Cells respond to protein-damaging (proteotoxic) stress by activation of the Heat Shock
Response (HSR). The HSR provides cells with an enhanced ability to endure proteotoxic …

Upon stress challenges, proteins/RNAs undergo liquid–liquid phase separation (LLPS) to
fine-tune cell physiology and metabolism to help cells adapt to adverse environments. The …

Research into crop yield and resilience has underpinned global food security, evident in
yields tripling in the past 5 decades. The challenges that global agriculture now faces are …

Cells respond to stress by blocking translation, rewiring metabolism and forming transient
messenger ribonucleoprotein assemblies called stress granules (SGs). After stress release …

While cellular proteins were initially thought to be stable, research over the last decades has
firmly established that intracellular protein degradation is an active and highly regulated …

Stress granules (SGs) are among the most studied membraneless organelles that form upon
heat stress (HS) to sequester unfolded, misfolded, or aggregated protein, supporting protein …

The Bcl-2-associated athanogene (BAG) family, a group of co-chaperones that share
conservative domains in flora and fauna, is involved in plant growth, development, and …

Upon acute heat stress (HS), overall mRNA transcription, processing, and export are
inhibited, leading to cell growth arrest. However, how cells turn off mRNA metabolism is not …

Proper homeostasis of the proteome, referred to as proteostasis, is maintained by
chaperone-dependent refolding of misfolded proteins and by protein degradation via the …

J-domain proteins (JDPs) are critical components of the cellular protein quality control
machinery, playing crucial roles in preventing the formation and, solubilization of cytotoxic …