… Extracellular stimuli perturbing redox balance result in rapid phosphorylation, ubiquitination
and proteolytic degradation of IκBs. This process releases NF-κB and enables it to …

… fate of proteins are molecular chaperones, the … of molecular chaperones found in all domains
of life. They prevent irreversible aggregation of unfolded proteins and maintain proteostasis …

… by cytosolic molecular chaperones Hsp70 and Hsp90. Tom70 recognizes both chaperones
and internal targeting sequences within preproteins. A set of transfer chaperones, including …

… proteostasis network, ER-located proteins regulate folding and quality control through the
activity of multiple chaperones… , thus preventing abnormal protein aggregation and resultant …

… are frequently accompanied by deregulation of protein homeostasis (proteostasis) (Figure
1)… to the mitochondrial matrix lead to defects in proteostasis and activate a signaling pathway [ …

… Here, over 2,000 chaperones, including heat shock proteins, and degradative molecules
make up the proteostasis network (PN), which guides protein synthesis, folding, conformational …

… Sustaining neuronal proteostasis during the course of our life is a central aspect required
for brain function. The dynamic nature of synaptic composition and abundance is a requisite to …

… during spermatogenesis, molecular chaperones constitute a key component of the proteostasis
… (such as nutrient deprivation, proteostasis defects and redox imbalance) and leads to a …

… and hydrophobic regions of non-native proteins with high affinity, molecular chaperones
have a key function in cellular PQC and proteostasis (Hartl and Hayer-Hartl, 2002; Hartl et al., …

… and translational regulation [76]. The UPR upregulates the expression of molecular
chaperones and folding enzymes localized in the ER to increase the capacity of the protein-folding …