Pathways of chaperone-mediated protein folding in the cytosol

By J. Young, V. R. Agashe, K. Siegers, F. Hartl. Nature reviews. Molecular cell biology, 2004

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CHAPERONIN-MEDIATED PROTEIN FOLDING (2004, background): “Nucleic Acids Res, 46, D649-D655.”
Learning protein constitutive motifs from sequence data (2018, methodology): “Hsp70, together with other chaperone proteins, perform a variety of essential functions in the cell: they can assist folding and assembly of newly synthetized proteins, trigger refolding cycles of misfolded proteins, transport unfolded proteins through organelle membranes, and when necessary, delive”
SMYD2-dependent HSP90 methylation promotes cancer cell proliferation by regulating the chaperone complex formation. (2014, background): “HSP90 serves as an evolutionarily conserved molecular chaperone that assists a number of newly synthesized polypeptides and unstable folded proteins to fold correctly and prevent them misaggregating [2,25].”
Properties, Potentials, and Prospects of Antifreeze Proteins (2008, methodology): “…have also been made to solubilize heterologous proteins expressed as inclusion bodies by the use of in vitro folding methods after denaturation of inclusion bodies (for a review, see Frydman, 2001; Schlieker et al., 2002; Baneyx and Mujacic, 2004; Tan and Bardwell, 2004; Young et al., 2004).”