Chaperones, Endoplasmic Reticulum Stress, and the Unfolded Protein Response

  • Martin BeckermanEmail author
Part of the Biological and Medical Physics, Biomedical Engineering book series (BIOMEDICAL)

Failures to properly fold and dispose of damaged proteins are central to most if not all neurodegenerative disorders. The buildups discussed in the case of Alzheimer’s disease, of extracellular and intracellular aggregates and toxic oligomers, are not restricted to that disorder but are a common thread running through all the major neurodegenerative disorders and minor ones too.

Newly formed polypeptide chains exit the ribosome in unfolded states. The environment surrounding them upon leaving is a crowded one. Other polypeptides are leaving ribosomes from nearby sites, and cells contain large numbers of macromolecules in various states of folding and unfolding. Hydrophobic patches exposed on the not yet folded polypeptide chains promote inappropriate clumping together of chains and aberrant folded forms. Cells rely on an extensive network of molecular chaperones that assist in folding, in refolding, and in removal of aberrantly folded proteins to maintain protein homeostasis....


Unfold Protein Response Endoplasmic Reticulum Membrane Heat Shock Transcription Factor ATPase Domain Endoplasmic Reticulum Chaperone 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Copyright information

© Springer Science+Business Media, LLC 2009

Authors and Affiliations

  1. 1.Oak RidgeUSA

Personalised recommendations