Plants respond to various stresses by triggering the expression of genes that encode
proteins involved in plant growth, fruit ripening, cellular protein homeostasis, and tolerance …

Small heat shock proteins (sHsps) constitute a diverse chaperone family that shares the α-
crystallin domain, which is flanked by variable, disordered N-and C-terminal extensions …

Small heat shock proteins (sHSPs) are present in all kingdoms of life and play fundamental
roles in cell biology. sHSPs are key components of the cellular protein quality control …

Small heat shock proteins (sH sps) are an evolutionary conserved class of ATP‐
independent chaperones that protect cells against proteotoxic stress. sH sps form …

To be able to perform their biological function, a protein needs to be correctly folded into its
three dimensional structure. The protein folding process is spontaneous and does not …

Large-scale proteomic analyses in Escherichia coli have documented the composition and
physical relationships of multiprotein complexes, but not their functional organization into …

Metabolic traits are molecular phenotypes that can drive clinical phenotypes and may
predict disease progression. Here, we report results from a metabolome-and genome-wide …

Aggregation is an inherent characteristic of proteins. Risk management strategies to reduce
aggregation are critical for cells to survive upon stresses that induce aggregation. Cells cope …

Inclusion body–associated proteins IbpA and IbpB of MW 16 KDa are the two small heat-
shock proteins (sHSPs) of Escherichia coli, and they have only holding, but not folding …

Stress is an inevitable part of life. An organism is exposed to multiple stresses and
overcomes their negative consequences throughout its entire existence. A correlation was …