Principles of protein folding, misfolding and aggregation.

By Christopher M. Dobson. Seminars in Cell and Developmental Biology, 2004

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Inferring Stabilizing Mutations from Protein Phylogenies: Application to Influenza Hemagglutinin (2009, background): “Mutations can also be deleterious if they increase a protein’s propensity to aggregate [40–43] or interfere with its folding [44] or unfolding [16,45] kinetics—but quantifying a mutation’s impact on stability provides a partial proxy for these effects since aggregation propensity [40], folding rate ”
Endoplasmic reticulum stress signaling in disease. (2006, background): “, helices, due to the intrinsic properties of the amino acid sequence (39).”
Protein quality control in the early secretory pathway (2008, background): “Upon cotranslational translocation, nascent secretory proteins enter the crowded environment of the ER lumen and soon begin folding into more stable, lower energy, conformation(s) (Dobson, 2004).”
Islet amyloid polypeptide, islet amyloid, and diabetes mellitus. (2011, background): “Many small peptides and proteins are able to create fibrils in vitro with amyloid-like properties (86, 310).”