To maintain quality control in cells, mechanisms distinguish among improperly folded
peptides, mature and functional proteins, and proteins to be targeted for degradation. The …

Molecular chaperones are known to facilitate cellular protein folding. They bind non‐native
proteins and orchestrate the folding process in conjunction with regulatory cofactors that …

Proper folding of proteins (either newly synthesized or damaged in response to a stressful
event) occurs in a highly regulated fashion. Cytosolic chaperones such as Hsc/Hsp70 are …

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 …

How are biological structures maintained in a cellular environment that constantly threatens
protein integrity? Here we elucidate proteostasis mechanisms affecting the Z disk, a protein …

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

The BAG‐1 protein appears to inhibit cell death by binding to Bcl‐2, the Raf‐1 protein kinase,
and certain growth factor receptors, but the mechanism of inhibition remains enigmatic. …

Therapeutic efforts to restore biosynthetic processing of the cystic fibrosis transmembrane
conductance regulator lacking the F508 residue (ΔF508CFTR) are hampered by ubiquitin-…

Molecular chaperones act with folding co-chaperones to suppress protein aggregation and
refold stress damaged proteins. However, it is not clear how slowly folding or misfolded …

The effects of the human DnaJ homolog, Hsp40, on the ATPase and chaperone functions of
the constitutively expressed Hsp70 homolog, Hsc70, were analyzed. Hsp40 stimulates the …