Structure and in vivo function of Hsp90. Curr Opin Struct Biol. 2000;10:46 -51.Pearl LH, Prodromou C: Structure and in vivo function of Hsp90. Curr Opin Struc Biol 2000, 10:46-51.Pearl, L.H., and Prodromou, C. (2000). Structure and in vivo function of Hsp90. Current ...
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 (...
These modulating effects of divalent cations on structure and function of Hsp90 in vitro represent a potential mechanism for regulation of Hsp90 chaperone action in vivo. 展开 关键词: Escherichia coli Heat-Shock Proteins 90 Saccharomyces cerevisiae Cations Divalent 大肠杆菌 热休克蛋白质类90 酵母菌 ...
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...
Based on these data, it is suggested that smHSPs act in vivo as a type of molecular chaperone to bind partially denatured proteins preventing irreversible protein inactivation and aggregation, and that smHSP chaperone activity contributes to the development of thermotolerance. 展开 ...
Inhibition of heat shock protein 90 function by ansamycins causes the morphological and functional differentiation of breast cancer cells 17-(Allylamino)-17-demethoxygeldanamycin (17-AAG) is an ansamycin antibiotic that binds to a conserved pocket in Hsp90 and induces the degradation of prote...
Exploration and optimisation of structure-activity relationships of new triazole-based C-terminal Hsp90 inhibitors towards in vivo anticancer potency Author links open overlay panelJaka Dernovšek a, Živa Zajec a, Goran Poje b, Dunja Urbančič a, Caterina Sturtzel c, Tjaša Goričan d...
Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA Nature, 407 (2000), pp. 703-710 10.1038/35037509 11048710 View in ScopusGoogle Scholar 11 F.A. Kadyrov, L. Dzantiev, N. Constantin, P. Modrich Endonucleolytic function of MutLa in human mismatch repair...
The crystal structure of the bacterial chaperonin GroEL at 2.8 Å. Nature 371, 578–586 (1994). Article CAS PubMed Google Scholar Valpuesta, J.M., Carrascosa, J.L. & Willison, K.R. Structure and function of the cytosolic chaperonin CCT. in Protein Folding Handbook (eds. Buchner, ...
Heat shock protein 90 inhibition in lung cancer. Hsp90 inhibitors may be synergistic with other drugs that disrupt chaperone function, including inhibitors of histone deacetylase 6 and the proteasome and ... T Shimamura,GI Shapiro - 《Journal of Thoracic Oncology》 被引量: 152发表: 2008年 Effect...