Plants exposed to elevated temperatures, drought, salinity or pathogen attack rapidly upregulate a class of molecular chaperones known as heat shock proteins (HSPs). These proteins are grouped by ...

The first full-length structures of two heat shock chaperone proteins in a complex reveal the key structural region regulating their function, according to a new study from St. Jude Children's ...

HSP90 chaperone undergoes dynamic cycling process: HSP90 transits between open and closed states to promote maturation of polypeptide clients into functional proteins with the help of ATP and a ...

Researchers from The University of Texas MD Anderson Cancer Center identified a new role for heat shock protein 90 (HSP90) in cancer predisposition and treatment resistance. Their discovery, published ...

Cells must respond rapidly to heat stress by activating multiple signaling pathways that preserve proteostasis. In budding yeast, this includes induction of Hsf1 and Msn2/4-mediated transcription, ...

Molecular profiling of hepatoid adenocarcinoma and adenocarcinoma with enteroblastic differentiation. This is an ASCO Meeting Abstract from the 2024 ASCO Gastrointestinal Cancers Symposium. This ...

Heat shock protein 70 chaperones exert neuroprotective effects by preventing aggregation and regulating the proteostasis of pathological protein via its degradation. Neurodegenerative diseases such as ...

The paper E.W.J. Wallace et al., “Reversible, specific, active aggregates of endogenous proteins assemble upon heat stress,” Cell, 162:1286-98, 2015. Like cooking an egg, heating up a purified protein ...

Rising temperatures disrupt human cellular stability by impairing proteostasis, altering mitochondrial function, reprogramming gene expression, and reshaping immune responses, ultimately shifting ...

Protein activity can be precisely regulated via subtle changes in temperature using heat-sensitive switches. Underlying this capability is a novel modular design strategy developed by researchers at ...