Results 211 to 220 of about 59,353 (250)

Preliminary investigation of heat shock protein 90 gene diversity in Echinococcus granulosus sensu lato: a potential nuclear marker for species identification. [PDF]

open access: yesParasitol Res
Lamia Z   +11 more
europepmc   +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

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

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