Titlebook: Cell Stress Proteins; Stuart K. Calderwood Book 2007 Springer-Verlag New York 2007 Antigen.Cell Stress.Chaperone.Immunity.Nucleotide.Prote

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List of symbols and abbreviations,tide to HSP70, various co-chaperones interact with the HSP70-polypeptide binary complex. Many co-chaperones in mammals contain a tetratricopeptide repeat (TPR) domain(s), and this domain recognizes the EEVD sequence at the carboxyl-terminal of cytosolic HSP70 proteins in eu-karyotes. The combination

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Introduction: Heat Shock Proteins—From , Stress Proteins to Mediators of Human Diseasery (Ashburner, 1982). At this time, however, the functions of the HSP remained mysterious and the details of regulation of . gene expression were only beginning to emerge. All that was known was that the proteins appeared to possess “homeostatic activity” and were (as they are to this day) associate

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Biology of the Heat Shock Response and Stress Conditioningprimarily about tissue-level protection. Ultimately we would like to know how these responses are deployed in humans and how these inducible defenses may be used to prevent tissue damage from disease and from surgical intervention.

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Bacterial Stress Sensorsable to sense and respond to changes in temperature (heat and cold shock), external pH (alkaline and acid shock), reactive oxygen species (hydrogen peroxide and superoxide), osmolarity (hyper- and hypoosmotic shock), and nutrient availability to mention the most important ones. These changes are oft

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HSF1 and HSP Gene Regulation that activates or enhances transcription of hsp genes in response to these stresses (.; .). Gene knockouts confirmed this expected role of HSF1 (.; .; for ., see .). As it must be capable of carrying out the same function, the single HSF present in certain organisms will also be referred to as HSF1

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Small Heat Shock Proteins in Physiological and Stress-Related Processesers, or tetramers depending on the sHsp). From X-ray and electron microscopic data, these particles have a diameter of 10–18 nm with a hollow core. The number of subunits can vary from 12 (.) to 24 (. and yeast). The quaternary structure is quite variable with polydisperse complexes in the range of

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Regulation of Hsp70 Function: Hsp40 Co-Chaperones and Nucleotide Exchange Factorsic patches on unfolded or misfolded proteins. Hsp70 function can be regulated by specific Hsp40 partners and by nucleotide exchange factors (NEFs). Hsp90 chaperones are regulated by a distinct group of proteins, and although they also associate with polypeptides, Hsp90s do not bind preferentially to