Pharmacoperones: a new therapeutic approach for diseases caused by misfolded G protein-coupled receptors. Recent Pat Endocr Metab Immune Drug Discov. (2011); 5: 13-24.Ulloa-Aguirre A, Conn PM (2011) Pharmacoperones: a new therapeutic approach for diseases caused by misfolded G protein-coupled...
Prion diseases are a group of progressive neurodegenerative diseases that are caused by misfolded proteins, referred to as prions. During post-translational modification of proteins, prions act as a folding template, converting proteins into infectious prion form. The best-known human prion disease is...
As incredible as it might sound, these diseases are caused not bybacteriaor viruses but rather by something conceptually quite simple: incorrectproteinfolding. Introductory biology courses teach us that proteins are essential for theorganismbecause they participate in virtually every process within thecell...
By this mechanism, migrating complexes can transmit a disorder to distant regions of the brain and promote gradually transmitting degenerative processes. Molecular chaperones can counteract the toxicity of misfolded proteins. In this review, we discuss recent data on the possible cytoprotective functions ...
Johnston J. A., Ward C. L., and Kopito R. R. (1998) Aggresomes: a cellular response to misfolded proteins.J. Cell Biol.143, 1883–1898. ArticlePubMedCASGoogle Scholar Jousse C., Bruhat A., Carraro V., et al. (2001) Inhibition of CHOP translation by a peptide encoded by an open...
et al. IL-10 controls early microglial phenotypes and disease onset in ALS caused by misfolded superoxide dismutase 1. J. Neurosci. 36, 1031–1048 (2016). CAS PubMed PubMed Central Google Scholar Beers, D. R. et al. Neuroinflammation modulates distinct regional and temporal clinical ...
Within the mitochondrial matrix, ATP-dependent proteases, such as mitochondrial Lon peptidase 1 (LONP1) and caseinolytic protease X and protease P complex (CLPXP), maintain mitochondrial homeostasis by eliminating damaged or misfolded proteins [20]. Additionally, mitochondria can participate in the re...
Prion diseases, including bovine spongiform encephalopathy (mad cow) and Creutzfeldt鈥揓akob disease in humans, are caused by a misfolded protein in the brain that has the ability to convert the normal protein to the misfolded form. Prions in the brain lead to the formation of aggregates of ...
Proteins that form the unique fibril structures that underlie the pathological presentation of a disease. Conformational strains Forms of a protein with distinct fibril structures. Prion diseases A family of neurodegenerative disorders caused by misfolded prion protein that affect both humans and animals....
Mammalian cells remove misfolded proteins using various proteolytic systems, including the ubiquitin (Ub)-proteasome system (UPS), chaperone mediated autophagy (CMA) and macroautophagy. The majority of misfolded proteins are degraded by the UPS, in which