Structure and in vivo function of Hsp90. Pearl LH,Prodromou C. Current Opinion . 2000Pearl,L.H. and Prodromou,C. (2000) Structure and in vivo function of Hsp90. Curr. Opin. Struct. Biol. 10, 46±51.Pearl LH, Pro
Hsp90 can suppress protein aggregation in vitro, independent of ATP [7], [8]. In vivo, however, ATPase activity is essential for the Hsp90 working cycle hence cell viability. Mutant Hsp90s with either faster or slower ATPase rate result in temperature-sensitive growth phenotypes and they are...
Hsp90 is a highly abundant and ubiquitous molecular chaperone which plays an essential role in many cellular processes including cell cycle control, cell survival, hormone and other signalling pathways. It is important for the cell’s response to stress
et al. Reduced levels of hsp90 compromise steroid receptor action in vivo. Nature 348, 166–168 (1990). Article ADS CAS PubMed Google Scholar Pratt, W. B. & Toft, D. O. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocrine Rev. 18, 306–360 (...
The use of yeast as a model system for cellular and genetic studies on the role of hsp90 in the activities of steroid receptors and pp60v-src has been, and will continue to be, of great value. In other cells, the use of the benzoquinone ansamycin inhibitors will continue to assist in...
The Hsp90 family of proteins consist of four isoforms. Hsp90β is constitutively expressed in the cytoplasm, Hsp90α is expressed in the cytosol in response to cellular stress, Grp94 resides in the endoplasmic reticulum, and Trap-1 is localized to the mitochondria1,2,3. Together, these molec...
scaffolding protein: Structure and function David R Adams1, Dorit Ron2 and Patrick A Kiely3* Abstract The Receptor for Activated C Kinase 1 (RACK1) is a member of the tryptophan-aspartate repeat (WD-repeat) family of proteins and shares significant homology to the b subunit of G-proteins ...
Mitochondria are dynamic organelles displaying considerable structural complexity and diversity in terms of the folding of their inner membrane in particular. The elaborate topology of the inner membrane, which provides sites for assembly of OXPHOS compl
2. The structure of eukaryotic Photosystem I 3. The eukaryotic light-harvesting antenna associated with PSI 4. Electron transfer between the donor and acceptor side of PSI and its soluble electron transfer carrier proteins 5. Structure and function of PSI in cyclic electron transfer Acknowledgments ...
Thus the aggregation control in the HET-s/S system is a little more complex in that the two “isoforms” (95% identical) have very different aggregation propensities. HET-S does not aggregate in vivo whereas HET-s spontaneously forms aggregates in vivo and their in vitro behavior is ...