Small heat shock proteins (sHSPs) are an ubiquitous protein family found in archaea,
bacteria and eukaryotes. In plants, as in other organisms, sHSPs are upregulated by stress …

Mass spectrometry is a central technology in the life sciences, providing our most
comprehensive account of the molecular inventory of the cell. In parallel with developments …

Misfolding, aggregation, and aberrant accumulation of proteins are central components in
the progression of neurodegenerative disease. Cellular molecular chaperone systems …

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 …

Aberrant accumulation of misfolded proteins into amyloid deposits is a hallmark in many age-
related neurodegenerative diseases, including Alzheimer's disease (AD), Parkinson's …

Small heat shock proteins (sHSPs) have been thought to function as chaperones, protecting
their targets from denaturation and aggregation when organisms are subjected to various …

Small heat shock proteins (sHsps) bind unfolding proteins, thereby playing a pivotal role in
the maintenance of proteostasis in virtually all living organisms. Structural elucidation of …

Stressful environments often lead to protein unfolding and the formation of cytotoxic
aggregates that can compromise cell survival. The molecular chaperone heat shock protein …

Skeletal muscle and the nervous system depend on efficient protein quality control, and they
express chaperones and cochaperones at high levels to maintain protein homeostasis …

Proteins are tiny models of biological complexity: specific interactions among their many
amino acids cause proteins to fold into elaborate structures, assemble with other proteins …