Researchers at the VIB-KU Leuven Center for Microbiology and the VIB-KU Leuven Center for Brain & Disease Research revealed a mechanism involving protein aggregation that allows bacteria to enter a ...

The researchers discovered that when snowflake yeast evolved larger, tougher bodies, the expression of the chaperone protein Hsp90, which aids other proteins in acquiring their functional shape ...

Guarding these guardians, therefore, are chaperone proteins—molecules that ensure that proteins are folded properly so they ...

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.

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 ...

U. Hartl, "Chaperonin-mediated protein folding at the surface of groEL through a `molten globule'-like intermediate," Nature, 352:36-42, 1991. F.-Ulrich Hartl (Memorial Sloan Kettering Cancer Center, ...

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 ...

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 ...

The 70 kDa heat shock protein (Hsp70) chaperones control protein homeostasis in all ATP-containing cellular compartments. J-domain proteins (JDPs) coevolved with Hsp70s to trigger ATP hydrolysis and ...