Effective delivery of protein therapeutics to the central nervous system (CNS) has been
greatly restricted by the blood-brain barrier (BBB). We describe the development of a BBB …

A network of molecular chaperones is known to bind proteins (‘clients’) and balance their
folding, function and turnover. However, it is often unclear which chaperones are critical for …

Heat shock protein 70 (Hsp70) and heat shock protein 90 (Hsp90) require the help of
tetratricopeptide repeat (TPR) domain-containing cochaperones for many of their functions. Each …

Protein–protein interactions between E3 ubiquitin ligases and protein termini help shape
the proteome. These interactions are sensitive to proteolysis, which alters the ensemble of …

Heat shock protein 70 (Hsp70) is a chaperone that normally scans the proteome and initiates
the turnover of some proteins (termed clients) by linking them to the degradation pathways. …

RUVBL1 and RUVBL2 are ATPases associated with diverse cellular activities (AAAs) that form
a complex involved in a variety of cellular processes, including chromatin remodeling and …

… Affairs (VA) MVP. Electronic health record data were obtained from the VA Corporate Data
… ancestry, and who regularly received care at the VA for the 2 years before enrollment. All …

An expanded chemical space is essential for improved identification of small molecules for
emerging therapeutic targets. However, the identification of targets for novel compounds is …

The E3 ubiquitin ligase CHIP (C-terminus of Hsc70 Interacting Protein, a 70 kDa homodimer)
binds to the molecular chaperone Hsc70 (a 70 kDa monomer), and this complex is …

The constitutively expressed heat shock protein 70 kDa (Hsc70) is a major chaperone protein
responsible for maintaining proteostasis, yet how its structure translates into functional …