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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 turnExpand
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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 inExpand
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SEL1L and HRD1 are involved in the degradation of unassembled secretory Ig‐µ chains
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 orExpand
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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 massiveExpand
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Different redox sensitivity of endoplasmic reticulum associated degradation clients suggests a novel role for disulphide bonds in secretory proteins.
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
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[Status of rotational psychiatric training in teaching hospitals in Japan].