The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
RING-type E3 ligases: Master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination
Open accessAbstract
RING finger domain and RING finger-like ubiquitin ligases (E3s), such as U-box proteins, constitute the vast majority of known E3s. RING-type E3s function together with ubiquitin-conjugating enzymes (E2s) to mediate ubiquitination and are implicated in numerous cellular processes. In part because of their importance in human physiology and disease, these proteins and their cellular functions represent an intense area of study. Here we review recent advances in RING-type E3 recognition of substrates, their cellular regulation, and their varied architecture. Additionally, recent structural insights into RING-type E3 function, with a focus on important interactions with E2s and ubiquitin, are reviewed. This article is part of a Special Issue entitled: Ubiquitin-Proteasome System.
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Citations
Cites
Function and regulation of cullin–RING ubiquitin ligases
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BRCA1 and BRCA2 and the genetics of breast and ovarian cancer
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“BRCA1, an E3 that plays critical roles in DNA repair, is mutated in familial breast and ovarian cancers [2].”
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
Self-citationCarbia-Nagashima, A., Gerez, J., Perez-Castro, C., Paez-Pereda, M., Silberstein, S., Stalla, G. K., Holsboer, F., & Arzt, E. (2007) · Cell · doi:10.1016/j.cell.2007.07.044 · Cited by 318
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The ubiquitin ligase gp78 promotes sarcoma metastasis by targeting KAI1 for degradation
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Cited by
E2 enzymes: more than just middle men
Stewart, M. D., Ritterhoff, T., Klevit, R. E., & Brzovic, P. S. (2016) · Cell Research · doi:10.1038/cr.2016.35 · Cited by 594
Self-citationE3 ubiquitin ligases: styles, structures and functions
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Protein Language: Post-Translational Modifications Talking to Each Other
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Building and remodelling Cullin–RING E3 ubiquitin ligases
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Targeted degradation of aberrant tau in frontotemporal dementia patient-derived neuronal cell models
Silva, M. C., Ferguson, F. M., Cai, Q., Donovan, K. A., Nandi, G., Patnaik, D., Zhang, T., Huang, H.-T., Lucente, D. E., Dickerson, B. C., et al. (2019) · eLife · doi:10.7554/elife.45457 · Cited by 283
Metadata
- Authors
- Metzger, M. B., Pruneda, J. N., Klevit, R. E., & Weissman, A. M.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2014-01
- Volume
- 1843
- Issue
- 1
- Pages
- 47-60
- ISSN
- 0167-4889 (ISSN-L)
- OpenAlex
- W1973921769
- Cited by
- 611
- References
- 8
- FWCI
- 13.72
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Metzger, M. B., Pruneda, J. N., Klevit, R. E., & Weissman, A. M. (2014). RING-type E3 ligases: Master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. https://doi.org/10.1016/j.bbamcr.2013.05.026
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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