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 …

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 …

Recent proteogenomic studies revealed extensive translation outside of annotated protein
coding regions, such as non-coding RNAs and untranslated regions of mRNAs. This non …

Bcl-2 family proteins serve as critical regulators of pathways involved in apoptosis, acting to
either inhibit or promote cell death. Altered expression of these proteins occurs commonly in …

Heat Shock Protein 70 kDa (Hsp70) family molecular chaperones play critical roles in
protein folding and trafficking in all eukaryotic cells. The mechanisms by which Hsp70 family …

The BAG-1 protein modulates the chaperone activity of Hsc70 and Hsp70 in the mammalian
cytosol and nucleus. Remarkably, BAG-1 possesses a ubiquitin-like domain at its amino …

Regulated changes in protein conformation can have profound effects on protein function,
although routine laboratory methods often fail to detect them. The recently discovered BAG …

Background: Molecular chaperones recognize nonnative proteins and orchestrate cellular
folding processes in conjunction with regulatory cofactors. However, not every attempt to fold …

Bcl-2-associated athanogene (BAG)-family proteins are BAG domain-containing proteins
that interact with the heat shock proteins 70, both constitutive Hsc70 and inducible Hsp70 …

Initial apoptosis research characterized this form of cell death based on distinct nuclear
morphology that was subsequently shown to be associated with the appearance of …