Abstract Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that
facilitates the maturation of a wide range of proteins (known as clients). Clients are enriched …

Conserved families of molecular chaperones assist protein folding in the cell. Here we
review the conceptual advances on three major folding routes:(i) spontaneous, chaperone …

Parkinson's disease is the second most common neurodegenerative disorder. Although the
pathogenesis of Parkinson's disease is not entirely clear, the aberrant aggregation of α …

Between the 1960s and 1980s, most life scientists focused their attention on studies of
nucleic acids and the translation of the coded information. Protein degradation was a …

The ultimate mechanism that cells use to ensure the quality of intracellular proteins is the
selective destruction of misfolded or damaged polypeptides. In eukaryotic cells, the large …

Ubiquitin is the founding member of a family of structurally conserved proteins that regulate
a host of processes in eukaryotic cells. Ubiquitin and its relatives carry out their functions …

Each protein must be synthesized with the correct amino acid sequence, folded into its
native structure, and transported to a relevant subcellular location and protein complex. If …

Proteostasis, the controlled balance of protein synthesis, folding, assembly, trafficking and
degradation, is a paramount necessity for cell homeostasis. Impaired proteostasis is a …

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 …

Abstract Heat shock protein 90 (Hsp90) is a molecular chaperone essential for activating
many signaling proteins in the eukaryotic cell. Biochemical and structural analysis of Hsp90 …