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The landscape of biased agonism in aryl hydrocarbon receptor signaling: current clues and future directions. [PDF]
Front PharmacolDvořák Z, Přikryl J.
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Reactive Cysteines of the 90-kDa Heat Shock Protein, Hsp90
Archives of Biochemistry and Biophysics, 2000The 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
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Redefining the Phenotype of Heat Shock Protein 90 (Hsp90) Inhibitors
Chemistry – A European Journal, 2017AbstractThe 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
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Phylogenetic Analysis of Eukaryotes Using Heat-Shock Protein Hsp90
Journal of Molecular Evolution, 2003Most 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
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The glucose-regulated protein grp94 is related to heat shock protein hsp90
Journal of Molecular Biology, 1987We 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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Interaction of a Novel Chaperone PhLP2A With the Heat Shock Protein Hsp90
Journal of Cellular Biochemistry, 2016PhLP2 is a small cytosolic protein that belongs to the highly conserved phosducin-like family of proteins. In amniote genomes there are two PhLP2 homologs, PhLP2A and PhLP2B. It has been shown that mammalian PhLP2A modulates the CCT/TRiC chaperonin activity during folding of cytoskeletal proteins. In order to better understand the function of PhLP2A in
Łucja Krzemień-Ojak +4 more
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Heat shock protein HSP90 and its association with the cytoskeleton: a morphological study
Biochemistry and Cell Biology, 1992To investigate the cellular localization of the 90-kilodalton heat shock protein (HSP90) and its interaction with the cytoskeleton, we performed single- and double-staining immunofluorescence microscopy of cytoskeletal proteins and HSP90 in the absence and presence of cytoskeletal inhibitors. As a model, we used a human endometrial adenocarcinoma cell
Y, Fostinis +3 more
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Chromatin Immunoprecipitation (ChIP) of Heat Shock Protein 90 (Hsp90)
2017Chromatin 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.
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Prognostic Significance of Heat Shock Proteins HSP70 and HSP90 in Endometrial Carcinomas
Cancer Detection <html_ent glyph="@amp;" ascii="&"/> Prevention, 1998Heat 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
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Allosteric Modulators of Heat Shock Protein 90 (HSP90)
2016Heat 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
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