Heat shock Proteins (HSPs)
... Heat shock Proteins (HSPs) Heat shock proteins (HSP) are expressed in response to various biological stresses, including heat, high pressures, and toxic compounds. It is also one of the most abundant cellular proteins found under nonstress conditions ...
... Heat shock Proteins (HSPs) Heat shock proteins (HSP) are expressed in response to various biological stresses, including heat, high pressures, and toxic compounds. It is also one of the most abundant cellular proteins found under nonstress conditions ...
Summer 2011 Proposal for UNCA Undergraduate Research
... pathways. Due to the nature of its function, G12 has the potential to promote malignant, uncontrolled cell growth and metastasis, classifying it as a proto-oncoprotein. Indeed, analysis of cDNA libraries collected from sarcoma tissue samples has implicated G12 as a strong transforming oncoprotein ...
... pathways. Due to the nature of its function, G12 has the potential to promote malignant, uncontrolled cell growth and metastasis, classifying it as a proto-oncoprotein. Indeed, analysis of cDNA libraries collected from sarcoma tissue samples has implicated G12 as a strong transforming oncoprotein ...
Structural Studies of Sgt2, a Component of the GET Pathway that
... a glutamine/methionine-rich C-terminal domain. It was recently shown that Sgt2 binds to members of distinct ATP-dependent heat-shock protein families (3), notably Hsp70 and Hsp90, which feature a highly conserved EEVD motif at their C-termini. This interaction requires the Sgt2TPR domain, and likely ...
... a glutamine/methionine-rich C-terminal domain. It was recently shown that Sgt2 binds to members of distinct ATP-dependent heat-shock protein families (3), notably Hsp70 and Hsp90, which feature a highly conserved EEVD motif at their C-termini. This interaction requires the Sgt2TPR domain, and likely ...
Structures of GRP94-Nucleotide Complexes Reveal Mechanistic
... complex three-dimensional structures into which they fold. In this way, enzyme active sites are created, protein-protein recognition surfaces are formed, and the chemistry of life is set in motion. Although in principle the precise three-dimensional structure for each protein is encoded in its linea ...
... complex three-dimensional structures into which they fold. In this way, enzyme active sites are created, protein-protein recognition surfaces are formed, and the chemistry of life is set in motion. Although in principle the precise three-dimensional structure for each protein is encoded in its linea ...
Hsp90
Hsp90 (heat shock protein 90) is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation. It also stabilizes a number of proteins required for tumor growth, which is why Hsp90 inhibitors are investigated as anti-cancer drugs.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 ""90"" comes from the fact that it weighs roughly 90 kiloDaltons. A 90 kDa protein is considered fairly large for a non-fibrous protein. 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.This protein was first isolated by extracting proteins from cells stressed by heating, dehydrating or by other means, all of which caused the cell’s proteins to begin to denature. However it was later discovered that Hsp90 also has essential functions in unstressed cells.