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Cited by 386

The DOI matches its Crossref record; 131 of the 131 references it cites were found in a registry or an index.

Cleaning up in the endoplasmic reticulum: ubiquitin in charge

Open access
Christianson, John C, Ye, Yihong·2014·Nature Structural & Molecular Biology

Abstract

The eukaryotic endoplasmic reticulum (ER) maintains protein homeostasis by eliminating unwanted proteins through the evolutionarily conserved ER-associated degradation (ERAD) pathway. During ERAD, maturation-defective and surplus polypeptides are evicted from the ER lumen and/or lipid bilayer through the process of retrotranslocation and ultimately degraded by the proteasome. An integral facet of the ERAD mechanism is the ubiquitin system, composed of the ubiquitin modifier and the factors for assembling, processing and binding ubiquitin chains on conjugated substrates. Beyond simply marking polypeptides for degradation, the ubiquitin system is functionally intertwined with retrotranslocation machinery to transport polypeptides across the ER membrane.

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Metadata

Authors
Christianson, J. C., & Ye, Y.
Venue
Nature Structural & Molecular Biology
Published
2014-04
Volume
21
Issue
4
Pages
325-335
ISSN
  • 1545-9985 (ISSN-L)
  • 1545-9993
OpenAlex
W2083255287
Cited by
386
References
131
FWCI
14.60
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Cleaning up in the endoplasmic reticulum: ubiquitin in charge. https://app.cochat.ai/papers/10.1038/nsmb.2793
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Christianson, J. C., & Ye, Y. (2014). Cleaning up in the endoplasmic reticulum: ubiquitin in charge. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.2793

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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.