What is it about?
Under physical, oxidative or pathogenic stress many cells, including neurons, a variety of polynucleotide-binding proteins engage in formation of weak networks of reversible prion-like fibrils as a defense mechanism (such networks likely safeguard crucial genetic resources in the cell). For reasons that are not complete understood yet, once in a while such assemblies fail to completely dissociate after the threat has passed, and can lead to the seeds of a significant number of neuropathies including Alzheimer's, Parkinson's, ALS, Huntington's and other disorders.
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Why is it important?
Most drugs aimed at treating such neuropathies target downstream symptoms, rather than root causes. A better recognition of the fundamental causes of such disorders may finally crack the code to effective treatments and perhaps even cures.
Perspectives
Prions and related self-assembling peptides form a fascinating side-path in physiology, appreciably removed from the standard dogma of molecular biology. Only very recently have people begun to mine the wealth of supra-genetic knowledge and understanding contained in such (frequently transient) molecular actors.
Dr Gerald H Lushington
LiS Consulting
Read the Original
This page is a summary of: Neuropharmacology in Flux: Molecular Modeling Tools for Understanding Protein Conformational Shifts in Alzheimer’s Disease and Related Disorders, September 2017, Springer Science + Business Media,
DOI: 10.1007/978-1-4939-7404-7_20.
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