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

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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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BackgroundSelf-citation
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Sayin, V. I., Khan, O. M., Pehlivanoglu, L. E., Staffas, A., Ibrahim, M. X., Asplund, A., Ågren, P., Nilton, A., Bergström, G. M. L., Bergö, M. O., et al. (2014) · Circulation Research · doi:10.1161/circresaha.115.304992 · Cited by 48
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Nishii, K., Tsuzuki, T., Kumai, M., Takeda, N., Koga, H., Aizawa, S., Nishimoto, T., & Shibata, Y. (1999) · Genes to Cells · doi:10.1046/j.1365-2443.1999.00256.x · Cited by 45
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Buschmann, T., Lin, Y., Aithmitti, N., Fuchs, S. Y., Lu, H., Resnick‐Silverman, L., Manfredi, J. J., Ronai, Z. A., & Wu, X. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007955200 · Cited by 43
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Parant, J. M., & Lozano, G. (2003) · Human Mutation · doi:10.1002/humu.10186 · Cited by 47
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Small molecules that bind the Mdm2 RING stabilize and activate p53
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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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