Polypharmacology—the ability of a drug to affect more than one protein—should be studied early in the drug discovery pathway, and constantly monitored as the chemical structure is optimized in the design of the clinical ...
Biochemistry
Jun 2, 2021
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An international research team has identified a new function of Hsp90, one of the most common and studied proteins in the human body. The study has implications for the development of new drugs.
Cell & Microbiology
Sep 7, 2018
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25
Proteins do most of the work inside the human body, supporting the structure, function, regulation, and repair of organs, tissues and cells. Proteins are synthesized as extended chains of amino acids that must fold into intricate ...
Cell & Microbiology
Feb 23, 2017
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10
The protein p53 plays an essential role in the prevention of cancer by initiating the controlled death of a cell with damaged genes which is in danger to transform into a cancerous cell. The heat shock protein Hsp90, in turn, ...
Biotechnology
Sep 7, 2011
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0
Whitehead Institute researchers have determined that heat shock protein 90 (Hsp90) can create heritable traits in brewer's yeast (Saccharomyces cerevisiae) by affecting a large portion of the yeast genome. The finding has ...
Biotechnology
Dec 23, 2010
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0
The protein Hsp90 plays a significant role in the survival of cells that are exposed to stress. Researchers at the Technische Universitaet Muenchen (TUM) uncovered this protein's mode of operation some time ago - but now ...
Cell & Microbiology
Aug 23, 2010
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0
Hsp90 (heat shock protein 90) is a molecular chaperone and is one of the most abundant proteins expressed in cells. It is a member of the heat shock protein family, which is upregulated in response to stress. Hsp90 is found in bacteria and all branches of eukarya, but it is apparently absent in archaea. Whereas cytoplasmic Hsp90 is essential for viability under all conditions in eukaryotes, the bacterial homologue HtpG is dispensable under non-heat stress conditions.
Heat shock proteins, as a class, are among the most highly expressed cellular proteins across all species. As their name implies, heat shock proteins protect cells when stressed by elevated temperatures. They account for 1–2% of total protein in unstressed cells. However, when cells are heated, the fraction of heat shock proteins increases to 4–6% of cellular proteins.
Heat shock protein 90 (Hsp90) is one of the most common of the heat-related proteins. The protein is named "HSP" for obvious reasons, and the "90" comes from the fact that it weighs roughly 90 kiloDaltons. A 90 kDa protein is considered fairly large for a non-fibrous protein.
The function of Hsp90 includes assisting in protein folding, cell signaling, and tumor repression. This protein was first isolated by extracting proteins from stressed cells. These cells were stressed by heating, dehydrating or by other means, all of which caused the cell’s proteins to begin to denature. As discussed in more detail below, researchers later realized that Hsp90 has other essential functions in unstressed cells.
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