Cited by 1,280Cancer-related Molecular PathwaysDevelopmental Biology and Gene RegulationCell death mechanisms and regulation

The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.

Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53

Jones, Stephen N., Roe, Amy E., Donehower, Lawrence A., Bradley, Allan·1995·Nature

DOI 10.1038/378206a0

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Abstract

The Mdm2 proto-oncogene was originally identified as one of several genes contained on a mouse double minute chromosome present in a transformed derivative of 3T3 cells. Overexpression of Mdm2 can immortalize primary cultures of rodent fibroblasts. Human MDM2 is amplified in 30-40% of sarcomas, and is overexpressed in leukaemic cells. The Mdm2 oncoprotein forms a complex with the p53 tumour-suppressor protein and inhibits p53-mediated transregulation of gene expression. Because Mdm2 expression increases in response to p53, Mdm2-p53 binding may autoregulate Mdm2 expression and modulate the activity of p53 in the cell. We have created Mdm2-null and Mdm2/p53-null mice to determine whether Mdm2 possesses developmental functions in addition to the ability to complex with p53, and to investigate the biological role of Mdm2-p53 complex formation in development. Mice deficient for Mdm2 die early in development. In contrast, mice deficient for both Mdm2 and p53 develop normally and are viable. These results suggest that a critical role of Mdm2 in development is the regulation of p53 function.

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p53 Mutations in Human Cancers
Hollstein, M., Sidransky, D., Vogelstein, B., & Harris, C. C. (1991) · Science · doi:10.1126/science.1905840 · Cited by 8,018
Mice deficient for p53 are developmentally normal but susceptible to spontaneous tumours
Donehower, L. A., Harvey, M., Slagle, B. L., McArthur, M. J., Montgomery, C. A., Butel, J. S., & Bradley, A. (1992) · Nature · doi:10.1038/356215a0 · Cited by 4,649
Self-citation
Participation of p53 protein in the cellular response to DNA damage.
Kastan, M. B., Onyekwere, O. C., Sidransky, D., Vogelstein, B., & Craig, R. W. (1991) · PubMed · Cited by 3,761
The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation
Momand, 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
Amplification of a gene encoding a p53-associated protein in human sarcomas
Oliner, J. D., Kinzler, K. W., Meltzer, P. S., George, D. L., & Vogelstein, B. (1992) · Nature · doi:10.1038/358080a0 · Cited by 1,949
The p53-mdm-2 autoregulatory feedback loop.
Wu, X., Bayle, J. H., Olson, D., & Levine, A. J. (1993) · Genes & Development · doi:10.1101/gad.7.7a.1126 · Cited by 1,801
The Atlas of Mouse Development
Kaufman, M. H. (1992) · Medical Entomology and Zoology · Cited by 1,750
Disruption of the proto-oncogene int-2 in mouse embryo-derived stem cells: A general strategy for targeting mutations to non-selectable genes
Mansour, S. L., Thomas, K. R., & Capecchi, M. R. (1988) · Nature · doi:10.1038/336348a0 · Cited by 1,683
The atlas of mouse development
Beddington, R. S. P. (1993) · Trends in Genetics · doi:10.1016/0168-9525(93)90071-o · Cited by 1,416
α-lnhibin is a tumour-suppressor gene with gonadal specificity in mice
Matzuk, M. M., Finegold, M. J., Su, J.-G. J., Hsueh, A. J. W., & Bradley, A. (1992) · Nature · doi:10.1038/360313a0 · Cited by 893
Self-citation

Flagged first, then by citations

Show all 24 references

Research works printed but not linked: 5

Juven, T., Barak, Y., Zauberman, A., George, D. & Oren, M. Oncogene 8, 3411–3416 (1993).
Snow, M. H. L. J. Embryol. exp. Morph. 42, 293–303 (1977).
Baker, S. J., Markowitz, S., Fearon, E. R., Willson, J. K. V. & Vogelstein, B. Science 253, 49–53 (1990).
Kastan, M. B., Onyekwere, O., Sidransky, D., Vogelstein, B. & Craig, R. W. Cancer Res. 51, 6304–6311 (1991).
Olson, D. C. et al. Oncogene 8, 2353–2360 (1993).

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Self-citation
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Knappskog, S., Gansmo, L. B., Dibirova, K., Metspalu, A., Cybulski, C., Peterlongo, P., Aaltonen, L. A., VATTEN, L. J., Romundstad, P., Hveem, K., et al. (2014) · Oncotarget · doi:10.18632/oncotarget.1910 · Cited by 24
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Mairinger, F. D., Werner, R., Flom, E., Schmeller, J., Borchert, S., Wessolly, M., Wohlschlaeger, J., Hager, T., Mairinger, T., Kollmeier, J., et al. (2017) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/s00428-017-2133-z · Cited by 24
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Iwakuma, T., Parant, J. M., Fasulo, M., Zwart, E., Jacks, T., de Vries, A., & Lozano, G. (2004) · Oncogene · doi:10.1038/sj.onc.1207793 · Cited by 27
Apoptosis of tumoral and nontumoral lymphoid cells is induced by both mdm2 and p53 antisense oligodeoxynucleotides
Métay, C., Mir, L. M., Carlier, K., Lécluse, Y., Tétaud, C., Mishal, Z., & Wiels, J. (2001) · Blood · doi:10.1182/blood.v97.4.1043 · Cited by 23
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Candeias, M. M. (2011) · Biochimie · doi:10.1016/j.biochi.2011.06.010 · Cited by 23
HDM2 promotes WIP1-mediated medulloblastoma growth
Buss, M. C., Read, T., Schniederjan, M., Gandhi, K., & Castellino, R. C. (2012) · Neuro-Oncology · doi:10.1093/neuonc/nos001 · Cited by 25
Peptide Activators of the p53 Tumor Suppressor
Zhan, C., & Lu, W. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211795222577 · Cited by 23
Recent progress and open challenges in modeling p53 dynamics in single cells
Batchelor, E., & Loewer, A. (2017) · Current Opinion in Systems Biology · doi:10.1016/j.coisb.2017.04.007 · Cited by 23
Developmental Acquisition of p53 Functions
Jaiswal, S. K., Raj, S., & Depamphilis, M. (2021) · Genes · doi:10.3390/genes12111675 · Cited by 23
Novel MDM2 p53‐Independent Functions Identified through RNA Silencing Technologies
Zhang, Z., Wang, H., Li, M., Rayburn, E. R., Agrawal, S., & Zhang, R. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1359.030 · Cited by 22
Variable expressivity of the tumour suppressor protein TRP53 in cryopreserved human blastocysts
Chandrakanthan, V., Chami, O., Stojanov, T., & O’Neill, C. (2007) · Reproductive Biology and Endocrinology · doi:10.1186/1477-7827-5-39 · Cited by 22
A Functional Polymorphism (rs937283) in the MDM2 Promoter Region is Associated with Poor Prognosis of Retinoblastoma in Chinese Han Population
Jiao, Y., Jiang, Z., Wu, Y., Chen, X., Xiao, X., & Yu, H. (2016) · Scientific Reports · doi:10.1038/srep31240 · Cited by 21
MDM2 prevents spontaneous tubular epithelial cell death and acute kidney injury
Thomasová, D., Ebrahim, M., Fleckinger, K., Li, M., Molnar, J., Popper, B., Liapis, H., Kotb, A. M., Siegerist, F., Endlich, N., et al. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.390 · Cited by 21
MDM2 as a Critical Effector of the MYCN Oncogene in Tumorigenesis
Slack, A., & Shohet, J. M. (2005) · Cell Cycle · doi:10.4161/cc.4.7.1790 · Cited by 22
Ammonia inhibits neural cell adhesion molecule polysialylation in Chinese hamster ovary and small cell lung cancer cells
Zanghi, J. A., Mendoza, T. P., Knop, R. H., & Miller, W. M. (1998) · Journal of Cellular Physiology · doi:10.1002/(sici)1097-4652(199811)177:2 · Cited by 26
Characterization of the 5′ and 3′ untranslated regions in murine mdm2 mRNAs
Mendrysa, S. M., McElwee, M. K., & Perry, M. E. (2001) · Gene · doi:10.1016/s0378-1119(00)00589-8 · Cited by 22
MDM2 function
Lozano, G., & Luna, R. M. D. O. (1998) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(97)00037-1 · Cited by 22
The phenotype of MDM2 auto-degradation after DNA damage is due to epitope masking by phosphorylation
Cheng, Q., & Chen, J. (2011) · Cell Cycle · doi:10.4161/cc.10.7.15249 · Cited by 21
“However, current evidence suggests that MDM2 is a major and indispensable regulator of p53 level.(7,8) Elucidating how p53 is stabilized and activated after DNA damage is the subject of many studies.”
Background
Guardian of corpulence: a hypothesis on p53 signaling in the fat cell
Bazuine, M., Stenkula, K. G., Cam, M., Arroyo, M., & Cushman, S. W. (2009) · Clinical Lipidology · doi:10.2217/clp.09.2 · Cited by 21
The MDM2–p53 pathway: multiple roles in kidney development
El-Dahr, S. S., Hilliard, S. A., Aboudehen, K., & Saifudeen, Z. R. (2013) · Pediatric Nephrology · doi:10.1007/s00467-013-2629-y · Cited by 21
Identification and Characterization of Two Novel Isoforms of Pirh2 Ubiquitin Ligase That Negatively Regulate p53 Independent of RING Finger Domains
Corcoran, C. A., Montalbano, J., Hong, S., He, Q., Huang, Y. K., & Sheikh, M. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.024232 · Cited by 22
The ARF‐p16 Gene Locus in Carcinogenesis and Therapy of Head and Neck Squamous Cell Carcinoma
Yarbrough, W. G. (2002) · The Laryngoscope · doi:10.1097/00005537-200212000-00002 · Cited by 20
Distinct downstream targets manifest p53-dependent pathologies in mice
Pant, V., Xiong, S., Chau, G. P., Tsai, K. Y., Shetty, G., & Lozano, G. (2016) · Oncogene · doi:10.1038/onc.2016.111 · Cited by 21
MDMX acidic domain inhibits p53 DNA binding in vivo and regulates tumorigenesis
Huang, Q., Chen, L., Yang, L., Xie, X., Gan, L., Cleveland, J. L., & Chen, J. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1719090115 · Cited by 21

Authors: Jones, S. N., Roe, A. E., Donehower, L. A., & Bradley, A.
Affiliations: Howard Hughes Medical Institute (US)
Baylor College of Medicine (US)
ORCID: Bradley, Allan
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1995-11
Volume: 378
Issue: 6553
Pages: 206-208
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/378206a0
OpenAlex: W1993864973
Semantic Scholar: efc84bf5f5d1747443a3eb4555f9b5ede31b368f
Cited by: 1,280
References: 24
Citations by year: 2026: 9 · 2025: 17 · 2024: 30 · 2023: 31 · 2022: 28 · 2021: 35 · 2020: 41 · 2019: 28 · 2018: 31 · 2017: 38 · 2016: 54 · 2015: 34 · 2014: 59 · 2013: 30 · 2012: 60
FWCI: 14.50
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Keywords: MDM2, p53, embryonic lethality, developmental regulation, tumor suppressor, sarcoma, leukemia
MeSH terms: Proto-Oncogene Mas, Animals, Base Sequence, Cell Cycle, Cell Line, Crosses, Genetic, Female, Embryonic and Fetal Development, Genes, Lethal, Molecular Sequence Data, Mutation, Nuclear Proteins, Proto-Oncogene Proteins, Tumor Suppressor Protein p53, 3T3 Cells, DNA Primers, Gene Targeting, Mice, Proto-Oncogene Proteins c-mdm2

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Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53

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