Efficient folding of many newly synthesized proteins depends on assistance from molecular
chaperones, which serve to prevent protein misfolding and aggregation in the crowded …

Most proteins must fold into precise three-dimensional conformations to fulfill their biological
functions. Here we review recent concepts emerging from studies of protein folding in vitro …

HSPA8/HSC70 protein is a fascinating chaperone protein. It represents a constitutively
expressed, cognate protein of the HSP70 family, which is central in many cellular processes …

Biological macromolecules have evolved over billions of years to function inside cells, so it
is not surprising that researchers studying the properties of such molecules, either in extracts …

▪ Abstract Recent years have witnessed dramatic advances in our understanding of how
newly translated proteins fold in the cell and the contribution of molecular chaperones to this …

Proteins generally must fold into precise three-dimensional conformations to fulfill their
biological functions. In the cell, this fundamental process is aided by molecular chaperones …

Molecular chaperones are a functionally defined set of proteins which assist the structure
formation of proteins in vivo. Without certain protective mechanisms, such as binding …

Folding within the crowded cellular milieu often requires assistance from molecular
chaperones that prevent inappropriate interactions leading to aggregation and toxicity. The …

MHC class I molecules bind short peptides and present them to CD8+ T cells. Contrary to
textbook descriptions, the generation of MHC class-I-associated peptides from endogenous …

In eukaryotic cells a molecular chaperone network associates with translating ribosomes,
assisting the maturation of emerging nascent polypeptides. Hsp70 is perhaps the major …