The DOI matches its Crossref record; 183 of the 183 references it cites were found in a registry or an index.
The ubiquitin proteasome system — Implications for cell cycle control and the targeted treatment of cancer
Open accessAbstract
Two families of E3 ubiquitin ligases are prominent in cell cycle regulation and mediate the timely and precise ubiquitin-proteasome-dependent degradation of key cell cycle proteins: the SCF (Skp1/Cul1/F-box protein) complex and the APC/C (anaphase promoting complex or cyclosome). While certain SCF ligases drive cell cycle progression throughout the cell cycle, APC/C (in complex with either of two substrate recruiting proteins: Cdc20 and Cdh1) orchestrates exit from mitosis (APC/C(Cdc20)) and establishes a stable G1 phase (APC/C(Cdh1)). Upon DNA damage or perturbation of the normal cell cycle, both ligases are involved in checkpoint activation. Mechanistic insight into these processes has significantly improved over the last ten years, largely due to a better understanding of APC/C and the functional characterization of multiple F-box proteins, the variable substrate recruiting components of SCF ligases. Here, we review the role of SCF- and APC/C-mediated ubiquitylation in the normal and perturbed cell cycle and discuss potential clinical implications of SCF and APC/C functions. This article is part of a Special Issue entitled: Ubiquitin-Proteasome System. Guest Editors: Thomas Sommer and Dieter H. Wolf.
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1 retracted
Oncogenic role of the ubiquitin ligase subunit Skp2 in human breast cancer
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In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
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RING Domain E3 Ubiquitin Ligases
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The Mutational Landscape of Head and Neck Squamous Cell Carcinoma
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Cited by
Ruijtenberg, S., & van den Heuvel, S. (2016) · Cell Cycle · doi:10.1080/15384101.2015.1120925 · Cited by 553
A Practical Review of Proteasome Pharmacology
Thibaudeau, T. A., & Smith, D. M. (2019) · Pharmacological Reviews · doi:10.1124/pr.117.015370 · Cited by 344
Spatiotemporal regulation of the anaphase-promoting complex in mitosis
Sivakumar, S., & Gorbsky, G. J. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3934 · Cited by 259
Eichner, R., Heider, M., Fernández-Sáiz, V., van Bebber, F., Garz, A.-K., Lemeer, S., Rudelius, M., Targosz, B.-S., Jacobs, L., Knorn, A.-M., et al. (2016) · Nature Medicine · doi:10.1038/nm.4128 · Cited by 183
Self-citationRegulatory mechanisms of one-carbon metabolism enzymes
Petrova, B., Maynard, A. G., Wang, P., & Kanarek, N. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105457 · Cited by 103
Metadata
- Authors
- Bassermann, F., Eichner, R., & Pagano, M.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2014-01
- Volume
- 1843
- Issue
- 1
- Pages
- 150-162
- ISSN
- 0167-4889 (ISSN-L)
- OpenAlex
- W2064221650
- Cited by
- 268
- References
- 183
- FWCI
- 9.14
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Bassermann, F., Eichner, R., & Pagano, M. (2014). The ubiquitin proteasome system — Implications for cell cycle control and the targeted treatment of cancer. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. https://doi.org/10.1016/j.bbamcr.2013.02.028
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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.
