[HTML][HTML] Identification and characterization of a novel endoplasmic reticulum (ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is induced by …
Y Shen, L Meunier, LM Hendershot - Journal of Biological Chemistry, 2002 - ASBMB
The activity of Hsp70 proteins is regulated by accessory proteins, which include members of
the DnaJ-like protein family. Characterized by the presence of a highly conserved 70-amino
acid J domain, DnaJ homologues activate the ATPase activity of Hsp70 proteins and
stabilize their interaction with unfolded substrates. DnaJ homologues have been identified in
most organelles where they are involved in nearly all aspects of protein synthesis and
folding. Within the endoplasmic reticulum (ER), DnaJ homologues have also been shown to …
the DnaJ-like protein family. Characterized by the presence of a highly conserved 70-amino
acid J domain, DnaJ homologues activate the ATPase activity of Hsp70 proteins and
stabilize their interaction with unfolded substrates. DnaJ homologues have been identified in
most organelles where they are involved in nearly all aspects of protein synthesis and
folding. Within the endoplasmic reticulum (ER), DnaJ homologues have also been shown to …