The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
RINGs hold the key to ubiquitin transfer
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Citations
Cites
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
IAP Antagonists Induce Autoubiquitination of c-IAPs, NF-κB Activation, and TNFα-Dependent Apoptosis
Varfolomeev, E., Blankenship, J. W., Wayson, S. M., Fedorova, A. V., Kayagaki, N., Garg, P., Zobel, K., Dynek, J. N., Elliott, L. O., Wallweber, H. J. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.030 · Cited by 1,218
Autoregulation of Parkin activity through its ubiquitin‐like domain
Chaugule, V. K., Burchell, L., Barber, K. R., Sidhu, A., Leslie, S. J., Shaw, G. S., & Walden, H. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.204 · Cited by 339
Linke, K., Mace, P. D., Smith, C. A., Vaux, D. L., Silke, J., & Day, C. L. (2008) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402309 · Cited by 288
Self-citationSolution structure of the Hdm2 C2H2C4 RING, a domain critical for ubiquitination of p53
Kostic, M., Matt, T., Martinez-Yamout, M. A., Dyson, H. J., & Wright, P. E. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.08.027 · Cited by 128
Structural and Functional Comparison of the RING Domains of Two p53 E3 Ligases, Mdm2 and Pirh2
Shloush, J., Vlassov, J. E., Engson, I., Duan, S., Saridakis, V., Dhe-paganon, S., Raught, B., Sheng, Y., & Arrowsmith, C. H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.157669 · Cited by 42
Cited by
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
BIRC7–E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer
Dou, H., Buetow, L., Sibbet, G. J., Cameron, K., & Huang, D. T. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2379 · Cited by 319
Metadata
- Authors
- Budhidarmo, R., Nakatani, Y., & Day, C. L.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2012-02
- Volume
- 37
- Issue
- 2
- Pages
- 58-65
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2048320911
- Cited by
- 205
- References
- 6
- FWCI
- 1.14
- Type
- journal article
- Language
- en
- Open access
- closed
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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How to cite
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- This page
- CoChat. (2026). Citation check: RINGs hold the key to ubiquitin transfer. https://app.cochat.ai/papers/10.1016/j.tibs.2011.11.001
- The paper
- Budhidarmo, R., Nakatani, Y., & Day, C. L. (2012). RINGs hold the key to ubiquitin transfer. Trends in Biochemical Sciences. https://doi.org/10.1016/j.tibs.2011.11.001
Data sources
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.
