The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Ubiquitin and ubiquitin-like proteins in cancer pathogenesis
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Citations
Cites
In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., et al. (2004) · Science · doi:10.1126/science.1092472 · Cited by 4,661
WNT and β-catenin signalling: diseases and therapies
Moon, R. T., Kohn, A. D., Ferrari, G. V. D., & Kaykas, A. (2004) · Nature Reviews Genetics · doi:10.1038/nrg1427 · Cited by 1,763
Small-molecule inhibitors of protein–protein interactions: progressing towards the dream
Arkin, M. R., & Wells, J. A. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1343 · Cited by 1,705
Post-translational modification of p53 in tumorigenesis
Bode, A. M., & Dong, Z. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1455 · Cited by 1,270
Ubiquitin signalling in the NF-κB pathway
Chen, Z. J. (2005) · Nature Cell Biology · doi:10.1038/ncb0805-758 · Cited by 1,184
The SCF ubiquitin ligase: insights into a molecular machine
Cardozo, T., & Pagano, M. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1471 · Cited by 1,114
p53 ubiquitination: Mdm2 and beyond
Brooks, C. L., & Gu, W. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.020 · Cited by 924
Mono- Versus Polyubiquitination: Differential Control of p53 Fate by Mdm2
Li, M., Brooks, C. L., Wu-Baer, F., Chen, D., Baer, R., & Gu, W. (2003) · Science · doi:10.1126/science.1091362 · Cited by 804 · cited 1×
“If MDM2 is expressed at a low level it will primarily monoubiquitylate p53, which leads to the nuclear export but not to the proteasomal degradation of p53 (Ref”
BackgroundUbiquitin-binding domains in Y-family polymerases regulate translesion synthesis.
Bienko, M., Green, C. M., Crosetto, N., Rudolf, F., Zapart, G., Coull, B., Kannouche, P., Wider, G., Peter, M., Lehmann, A. R., et al. (2005) · Science · doi:10.1126/science.1120615 · Cited by 712
The Cbl interactome and its functions
Schmidt, M. H. H., & Dikic, I. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1762 · Cited by 395
Cited by
Ubiquitination regulates PTEN nuclear import and tumor suppression
Trotman, L. C., Wang, X., Alimonti, A., Chen, Z., Teruya-Feldstein, J., Yang, H., Pavletich, N. P., Carver, B. S., Cordon-Cardo, C., Erdjument-Bromage, H., et al. (2007) · Cell · doi:10.1016/j.cell.2006.11.040 · Cited by 748
The role of ubiquitination in tumorigenesis and targeted drug discovery
Deng, L., Meng, T., Chen, L., Wei, W., & Wang, P. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0107-0 · Cited by 744
Chauhan, D., Tian, Z., Nicholson, B., Kumar, K. G. S., Zhou, B., Carrasco, R., McDermott, J. L., Leach, C. A., Fulcinniti, M., Kodrasov, M. P., et al. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.08.007 · Cited by 589
Okuhira, K., Ohoka, N., Sai, K., Nishimaki-Mogami, T., Itoh, Y., Ishikawa, M., Hashimoto, Y., & Naito, M. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.03.019 · Cited by 118
The E3 ubiquitin ligase Rnf8 stabilizes Tpp1 to promote telomere end protection.
Rai, R., Li, J.-M., Zheng, H., Lok, G. T.-M., Deng, Y., Huen, M. S.-Y., Chen, J., Jin, J., & Chang, S. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2172 · Cited by 88
Identification and structure-guided development of pyrimidinone based USP7 inhibitors
O’Dowd, C. R., Helm, M. D., Rountree, J. S. S., Flasz, J. T., Arkoudis, E., Miel, H., Hewitt, P. R., Jordan, L., Barker, O., Hughes, C., et al. (2018) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.7b00512 · Cited by 71
Zhang, S., Guo, M., Jiang, X., Tang, L., Wu, T., Bi, G., Yang, X., Fan, S., & Bi, H. (2023) · Pharmacological Research · doi:10.1016/j.phrs.2023.106666 · Cited by 37
Modification of Drosophila p53 by SUMO Modulates Its Transactivation and Pro-apoptotic Functions
Mauri, F., McNamee, L. M., Lunardi, A., Chiacchiera, F., Del Sal, G., Brodsky, M. H., & Collavin, L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710186200 · Cited by 33
Metadata
- Authors
- Hoeller, D., Hecker, C.-M., & Dikic, I.
- Venue
- Nature Reviews Cancer
- Published
- 2006-10
- Volume
- 6
- Issue
- 10
- Pages
- 776-788
- ISSN
- 1474-175X (ISSN-L)
- 1474-1768
- OpenAlex
- W1979250970
- Cited by
- 408
- References
- 13
- FWCI
- 1.49
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
