Sep 18, 2013 · 5:30 PM
Come join IdeaLab, the global DIYbio Journal Club. Every other week, we will be discussing in detail a recent paper from the bioscience literature, with online participants from Counter Culture Labs, BioCurious, Genspace, and other DIYbio groups.
Abstract for the paper we will be discussing today:
Self-propagation of pathogenic protein aggregates in neurodegenerative diseases.
Jucker M, Walker LC. Nature. 2013 Sep 5;[masked]):45-51. doi:[masked]/nature12481.
For several decades scientists have speculated that the key to understanding age-related neurodegenerative disorders may be found in the unusual biology of the prion diseases. Recently, owing largely to the advent of new disease models, this hypothesis has gained experimental momentum. In a remarkable variety of diseases, specific proteins have been found to misfold and aggregate into seeds that structurally corrupt like proteins, causing them to aggregate and form pathogenic assemblies ranging from small oligomers to large masses of amyloid. Proteinaceous seeds can therefore serve as self-propagating agents for the instigation and progression of disease. Alzheimer's disease and other cerebral proteopathies seem to arise from the de novo misfolding and sustained corruption of endogenous proteins, whereas prion diseases can also be infectious in origin. However, the outcome in all cases is the functional compromise of the nervous system, because the aggregated proteins gain a toxic function and/or lose their normal function. As a unifying pathogenic principle, the prion paradigm suggests broadly relevant therapeutic directions for a large class of currently intractable diseases.
Our own Ryan Bethencourt will be leading the discussion and will be the primary contact if you have any questions.
If you would like to participate online instead of joining us in person, please sign up for a zoom.us account in advance.