PERK-dependent compartmentalization of ERAD and unfolded protein response machineries during ER stress

This publication has 55 references indexed in Scilit:

• The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response
  Proceedings of the National Academy of Sciences, 2006
• The E3 Ubiquitin Ligases HRD1 and SCF^Fbs2 Recognize the Protein Moiety and Sugar Chains, Respectively, of an ER‐Associated Degradation Substrate
  Israel Journal of Chemistry, 2006
• Distinct Ubiquitin-Ligase Complexes Define Convergent Pathways for the Degradation of ER Proteins
  Cell, 2006
• The protein translocation channel binds proteasomes to the endoplasmic reticulum membrane
  The EMBO Journal, 2005
• Search and Destroy: ER Quality Control and ER-Associated Protein Degradation
  Critical Reviews in Biochemistry and Molecular Biology, 2005
• Formation of aggresome-like structures in herpes simplex virus type 2-infected cells and a potential role in virus assembly
  Experimental Cell Research, 2004
• A Striking Quality Control Subcompartment inSaccharomyces cerevisiae: The Endoplasmic Reticulum-associated Compartment
  Molecular Biology of the Cell, 2004
• An Integrated Stress Response Regulates Amino Acid Metabolism and Resistance to Oxidative Stress
  Molecular Cell, 2003
• Probing for Membrane Domains in the Endoplasmic Reticulum: Retention and Degradation of Unassembled MHC Class I Molecules
  Molecular Biology of the Cell, 2002
• The Glycoprotein gp48 of Murine Cytomegalovirus
  Journal of Biological Chemistry, 2002