Browse the search results

Lab-evolved 'super Spy' chaperones show enhanced flexibility, which allows them to bind to and stabilize proteins more effectively than natural chaperones.

Food overconsumption impairs cellular protein folding through a novel aging-related signaling pathway.

Chaperoning defects in axonemal dynein subunits trigger proteostatic clearance of dynein motors opening up the possibility of trialling proteostasis modulators to treat the motile ciliopathy primary ciliary dyskinesia (PCD).

A novel co-translational mechanism continuously adjusts the expression levels of ribosomal proteins Rpl3 and Rpl4 to their consumption during ribosome synthesis by regulating the abundance of their mRNAs.

ATP consumption enables chaperones to exploit the different kinetic properties of their conformational states to exhibit a non-equilibrium affinity for their substrates that is orders of magnitude higher than its equilibrium value.

Protein biosynthesis and protein quality control jointly determine protein production costs.

Various genotoxic stresses trigger widespread aggregation of abundant, liquid-liquid phase separation-prone proteins, suggesting that genotoxic stress is a potential driver of disease-associated protein aggregation.

Hsp70 chaperone provides Hsp104 with high efficiency in disaggregation and specificity towards aggregated substrates at the, otherwise limiting, cellular concentrations of adenine nucleotides.

A widespread family of chaperones functions to stabilize membrane protein effectors by mimicking transmembrane helical environments and promotes effector export by the bacterial type VI secretion system.

Biochemical and cellular analyses reveal the mechanism by which EROS regulates NOX2 and P2X7 abundance in mouse and human.