The heat shock proteins (HSPs) are ubiquitous and conserved protein families in both
prokaryotic and eukaryotic organisms, and they maintain cellular proteostasis and protect …

The 70-kDa heat shock proteins (Hsp70s) are ubiquitous molecular chaperones that act in a
large variety of cellular protein folding and remodelling processes. They function virtually at …

Hsp70 chaperones are central hubs of the protein quality control network and collaborate
with co-chaperones having a J-domain (an∼ 70-residue–long helical hairpin with a flexible …

Hsp70 proteins are central components of the cellular network of molecular chaperones and
folding catalysts. They assist a large variety of protein folding processes in the cell by …

▪ Abstract Iron-sulfur [Fe-S] clusters are ubiquitous and evolutionary ancient prosthetic
groups that are required to sustain fundamental life processes. Owing to their remarkable …

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 …

The role of cytosolic factors in protein targeting to mitochondria is poorly understood. Here,
we show that in mammals, the cytosolic chaperones Hsp90 and Hsp70 dock onto a …

Hepadnaviruses, including human hepatitis B virus (HBV), replicate through reverse
transcription of an RNA intermediate, the pregenomic RNA (pgRNA). Despite this kinship to …

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 …

Molecular chaperones assist folding processes and conformational changes in many
proteins. In order to do so, they progress through complex conformational cycles …