||p.2/16 right column top paragraph:"In unstressed human cells, the members of the chaperome network may sum up into 10 % of the total protein mass, where they act as key regulators of cellular proteostasis (primary sources). Chaperones assist the de novo folding of nascent polypeptides, serve as translocating/pulling and unfolding motors of polypeptides across cellular compartments, regulate protein activity, control vesicular trafficking, and can mediate lysosomal and proteasomal protein degradation (Cassina and Casari 2009 Dittmar et al. 1997 Eisenberg and Greene 2007 Finka and Goloubinoff 2013 Goloubinoff and De Los Rios 2007 Kalia et al. 2011 Rampelt et al. 2012 Schuermann et al. 2008)." p.9/16 right column bottom paragraph:"The chaperome network, which can accumulate even without stress into 10 % of the total protein content of human cells (primary source Finka and Goloubinoff
2013), controls protein homeostasis in cellular growth, differentiation, steady-state functions, defenses, stress management, and programmed cell death (Brehme et al. 2014 Bromberg et al. 2013 Finka et al. 2012 Kim et al. 2013 Weiss et al. 2007)."