in vitro , the inhibitory effects of 20 metal ions were analysed on steroid-binding capacity for renal receptor cross-linked to 90-kDa heat-shock protein (hsp90) by pretreatment with dimethyl pimelimidate. Cross-linking...