The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
SUMO-1 modification activates the transcriptional response of p53
Open accessOverview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Lane, D. P. (1992) · Nature · doi:10.1038/358015a0 · Cited by 5,138
Self-citationMdm2 promotes the rapid degradation of p53
Haupt, Y., Maya, R., Kazaz, A., & Oren, M. (1997) · Nature · doi:10.1038/387296a0 · Cited by 4,506
Regulation of p53 stability by Mdm2
Kubbutat, M. H. G., Jones, S. N., & Vousden, K. H. (1997) · Nature · doi:10.1038/387299a0 · Cited by 3,312 · cited 2×
“The rapid turnover of the p53 protein is via the ubiquitin–proteasome pathway (Maki et al., 1996) and this is mediated by association with mdm2 (Bottger et al., 1997; Haupt et al., 1997; Kubbutat et al., 1997).”
BackgroundMomand, J., Zambetti, G. P., Olson, D. C., George, D., & Levine, A. J. (1992) · Cell · doi:10.1016/0092-8674(92)90644-r · Cited by 3,113
Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206
DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
Shieh, S.-Y., Ikeda, M., Taya, Y., & Prives, C. (1997) · Cell · doi:10.1016/s0092-8674(00)80416-x · Cited by 2,100
Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
Honda, R., Tanaka, H., & Yasuda, H. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01480-4 · Cited by 1,951
Pomerantz, J., Schreiber-Agus, N., Liégeois, N. J., Silverman, A., Alland, L., Chin, L., Potes, J., Chen, K., Orlow, I., Lee, H.-W., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)81400-2 · Cited by 1,521
Radiation-induced cell cycle arrest compromised by p21 deficiency
Brugarolas, J., Chandrasekaran, C., Gordon, J. I., Beach, D., Jacks, T., & Hannon, G. J. (1995) · Nature · doi:10.1038/377552a0 · Cited by 1,242 · cited 2×
“This accumulation of p53 is responsible for the increased transcription of cellular genes, the products of which are associated with cell cycle arrest (p21Waf1Cip1) or apoptosis (Bax), and constitute a significant part of the p53 response (Lu and Lane, 1993; Brugarolas et al., 1995; Waldman et al., 1995; McCurrach et…”
BackgroundAssociation of p19ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53
Honda, R., & Yasuda, H. (1999) · The EMBO Journal · doi:10.1093/emboj/18.1.22 · Cited by 724
Cited by
Post-translational modification of p53 in tumorigenesis
Bode, A. M., & Dong, Z. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1455 · Cited by 1,270
p53 ubiquitination: Mdm2 and beyond
Brooks, C. L., & Gu, W. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.020 · Cited by 924
Regulation and function of the p53 tumor suppressor protein
Ryan, K. M., Phillips, A. C., & Vousden, K. H. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00216-7 · Cited by 721
Mdm2-Mediated NEDD8 Conjugation of p53 Inhibits Its Transcriptional Activity
Xirodimas, D. P., Saville, M. K., Bourdon, J.-C., Hay, R. T., & Lane, D. P. (2004) · Cell · doi:10.1016/j.cell.2004.06.016 · Cited by 570
Self-citationThe p53 orchestra: Mdm2 and Mdmx set the tone
Wade, M., Wang, Y. V., & Wahl, G. M. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.01.009 · Cited by 450
Regulating tumor suppressor genes: post-translational modifications
Chen, L., Liu, S., & Tao, Y. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0196-9 · Cited by 449
The MDM2 RING-finger domain is required to promote p53 nuclear export
Geyer, R. K., Yu, Z. K., & Maki, C. G. (2000) · Nature Cell Biology · doi:10.1038/35023507 · Cited by 361
Ginkgolic Acid Inhibits Protein SUMOylation by Blocking Formation of the E1-SUMO Intermediate
Fukuda, I., Ito, A., Hirai, G., Nishimura, S., Kawasaki, H., Saitoh, H., Kimura, K.-I., Sodeoka, M., & Yoshida, M. (2009) · Chemistry & Biology · doi:10.1016/j.chembiol.2009.01.009 · Cited by 355
An intact HDM2 RING-finger domain is required for nuclear exclusion of p53
Boyd, S. D., Tsai, K. Y., & Jacks, T. (2000) · Nature Cell Biology · doi:10.1038/35023500 · Cited by 334
Small Ubiquitin-like Modifier (SUMO) Modification of Natively Unfolded Proteins Tau and α-Synuclein
Dorval, V., & Fraser, P. E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510127200 · Cited by 319
A Gain-of-Function Mutation in DHT Synthesis in Castration-Resistant Prostate Cancer
Chang, K.-H., Li, R., Kuri, B., Lotan, Y., Roehrborn, C. G., Liu, J., Vessella, R., Nelson, P. S., Kapur, P., Guo, X., et al. (2013) · Cell · doi:10.1016/j.cell.2013.07.029 · Cited by 312
Oncogenic ras and p53 Cooperate To Induce Cellular Senescence
Ferbeyre, G., de Stanchina, E., Lin, A. W., Querido, E., McCurrach, M. E., Hannon, G. J., & Lowe, S. W. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.10.3497-3508.2002 · Cited by 290
Dynamic Interplay of the SUMO and ERK Pathways in Regulating Elk-1 Transcriptional Activity
Yang, S.-H., Jaffray, E., Hay, R. T., & Sharrocks, A. D. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00265-x · Cited by 253
Self-citationRegulation of transcription factor activity by interconnected post-translational modifications
Filtz, T. M., Vogel, W. K., & Leid, M. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.11.005 · Cited by 242
SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities
David, G., Neptune, M. A., & DePinho, R. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203690200 · Cited by 236
Feng, L., Lin, T., Uranishi, H., Gu, W., & Xu, Y. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.13.5389-5395.2005 · Cited by 236
C-terminal modifications regulate MDM2 dissociation and nuclear export of p53
Carter, S., Bischof, O., Dejean, A., & Vousden, K. H. (2007) · Nature Cell Biology · doi:10.1038/ncb1562 · Cited by 225
Comerford, K. M., Leonard, M. O., Karhausen, J., Carey, R., Colgan, S. P., & Taylor, C. T. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0337412100 · Cited by 185
Different effects of p14ARF on the levels of ubiquitinated p53 and Mdm2 in vivo
Xirodimas, D., Saville, M. K., Edling, C., Lane, D. P., & Laín, S. (2001) · Oncogene · doi:10.1038/sj.onc.1204656 · Cited by 169
Self-citationPotentiation of glucocorticoid receptor transcriptional activity by sumoylation
Le Drean, Y., Mincheneau, N., Le Goff, P., & Michel, D. (2002) · Endocrinology · doi:10.1210/en.2002-220135 · Cited by 159
Therapeutics targeting p53-MDM2 interaction to induce cancer cell death
Koo, N., Sharma, A. K., & Narayan, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23095005 · Cited by 153
MDM2-ARF complex regulates p53 sumoylation
Chen, L., & Chen, J. (2003) · Oncogene · doi:10.1038/sj.onc.1206851 · Cited by 134
Wu, S., & Chiang, C. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.83 · Cited by 125
P14ARF promotes accumulation of SUMO-1 conjugated (H)Mdm2
Xirodimas, D. P., Chisholm, J., Desterro, J. M. S., Lane, D. P., & Hay, R. T. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03310-0 · Cited by 94
Self-citationIdentification and Characterization of a Novel p300-mediated p53 Acetylation Site, Lysine 305
Wang, Y.-H., Tsay, Y.-G., Tan, B. C.-M., Lo, W.-Y., & Lee, S.-C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212574200 · Cited by 92
Rui, H.-L., Fan, E., Zhou, H.-M., Xu, Z., Zhang, Y., & Lin, S.-C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208099200 · Cited by 83
Regulation of p53 family members by the ubiquitin-like SUMO system
Stehmeier, P., & Muller, S. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.01.002 · Cited by 83
Baron, C. A., Tepper, C. G., Liu, S. Y., Davis, R. R., Wang, N. J., Schanen, N. C., & Gregg, J. P. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl004 · Cited by 80
Yates, K. E., Korbel, G. A., Shtutman, M., Roninson, I. B., & DiMaio, D. (2008) · Aging Cell · doi:10.1111/j.1474-9726.2008.00411.x · Cited by 77
Deciphering the acetylation code of p53 in transcription regulation and tumor suppression
Xia, Z., Kon, N., Gu, A. P., Tavana, O., & Gu, W. (2022) · Oncogene · doi:10.1038/s41388-022-02331-9 · Cited by 60
Seo, Y. R., & Jung, H. J. (2004) · Experimental & Molecular Medicine · doi:10.1038/emm.2004.64 · Cited by 56
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
SUMOylation regulates the homologous to E6-AP carboxyl terminus (HECT) ubiquitin ligase Rsp5p
Novoselova, T. V., Rose, R.-S., Marks, H. M., & Sullivan, J. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.424234 · Cited by 9
Metadata
- Authors
- Rodriguez, M. S., Desterro, J. M. P., Lain, S., Midgley, C. A., Lane, D. P., & Hay, R. T.
- Venue
- The EMBO Journal
- Published
- 1999-11-15
- Volume
- 18
- Issue
- 22
- Pages
- 6455-6461
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- OpenAlex
- W1972166544
- Cited by
- 639
- References
- 11
- FWCI
- 14.79
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
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.
