Recent Decisions

Comments on recent decisions by Walter B. Bieschke, Thomas Broden, John C. Castelli, Edward G. Coleman, Louis F. DiGiovanni, John L. Globensky, John H. O\u27Hara, L. G. Sculthorp, and Joseph V. Wilcox

The disruption of proteostasis in neurodegenerative diseases

Cells count on surveillance systems to monitor and protect the cellular proteome which, besides being highly heterogeneous, is constantly being challenged by intrinsic and environmental factors. In this context, the proteostasis network (PN) is essential to achieve a stable and functional proteome. Disruption of the PN is associated with aging and can lead to and/or potentiate the occurrence of many neurodegenerative diseases (ND). This not only emphasizes the importance of the PN in health span and aging but also how its modulation can be a potential target for intervention and treatment of human diseases.info:eu-repo/semantics/publishedVersio

Recent Decisions

Comments on recent decisions by Walter B. Bieschke, Thomas Broden, John C. Castelli, Edward G. Coleman, Louis F. DiGiovanni, John L. Globensky, John H. O\u27Hara, L. G. Sculthorp, and Joseph V. Wilcox

Recent Decisions

Comments on recent decisions by Walter B. Bieschke, Thomas Broden, John C. Castelli, Edward G. Coleman, Louis F. DiGiovanni, John L. Globensky, John H. O\u27Hara, L. G. Sculthorp, and Joseph V. Wilcox

Small Molecule Activators of the Heat Shock Response: Chemical Properties, Molecular Targets, and Therapeutic Promise

All cells have developed various mechanisms to respond and adapt to a variety of environmental challenges, including stresses that damage cellular proteins. One such response, the heat shock response (HSR), leads to the transcriptional activation of a family of molecular chaperone proteins that promote proper folding or clearance of damaged proteins within the cytosol. In addition to its role in protection against acute insults, the HSR also regulates lifespan and protects against protein misfolding that is associated with degenerative diseases of aging. As a result, identifying pharmacological regulators of the HSR has become an active area of research in recent years. Here, we review progress made in identifying small molecule activators of the HSR, what cellular targets these compounds interact with to drive response activation, and how such molecules may ultimately be employed to delay or reverse protein misfolding events that contribute to a number of diseases. © 2012 American Chemical Society