Houben B, et al. Protein structure and aggregation: a marriage of necessity ruled by aggregation gatekeepers. Trends Biochem Sci 47 (3):194-205, 2022
Our recent Opinion piece in TIBS discusses that since the stability of the native and aggregated states of proteins are correlated thermodynamically (a relationship strengthened by codon usage) the folding of stable proteins requires kinetic control to avoid aggregation. This kinetic control is provided by aggregation gatekeepers that favour native folding, either on their own or by recruiting chaperones.
Read the full paper here.