Cited by 521Cancer-related Molecular PathwaysCell death mechanisms and regulationUbiquitin and proteasome pathways

The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.

Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53

Parant, John, Chavez-Reyes, Arturo, Little, Natalie A., Yan, Wen, Reinke, Valerie, Jochemsen, Aart G., Lozano, Guillermina·2001·Nature Genetics

DOI 10.1038/ng714

Open this paper in CoChat — free account

Abstract

The p53 protein can inhibit cell cycling or induce apoptosis, and is thus a critical regulator of tumorigenesis. This protein is negatively regulated by a physical interaction with MDM2, an E3 ubiquitin ligase. This interaction is critical for cell viability; loss of Mdm2 causes cell death in vitro and in vivo in a p53-dependent manner. The recently discovered MDM2-related protein MDM4 (also known as MDMX) has some of the same properties as MDM2. MDM4 binds and inhibits p53 transcriptional activity in vitro. Unlike MDM2, however, MDM4 does not cause nuclear export or degradation of p53 (refs. 9,10). To study MDM4 function in vivo, we deleted Mdm4 in mice. Mdm4-null mice died at 7.5-8.5 dpc, owing to loss of cell proliferation and not induction of apoptosis. To assess the importance of p53 in the death of Mdm4-/- embryos, we crossed in the Trp53-null allele. The loss of Trp53 completely rescued the Mdm4-/- embryonic lethality. Thus, MDM2 and MDM4 are nonoverlapping critical regulators of p53 in vivo. These data define a new pathway of p53 regulation and raise the possibility that increased MDM4 levels and the resulting inactivation of p53 contribute to the development of human tumors.

Integrity signals

Registry

Crossref · 10.1038/ng714

Cites

19 of 19 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation.
Gavrieli, Y., Sherman, Y., & Ben-Sasson, S. A. (1992) · The Journal of cell biology · doi:10.1083/jcb.119.3.493 · Cited by 9,444
Surfing the p53 network
Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607 · cited 1×
“gif" NDATA ITEM> ]> The p53 protein can inhibit cell cycling or induce apoptosis, and is thus a critical regulator of tumorigenesi”
Background
Mdm2 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 1×
“This protein is negatively regulated by a physical interaction with MDM2, an E3 ubiquitin ligas”
Background
Tumor spectrum analysis in p53-mutant mice
Jacks, T., Remington, L., Williams, B. O., Schmitt, E. M., Halachmi, S., Bronson, R. T., & Weinberg, R. A. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00002-6 · Cited by 2,051
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
The Wnt-1 (int-1) proto-oncogene is required for development of a large region of the mouse brain
McMahon, A. P., & Bradley, A. (1990) · Cell · doi:10.1016/0092-8674(90)90385-r · Cited by 1,540
Oncoprotein MDM2 conceals the activation domain of tumour suppressor p53
Oliner, J. D., Pietenpol, J. A., Thiagalingam, S., Gyuris, J., Kinzler, K. W., & Vogelstein, B. (1993) · Nature · doi:10.1038/362857a0 · Cited by 1,474
Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
de Oca Luna, R. M., Wagner, D. S., & Lozano, G. (1995) · Nature · doi:10.1038/378203a0 · Cited by 1,420 · cited 1×
“This interaction is critical for cell viability; loss of Mdm2 causes cell death in vitro and in vivo in a p53-dependent manne”
BackgroundSelf-citation
Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
Jones, S. N., Roe, A. E., Donehower, L. A., & Bradley, A. (1995) · Nature · doi:10.1038/378206a0 · Cited by 1,280 · cited 1×
“This interaction is critical for cell viability; loss of Mdm2 causes cell death in vitro and in vivo in a p53-dependent manne”
Background

Flagged first, then by citations

Show all 19 references

Sorted by citations

Items 401–500 of 521

MDM2/P53 Inhibitors as Sensitizing Agents for Cancer Chemotherapy
Zhu, Y. Y., Wang, H., & Thuraisamy, A. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816435-8.00015-8 · Cited by 7
MDMX is essential for the regulation of p53 protein levels in the absence of a functional MDM2 C-terminal tail
Sanford, J. D., Yang, J., Han, J., Tollini, L. A., Jin, A., & Zhang, Y. (2021) · BMC Molecular and Cell Biology · doi:10.1186/s12860-021-00385-3 · Cited by 7
Modelling the p53 gene regulatory network.
Brewer, D. S. (2006) · OpenGrey (Institut de l'Information Scientifique et Technique) · Cited by 7
Targeting mutant p53 in cancer: from mechanistic insights to therapeutic strategies
Wu, H. H., Leng, S., Eisenstat, D. D., Sergi, C. M., & Leng, R. P. (2026) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-026-00907-x · Cited by 6
MDMX elevation by a novel Mdmx–p53 interaction inhibitor mitigates neuronal damage after ischemic stroke
Yan, H., Sasaki, T., Kanki, H., Hirata, Y., Nishiyama, K., Hisada, S., Matsumura, S., Nagaoka, Y., Sumiyoshi, T., Nagano, S., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-25427-4 · Cited by 6
Maternal exposure to deltamethrin during pregnancy and lactation impairs hippocampal learning and memory function of male offspring by ferroptosis
Huang, S., Li, W., Wang, D., Feng, H., Wang, B., Dong, X., Zhao, W., Liu, D., & Wang, Y. (2025) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2025.117729 · Cited by 7
MDMX/MDM4 is highly expressed and contributes to cell growth and survival in anaplastic large cell lymphoma
Sinatkas, V., Σταθοπούλου, Κ., Xagoraris, I., Ye, J., Vyrla, D., Atsaves, V., Leventaki, V., Medeiros, L. J., Rassidakis, G. Z., & Drakos, E. (2021) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428194.2021.1876871 · Cited by 6
Cryptic in vitro ubiquitin ligase activity of HDMX towards p53 is probably regulated by an induced fit mechanism
Calderón-González, K. G., Medina‐Medina, I., Hároníková, L., Hernychová, L., Bonczek, O., Uhrík, L., Hrabal, V., Vojtěšek, B., Fåhræus, R., Hernández‐Monge, J., et al. (2022) · Bioscience Reports · doi:10.1042/bsr20220186 · Cited by 6
FAM193A is a positive regulator of p53 activity
Szwarc, M. M., Guarnieri, A. L., Joshi, M., Duc, H. N., Laird, M. C., Pandey, A., Khanal, S., Dohm, E., Bui, A. K., Sullivan, K. D., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112230 · Cited by 6
p53 Activity Dominates That of p73 upon Mdm4 Loss in Development and Tumorigenesis
Tashakori, M., Zhang, Y., Xiong, S., You, M. J., & Lozano, G. (2015) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-15-0346 · Cited by 6
Self-citation
The DNA Damage Response Mediates Apoptosis and Tumor Suppression
Baran, K., Rodríguez, D. A., & Green, D. R. (2013) · Springer eBooks · doi:10.1007/978-1-4614-9302-0_7 · Cited by 6
MDMX is a prognostic factor for non-small cell lung cancer and regulates its sensitivity to cisplatin
Zhao, H., Xie, Y., Xing, R., Sun, M., Chi, F., & Zeng, Y. (2017) · Cellular Oncology · doi:10.1007/s13402-017-0325-9 · Cited by 6
Contemplations on MDMX (MDM4) driving triple negative breast cancer circulating tumor cells and metastasis
Gao, C., Xiao, G., & Bargonetti, J. (2019) · Oncotarget · doi:10.18632/oncotarget.27134 · Cited by 6
Activating p53 function by targeting RLIP
Singhal, S. S., Horne, D. A., Singhal, J., Awasthi, S., & Salgia, R. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2021.188512 · Cited by 5
Therapeutic considerations for Mdm2: not just a one trick pony
Lehman, J. A., Eitel, J. A., Batuello, C. N., & Mayo, L. D. (2008) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.3.11.1309 · Cited by 6
MDM2: RING Finger Protein and Regulator of p53
Wu, L., & Maki, C. G. (2005) · Springer eBooks · doi:10.1007/0-387-27421-9_34 · Cited by 4
p53 E3 ubiquitin protein ligase homolog regulates p53 in vivo in the adult mouse eye lens.
Jaramillo‐Rangel, G., Ortega‐Martínez, M., Sepúlveda‐Saavedra, J., Cárdenas, O. S., & Montes‐de‐Oca‐Luna, R. (2013) · Europe PMC (PubMed Central) · Cited by 4
The MDM2/MDMX/p53 axis in the adaptive stress response
Wang, B., Rasmussen-Ivey, C. R., Little, J. B., & Yuan, Z.-M. (2020) · Translational Cancer Research · doi:10.21037/tcr.2019.12.89 · Cited by 4
MDMX under stress: the MDMX-MDM2 complex as stress signals hub
de Polo, A., Vivekanandan, V., Little, J. B., & Yuan, Z.-M. (2016) · Translational Cancer Research · doi:10.21037/tcr.2016.12.18 · Cited by 4
Endogenous p53 inhibitor TIRR dissociates systemic metabolic health from oncogenic activity
Tsaousidou, E., Chrzanowski, J., Drané, P., Lee, G. Y., Bahour, N., Wang, Z. B., Deng, S., Cao, Z., Huang, K., He, Y. J., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114337 · Cited by 4
Ubiquitin Family Members in the Regulation of the Tumor Suppressor p53
Xirodimas, D. P., & Scheffner, M. (2010) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4419-6676-6_10 · Cited by 5
Caspase-dependent degradation of MDMx/MDM4 cell cycle regulatory protein in amyloid β-induced neuronal damage
Colacurcio, D. J., Zyskind, J. W., Jordan‐Sciutto, K. L., & Akay, C. (2015) · Neuroscience Letters · doi:10.1016/j.neulet.2015.10.031 · Cited by 4
HDM2 and HDMX Proteins in Human Cancer
Hároníková, L., & Vojtěšek, B. (2018) · Klinicka onkologie · doi:10.14735/amko20182s63 · Cited by 4
Unraveling the mechanisms of glioblastoma’s resistance: investigating the influence of tumor suppressor p53 and non-coding RNAs
Alshammari, Q. A., Alshammari, S. O., Alshammari, A., Alfarhan, M., & Baali, F. H. (2024) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-024-03564-z · Cited by 3
Dissociating the metabolic and tumor-suppressive activity of p53
Sakurai, Y., Kubota, N., & Kadowaki, T. (2024) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2024.07.018 · Cited by 3
Targeting the MDM2–p53 Protein–Protein Interaction
Hardcastle, I. R. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-396521-9.00013-9 · Cited by 3
RING Fingers and Relatives: Determinators of Protein Fate
Lorick, K. L., Tsai, Y. C., Yang, Y., & Weissman, A. M. (2007) · Wiley eBooks · doi:10.1002/9783527619320.ch4 · Cited by 3
Chromosome instability and tumor lethality suppression in carcinogenesis
Shen, C., Zhou, Y., Zhan, J., Reske, S. N., & Buck, A. K. (2008) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21937 · Cited by 3
Characterization of the E3 Ubiquitin Ligase Pirh2
Tai, E. (2010) · TSpace (University of Toronto) · Cited by 3
Long-Read MDM4 Sequencing Reveals Aberrant Isoform Landscape in Metastatic Melanomas
Patrick, N., & Markey, M. P. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25179415 · Cited by 2
Burkitt’s Lymphoma and Early B Cell Transformation as Paradigms of How Epstein-Barr Virus Overcomes Apoptosis and Ferroptosis
Bornkamm, G. W., Kelly, G. L., & Ross, A. M. (2025) · Current topics in microbiology and immunology · doi:10.1007/82_2025_301 · Cited by 2
p53: defender of lineage fidelity and foe of plasticity in cancer and regeneration
Attardi, L. D., & Rajeevan, A. (2026) · Trends in cancer · doi:10.1016/j.trecan.2026.02.004 · Cited by 2
Regulation of p53 Activity and Associated Checkpoint Controls
Post, S. M., Quintás‐Cardama, A., & Lozano, G. (2009) · Humana Press eBooks · doi:10.1007/978-1-60761-178-3_11 · Cited by 2
Self-citation
Cooperation between MDM2 and MDMX in the Regulation of p53
Blaydes, J. P. (2010) · Molecular biology intelligence unit · doi:10.1007/978-1-4419-8231-5_6 · Cited by 2
Suppression of the mouse double minute 4 gene causes changes in cell cycle control in a human mesothelial cell line responsive to ultraviolet radiation exposure
Bunderson‐Schelvan, M., Erbe, A. K., Schwanke, C. M., & Pershouse, M. A. (2009) · Environmental and Molecular Mutagenesis · doi:10.1002/em.20498 · Cited by 2
The p53-Mdm2 Loop: A Critical Juncture of Stress Response
Levav-Cohen, Y., Goldberg, Z., Alsheich-Bartok, O., Zuckerman, V., Haupt, S., & Haupt, Y. (2010) · Molecular biology intelligence unit · doi:10.1007/978-1-4419-8231-5_5 · Cited by 2
Murine double minute X plays a central role in leukemic transformation and may be a promising target for leukemia prevention strategies
Ueda, K. (2023) · Experimental Hematology · doi:10.1016/j.exphem.2023.04.001 · Cited by 2
Novel p53-Based Therapies: Strategies and Future Prospects
Laı́n, S., & Lane, D. P. (2005) · Springer eBooks · doi:10.1007/978-1-4020-2922-6_16 · Cited by 2
Oncogenic and teratogenic effects of Trp53Y217C, an inflammation-prone mouse model of the human hotspot mutant TP53Y220CPreprint
Jaber, S., Eldawra, E., Rakotopare, J., Simeonova, I., Lejour, V., Gabriel, M., Cañeque, T., Volochtchouk, V., Licaj, M., Fajac, A., et al. (2024) · eLife · doi:10.7554/elife.102434 · Cited by 2
Cancer-associated MDM2 W329G mutant attenuates ribosomal stress-mediated p53 responses to promote cell survival and glycolysis
Lien, S. (2024) · American Journal of Cancer Research · doi:10.62347/qifc4021 · Cited by 1
MDM4 haploinsufficiency leads to p53-mediated bone marrow failure
Sharma, R., Bhoopalan, S. V., Meyer, R., Han, L., Beesetti, S., Liu, N., Singh, P., Palmer, L., Hansen, B. S., Khiami, M., et al. (2026) · Blood · doi:10.1182/blood.2024027180 · Cited by 1
Oncogenic and teratogenic effects of Trp53Y217C, an inflammation-prone mouse model of the human hotspot mutant TP53Y220C
Jaber, S., Eldawra, E., Rakotopare, J., Simeonova, I., Lejour, V., Gabriel, M., Cañeque, T., Volochtchouk, V., Licaj, M., Fajac, A., et al. (2025) · eLife · doi:10.7554/elife.102434.3 · Cited by 1
MDM2 and MDMX Regulators of p53 Activity
Momand, J. A., Aspuria, P. J., & Furuta, S. (2007) · Springer eBooks · doi:10.1007/0-387-30127-5_7 · Cited by 1
“The 10th International MDM2 Workshop”: Opening up new avenues for MDM2 and p53 research, the First International MDM2 Workshop in Asia
Ohki, R., Itahana, K., & Iwakuma, T. (2024) · Genes to Cells · doi:10.1111/gtc.13114 · Cited by 1
Complex regulation of Forkhead Box O transcription factors
van den Berg, M. C. W. (2013) · Utrecht University Repository (Utrecht University) · Cited by 1
The p53-p21 axis plays a central role in lymphatic homeostasis and diseasePreprint
Mylavarapu, R., Kulikauskas, M. R., Dierkes, C., Sobhani, N., Mangette, M., Finlon, J. M., Stevens, W., Arbab, F., Box, N. F., Lovell, M. A., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.18.992784 · Cited by 1
All activated signaling pathways lead to anaplastic large cell lymphoma (ALCL)
Bonzheim, I., & Quintanilla‐Martínez, L. (2021) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428194.2021.1924373 · Cited by 1
Targeting HAUSP: Killing Two Birds with One Stone
Brooks, C. L., & Gu, W. J. (2009) · Springer eBooks · doi:10.1007/978-0-387-69147-3_3
Targeting the Cell Cycle and p53 in Combination with BRAF-Directed Therapy
Han, D., & Smalley, K. S. M. (2014) · Cancer drug discovery and develogment/Cancer drug discovery and development · doi:10.1007/978-1-4939-2143-0_7
Genetic Control of Susceptibility to Testicular Cancer
Lam, M.-Y. (2005) · OhioLink ETD Center (Ohio Library and Information Network)
Tumor suppressor p53 and transcriptional changes in cellular stress responses to UV radiation
Latonen, L. (2003) · Työväentutkimus Vuosikirja
THE CONSEQUENCES OF DISRUPTING THE MDM2-P53 BALANCE IN HEMATOPOIESIS
Abbas, H. A. (2010)
Regulation of the p53 Tumor‐Suppressor Protein by Ubiquitin and Ubiquitin‐Like Molecules
Xirodimas, D. P. (2007) · Wiley eBooks · doi:10.1002/9783527619320.ch2c
Expression levels of MDM2 and MDMX proteins and their associated effects on P53 in human liposarcomas
Touqan, N. (2014) · UPT. Syiah Kuala University Library (Syiah Kuala University)
Ubiquitin-specific Protease 7 Plays a Critical Role in Control of Lytic Infection and Cell Transformation by Human Adenovirus Type 5
Koyuncu, E. (2009)
Modulation of p53 activities by the prolyl-isomerase PIN1 and the bromodomain protein BRD7
Tocco, F. (2008) · OpenstarTs (Univeristy of Trieste https://www.units.it/)
Molecular mechanisms of growth suppression by pharmacologically activated p53
Hedström, E. (2009) · Figshare
THE NOVEL UPSTREAM REGULATOR OF FBXW7
Shin, J. (2014) · Digital Commons-TMC (Texas Medical Center)
Modulation of p53's transcriptional function by small molecules
Nikulenkov, F. (2011) · Figshare
Analysis of p53 and c-MYC, two key transcription factors involved in tumorigenesis
Jung, P. (2008) · doi:10.5282/edoc.10559
Modification of MDMX by Ubiquitination and Sumoylation
Pan, Y. (2005) · Digital Commons - University of South Florida (University of South Florida)
Assessment of therapeutic targets in experimental models of Myc-induced lymphoma
Forshell, L. P. (2011)
Novel Role of CHK2 in the Intrinsic and Extrinsic Apoptosis Pathway
Agarwal, A. (2014) · Open Scholarship Institutional Repository (Washington University in St. Louis) · doi:10.7936/k7ng4nnv
p53 and DNA damage checkpoint responses in the human prostate
af Hällström, T. (2007)
Pharmacological targeting of mutant p53 family members
Rökaeus, N. (2011) · Figshare
The role of p53 in normal development and teratogen-induced apoptosis and birth defects in mouse embryos
Hosako, H. (2009) · OakTrust (Texas A&M University Libraries)
Loss of Tumor Suppressor RPL5/RPL11 Does Not Induce Cell-Cycle Arrest, but Impedes Proliferation Due to Reduced Ribosome Content and Translation Capacity: Implications in Diamond Blackfan Anemia
Teng, T. (2013) · OhioLink ETD Center (Ohio Library and Information Network)
IN VIVO SIGNIFICANCE OF THE MDM4 AND P73 INTERACTION DURING DEVELOPMENT AND TUMORIGENESIS
Tashakori, M. (2015) · Digital Commons-TMC (Texas Medical Center)
Characterization of the Ubiquitin/Nedd8 E3 ligase activity of the Mdm2/MdmX complex
Singh, R. K. (2007) · Kölner Universitäts PublikationsServer (Universität zu Köln)
A regulatory network of Mdm2 and members of the Polycomb Group (PcG) family
Wienken, M. M. (2016) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-5475
Study of MicroRNA-34a mediated post transcriptional regulation of MDM4
Mandke, P. (2012) · Journal of Bioresource Management
Progress and Prospects in Ocular Gene Therapy
Liu, X., Rasmussen, C. A., Bennett, J., Brandt, C. R., Gabelt, B. T., & Kaufman, P. L. (2008) · Elsevier eBooks · doi:10.1016/b978-012370585-3.50020-0
Longevity Assurance by Genome Maintenance
Hasty, P., Suh, Y., & Vijg, J. (2013) · CRC Press eBooks · doi:10.1201/b14587-3
p53 Tumor Suppressor Opens Gateways for Cancer Therapy
Dai, M., Gallegos, J. R., & Lu, H. (2008) · CRC Press eBooks · doi:10.1201/9780849387999.ch48
Exploring Chromatin-bound MDM2 Functions in Compromised Transcriptional Regulation of p53 Target Genes
Rosso, M. (2015) · CUNY Academic Works (City University of New York)
Transcriptional regulation of LAMB3 by p53
Jani, M. (2008) · CORE Scholar (Wright State University)
Structural and Functional Characterization of the Human Mdm2 and MdmX RING Domains
Egorova, O. (2014) · YorkSpace (York University)
An investigation of mutant p53 function.
Noll, J. E. (2011) · Adelaide Research & Scholarship (AR&S) (University of Adelaide)
Towards the Investigation of the Effects of Nitration on the Activity of the Human p53 Tumour Suppressor Protein. Nitration of the p53 Tumour Suppressor Protein
Husaini, R. (2014) · Bradford Scholars (University of Bradford)
Understanding p53 structure and targeting mutant p53 for improved cancer therapy
Zhang, Q. (2018) · Figshare
Estudo do efeito da remediação simultânea dos genes p16INK4a e p53 mediada pelo adenovírus bicistrônico Adp16IRESp53 em um modelo de carcinoma de pulmão humano.
Gregorio, J. C. (2019) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.87.2019.tde-22022010-115327
The role of P53 signaling pathway in aging and cancer
Zhao, Y. (2018) · doi:10.7282/t3-bzph-0b44
In Vivo Discoveries in MDM2-Mediated p53 Regulation
Tackmann, N. R. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/z7ta-7m83
Pharmacokinetic Study of Novel Anthraquinone Analogues
Guo, Y. (2019)
Hit-to-lead optimization of pharmaceutical interesting tryptophanol-derived scaffolds
Barcherini, V. (2016) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)
Characterization of synthetic lethality between Mdm2 overexpression and genotoxic agents and identification of a novel function of the Mdmx oncogene in DNA repair
Carrillo, A. M. (2014)
MdmX Regulates Mitotic Spindle Polarity of Human Breast Cancer Cells
Woods, K. (2013) · Digital WPI
A Novel Intramolecular Interaction in P53
He, F. (2020) · Digital Commons - University of South Florida (University of South Florida)
Regulation of the p53 Tumor‐Suppressor Protein by Ubiquitin and Ubiquitin‐Like Molecules
Xirodimas, D. P. (2007) · Wiley eBooks · doi:10.1002/9783527620234.ch2
The role of microRNAs in the p53 tumor suppressor pathway
Zhang, X. (2011) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3171
MDM4 (Murine Double Minute 4)
Huang, A., Yang, E., & Kurokawa, M. (2016) · Springer eBooks · doi:10.1007/978-1-4614-6438-9_101575-1
MDM4 (Murine Double Minute 4)
Huang, A., Yang, E., & Kurokawa, M. (2017) · Springer eBooks · doi:10.1007/978-3-319-67199-4_101575
Data from RING Domain–Mediated Interaction Is a Requirement for MDM2's E3 Ligase Activity
Kawai, H., Lopez-Pajares, V., Kim, M. M., Wiederschain, D., & Yuan, Z.-M. (2023) · doi:10.1158/0008-5472.c.6495950
Data from RING Domain–Mediated Interaction Is a Requirement for MDM2's E3 Ligase Activity
Kawai, H., Lopez-Pajares, V., Kim, M. M., Wiederschain, D., & Yuan, Z.-M. (2023) · doi:10.1158/0008-5472.c.6495950.v1
Data from Alteration of MDM2 by the Small Molecule YF438 Exerts Antitumor Effects in Triple-Negative Breast Cancer
Shan, P., Yang, F., Qi, H., Hu, Y., Zhu, S., Sun, Z., Zhang, Z., Wang, C., Hou, C., Yu, J., et al. (2023) · doi:10.1158/0008-5472.c.6513258.v1
Data from Spontaneous Tumorigenesis in Mice Overexpressing the p53-Negative Regulator Mdm4
Xiong, S., Pant, V., Suh, Y., Pelt, C. S. V., Wang, Y., Valentin-Vega, Y. A., Post, S. M., & Lozano, G. (2023) · doi:10.1158/0008-5472.c.6500723
Self-citation
Data from High-Resolution Array-Based Comparative Genomic Hybridization of Bladder Cancers Identifies Mouse Double Minute 4 (MDM4) as an Amplification Target Exclusive of MDM2 and TP53
Veerakumarasivam, A., Scott, H. E., Chin, S., Warren, A. Y., Wallard, M. J., Grimmer, D., Ichimura, K., Caldas, C., Collins, V. P., Neal, D. E., et al. (2023) · doi:10.1158/1078-0432.c.6516990
Data from High-Resolution Array-Based Comparative Genomic Hybridization of Bladder Cancers Identifies Mouse Double Minute 4 (MDM4) as an Amplification Target Exclusive of MDM2 and TP53
Veerakumarasivam, A., Scott, H. E., Chin, S., Warren, A. Y., Wallard, M. J., Grimmer, D., Ichimura, K., Caldas, C., Collins, V. P., Neal, D. E., et al. (2023) · doi:10.1158/1078-0432.c.6516990.v1
Germ cell tumor treatment resistance and liquid biopsy-based microRNA biomarkers
Timmerman, D. M. (2024) · Utrecht University Repository (Utrecht University) · doi:10.33540/2055
Hdm2 disrupts HdmX-mediated nuclear export of p53 by sequestering it in nucleus
Ni, Y., Chen, H., Cheng, X., Sun, B., Wu, Z., Zhan, Q., & Zhuang, Z. (2024) · Experimental Cell Research · doi:10.1016/j.yexcr.2024.114185

Authors: Parant, J., Chavez-Reyes, A., Little, N. A., Yan, W., Reinke, V., Jochemsen, A. G., & Lozano, G.
Affiliations: The University of Texas MD Anderson Cancer Center (US)
Leiden University Medical Center (NL)
Corresponding author: Lozano, Guillermina
ORCID: Parant, John
Yan, Wen
Reinke, Valerie
Jochemsen, Aart G.
Lozano, Guillermina
Venue: Nature Genetics
Publisher: Springer Science and Business Media LLC
Published: 2001-08-20
Volume: 29
Issue: 1
Pages: 92-95
ISSN: 1061-4036 (ISSN-L)
1546-1718
DOI: 10.1038/ng714
OpenAlex: W1598779357
Cited by: 517
References: 19
Citations by year: 2026: 4 · 2025: 8 · 2024: 15 · 2023: 15 · 2022: 13 · 2021: 20 · 2020: 20 · 2019: 14 · 2018: 15 · 2017: 22 · 2016: 34 · 2015: 14 · 2014: 35 · 2013: 18 · 2012: 23
FWCI: 7.94
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Genetics (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: MDM4, MDM2, p53 regulation, Trp53, embryonic lethality, cell proliferation, E3 ubiquitin ligase, tumor suppressor, p53 inactivation
MeSH terms: Animals, Base Sequence, Embryo, Mammalian, Genes, Lethal, Nuclear Proteins, Precipitin Tests, Proto-Oncogene Proteins, Blotting, Western, Polymerase Chain Reaction, Genes, p53, Tumor Suppressor Protein p53, DNA Primers, Mice, Knockout, In Situ Nick-End Labeling, Mice, Proto-Oncogene Proteins c-mdm2

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

Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks