Results 181 to 190 of about 59,092 (215)

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

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

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
openaire   +2 more sources

Interaction of a Novel Chaperone PhLP2A With the Heat Shock Protein Hsp90

Journal of Cellular Biochemistry, 2016
PhLP2 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
  +5 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

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