Human OS-9, a Lectin Required for Glycoprotein Endoplasmic Reticulum-associated Degradation, Recognizes Mannose-trimmed N-Glycans

This publication has 38 references indexed in Scilit:

• SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins
  Proceedings of the National Academy of Sciences, 2008
• Human XTP3-B Forms an Endoplasmic Reticulum Quality Control Scaffold with the HRD1-SEL1L Ubiquitin Ligase Complex and BiP
  Journal of Biological Chemistry, 2008
• Getting In and Out from Calnexin/Calreticulin Cycles
  Journal of Biological Chemistry, 2008
• The Recognition and Retrotranslocation of Misfolded Proteins from the Endoplasmic Reticulum
  Traffic, 2008
• OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1–SEL1L ubiquitin ligase complex for ERAD
  Nature Cell Biology, 2008
• Protein quality control in the early secretory pathway
  The EMBO Journal, 2008
• Endoplasmic Reticulum (ER) Mannosidase I Is Compartmentalized and Required for N-Glycan Trimming to Man_5–6GlcNAc₂ in Glycoprotein ER-associated Degradation
  Molecular Biology of the Cell, 2008
• Stimulation of ERAD of misfolded null Hong Kong α1-antitrypsin by Golgi α1,2-mannosidases
  Biochemical and Biophysical Research Communications, 2007
• SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER
  The Journal of cell biology, 2006
• Distinct Ubiquitin-Ligase Complexes Define Convergent Pathways for the Degradation of ER Proteins
  Cell, 2006