MDMX: from bench to bedside
Open accessAbstract
The tumor suppressor protein p53 is negatively regulated by Mdm2, a ubiquitin ligase protein that targets p53 for degradation. Mdmx (also known as Mdm4) is a relative of Mdm2 that was identified on the basis of its ability to physically interact with p53. An increasing body of evidence, including recent genetic studies, suggests that Mdmx also acts as a key negative regulator of p53. Aberrant expression of MDMX could thus contribute to tumor formation. Indeed, MDMX amplification and/or overexpression occurs in several diverse tumors. Strikingly, recent work identifies MDMX as a specific chemotherapeutic target for treatment of retinoblastoma. Specific MDMX antagonists should therefore be developed as a tool to ensure activation of `dormant' p53 activity in tumors that retain wild-type p53.
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Mdmx is overexpressed in many human malignancies and, together with Mdm2, negatively regulates the p53 tumor suppressor.
“The oncogene Mdmx is overexpressed in many human malignancies, and together with Mdm2, negatively regulates the p53 tumor suppressor.”
From Mdmx promotes genomic instability independent of p53 and Mdm2 (2015) · cites this paper as [25]
Mdmx negatively regulates p53 by inhibiting p53 transcriptional activity rather than by promoting p53 degradation through ubiquitination.
“While Mdmx negatively regulates p53, it does so through inhibiting p53 transcriptional activity rather than promoting p53 degradation through ubiquitination, as is the case for Mdm2.24,25”
From Mdmx promotes genomic instability independent of p53 and Mdm2 (2015) · cites this paper as [25]
Mdmx regulates p53.
“While it is clear Mdmx regulates p53,25,43”
From Mdmx promotes genomic instability independent of p53 and Mdm2 (2015) · cites this paper as [25]
Mdmx can regulate p53 independently of Mdm2.
“it is known that Mdmx can regulate p53 independent of Mdm2.25,43”
From Mdmx promotes genomic instability independent of p53 and Mdm2 (2015) · cites this paper as [25]
During development, p53 is the main cellular target of both Mdm2 and Mdmx.
“Genetic analyses demonstrate that the major cellular target (at least in development) for both Mdm2 and Mdmx is p53 [49].”
From The p53 orchestra: Mdm2 and Mdmx set the tone (2010) · cites this paper as [49]
Modifications of Mdm2 and Mdmx triggered by damage make these proteins less stable and cause their breakdown, which lowers their capacity to oppose p53.
“In vitro and in vivo studies show that damage-induced modifications of Mdm2 and Mdmx lead to their destabilization and degradation, reducing their ability to antagonize p53 [49,50].”
From The p53 orchestra: Mdm2 and Mdmx set the tone (2010) · cites this paper as [49]
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Cites
WAF1, a potential mediator of p53 tumor suppression
El-Deiry, W. S., Tokino, T., Velculescu, V. E., Levy, D. B., Parsons, R., Trent, J. M., Lin, D., Mercer, W. E., Kinzler, K. W., & Vogelstein, B. (1993) · Cell · doi:10.1016/0092-8674(93)90500-p · Cited by 8,321 · see citing works
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 · see citing works
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 · see citing works
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× · see citing works
“Mdm2 is a RING-finger-containing protein that acts as an E3 ligase, which is essential for ubiquitylation and subsequent degradation of p53 (Haupt et al., 1997; Kubbutat et al., 1997).”
BackgroundLive or let die: the cell's response to p53
Vousden, K. H., & Lü, X. (2002) · Nature reviews. Cancer · doi:10.1038/nrc864 · Cited by 3,177 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
The RB and p53 pathways in cancer
Sherr, C. J., & McCormick, F. (2002) · Cancer Cell · doi:10.1016/s1535-6108(02)00102-2 · Cited by 1,690 · see citing works
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× · see citing works
“Mdm2-deficient mice die very early in development prior to implantation, whereas mice lacking both p53 and Mdm2 are viable and indistinguishable from mice lacking only p53 (Montes de Oca Luna et al., 1995; Jones et al., 1995).”
Backgroundmdm2 expression is induced by wild type p53 activity.
Barak, Y., Juven, T., Haffner, R., & Oren, M. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05678.x · Cited by 1,290 · see citing works
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× · see citing works
“Mdm2-deficient mice die very early in development prior to implantation, whereas mice lacking both p53 and Mdm2 are viable and indistinguishable from mice lacking only p53 (Montes de Oca Luna et al., 1995; Jones et al., 1995).”
BackgroundPirh2, a p53-Induced Ubiquitin-Protein Ligase, Promotes p53 Degradation
Leng, R. P., Lin, Y., Ma, W., Wu, H., Lemmers, B., Chung, S., Parant, J. M., Lozano, G., Hakem, R., & Benchimol, S. (2003) · Cell · doi:10.1016/s0092-8674(03)00193-4 · Cited by 717 · see citing works
The ubiquitin ligase COP1 is a critical negative regulator of p53
Dornan, D., Wertz, I. E., Shimizu, H., Arnott, D. P., Frantz, G. D., Dowd, P., Rourke, K. O., Koeppen, H., & Dixit, V. M. (2004) · Nature · doi:10.1038/nature02514 · Cited by 700 · see citing works
A dynamic role of HAUSP in the p53-Mdm2 pathway
Li, M., Brooks, C. L., Kon, N., & Gu, W. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00157-1 · Cited by 679 · see citing works
Sherr, C. J., & Weber, J. D. (2000) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(99)00038-6 · Cited by 654 · see citing works
MDMX: a novel p53‐binding protein with some functional properties of MDM2.
Shvarts, A., Steegenga, W. T., Riteco, N., van Laar, T., Dekker, P., Bazuine, M., van Ham, R. C., van der Houven van Oordt, W., Hateboer, G., van der Eb, A. J., et al. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00919.x · Cited by 648 · see citing works
Self-citationKortlever, R. M., Higgins, P. J., & Bernards, R. (2006) · Nature Cell Biology · doi:10.1038/ncb1448 · Cited by 637 · cited 2× · see citing works
“Key targets are the proapoptotic genes Bax, Puma and Noxa (Michalak et al., 2005), the genes encoding the cell cycle regulators p21 (el-Deiry et al., 1993) and Ptprv (Doumont et al., 2005) and the senescence-inducing gene Plasminogen activator inhibitor 1 (Kortlever et al., 2006).”
BackgroundInactivation of the p53 pathway in retinoblastoma
Laurie, N. A., Donovan, S. L., Shih, C.-S., Zhang, J., Mills, N., Fuller, C., Teunisse, A., Lam, S., Ramos, Y., Mohan, A., et al. (2006) · Nature · doi:10.1038/nature05194 · Cited by 595 · see citing works
Self-citationMdm2-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 · see citing works
ARF-BP1/Mule Is a Critical Mediator of the ARF Tumor Suppressor
Chen, D., Kon, N., Li, M., Zhang, W., Qin, J., & Gu, W. J. (2005) · Cell · doi:10.1016/j.cell.2005.03.037 · Cited by 539 · see citing works
Parant, J., Chavez-Reyes, A., Little, N. A., Yan, W., Reinke, V., Jochemsen, A. G., & Lozano, G. (2001) · Nature Genetics · doi:10.1038/ng714 · Cited by 517 · see citing works
Self-citationAccelerated MDM2 auto‐degradation induced by DNA‐damage kinases is required for p53 activation
Stommel, J. M., & Wahl, G. M. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600145 · Cited by 386 · see citing works
Disruption of HAUSP gene stabilizes p53.
Cummins, J. M., Rago, C., Kohli, M., Kinzler, K. W., Lengauer, C., & Vogelstein, B. (2004) · Nature · doi:10.1038/nature02501 · Cited by 379 · see citing works
Langheinrich, U., Hennen, E., Stott, G. M., & Vacun, G. (2002) · Current Biology · doi:10.1016/s0960-9822(02)01319-2 · Cited by 368 · see citing works
HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53
Linares, L. K., Hengstermann, A., Ciechanover, A., Müller, S., & Scheffner, M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2030930100 · Cited by 361 · see citing works
CAHILLY, L. A., Yang‐Feng, T. L., Francke, U., & George, D. L. (1987) · Somatic Cell and Molecular Genetics · doi:10.1007/bf01535205 · Cited by 355 · see citing works
Keeping p53 in check: essential and synergistic functions of Mdm2 and Mdm4
Marine, J.-C., Francoz, S., Maetens, M., Wahl, G., Toledo, F., & Lozano, G. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401912 · Cited by 352 · see citing works
Self-citationMDM2 interacts with MDMX through their RING finger domains
Tanimura, S., Ohtsuka, S., Mitsui, K., Shirouzu, K., Yoshimura, A., & Ohtsubo, M. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00254-9 · Cited by 324 · see citing works
Migliorini, D., Denchi, E. L., Danovi, D., Jochemsen, A., Capillo, M., Gobbi, A., Helin, K., Pelicci, P. G., & Marine, J.-C. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.15.5527-5538.2002 · Cited by 313 · see citing works
Self-citationDanovi, D., Meulmeester, E., Pasini, D., Migliorini, D., Capra, M., Frenk, R., de Graaf, P., Francoz, S., Gasparini, P., Gobbi, A., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.13.5835-5843.2004 · Cited by 310 · see citing works
Self-citationHowes, K. A., Ransom, N. L., Papermaster, D. S., Lasudry, J., Albert, D. M., & Windle, J. J. (1994) · Genes & Development · doi:10.1101/gad.8.11.1300 · Cited by 298 · see citing works
Stabilization of the MDM2 Oncoprotein by Interaction with the Structurally Related MDMX Protein
Sharp, D. A., Kratowicz, S. A., Sank, M. J., & George, D. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.53.38189 · Cited by 286 · see citing works
Repression of p53-mediated transcription by MDM2: a dual mechanism
Thut, C. J., Goodrich, J. A., & Tjian, R. (1997) · Genes & Development · doi:10.1101/gad.11.15.1974 · Cited by 272 · see citing works
Mutual Dependence of MDM2 and MDMX in Their Functional Inactivation of p53
Gu, J., Kawai, H., Nie, L., Kitao, H., Wiederschain, D., Jochemsen, A. G., Parant, J. M., Lozano, G., & Yuan, Z.-M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200150200 · Cited by 265 · see citing works
Self-citationMdm4 and Mdm2 cooperate to inhibit p53 activity in proliferating and quiescent cells <i>in vivo</i>
Francoz, S., Froment, P., Bogaerts, S., De Clercq, S., Maetens, M., Doumont, G., Bellefroid, E., & Marine, J.-C. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508476103 · Cited by 260 · see citing works
Self-citationMeulmeester, E., Maurice, M. M., Boutell, C., Teunisse, A. F. A. S., Ovaa, H., Abraham, T. E., Dirks, R. W., & Jochemsen, A. G. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.024 · Cited by 260 · see citing works
Self-citationATM and Chk2-dependent phosphorylation of MDMX contribute to p53 activation after DNA damage
Chen, L., Gilkes, D. M., Pan, Y., Lane, W. S., & Chen, J. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600812 · Cited by 260 · see citing works
Riemenschneider, M. J., Büschges, R., Wolter, M., REIFENBERGER, J., Boström, J. P., Kraus, J. A., Schlegel, U. S., & Reifenberger, G. (1999) · PubMed · Cited by 247 · see citing works
MDM2 promotes ubiquitination and degradation of MDMX
Pan, Y., & Chen, J. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.15.5113-5121.2003 · Cited by 246 · cited 1× · see citing works
“Several groups have shown that Mdm2 can bind to and ubiquitylate Mdmx to stimulate its proteasome-dependent degradation (Pan and Chen, 2003; de Graaf et al., 2003; Kawai et al., 2003).”
BackgroundMdmx stabilizes p53 and Mdm2 via two distinct mechanisms
Stad, R., Little, N. A., Xirodimas, D. P., Frenk, R., van der Eb, A. J., Lane, D. P., Saville, M. K., & Jochemsen, A. G. (2001) · The EMBO Reports · doi:10.1093/embo-reports/kve227 · Cited by 234 · see citing works
Self-citationMendrysa, S. M., McElwee, M. K., Michalowski, J., O'Leary, K. A., Young, K. M., & Perry, M. E. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.2.462-473.2003 · Cited by 234 · see citing works
MdmX Protects p53 from Mdm2-Mediated Degradation
Jackson, M. W., & Berberich, S. J. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.3.1001-1007.2000 · Cited by 211 · cited 1× · see citing works
“Mdmx has been reported to act as a ubiquitin ligase in vitro (Badciong and Haas, 2002), but Mdmx overexpression in cells does not lead to p53 ubiquitylation and degradation (Jackson and Berberich, 2000; Stad et al., 2000; Migliorini et al., 2002a).”
BackgroundPrives, C. L., & Manley, J. L. (2001) · Cell · doi:10.1016/s0092-8674(01)00619-5 · Cited by 210 · see citing works
The RING domain of Mdm2 mediates histone ubiquitylation and transcriptional repression
Minsky, N., & Oren, M. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.016 · Cited by 204 · see citing works
Toledo, F., Krummel, K. A., Lee, C. J., Liu, C.-W., Rodewald, L.-W., Tang, M., & Wahl, G. M. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.03.014 · Cited by 199 · cited 4× · see citing works
“Analyses of p53 P regulation by Mdm2 and Mdmx produced similar results (Toledo et al., 2006). p53 interacts with the p300 histone acetyltransferase and this interaction appears to be essential for p53-dependent activation of the promoter of the p53-target gene p21 (Liu et al., 2003). p53 itself is…”
BackgroundResultInfluentialmdmx is a negative regulator of p53 activity in vivo.
Finch, R. A., Donoviel, D. B., Potter, D., Shi, M., Fan, A., Freed, D. D., Wang, C.-Y., Zambrowicz, B., Ramírez‐Solis, R., Sands, A., et al. (2002) · PubMed · Cited by 192 · see citing works
Levels of HdmX expression dictate the sensitivity of normal and transformed cells to Nutlin-3
Patton, J. T., Mayo, L. D., Singhi, A. D., Gudkov, A. V., Stark, G. R., & Jackson, M. W. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3832 · Cited by 189 · see citing works
Comparative study of the p53-mdm2 and p53-MDMX interfaces
Böttger, V., Böttger, A., Garcia-Echeverria, C., Ramos, Y. F., van der Eb, A. J., Jochemsen, A. G., & Lane, D. P. (1999) · Oncogene · doi:10.1038/sj.onc.1202281 · Cited by 189 · see citing works
Self-citationMdmx as an essential regulator of p53 activity
Marine, J., & Jochemsen, A. G. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.03.151 · Cited by 186 · see citing works
Self-citationPhosphorylation of Hdmx mediates its Hdm2- and ATM-dependent degradation in response to DNA damage
Pereg, Y., Shkedy, D., de Graaf, P., Meulmeester, E., Edelson-Averbukh, M., Salek, M., Biton, S., Teunisse, A. F. A. S., Lehmann, W. D., Jochemsen, A. G., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408595102 · Cited by 181 · see citing works
Self-citationThe First Knockout Mouse Model of Retinoblastoma
Zhang, J., Schweers, B. A., & Dyer, M. A. (2004) · Cell Cycle · doi:10.4161/cc.3.7.1002 · Cited by 170 · see citing works
Self-citationThe search for the retinoblastoma cell of origin
Dyer, M. A., & Bremmer, R. (2005) · American Journal of Ophthalmology · doi:10.1016/j.ajo.2005.05.013 · Cited by 170 · see citing works
Self-citationThe search for the retinoblastoma cell of origin
Dyer, M. A., & Bremner, R. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1545 · Cited by 170 · cited 1× · see citing works
“In addition, they show that retinoblastoma does not arise from an intrinsically death-resistant cell as previously believed (Dyer and Bremner, 2005).”
BackgroundSelf-citationRepression of the Arf tumor suppressor by E2F3 is required for normal cell cycle kineticsPreprint
Aslanian, A., Iaquinta, P. J., Verona, R. I., & Lees, J. A. (2004) · Genes & Development · doi:10.1101/gad.1196704 · Cited by 170 · see citing works
DNA damage-induced MDMX degradation is mediated by MDM2
Kawai, H., Wiederschain, D., Kitao, H., Stuart, J., Tsai, K. K. C., & Yuan, Z.-M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308295200 · Cited by 163 · cited 1× · see citing works
“Several groups have shown that Mdm2 can bind to and ubiquitylate Mdmx to stimulate its proteasome-dependent degradation (Pan and Chen, 2003; de Graaf et al., 2003; Kawai et al., 2003).”
BackgroundSynergistic roles of Mdm2 and Mdm4 for p53 inhibition in central nervous system development
Xiong, S., Van Pelt, C. S., Elizondo-Fraire, A. C., Liu, G., & Lozano, G. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508500103 · Cited by 155 · see citing works
Isolation and Identification of the Human Homolog of a New p53-Binding Protein, Mdmx
Shvarts, A., Bazuine, M., Dekker, P., Ramos, Y. F., Steegenga, W. T., Merckx, G., van Ham, R. C. A., van Oordt, C. W. M. D. H., van der Eb, A. J., & Jochemsen, A. G. (1997) · Genomics · doi:10.1006/geno.1997.4775 · Cited by 152 · see citing works
Self-citationTissue-specific differences of p53 inhibition by Mdm2 and Mdm4
Grier, J. D., Xiong, S., Elizondo-Fraire, A. C., Parant, J. M., & Lozano, G. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.1.192-198.2006 · Cited by 149 · see citing works
Aberrant expression of HDMX proteins in tumor cells correlates with wild-type p53.
Ramos, Y. F., Stad, R. K., Attema, J., Peltenburg, L. T. C., van der Eb, A. J., & Jochemsen, A. G. (2001) · PubMed · Cited by 149 · see citing works
Self-citation(2003) · PubMed · Cited by 147 · see citing works
Stad, R., Ramos, Y. F. M., Little, N., Grivell, S., Attema, J., van der Eb, A. J., & Jochemsen, A. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003496200 · Cited by 145 · see citing works
Self-citationHdmx protein stability is regulated by the ubiquitin ligase activity of Mdm2
de Graaf, P., Little, N. A., Ramos, Y. F. M., Meulmeester, E., Letteboer, S. J. F., & Jochemsen, A. G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213034200 · Cited by 143 · cited 1× · see citing works
“Several groups have shown that Mdm2 can bind to and ubiquitylate Mdmx to stimulate its proteasome-dependent degradation (Pan and Chen, 2003; de Graaf et al., 2003; Kawai et al., 2003).”
BackgroundSelf-citationOkamoto, K., Kashima, K., Pereg, Y., Ishida, M., Yamazaki, S., Nota, A., Teunisse, A., Migliorini, D., Kitabayashi, I., Marine, J.-C., et al. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.21.9608-9620.2005 · Cited by 129 · see citing works
Self-citationRegulation of MDMX nuclear import and degradation by Chk2 and 14-3-3
LeBron, C., Chen, L., Gilkes, D. M., & Chen, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601032 · Cited by 122 · see citing works
Death squads enlisted by the tumour suppressor p53
Michalak, E. M., Villunger, A., Erlacher, M., & Strasser, A. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.03.183 · Cited by 114 · see citing works
Rallapalli, R., Strachan, G. D., Cho, B., Mercer, W. E., & Hall, D. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.12.8299 · Cited by 113 · see citing works
14‐3‐3γ binds to MDMX that is phosphorylated by UV‐activated Chk1, resulting in p53 activation
Jin, Y., Dai, M., Lu, S. Z., Xu, Y., Luo, Z., Zhao, Y., & Lu, H. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601010 · Cited by 113 · see citing works
Liu, G., Xia, T., & Chen, X. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210696200 · Cited by 107 · see citing works
(1991) · Archives of Ophthalmology · doi:10.1001/archopht.1991.01080100041027 · Cited by 106 · see citing works
MdmX Is a RING Finger Ubiquitin Ligase Capable of Synergistically Enhancing Mdm2 Ubiquitination
Badciong, J. C., & Haas, A. L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208593200 · Cited by 106 · see citing works
Flexible lid to the p53-binding domain of human Mdm2: Implications for p53 regulation
McCoy, M. A., Gesell, J. J., Senior, M. M., & Wyss, D. F. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0334477100 · Cited by 95 · see citing works
MDM2 and MDMX can interact differently with ARF and members of the p53 family
Wang, X., Arooz, T., Siu, W. Y., Chiu, C. H. S., Lau, A., Yamashita, K., & Poon, R. Y. C. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02124-x · Cited by 94 · see citing works
Differential Roles of ATM- and Chk2-Mediated Phosphorylations of Hdmx in Response to DNA Damage
Pereg, Y., Lam, S., Teunisse, A., Biton, S., Meulmeester, E., Mittelman, L., Buscemi, G., Okamoto, K., Taya, Y., Shiloh, Y., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00562-06 · Cited by 93 · see citing works
Self-citationRegulation of p53-MDMX interaction by casein kinase 1 alpha
Chen, L., Li, C., Pan, Y., & Chen, J. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.15.6509-6520.2005 · Cited by 88 · see citing works
Migliorini, D., Danovi, D., Colombo, E., Carbone, R., Pelicci, P. G., & Marine, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108795200 · Cited by 86 · see citing works
Self-citationRiemenschneider, M. J., Knobbe-Thomsen, C. B., & Reifenberger, G. (2003) · International Journal of Cancer · doi:10.1002/ijc.11023 · Cited by 85 · see citing works
Mdmx and Mdm2: Brothers in Arms?
Marine, J., & Jochemsen, A. G. (2004) · Cell Cycle · doi:10.4161/cc.3.7.998 · Cited by 77 · see citing works
Self-citationBoesten, L. S. M., Zadelaar, S. M., De Clercq, S., Francoz, S., van Nieuwkoop, A., Biessen, E. A. L., Hofmann, F., Feil, S., Feil, R., Jochemsen, A. G., et al. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401973 · Cited by 70 · see citing works
Self-citationp53 Regulates Apoptosis in Human Retinoblastoma
Nork, T. M. (1997) · Archives of Ophthalmology · doi:10.1001/archopht.1997.01100150215011 · Cited by 69 · see citing works
MDMX inhibits the p300/CBP-mediated acetylation of p53
Sabbatini, P., & McCormick, F. (2002) · DNA and Cell Biology · doi:10.1089/104454902320219077 · Cited by 62 · see citing works
Loss of heterozygosity on chromosome 17 and mutation of the p53 gene in retinoblastoma
Kato, M. V., Shimizu, T., Ishizaki, K., Kaneko, A., Yandell, D. W., Toguchida, J., & Sasaki, M. S. (1996) · Cancer Letters · doi:10.1016/0304-3835(96)04305-4 · Cited by 60 · see citing works
Giglio, S., Mancini, F., Gentiletti, F., Sparaco, G., Felicioni, L., Barassi, F., Martella, C., Prodosmo, A., Iacovelli, S., Buttitta, F., et al. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-0450 · Cited by 58 · see citing works
Conditional allele of mdm2 which encodes a p53 inhibitor
Grier, J. D., Yan, W., & Lozano, G. (2002) · genesis · doi:10.1002/gene.10066 · Cited by 57 · see citing works
Use of Preclinical Models to Improve Treatment of Retinoblastoma
Dyer, M. A., Galindo, C. R., & Wilson, M. W. (2005) · PLoS Medicine · doi:10.1371/journal.pmed.0020332 · Cited by 57 · see citing works
Self-citationRescue of Mdm4-deficient mice by Mdm2 reveals functional overlap of Mdm2 and Mdm4 in development
Steinman, H. A., Hoover, K. L., Keeler, M. L., Sands, A., & Jones, S. N. (2005) · Oncogene · doi:10.1038/sj.onc.1208930 · Cited by 52 · see citing works
Bartel, F., Harris, L. C., Würl, P., & Taubert, H. W. (2004) · Molecular Cancer Research · doi:10.1158/1541-7786.29.2.1 · Cited by 52 · see citing works
Rallapalli, R., Strachan, G. D., Tuan, R. S., & Hall, D. J. (2003) · Journal of Cellular Biochemistry · doi:10.1002/jcb.10535 · Cited by 45 · see citing works
G1 checkpoint failure and increased tumor susceptibility in mice lacking the novel p53 target Ptprv
Doumont, G., Martoriati, A., Beekman, C., Bogaerts, S., Mee, P. J., Bureau, F., Colombo, E., Alcalay, M., Bellefroid, E., Marchesi, F., et al. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600769 · Cited by 38 · see citing works
Self-citationMouse bites dogma: how mouse models are changing our views of how P53 is regulated in vivo
Wahl, G. M. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401911 · Cited by 37 · see citing works
Sex change and relative body size in animals
Buston, P. M., Munday, P. L., & Warner, R. R. (2004) · Nature · doi:10.1038/nature02512a · Cited by 35 · see citing works
Phosphorylation of MdmX by CDK2/Cdc2p34 is required for nuclear export of Mdm2
Elias, B. C., Laine, A. M., & Ronai, Z. A. (2005) · Oncogene · doi:10.1038/sj.onc.1208488 · Cited by 24 · see citing works
Modification of MDMX by sumoylation
Pan, Y., & Chen, J. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.05.012 · Cited by 20 · see citing works
Generation of an Mdm2 conditional allele in mice
Steinman, H. A., & Jones, S. N. (2002) · genesis · doi:10.1002/gene.10035 · Cited by 14 · see citing works
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Blinded by the Light: The Growing Complexity of p53
Vousden, K. H., & Prives, C. (2009) · Cell · doi:10.1016/j.cell.2009.04.037 · Cited by 3,163 · see citing works
Mutant p53: one name, many proteinsPreprint
Freed-Pastor, W. A., & Prives, C. L. (2012) · Genes & Development · doi:10.1101/gad.190678.112 · Cited by 1,246 · see citing works
Linking the p53 tumour suppressor pathway to somatic cell reprogramming
Kawamura, T., Suzuki, J., Wang, Y. V., Menendez, S., Morera, L. B., Raya, A., Wahl, G. M., & Belmonte, J. C. I. (2009) · Nature · doi:10.1038/nature08311 · Cited by 1,115 · see citing works
Chang, Y. S., Graves, B. J., Guerlavais, V., Tovar, C., Packman, K. E., To, K.-H., Olson, K. A., Kesavan, K. P., Gangurde, P., Mukherjee, A., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303002110 · Cited by 666 · see citing works
p53 post-translational modification: deregulated in tumorigenesis
Dai, C., & Gu, W. J. (2010) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.09.002 · Cited by 523 · see citing works
Posttranslational Modification of p53: Cooperative Integrators of FunctionPreprint
Meek, D. W., & Anderson, C. W. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000950 · Cited by 487 · see citing works
The 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 · see citing works
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 · see citing works
Structural basis for high-affinity peptide inhibition of p53 interactions with MDM2 and MDMX
Pazgier, M., Liu, M., Zou, G., Yuan, W., Li, C., Li, C., Li, J., Monbo, J., Zella, D., Tarasov, S. G., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900947106 · Cited by 391 · see citing works
Brady, C. A., & Attardi, L. D. (2010) · Journal of Cell Science · doi:10.1242/jcs.064501 · Cited by 374 · see citing works
Shaping Genetic Alterations in Human Cancer: The p53 Mutation Paradigm
Soussi, T., & Wiman, K. G. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.10.001 · Cited by 366 · see citing works
Mdm2-mediated ubiquitylation: p53 and beyond
Marine, J.-C., & Lozano, G. (2010) · Cell Death & Differentiation · doi:10.1038/cdd.2009.68 · Cited by 354 · see citing works
Self-citationThe Tumor Suppressor p53: From Structures to Drug DiscoveryPreprint
Joerger, A. C., & Fersht, A. R. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000919 · Cited by 356 · see citing works
The Mdm2–p53 relationship evolves: Mdm2 swings both ways as an oncogene and a tumor suppressor
Manfredi, J. J. (2010) · Genes & Development · doi:10.1101/gad.1941710 · Cited by 344 · see citing works
MDM4 is a key therapeutic target in cutaneous melanoma
Gembarska, A., Luciani, F., Fedele, C., Russell, E. A., Dewaele, M., Villar, S., Zwolinska, A., Haupt, S., de Lange, J., Yip, D., et al. (2012) · Nature Medicine · doi:10.1038/nm.2863 · Cited by 327 · see citing works
Self-citationRegulation of the p53 response and its relationship to cancer
Meek, D. W. (2015) · Biochemical Journal · doi:10.1042/bj20150517 · Cited by 291 · see citing works
Linke, K., Mace, P. D., Smith, C. A., Vaux, D. L., Silke, J., & Day, C. L. (2008) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402309 · Cited by 288 · see citing works
A Stapled p53 Helix Overcomes HDMX-Mediated Suppression of p53
Bernal, F., Wade, M. R., Godes, M., Davis, T. N., Whitehead, D. G., Kung, A. L., Wahl, G. M., & Walensky, L. D. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.10.024 · Cited by 284 · see citing works
MDM2 and MDM4: p53 regulators as targets in anticancer therapy
Toledo, F., & Wahl, G. M. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.03.022 · Cited by 261 · see citing works
Shi, Y., Nikulenkov, F., Zawacka‐Pankau, J., Li, H., Gabdoulline, R. R., Xu, J., Eriksson, S. E., Hedström, E., Issaeva, N., Kel, A. E., et al. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2013.186 · Cited by 232 · see citing works
Popowicz, G. M., Czarna, A., Wolf, S., Wang, K., Wang, W., Dömling, A. S. S., & Holak, T. A. (2010) · Cell Cycle · doi:10.4161/cc.9.6.10956 · Cited by 232 · see citing works
Liu, M., Li, C., Pazgier, M., Li, C., Mao, Y., Lv, Y., Gu, B., Wei, G., Yuan, W., Zhan, C., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008930107 · Cited by 229 · see citing works
Ribosomal Protein S7 Is Both a Regulator and a Substrate of MDM2
Zhu, Y. Y., Poyurovsky, M. V., Li, Y., Biderman, L., Stahl, J., Jacq, X., & Prives, C. L. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.07.014 · Cited by 206 · see citing works
Identification and Characterization of the First Small Molecule Inhibitor of MDMX
Reed, D., Shen, Y., Shelat, A. A., Arnold, L. A., Ferreira, A. M., Zhu, F., Mills, N., Smithson, D. C., Regni, C. A., Bashford, D., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.056747 · Cited by 198 · see citing works
Self-citationThe p53 inhibitors MDM2/MDMX complex is required for control of p53 activity in vivo
Huang, L., Yan, Z., Liao, X., Li, Y., Yang, J., Wang, Z.-G., Zuo, Y., Kawai, H., Shadfan, M., Ganapathy, S., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102309108 · Cited by 193 · see citing works
Wynendaele, J., Böhnke, A., Leucci, E., Nielsen, S. J., Lambertz, I., Hammer, S., Sbrzesny, N., Kubitza, D., Wolf, A. A., Gradhand, E., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-0527 · Cited by 171 · see citing works
Self-citationTargeting Mdm2 and Mdmx in cancer therapy: better living through medicinal chemistry?
Wade, M., & Wahl, G. M. (2009) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-08-0423 · Cited by 170 · see citing works
The Structure‐Based Design of Mdm2/Mdmx–p53 Inhibitors Gets Serious
Popowicz, G. M., Dömling, A. S. S., & Holak, T. A. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201003863 · Cited by 166 · see citing works
Monoallelic but not biallelic loss of Dicer1 promotes tumorigenesis in vivo
Lambertz, I. U., Nittner, D., Mestdagh, P., Denecker, G., Vandesompele, J., Dyer, M. A., & Marine, J. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.202 · Cited by 161 · see citing works
Self-citationSystematic Mutational Analysis of Peptide Inhibition of the p53–MDM2/MDMX Interactions
Li, C. V., Pazgier, M., Li, C., Yuan, W., Liu, M., Wei, G., Lu, W., & Lu, W. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.03.005 · Cited by 146 · see citing works
Pant, V., Xiong, S., Iwakuma, T., Quintás-Cardama, A., & Lozano, G. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102241108 · Cited by 134 · see citing works
Zhuang, C., Miao, Z., Zhu, L., Dong, G., Guo, Z., Wang, S., Zhang, Y., Wu, Y., Yao, J., Sheng, C., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300969t · Cited by 131 · see citing works
Molecular Basis for the Inhibition of p53 by Mdmx
Popowicz, G. M., Czarna, A., Rothweiler, U., Szwagierczak, A., Krajewski, M., Weber, L., & Holak, T. A. (2007) · Cell Cycle · doi:10.4161/cc.6.19.4740 · Cited by 131 · see citing works
Small molecular weight protein–protein interaction antagonists—an insurmountable challenge?
Dömling, A. S. S. (2008) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2008.04.603 · Cited by 128 · see citing works
Lee, J. H., Zhang, Q., Jo, S., Chai, S. C., Oh, M., Im, W., Lu, H., & Lim, H. (2010) · Journal of the American Chemical Society · doi:10.1021/ja108230s · Cited by 126 · see citing works
Dissenting degradation: Deubiquitinases in cell cycle and cancer
Bonacci, T., & Emanuele, M. J. (2020) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2020.03.008 · Cited by 125 · see citing works
A Small-Molecule Inhibitor of MDMX Activates p53 and Induces Apoptosis
Wang, H., Ma, X., Ren, S., Buolamwini, J. K., & Yan, C. (2011) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-10-0581 · Cited by 117 · see citing works
Hu, W., Feng, Z., Modica, I., Klimstra, D. S., Song, L., Allen, P. J., Brennan, M. F., Levine, A. J., & Tang, L. H. (2010) · Genes & Cancer · doi:10.1177/1947601910371979 · Cited by 116 · see citing works
A Left‐Handed Solution to Peptide Inhibition of the p53–MDM2 Interaction
Liu, M., Pazgier, M., Li, C., Yuan, W., Li, C., & Lu, W. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201000329 · Cited by 115 · see citing works
MALAT1: A key regulator in lung cancer pathogenesis and therapeutic targeting
Bhat, A. A., Afzal, O., Afzal, M., Gupta, G., Thapa, R., Ali, H., Almalki, W. H., Kazmi, I. A., Alzarea, S. I., Saleem, S., et al. (2023) · Pathology - Research and Practice · doi:10.1016/j.prp.2023.154991 · Cited by 111 · see citing works
Identification of ribosomal protein S25 (RPS25)–MDM2–p53 regulatory feedback loop
Zhang, X., Wang, W., Wang, H., Wang, M.-H., Xu, W., & Zhang, R. (2012) · Oncogene · doi:10.1038/onc.2012.289 · Cited by 106 · see citing works
Yan, S., Yan, J., Liu, D., Li, X., Kang, Q., You, W., Zhang, J., Wang, L., Tian, Z., Lu, W., et al. (2021) · Theranostics · doi:10.7150/thno.59020 · Cited by 107 · see citing works
Discovery of Mdm2-MdmX E3 Ligase Inhibitors Using a Cell-Based Ubiquitination Assay
Herman, A. G., Hayano, M., Poyurovsky, M. V., Shimada, K., Skouta, R., Prives, C., & Stockwell, B. R. (2011) · Cancer Discovery · doi:10.1158/2159-8290.cd-11-0104 · Cited by 100 · see citing works
MdmX is a substrate for the deubiquitinating enzyme USP2a
Allende-Vega, N., Sparks, A., Lane, D. P., & Saville, M. K. (2010) · Oncogene · doi:10.1038/onc.2009.330 · Cited by 100 · see citing works
New Insights in Thyroid Cancer and p53 Family Proteins
Manzella, L., Stella, S., Pennisi, M. S., Tirrò, E., Massimino, M., Romano, C., Puma, A., Tavarelli, M., & Vigneri, P. G. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061325 · Cited by 98 · see citing works
p53 is activated in response to disruption of the pre-mRNA splicing machinery
Allende-Vega, N., Dayal, S., Agarwala, U., Sparks, A., Bourdon, J., & Saville, M. K. (2012) · Oncogene · doi:10.1038/onc.2012.38 · Cited by 96 · see citing works
Melatonin down‐regulates MDM 2 gene expression and enhances p53 acetylation in MCF ‐7 cells
Proietti, S., Cucina, A., Dobrowolny, G., D’Anselmi, F., Dinicola, S., Masiello, M. G., Pasqualato, A., Palombo, A., Morini, V., Reiter, R. J., et al. (2014) · Journal of Pineal Research · doi:10.1111/jpi.12150 · Cited by 96 · see citing works
Structure of human MDM2 complexed with RPL11 reveals the molecular basis of p53 activationPreprint
Zheng, J., Lang, Y., Zhang, Q., Cui, D., Sun, H., Jiang, L., Chen, Z., Zhang, R., Gao, Y., Tian, W., et al. (2015) · Genes & Development · doi:10.1101/gad.261792.115 · Cited by 91 · see citing works
Small molecule agents targeting the p53‐MDM2 pathway for cancer therapy
Wang, W., & Hu, Y. (2011) · Medicinal Research Reviews · doi:10.1002/med.20236 · Cited by 85 · see citing works
Validation of MdmX as a therapeutic target for reactivating p53 in tumors
Garcia, D., Warr, M. R., Martins, C. P., Brown Swigart, L., Passegué, E., & Evan, G. I. (2011) · Genes & Development · doi:10.1101/gad.16722111 · Cited by 83 · see citing works
The role of MDM2 and MDM4 in breast cancer development and prevention
Haupt, S., Vijayakumaran, R., Miranda, P. J., Burgess, A., Lim, E., & Haupt, Y. (2017) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjx007 · Cited by 80 · see citing works
An Ultrahigh Affinity d -Peptide Antagonist Of MDM2
Zhan, C., Zhao, L., Wei, X., Wu, X., Chen, X., Yuan, W., Lu, W., Pazgier, M., & Lu, W. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm3005465 · Cited by 80 · see citing works
Mancini, F., Conza, G. D., Pellegrino, M., Rinaldo, C., Prodosmo, A., Giglio, S., D’Agnano, I., Florenzano, F., Felicioni, L., Buttitta, F., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.154 · Cited by 81 · see citing works
Wang, Y. V., Leblanc, M., Wade, M., Jochemsen, A. G., & Wahl, G. M. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.05.008 · Cited by 79 · see citing works
Self-citationLimitations of Peptide Retro-inverso Isomerization in Molecular Mimicry
Li, C., Pazgier, M., Li, J., Li, C., Liu, M., Zou, G., Li, Z., Chen, J., Tarasov, S. G., Lu, W., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.116814 · Cited by 79 · see citing works
Apamin as a Template for Structure‐Based Rational Design of Potent Peptide Activators of p53
Li, C., Pazgier, M., Liu, M., Lu, W., & Lu, W. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200904550 · Cited by 79 · see citing works
Clancy, A. A., Spaans, J. N., & Weberpals, J. I. (2016) · Annals of Oncology · doi:10.1093/annonc/mdw242 · Cited by 76 · see citing works
Meek, D. W., & Hupp, T. R. (2010) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2009.10.005 · Cited by 76 · see citing works
Turning a Scorpion Toxin into an Antitumor Miniprotein
Li, C., Liu, M., Monbo, J., Zou, G., Li, C., Yuan, W., Zella, D., Lu, W., & Lu, W. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8042036 · Cited by 75 · see citing works
Targeting RNA polymerase I to treat MYC-driven cancer
Poortinga, G., Quinn, L. M., & Hannan, R. D. (2014) · Oncogene · doi:10.1038/onc.2014.13 · Cited by 74 · see citing works
Benedetti, F., Curreli, S., & Zella, D. (2020) · Microorganisms · doi:10.3390/microorganisms8091351 · Cited by 75 · see citing works
Kallen, J. A., Goepfert, A., Blechschmidt, A., Izaac, A., Geiser, M., Tavares, G., Ramage, P., Furet, P., Masuya, K., & Lisztwan, J. H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809096200 · Cited by 72 · see citing works
Mdmx promotes genomic instability independent of p53 and Mdm2
Carrillo, A. M., Bouska, A., Arrate, M. P., & Eischen, C. M. (2015) · Oncogene · doi:10.1038/onc.2014.27 · Cited by 69 · see citing works
The p53-MDM2/MDMX axis – A chemotype perspective
Khoury, K., Popowicz, G. M., Holak, T. A., & Dömling, A. S. S. (2011) · MedChemComm · doi:10.1039/c0md00248h · Cited by 70 · see citing works
Inhibition of p53 DNA Binding Function by the MDM2 Protein Acidic Domain
Cross, B. L., Chen, L., Cheng, Q., Li, B., Yuan, Z.-M., & Chen, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.228981 · Cited by 69 · see citing works
PML enhances the regulation of p53 by CK1 in response to DNA damage
Alsheich-Bartok, O., Haupt, S., Snir-Alkalay, I., Saito, S., Appella, E., & Haupt, Y. (2008) · Oncogene · doi:10.1038/sj.onc.1211036 · Cited by 69 · see citing works
c-Abl Phosphorylates Hdmx and Regulates Its Interaction with p53
Zuckerman, V., Lenos, K., Popowicz, G. M., Silberman, I., Grossman, T., Marine, J.-C., Holak, T. A., Jochemsen, A. G., & Haupt, Y. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809211200 · Cited by 68 · see citing works
Self-citationYu, Q., Li, Y., Mu, K., Li, Z., Meng, Q., Wu, X., Wang, Y., & Li, L. (2014) · Diagnostic Pathology · doi:10.1186/1746-1596-9-71 · Cited by 64 · see citing works
Ensemble-based virtual screening reveals dual-inhibitors for the p53–MDM2/MDMX interactions
Barakat, K., Mane, J. Y., Friesen, D. E., & Tuszyński, J. A. (2009) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2009.12.003 · Cited by 61 · see citing works
Tiu, G. C., Kerr, C. H., Forester, C. M., Krishnarao, P. S., Rosenblatt, H. D., Raj, N., Lantz, T. C., Zhulyn, O., Bowen, M. E., Shokat, L., et al. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.06.013 · Cited by 57 · see citing works
Classification of food vegetable oils by fluorimetry and artificial neural networks
da Silva, C. E. T., Filardi, V. L., Pepe, I. M., Chaves, M. A., & Santos, C. M. S. (2014) · Food Control · doi:10.1016/j.foodcont.2014.06.030 · Cited by 59 · see citing works
The p53-mediated cytotoxicity of photodynamic therapy of cancer: Recent advances
Zawacka‐Pankau, J., Krachulec, J., Grulkowski, I., Bielawski, K. P., & Selivanova, G. (2008) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2008.07.012 · Cited by 59 · see citing works
Potent in vitro and in vivo antitumor effects of MDM2 inhibitor nutlin‐3 in gastric cancer cells
Endo, S., Yamato, K., Hirai, S., Moriwaki, T., Fukuda, K., Suzuki, H., Abei, M., Nakagawa, I., & Hyodo, I. (2010) · Cancer Science · doi:10.1111/j.1349-7006.2010.01821.x · Cited by 58 · see citing works
Najem, A., Krayem, M., Salès, F., Hussein, N., Badran, B. M., Robert, C., Awada, A. H., Journé, F., & Ghanem, G. (2017) · European Journal of Cancer · doi:10.1016/j.ejca.2017.06.033 · Cited by 57 · see citing works
Matijasevic, Z., Steinman, H. A., Hoover, K., & Jones, S. N. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01108-07 · Cited by 58 · see citing works
Targeting the Ubiquitin-Mediated Proteasome Degradation of p53 for Cancer Therapy
DeVine, T., & Dai, M. (2013) · Current Pharmaceutical Design · doi:10.2174/1381612811319180009 · Cited by 57 · see citing works
Prodosmo, A., Giglio, S., Moretti, S., Mancini, F., Barbi, F., Avenia, N., Conza, G. D., Schünemann, H. J., Pistola, L., Ludovini, V., et al. (2008) · Journal of Molecular Medicine · doi:10.1007/s00109-008-0322-6 · Cited by 57 · see citing works
Unravelling mechanisms of cisplatin sensitivity and resistance in testicular cancer
Koster, R., van Vugt, M. A. T. M., Timmer‐Bosscha, H., Gietema, J. A., & de Jong, S. (2013) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2013.13 · Cited by 57 · see citing works
On the Mechanism of Action of SJ-172550 in Inhibiting the Interaction of MDM4 and p53
Bista, M., Smithson, D., Pecak, A., Salinas, G., Pustelny, K., Min, J., Pirog, A., Finch, K., Zdzalik, M., Waddell, B., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037518 · Cited by 58 · see citing works
Self-citationMandl, A., Pham, L. H., Tóth, K., Zambetti, G., & Erhardt, P. (2011) · Circulation · doi:10.1161/circulationaha.110.988303 · Cited by 57 · see citing works
p53 ubiquitination by Mdm2: A never ending tail?
Coutts, A. S., Adams, C., & Thangue, N. B. L. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.01.008 · Cited by 56 · see citing works
Using Mice to Examine p53 Functions in Cancer, Aging, and LongevityPreprint
Donehower, L. A. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a001081 · Cited by 56 · see citing works
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McEvoy, J. D., & Dyer, M. A. (2015) · Critical Reviews™ in Oncogenesis · doi:10.1615/critrevoncog.2015013711 · Cited by 53 · see citing works
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Renert, A.-F., Leprince, P., Dieu, M., Renaut, J., Raes, M. J., Bours, V., Chapelle, J.-P., Piette, J. G., Merville, M.-P., & Fillet, M. (2009) · Journal of Proteome Research · doi:10.1021/pr9005316 · Cited by 51 · see citing works
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Li, M., & Gu, W. J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.020 · Cited by 50 · see citing works
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Wu, L., Yu, H., Zhao, Y., Zhang, C., Wang, J., Yue, X., Yang, Q., & Hu, W. (2015) · Oncotarget · doi:10.18632/oncotarget.3017 · Cited by 49 · see citing works
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Arlt, C., Ihling, C. H., & Sinz, A. (2015) · PROTEOMICS · doi:10.1002/pmic.201400549 · Cited by 49 · see citing works
Zhan, C., Varney, K. M., Yuan, W., Zhao, L., & Lu, W. (2012) · Journal of the American Chemical Society · doi:10.1021/ja301255n · Cited by 49 · see citing works
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Rayburn, E. R., Ezell, S. J., & Zhang, R. (2009) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/187152009789124628 · Cited by 48 · see citing works
An Update on MDMX and Dual MDM2/X Inhibitors
Espadinha, M., Barcherini, V., Lopes, E. A., & Santos, M. M. M. (2018) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026618666180604080119 · Cited by 49 · see citing works
Esfandiari, A., Hawthorne, T. A., Nakjang, S., & Lunec, J. (2016) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-15-0651 · Cited by 46 · see citing works
Dyer, M. A. (2016) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.07.010 · Cited by 46 · see citing works
Self-citationRole of Mdm2 and Mdmx in DNA repair
Eischen, C. M. (2016) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjw052 · Cited by 45 · see citing works
Mdm2 and Tumorigenesis: Evolving Theories and Unsolved Mysteries
Senturk, E., & Manfredi, J. J. (2012) · Genes & Cancer · doi:10.1177/1947601912457368 · Cited by 46 · see citing works
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Song, Y., Dong, Q., Ni, Y.-K., Xu, X., Chen, C.-X., & Chen, W. (2024) · International Journal of Nanomedicine · doi:10.2147/ijn.s448684 · Cited by 44 · see citing works
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Qu, J., Yang, S., Zhu, Y., Guo, T., Thannickal, V. J., & Zhou, Y. (2021) · The Journal of Experimental Medicine · doi:10.1084/jem.20202033 · Cited by 43 · see citing works
p53, SKP2, and DKK3 as MYCN Target Genes and Their Potential Therapeutic Significance
Chen, L., & Tweddle, D. A. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00173 · Cited by 43 · see citing works
- Authors
- Marine, J.-C. W., Dyer, M. A., & Jochemsen, A. G.
- Affiliations
- Vlaams Instituut voor Biotechnologie (BE)
- St. Jude Children's Research Hospital (US)
- Leiden University Medical Center (NL)
- Corresponding author
- Marine, Jean-Christophe W.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2007-02-01
- Volume
- 120
- Issue
- 3
- Pages
- 371-378
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2141224144
- Cited by
- 228
- References
- 95
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 5 · 2023: 3 · 2022: 3 · 2021: 8 · 2020: 10 · 2019: 2 · 2018: 8 · 2017: 6 · 2016: 12 · 2015: 10 · 2014: 18 · 2013: 14 · 2012: 21
- FWCI
- 2.78
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Cell Science (publishedVersion)
- PubMed (publishedVersion)
- Ghent University Academic Bibliography (Ghent University) (submittedVersion, other-oa)
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- MDMX, MDM2, p53, tumor suppressor regulation, ubiquitin ligase, retinoblastoma, chemotherapeutic target, wild-type p53
- MeSH terms
- Animals, Humans, Models, Biological, Neoplasms, Nuclear Proteins, Proto-Oncogene Proteins, Gene Expression Regulation, Neoplastic, Tumor Suppressor Protein p53, Cell Cycle Proteins
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