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Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone which is essential in eukaryotes. It is required for the activation and stabilization of a wide variety of client proteins and many of them are involved in important cellular pathways. Since Hsp90 affects numerous physiological processes such as signal transduction, intracellular transport, and protein degradation, it became an interesting target for cancer therapy. Structurally, Hsp90 is a flexible dimeric protein composed of three different domains which adopt structurally distinct conformations. ATP binding triggers directionality in these conformational changes and leads to a more compact state. To achieve its function, Hsp90 works together with a large group of cofactors, termed co-chaperones. Co-chaperones form defined binary or ternary complexes with Hsp90, which facilitate the maturation of client proteins. In addition, posttranslational modifications of Hsp90, such as phosphorylation and acetylation, provide another level of regulation. They influence the conformational cycle, co-chaperone interaction, and inter-domain communications. In this review, we discuss the recent progress made in understanding the Hsp90 machinery.

This chapter contains sections titled: What i s Community Psychology? CP Paradigm: The Integration of Theory, Research, and Action Social Change Characteristics of CP Roles and Skills of CP The Context of CP ‐ Social Issues and Trends References

This chapter contains sections titled: Introduction Social Referencing Reading Intentions Quarantine Pretense Play as Symbolic Pretend Play and Social Cognition Pretense and Cognitive Neuroscience Conclusion References

This chapter contains sections titled: Narrative

The need for enantiopure compounds Determination of enantiomeric purity Chirality and thermodynamic principles of asymmetric induction Methods for obtaining chiral compounds References