Molecular chaperones were originally discovered as heat shock-induced proteins that
facilitate proper folding of proteins with non-native conformations. While the function of …

Cells regularly synthesize new proteins to replace old and abnormal proteins for normal
cellular functions. Two significant protein quality control pathways inside the cellular milieu …

Major neurodegenerative disorders are characterized by the formation of misfolded proteins
aggregates inside or outside the neuronal cells. Previous studies suggest that aberrant …

Accumulation of misfolded proteins compromises overall cellular health and fitness. The
failure to remove misfolded proteins is a critical reason for their unwanted aggregation in …

Human telomerase reverse transcriptase (hTERT) is the catalytic subunit of telomerase, an
RNA‐dependent DNA polymerase that elongates telomeric DNA. hTERT displays several …

Impairment in the elimination of misfolded proteins generates cellular toxicity and leads to
various late-onset neurodegenerative diseases. However, the mechanisms by which cells …

The polyubiquitin gene Ubc is upregulated under oxidative stress induced by arsenite [As
(III)]. However, the detailed mechanism of Ubc upregulation and the exact role of ubiquitin …

A common feature in most neurodegenerative diseases and aging is the progressive
accumulation of damaged proteins. Proteins are essential for all crucial biological functions …

An inducible protein-knockdown system is highly effective for investigating the functions of
proteins and mechanisms essential for the survival and growth of organisms. However, this …

The protein quality control (QC) system protects cells against cellular toxicity induced by
misfolded proteins and maintains overall cellular fitness. Inefficient clearance of or failure to …