All Stories

  1. Proteasomal and lysosomal clearance of misfolded proteins from the endoplasmic reticulum
  2. The reductase TMX1 contributes to ERAD by preferentially acting on membrane-associated folding-defective polypeptides
  3. ER ‐to‐lysosome‐associated degradation of proteasome‐resistant ATZ polymers occurs via receptor‐mediated vesicular transport
  4. Three branches to rule them all? UPR signalling in response to chemically versus misfolded proteins-induced ER stress
  5. Eat it right: ER-phagy and recovER-phagy
  6. Endoplasmic reticulum turnover
  7. Chemical stresses fail to mimic the unfolded protein response resulting from luminal load with unfolded polypeptides
  8. ER-phagy and recovER-phag: SEC62-mediated endoplasmic reticulum turnover on recovery from ER stress
  9. Five Questions (with their Answers) on ER-Associated Degradation
  10. Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)
  11. Quality control mechanisms of protein biogenesis: proteostasis dies hard
  12. Division of labor among oxidoreductases: TMX1 preferentially acts on transmembrane polypeptides
  13. The Protein-disulfide Isomerase ERp57 Regulates the Steady-state Levels of the Prion Protein
  14. Glycoprotein maturation and quality control
  15. N-linked sugar-regulated protein folding and quality control in the ER
  16. A novel UGGT1 and p97-dependent checkpoint for native ectodomains with ionizable intramembrane residue
  17. Correction for Noack et al., How Viruses Hijack the ERAD Tuning Machinery
  18. Proteostasis: Bad news and good news from the endoplasmic reticulum
  19. How Viruses Hijack the ERAD Tuning Machinery
  20. Non-Lipidated LC3 is Essential for Mouse Hepatitis Virus Infection
  21. Transgenic expression of β1 antibody in brain neurons impairs age-dependent amyloid deposition in APP23 mice
  22. UDP-glucose:glycoprotein glucosyltransferase (UGGT1) promotes substrate solubility in the endoplasmic reticulum
  23. Specificity and Regulation of the Endoplasmic Reticulum-Associated Degradation Machinery
  24. Unconventional roles of nonlipidated LC3 in ERAD tuning and coronavirus infection
  25. Flagging and docking: dual roles for N-glycans in protein quality control and cellular proteostasis
  26. Chronic Delivery of Antibody Fragments Using Immunoisolated Cell Implants as a Passive Vaccination Tool
  27. ERAD and ERAD tuning: disposal of cargo and of ERAD regulators from the mammalian ER
  28. Malectin Participates in a Backup Glycoprotein Quality Control Pathway in the Mammalian ER
  29. Autophagy-independent LC3 function in vesicular traffic
  30. Cyclosporine A-Sensitive, Cyclophilin B-Dependent Endoplasmic Reticulum-Associated Degradation
  31. Coronaviruses Hijack the LC3-I-Positive EDEMosomes, ER-Derived Vesicles Exporting Short-Lived ERAD Regulators, for Replication
  32. N-glycan structures: recognition and processing in the ER
  33. Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LSsubstrates
  34. Consequences of Individual N-glycan Deletions and of Proteasomal Inhibition on Secretion of Active BACE
  35. Segregation and rapid turnover of EDEM1 by an autophagy-like mechanism modulates standard ERAD and folding activities
  36. A Dual Task for the Xbp1-responsive OS-9 Variants in the Mammalian Endoplasmic Reticulum
  37. The Endoplasmic Reticulum: Crossroads for Newly Synthesized Polypeptide Chains
  38. In and Out of the ER: Protein Folding, Quality Control, Degradation, and Related Human Diseases
  39. Substrate-Specific Requirements for UGT1-Dependent Release from Calnexin
  40. N-glycan structure dictates extension of protein folding or onset of disposal
  41. Glycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding-defective glycoproteins
  42. N-glycan processing in ER quality control
  43. Microbiology: Death of a chaperone
  44. N-linked glycan recognition and processing: the molecular basis of endoplasmic reticulum quality control
  45. Consequences of ERp57 Deletion on Oxidative Folding of Obligate and Facultative Clients of the Calnexin Cycle
  46. The glycan code of the endoplasmic reticulum: asparagine-linked carbohydrates as protein maturation and quality-control tags
  47. The Use of Calnexin and Calreticulin by Cellular and Viral Glycoproteins
  48. Degradation of Trafficking-defective Long QT Syndrome Type II Mutant Channels by the Ubiquitin-Proteasome Pathway
  49. Analyzing folding and degradation of metabolically labelled polypeptides by conventional and diagonal sodium dodecyl sulfate-polyacrylamide gel electrophoresis
  50. A Novel Stress-induced EDEM Variant Regulating Endoplasmic Reticulum-associated Glycoprotein Degradation
  51. EDEM Contributes to Maintenance of Protein Folding Efficiency and Secretory Capacity
  52. Contrasting Functions of Calreticulin and Calnexin in Glycoprotein Folding and ER Quality Control
  53. Role of EDEM in the Release of Misfolded Glycoproteins from the Calnexin Cycle
  54. Early Postnatal Death and Motor Disorders in Mice Congenitally Deficient in Calnexin Expression
  55. The disulphide bonds in the catalytic domain of BACE are critical but not essential for amyloid precursor protein processing activity
  56. [4] Analyzing cotranslational protein folding and disulfide formation by diagonal sodium dodecyl sulfate-polyacrylamide gel electrophoresis
  57. Folding of viral glycoproteins in the endoplasmic reticulum
  58. Chaperone Selection During Glycoprotein Translocation into the Endoplasmic Reticulum
  59. Setting the Standards: Quality Control in the Secretory Pathway
  60. Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
  61. The Helicobacter pylori neutrophil-activating protein is an iron-binding protein with dodecameric structure
  62. Calpain: A Protease in Search of a Function?
  63. The Acid Activation ofHelicobacter pyloriToxin VacA: Structural and Membrane Binding Studies
  64. Calpain: A Protease in Search of a Function?
  65. Selective Inhibition of Ii-dependent Antigen Presentation byHelicobacter pyloriToxin VacA
  66. Calpain: A Cytosolic Proteinase Active at the Membranes
  67. Purification of μ-Calpain by a Novel Affinity Chromatography Approach. NEW INSIGHTS INTO THE MECHANISM OF THE INTERACTION OF THE PROTEASE WITH TARGETS
  68. PEST Sequences Do Not Influence Substrate Susceptibility to Calpain Proteolysis