Both acute proteotoxic stresses that unfold proteins and expression of disease-causing
mutant proteins that expose aggregation-prone regions can promote protein aggregation …

Protein aggregation occurs as a consequence of perturbations in protein homeostasis that
can be triggered by environmental and cellular stresses. The accumulation of protein …

The aggregation of misfolded proteins is associated with the perturbation of cellular function,
ageing and various human disorders. Mounting evidence suggests that protein aggregation …

The past 20 years have seen enormous progress in the understanding of the mechanisms
used by the enteric bacterium Escherichia coli to promote protein folding, support protein …

Biomarkers of the meat quality are of prime importance for meat industry, which has to satisfy
consumers' expectations and, for them, meat tenderness is and will remain the primary and …

Bacteria, fungi, protozoa, chromista and plants all harbor homologues of Hsp104, a AAA+
ATPase that collaborates with Hsp70 and Hsp40 to promote protein disaggregation and …

Accumulation of aggregation‐prone misfolded proteins disrupts normal cellular function and
promotes ageing and disease. Bacteria, fungi and plants counteract this by solubilizing and …

Protein quality control within the cell requires the interplay of many molecular chaperones
and proteases. When this quality control system is disrupted, polypeptides follow pathways …

The chaperone protein network controls both initial protein folding and subsequent
maintenance of proteins in the cell. Although the native structure of a protein is principally …

Unicellular and sessile organisms are particularly exposed to environmental stress such as
heat shock causing accumulation and aggregation of misfolded protein species. To …