An essential cellular machinery that has been identified and studied only relatively recently
is a collective of specialized proteins, molecular chaperones, that bind nonnative states of …

Interferon-induced protein with tetratricopeptide repeats (IFIT) genes are prominent
interferon-stimulated genes (ISGs). The human IFIT gene family consists of four genes …

Heat shock and other proteotoxic stresses cause accumulation of nonnative proteins that
trigger activation of heat shock protein (Hsp) genes. A chaperone/Hsp functioning as …

The adaptor protein Hop mediates the association of the molecular chaperones Hsp70 and
Hsp90. The TPR1 domain of Hop specifically recognizes the C-terminal heptapeptide of …

▪ 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 …

Physical, genetic, and chemical-genetic interactions centered on the conserved chaperone
Hsp90 were mapped at high resolution in yeast using systematic proteomic and genomic …

Heat shock proteins (Hsps) are a family of highly homologous chaperone proteins that are
induced in response to environmental, physical and chemical stresses and that limit the …

Heat shock proteins (Hsps) have been studied for many years and there is now a large body
of evidence that demonstrates the role of Hsp upregulation in tissue and cell protection in a …

Protein accumulation is a hallmark of many neurodegenerative disorders. In Alzheimer's
disease (AD), a hyperphosphorylated form of the protein tau (p-tau) forms intracellular …

Heat shock protein 90 (Hsp90), an abundant molecular chaperone in the eukaryotic cytosol,
is involved in the folding of a set of cell regulatory proteins and in the re-folding of stress …