Small heat shock proteins (sHsps) are a ubiquitous and ancient family of ATP-independent
molecular chaperones. A key characteristic of sHsps is that they exist in ensembles of iso …

Small heat shock proteins (sHsps) are virtually ubiquitous molecular chaperones that can
prevent the irreversible aggregation of denaturing proteins. sHsps complex with a variety of …

The protein quality control (PQC) system maintains protein homeostasis by counteracting
the accumulation of misfolded protein conformers. Substrate degradation and refolding …

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 (sHsps) are a diverse family of intra-cellular molecular chaperone
proteins that play a critical role in mitigating and preventing protein aggregation under stress …

Small heat-shock proteins, including αB-crystallin (αB), play an important part in protein
homeostasis, because their ATP-independent chaperone activity inhibits uncontrolled …

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

Infectious diseases are a major threat to global human health, yet prophylactic treatment
options can be limited, as safe and efficacious vaccines exist only for a fraction of all …

We present a perspective of our view of the application of cryoelectron microscopy (cryo-EM)
to structure-based drug design (SBDD). We discuss the basic needs and requirements for …