The expression of correctly folded and functional heterologous proteins is important in many
biotechnological production processes, whether it is enzymes, biopharmaceuticals or …

Members of the HSP70/HSP110 family (HSP70s) form a central hub of the chaperone
network controlling all aspects of proteostasis in bacteria and the ATP-containing …

The endoplasmic reticulum (ER) is susceptible to wear-and-tear and proteotoxic stress,
necessitating its turnover. Here, we show that the N-degron pathway mediates ER-phagy …

Molecular chaperones control the cellular folding, assembly, unfolding, disassembly,
translocation, activation, inactivation, disaggregation, and degradation of proteins. In 1989 …

Endothelial cell (EC) metabolism is thought to be one of the driving forces for angiogenesis.
Here we report the identification of the hexosamine D-mannosamine (ManN) as an EC …

Abstract Hereditary Spastic Paraplegia (HSP) is a group of rare inherited disorders
characterized by progressive weakness and spasticity of the legs. Recent newly discovered …

Andrographolide sodium bisulfate as a kind of soluble derivative of andrographolide (AD), is
obviously known to be nephrotoxicity, but AD has not been reported clearly. Our study aimed …

The aberrant release of endoplasmic reticulum (ER) calcium leads to the disruption of
intracellular calcium homeostasis, which is associated with the occurrence of ER stress and …

Polypeptide chains experience mechanical tension while translocating through cellular
tunnels, which are subsequently folded by molecular chaperones. However, interactions …

Pathogenic variants in GFPT1, encoding a key enzyme to synthesize UDP-N-
acetylglucosamine (UDP-GlcNAc), cause congenital myasthenic syndrome (CMS). We …