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Titlebook: Small Stress Proteins; André-Patrick Arrigo,W. E. G. Müller Book 2002 Springer-Verlag Berlin Heidelberg 2002 Chaperone.aging.apoptosis.bio

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Chaperone Function of sHsps,α-crystallin. How these different functions can be explained by a common mechanism is unclear at the present state of investigations. However, as most of the observed phenomena involve non-native protein, the repeatedly reported chaperone properties of sHsps seem to be of key importance for understanding their function.
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The Developmental Expression of Small HSP,n of nascent ones - and more specific functions, such as the activity of HSP/HSC70 in uncoating clathrin cages. At least two of the functions thus far demonstrated for small HSP (sHSP)—protection against apoptosis and modulation of the cytoskeletal structure—are amply sufficient to explain a developmental role of sHSP.
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Book 2002, from prokaryotes to humans. It provides an overview of the diversity and complex evolutionary history of sHsps and describes their function and expression in different eukaryote models. Additional chapters discuss the role of sHsps in pathological conditions and gene therapy approaches towards a c
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Evolution and Diversity of Prokaryotic Small Heat Shock Proteins,ultichaperone networks is a great challenge (.). Considerable information is already available on the evolution of the Hsp60 and Hsp70 families (e.g., .; .; .; .; .; .). Relatively less is known about the early evolution of the small heat shock proteins (sHsps), which are considerably more divergent
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