The chaperone protein DnaK can literally pull proteins out of the condensates and reactivate bacterial metabolism. "There are different states of dormancy," explains Prof. Michiels.

The functional or native conformation of non-membrane-bound proteins is typically water soluble. Chaperones will help unstable proteins fold correctly, although some proteins misfold anyway.

Previous studies have shown that mammalian cells express several hundreds of molecular chaperones, proteins that preserve or change the three-dimensional conformation of existing proteins.

as chaperones to rescue misfolded proteins is a novel concept. To set the record straight, we draw your attention to the paper where it was first reported in 1997 that specific substrates and ...

This is the metadata section. Skip to content viewer section. J-domain proteins (JDPs) are the largest family of chaperones in most organisms, but much of how they function within the network of other ...

Proteins are the end products of the decoding process that starts with the information in cellular DNA. As workhorses of the cell, proteins compose structural and motor elements in the cell, and ...

1. Chaperone-assisted Adaptor Protein Assembly (CAPA). Our group discovered the CAPA pathway while identifying endocytic regulators. Adaptor proteins (APs) are heterotetrameric complexes that function ...

To accomplish this, cells have evolved a sophisticated network of protein quality control machines consisting of molecular chaperones and energy-dependent proteases, which monitor the protein folding ...

ID GSE266025. The asymmetric expression of HSPA2 in blastomeres governs the first embryonic cell-fate decision. ID PXD052193. differentially expressed proteins (DEPs) at the blastocyst stage in the ...