Converging concepts of protein folding in vitro and in vivo

By U. Hartl, M. Hayer-Hartl. Nature Structural &Molecular Biology, 2009

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Quality control: ER-associated degradation: protein quality control and beyond. (2014, neutral): “Despite all the resources dedicated to protein folding, a significant fraction of newly synthesized polypeptides entering the ER fails to acquire a native conformation (Hartl and Hayer-Hartl, 2009).”
The endoplasmic reticulum: structure, function and response to cellular signaling (2015, background): “On the other hand, even with several proteins and complexes dedicated to folding proteins properly, a fraction of proteins do not achieve native and functional form and are either misfolded or aggregated [22].”
The Hsp70 chaperone machinery: J-proteins as drivers of functional specificity (2010, neutral): “b | If the J domain is tethered to a particular site in a cellular compartment, on initiation of client protein binding by HSP70–ATP (1), a high concentration of J domains is present (2), allowing efficient stimulation of ATP hydrolysis and thus client capturing by HSP70 (3).”
The plant heat stress transcription factor (Hsf) family: structure, function and evolution. (2012, background): “They are essential for maintenance and/or restoration of protein homeostasis [12–17].”