The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Perilous journey: a tour of the ubiquitin–proteasome system
Open accessAbstract
Eukaryotic cells are equipped to degrade proteins via the ubiquitin–proteasome system (UPS). Proteins become degraded upon their conjugation to chains of ubiquitin where they are then directed to the 26S proteasome, a macromolecular protease. The transfer of ubiquitin to proteins and their subsequent degradation are highly complex processes, and new research is beginning to uncover the molecular details of how ubiquitination and degradation take place in the cell. We review some of the new data providing insights into how these processes occur. Although distinct mechanisms are often observed, some common themes are emerging for how the UPS guides protein substrates through their final journey.
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Cites
Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679
RING Domain E3 Ubiquitin Ligases
Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679
An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer
Soucy, T. A., Smith, P. G., Milhollen, M. A., Berger, A. J., Gavin, J. M., Adhikari, S., Brownell, J. E., Burke, K. E., Cardin, D. P., Critchley, S., et al. (2009) · Nature · doi:10.1038/nature07884 · Cited by 1,990
A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
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Complete subunit architecture of the proteasome regulatory particle
Lander, G. C., Estrin, E., Matyskiela, M. E., Bashore, C., Nogales, E., & Martin, A. (2012) · Nature · doi:10.1038/nature10774 · Cited by 608
Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
Plechanovová, A., Jaffray, E. G., Tatham, M. H., Naismith, J. H., & Hay, R. T. (2012) · Nature · doi:10.1038/nature11376 · Cited by 521
Structure of an E3:E2∼Ub Complex Reveals an Allosteric Mechanism Shared among RING/U-box Ligases
Pruneda, J. N., Littlefield, P. J., Soss, S. E., Nordquist, K. A., Chazin, W. J., Brzovic, P. S., & Klevit, R. E. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.07.001 · Cited by 333
Conformational switching of the 26S proteasome enables substrate degradation
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Mechanism of ubiquitin ligation and lysine prioritization by a HECT E3
Kamadurai, H. B., Qiu, Y., Deng, A., Harrison, J. S., MacDonald, C., Actis, M., Rodrigues, P., Miller, D. J., Souphron, J., Lewis, S. M., et al. (2013) · eLife · doi:10.7554/elife.00828 · Cited by 165
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Protein degraders enter the clinic — a new approach to cancer therapy
Chirnomas, D., Hornberger, K. R., & Crews, C. M. (2023) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-023-00736-3 · Cited by 658
Protac-Induced Protein Degradation in Drug Discovery: Breaking the Rules or Just Making New Ones?
Churcher, I. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01272 · Cited by 491
The combination of disulfiram and copper for cancer treatment
Li, H., Wang, J., Wu, C., Wang, L., Chen, Z.-S., & Cui, W. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.04.003 · Cited by 185
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Metadata
- Authors
- Kleiger, G., & Mayor, T.
- Venue
- Trends in Cell Biology
- Publisher
- Elsevier BV
- Published
- 2014-06
- Volume
- 24
- Issue
- 6
- Pages
- 352-359
- ISSN
- 0962-8924 (ISSN-L)
- OpenAlex
- W2129805026
- Cited by
- 409
- References
- 9
- FWCI
- 1.59
- Type
- journal article
- Language
- en
- Open access
- green
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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.
