ER stress differentially regulates the stabilities of ERAD ubiquitin ligases and their substrates
- 1 January 2007
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 352 (4) , 919-924
- https://doi.org/10.1016/j.bbrc.2006.11.121
Abstract
No abstract availableKeywords
Funding Information
- National Institutes of Health (R01 GM69967)
This publication has 24 references indexed in Scilit:
- Ubiquitin ligase gp78 increases solubility and facilitates degradation of the Z variant of α-1-antitrypsinBiochemical and Biophysical Research Communications, 2006
- Human Homologs of Ubc6p Ubiquitin-conjugating Enzyme and Phosphorylation of HsUbc6e in Response to Endoplasmic Reticulum StressJournal of Biological Chemistry, 2006
- The AAA ATPase p97 links peptide N -glycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptorProceedings of the National Academy of Sciences, 2006
- ERAD: the long road to destructionNature Cell Biology, 2005
- The unfolded protein response—a stress signaling pathway of the endoplasmic reticulumJournal of Chemical Neuroanatomy, 2004
- Human HRD1 Is an E3 Ubiquitin Ligase Involved in Degradation of Proteins from the Endoplasmic ReticulumJournal of Biological Chemistry, 2004
- IRE1Developmental Cell, 2003
- Retro-translocation of proteins from the endoplasmic reticulum into the cytosolNature Reviews Molecular Cell Biology, 2002
- Endoplasmic Reticulum (ER)-associated Degradation of T Cell Receptor SubunitsJournal of Biological Chemistry, 2001
- RING Finger ProteinsCell, 2000