The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
The lore of the RINGs: substrate recognition and catalysis by ubiquitin ligases
Open accessAbstract
Recently, many new examples of E3 ubiquitin ligases or E3 enzymes have been found to regulate a host of cellular processes. These E3 enzymes direct the formation of multiubiquitin chains on specific protein substrates, and - typically - the subsequent destruction of those proteins. We discuss how the modular architecture of E3 enzymes connects one of two distinct classes of catalytic domains to a wide range of substrate-binding domains. In one catalytic class, a HECT domain transfers ubiquitin directly to substrate bound to a non-catalytic domain. Members of the other catalytic class, found in the SCF, VBC and APC complexes, use a RING finger domain to facilitate ubiquitylation. The separable substrate-recognition domains of E3 enzymes provides a flexible means of linking a conserved ubiquitylation function to potentially thousands of ubiquitylated substrates in eukaryotic cells.
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Cites
The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis
Maxwell, P. H., Wiesener, M. S., Chang, G.-W., Clifford, S. C., Vaux, E. C., Cockman, M. E., Wykoff, C. C., Pugh, C. W., Maher, E. R., & Ratcliffe, P. J. (1999) · Nature · doi:10.1038/20459 · Cited by 5,180
Ohh, M., Park, C. W., Ivan, M., Hoffman, M. A., Kim, T.-Y., Huang, L. E., Pavletich, N., Chau, V., & Kaelin, W. G. (2000) · Nature Cell Biology · doi:10.1038/35017054 · Cited by 1,577
Control of Cyclin Ubiquitination by CDK-Regulated Binding of Hct1 to the Anaphase Promoting Complex
Zachariae, W., Schwab, M., Nasmyth, K., & Seufert, W. (1998) · Science · doi:10.1126/science.282.5394.1721 · Cited by 511
Cited by
Signals for Sorting of Transmembrane Proteins to Endosomes and Lysosomes
Bonifacino, J. S., & Traub, L. M. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161800 · Cited by 2,040
Protein degradation by the ubiquitin-proteasome pathway in normal and disease states
Lecker, S. H., Goldberg, A. L., & Mitch, W. E. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006010083 · Cited by 1,234
Imai, Y., Soda, M., Inoue, H., Hattori, N., Mizuno, Y., & Takahashi, R. (2001) · Cell · doi:10.1016/s0092-8674(01)00407-x · Cited by 1,050
Masson, N., Willam, C., Maxwell, P. H., Pugh, C. W., & Ratcliffe, P. J. (2001) · The EMBO Journal · doi:10.1093/emboj/20.18.5197 · Cited by 1,014
EIN3-Dependent Regulation of Plant Ethylene Hormone Signaling by Two Arabidopsis F Box Proteins
Potuschak, T., Lechner, E., Parmentier, Y., Yanagisawa, S., Grava, S., Koncz, C., & Genschik, P. (2003) · Cell · doi:10.1016/s0092-8674(03)00968-1 · Cited by 733
Metadata
- Authors
- Jackson, P. K., Eldridge, A. G., Freed, E., Furstenthal, L., Hsu, J. Y., Kaiser, B. K., & Reimann, J. D. R.
- Venue
- Trends in Cell Biology
- Publisher
- Elsevier BV
- Published
- 2000-10
- Volume
- 10
- Issue
- 10
- Pages
- 429-439
- ISSN
- 0962-8924 (ISSN-L)
- OpenAlex
- W2075470465
- Cited by
- 634
- References
- 3
- FWCI
- 4.03
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Jackson, P. K., Eldridge, A. G., Freed, E., Furstenthal, L., Hsu, J. Y., Kaiser, B. K., & Reimann, J. D. R. (2000). The lore of the RINGs: substrate recognition and catalysis by ubiquitin ligases. Trends in Cell Biology. https://doi.org/10.1016/s0962-8924(00)01834-1
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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.
