Folding proteins in fatal ways

By D. Selkoe. Nature, 2003

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How researchers see this paper

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Endoplasmic Reticulum Stress and Oxidative Stress: A Vicious Cycle or a Double-Edged Sword? (2007, neutral): “Oxidative stress and protein misfolding play critical roles in the pathogenesis of these neurodegenerative diseases (33) that are characterized by fibrillar aggregates composed of misfolded proteins (124).”
Mechanisms of diabetic complications. (2013, background): “These dysfunctional proteins are often unable to perform their normal intracellular functions and may not be able to be secreted from cells to complete their extracellular functions (529).”
Pathways of chaperone-mediated protein folding in the cytosol (2004, background): “Molecular chaperones are a crucial, natural cellular defence against such toxicit”
Amyloid formation by globular proteins under native conditions. (2009, background): “131" language="eng" publish="issue" relation="no"> A wide range of human pathologies are associated with the conversion of polypeptide chains from their soluble states into well-organized fibrillar aggregates having extensive β-sheet structur”
Deep Learning and Its Applications in Biomedicine (2018, background): “The correct 3D structure of a protein is crucial to its function, and improper structures could lead to a wide range of diseases [166–168].”