The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
ER Degradation of a Misfolded Luminal Protein by the Cytosolic Ubiquitin-Proteasome Pathway
Abstract
Secretion of proteins is initiated by their uptake into the endoplasmic reticulum (ER), which possesses a proteolytic system able to degrade misfolded and nonassembled proteins. The ER degradation system was studied with yeast mutants defective in the breakdown of a mutated soluble vacuolar protein, carboxypeptidase yscY (CPY*). The ubiquitin-conjugating enzyme Ubc7p participated in the degradation process, which was mediated by the cytosolic 26 S proteasome. It is likely that CPY* entered the ER, was glycosylated, and was then transported back out of the ER lumen to the cytoplasmic side of the organelle, where it was conjugated with ubiquitin and degraded.
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Cites
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Cited by
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Oxidative Stress in Aging Human Skin
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Metadata
- Authors
- Hiller, M. M., Finger, A., Schweiger, M., & Wolf, D. H.
- Venue
- Science
- Published
- 1996-09-20
- Volume
- 273
- Issue
- 5282
- Pages
- 1725-1728
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1986342078
- Cited by
- 708
- References
- 42
- FWCI
- 22.47
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: ER Degradation of a Misfolded Luminal Protein by the Cytosolic Ubiquitin-Proteasome Pathway. https://app.cochat.ai/papers/10.1126/science.273.5282.1725
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- Hiller, M. M., Finger, A., Schweiger, M., & Wolf, D. H. (1996). ER Degradation of a Misfolded Luminal Protein by the Cytosolic Ubiquitin-Proteasome Pathway. Science. https://doi.org/10.1126/science.273.5282.1725
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
