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Scannevin, Robert H
Current opinion in chemical biology, June 2018, 2018-06-00, 20180601, Letnik: 44Journal Article
Neurodegenerative diseases can arise from a multitude of different pathological drivers, however protein misfolding appears to be a common molecular feature central to several disorders. Protein folding, and attainment of correct secondary and tertiary structure, is essential for proper protein function. Protein misfolding gives rise to structural perturbations that can result in loss of protein function or a gain of toxic function, such as through aggregation, either of which can initiate and propagate biological responses that are deleterious to cells. Several neurodegenerative diseases, such as Alzheimer’s disease, amyotrophic lateral sclerosis, Huntington’s disease and Parkinson’s disease, each have identified molecular components in which protein misfolding perturbs cellular systems that ultimately lead to cell death, and this predominately occurs in neurons. Current efforts focused on developing therapies for protein misfolding disorders have employed diverse strategies; inhibiting the production of disease-relevant proteins prone to misfolding, inhibiting the aggregation of misfolded proteins, removing and preventing spread of aggregated misfolded proteins and manipulating cellular systems to mitigate the toxic effects of misfolded proteins. Each of these strategies has yielded therapeutic agents that have transitioned from preclinical proof of concept studies into human clinical testing. These approaches and therapies are described herein.
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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