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Prognostic Significance of Heat Shock Proteins HSP70 and HSP90 in Endometrial Carcinomas

Cancer Detection <html_ent glyph="@amp;" ascii="&amp;"/> Prevention, 1998
Heat shock proteins HSP70 and HSP90 are sex steroid receptor-associated proteins, and HSP90 expression has reportedly been correlated with sex steroid receptor status in endometrial carcinomas. HSP70 is also known to associate with several oncogene products such as p53 protein, and expression of HSP70 has been reported to be a prognostic factor in ...
K, Nanbu   +6 more
openaire   +3 more sources

Heat shock protein 90 (Hsp90) Inhibitors: An Update on Achievements, Challenges, and Future Directions.

Journal of Medicinal Chemistry, 2020
Hsp90 is one of the most important chaperones involved in regulating the maturation of more than 300 client proteins, many of which are closely associated with refractory diseases, including cancer, neurodegenerative diseases and viral infections ...
Li Li, Lei Wang, Q. You, Xiao-li Xu
semanticscholar   +1 more source

Phylogenetic Analysis of Eukaryotes Using Heat-Shock Protein Hsp90

Journal of Molecular Evolution, 2003
Most eukaryote molecular phylogenies have been based on small-subunit ribosomal RNA as its database includes the most species, but serious problems have been encountered that can make these trees misleading. More recent studies using concatenated protein sequences have increased the data per organism, reducing misleading signals from a single sequence,
Alexandra, Stechmann   +1 more
openaire   +2 more sources

Clinical, Prognostic and Therapeutic Significance of Heat Shock Proteins in Cancer.

Current Drug Targets, 2017
BACKGROUND Heat Shock Proteins (HSPs) constitute a group of proteins that play a crucial role in the process of protein folding. HSPs are also known to modulate a number of key apoptotic factors.
Jasleen Saini, P. Sharma
semanticscholar   +1 more source

Reactive Cysteines of the 90-kDa Heat Shock Protein, Hsp90

Archives of Biochemistry and Biophysics, 2000
The 90-kDa heat shock protein (Hsp90) is the most abundant molecular chaperone of the eukaryotic cytoplasm. Its cysteine groups participate in the interactions of Hsp90 with the heme-regulated eIF-2alpha kinase and molybdate, a stabilizer of Hsp90-protein complexes. In our present studies we investigated the reactivity of the sulfhydryl groups of Hsp90.
G, Nardai   +4 more
openaire   +2 more sources

Redefining the Phenotype of Heat Shock Protein 90 (Hsp90) Inhibitors

Chemistry – A European Journal, 2017
AbstractThe phenotypes produced when cells are treated with the heat shock protein 90 (Hsp90) inhibitors AUY922 or 17‐AAG (classical inhibitors) are different to those produced when cells are knocked down with Hsp90α. Pull‐down assays using classical inhibitors suggest that these molecules bind to multiple targets other than Hsp90. Classical inhibitors
Yao Wang   +2 more
openaire   +2 more sources

Chromatin Immunoprecipitation (ChIP) of Heat Shock Protein 90 (Hsp90)

2017
Chromatin immunoprecipitation followed by sequencing (ChIP-seq) is a widely used technique for genome-wide mapping of protein-DNA interactions and epigenetic marks in vivo. Recent studies have suggested an important role of heat shock protein 90 (Hsp90) at chromatin. This molecular chaperone assists other proteins to acquire their mature and functional
Yoveva, A., Sawarkar, R.
openaire   +3 more sources

Heat Shock Protein 90-antagonist Destabilizes Bcr-Abl/HSP90 Chaperone Complex

Leukemia & Lymphoma, 2002
(2002). Heat Shock Protein 90-antagonist Destabilizes Bcr-Abl/HSP90 Chaperone Complex. Leukemia & Lymphoma: Vol. 43, No. 5, pp. 961-968.
Yukimasa, Shiotsu   +2 more
openaire   +2 more sources

The glucose-regulated protein grp94 is related to heat shock protein hsp90

Journal of Molecular Biology, 1987
We report the sequence of a cDNA clone that encodes the C-terminal half of the hamster 94 X 10(3) Mr glucose-regulated protein, grp94. The amino acid sequence of this protein is about 50% homologous to Drosophila hsp83 and yeast hsp90, suggesting that grp94 and hsp90 have similar functional properties.
P K, Sorger, H R, Pelham
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Allosteric Modulators of Heat Shock Protein 90 (HSP90)

2016
Heat shock proteins (HSP) are a family of molecular chaperones that are the most conserved proteins present in both prokaryotes and eukaryotes. HSPs facilitate numerous events in cellular physiology including: protein recycling, transportation, migration, post-translational modification, and the regulation of signalling pathways.
Yen Chin Koay, Shelli McAlpine
openaire   +1 more source

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