The DOI matches its Crossref record; 213 of the 213 references it cites were found in a registry or an index.
Principles of Ubiquitin-Dependent Signaling
Abstract
Ubiquitylation is an essential posttranslational modification that controls cell division, differentiation, and survival in all eukaryotes. By combining multiple E3 ligases (writers), ubiquitin-binding effectors (readers), and de-ubiquitylases (erasers) with functionally distinct ubiquitylation tags, the ubiquitin system constitutes a powerful signaling network that is employed in similar ways from yeast to humans. Here, we discuss conserved principles of ubiquitin-dependent signaling that illustrate how this posttranslational modification shapes intracellular signaling networks to establish robust development and homeostasis throughout the eukaryotic kingdom.
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“With more than 600 human ubiquitin E3 ligases79,80 to potentially explore”
From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [79]
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Items 201–213 of 213
Expanding the host cell ubiquitylation machinery targeting cytosolic Salmonella
Polajnar, M., Dietz, M. S., Heilemann, M., & Behrends, C. (2017) · EMBO Reports · doi:10.15252/embr.201643851 · Cited by 68
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Mapping the Landscape of a Eukaryotic Degronome
Geffen, Y., Chappleboim, A., Gardner, R. G., Friedman, N., Sadeh, R., & Ravid, T. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.005 · Cited by 53
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Regulation of Clathrin-Mediated Endocytosis by Dynamic Ubiquitination and Deubiquitination
Weinberg, J., & Drubin, D. G. (2014) · Current Biology · doi:10.1016/j.cub.2014.03.038 · Cited by 45
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Sorting of a multi-subunit ubiquitin ligase complex in the endolysosome system
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The BioGRID interaction database: 2019 update
Oughtred, R., Stark, C., Breitkreutz, B., Rust, J., Boucher, L., Chang, C., Kolas, N. K., O’Donnell, L., Leung, G. C., McAdam, R. F., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky1079 · Cited by 1,474
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Advancing targeted protein degradation for cancer therapy
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Metadata
- Authors
- Oh, E., Akopian, D., & Rape, M.
- Affiliations
- Howard Hughes Medical Institute (US)
- University of California, Berkeley (US)
- Howard Hughes Medical Institute, University of California, Berkeley, California 94720, USA;
- Corresponding author
- Oh, Eugene
- Akopian, David
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 2018-10-06
- Volume
- 34
- Issue
- 1
- Pages
- 137-162
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- OpenAlex
- W2885686631
- Cited by
- 339
- References
- 213
- Citations by year
- 2026: 32 · 2025: 44 · 2024: 54 · 2023: 39 · 2022: 50 · 2021: 53 · 2020: 42 · 2019: 24 · 2018: 1
- FWCI
- 2.97
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Cell and Developmental Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institute of General Medical Sciences (F32GM123716)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Keywords
- ubiquitination, post-translational modification, E3 ubiquitin ligase, intracellular signaling networks, cell division, cell differentiation, cell survival, homeostasis
- MeSH terms
- Eukaryotic Cells, Humans, Protein Processing, Post-Translational, Saccharomyces cerevisiae, Signal Transduction, Ubiquitin, Ubiquitin-Protein Ligases, Ubiquitination
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