Molecular chaperones in protein folding and proteostasis

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The CamSol method of rational design of protein mutants with enhanced solubility. (2015, neutral): “living organisms [16–18].”
The Logic of the 26S Proteasome. (2017, positive): “Because the rapid degradation of such proteins is of clear selective advantage and is important for longevity (Hartl et al., 2011), theremustbenegativeconsequences if proteasomes always functioned with maximal efficiency, perhaps by causing excessive degradation of key proteins.”
Essential Oils in Food Preservation: Mode of Action, Synergies, and Interactions with Food Matrix Components (2012, background): “enterica upregulated production of the chaperon proteins Heat Shock Protein 60 (GroEL), and Heat Shock Protein 70 (DnaK), which are key proteins in the protection against thermal stress and misfolding of proteins (Di Pasqua et al., 2010; Hartl et al., 2011).”
Large-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 Chaperones (2015, neutral): “role in multiple proteostasis pathways [1,2].”