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Dynamic retention of Ero1α and Ero1β in the endoplasmic reticulum by interactions with PDI and ERp44
Disulfide bonds are formed in the endoplasmic reticulum (ER) by sequential interchange reactions: Ero1α and Ero1β transfer oxidative equivalents to protein disulfide isomerase (PDI), which in turn… Expand
Dynamic retention of Ero1alpha and Ero1beta in the endoplasmic reticulum by interactions with PDI and ERp44.
Disulfide bonds are formed in the endoplasmic reticulum (ER) by sequential interchange reactions: Ero1alpha and Ero1beta transfer oxidative equivalents to protein disulfide isomerase (PDI), which in… Expand
SEL1L and HRD1 are involved in the degradation of unassembled secretory Ig‐µ chains
- M. Cattaneo, M. Otsu, +4 authors I. Biunno
- Biology, Medicine
- Journal of cellular physiology
- 1 June 2008
When expressed in the absence of light chains, secretory Ig‐µ chains (µs) undergo endoplasmic reticulum associated degradation (ERAD). This process involves the recognition of terminally misfolded or… Expand
Diseases originating from altered protein quality control in the endoplasmic reticulum.
A challenging question in biology is how cells control their shape and volume. The relative abundance of organelles can be radically modified to comply with a new task, an example being the massive… Expand
Different redox sensitivity of endoplasmic reticulum associated degradation clients suggests a novel role for disulphide bonds in secretory proteins.
- Iria Medraño-Fernandez, C. Fagioli, A. Mezghrani, M. Otsu, R. Sitia
- Biology, Medicine
- Biochemistry and cell biology = Biochimie et…
- 4 February 2014
To maintain proteostasis in the endoplasmic reticulum (ER), terminally misfolded secretory proteins must be recognized, partially unfolded, and dislocated to the cytosol for proteasomal destruction,… Expand