Regulation of MDMX nuclear import and degradation by Chk2 and 14-3-3

The hallmarks of cancer

Hanahan, D., & Weinberg, R. A. (2000) · Cell · doi:10.1016/s0092-8674(00)81683-9 · Cited by 29,219 · see citing works

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

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 · see citing works

Surfing the p53 network

Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607 · see citing works

Akt Promotes Cell Survival by Phosphorylating and Inhibiting a Forkhead Transcription Factor

Brunet, A., Bonni, A., Zigmond, M. J., Lin, M. Z., Juo, P., Hu, L. S., Anderson, M. J., Arden, K. C., Blenis, J., & Greenberg, M. E. (1999) · Cell · doi:10.1016/s0092-8674(00)80595-4 · Cited by 6,535 · see citing works

p53, guardian of the genome

Lane, D. P. (1992) · Nature · doi:10.1038/358015a0 · Cited by 5,138 · 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

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 · 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

The Bcl2 family: regulators of the cellular life-or-death switch

Cory, S., & Adams, J. M. (2002) · Nature Reviews Cancer · doi:10.1038/nrc883 · Cited by 4,032 · see citing works

The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53

Scheffner, M., Werness, B. A., Huibregtse, J. M., Levine, A. J., & Howley, P. M. (1990) · Cell · doi:10.1016/0092-8674(90)90409-8 · Cited by 3,995 · see citing works

The p53 tumour suppressor gene

Levine, A. J., Momand, J. A., & Finlay, C. A. (1991) · Nature · doi:10.1038/351453a0 · Cited by 3,785 · see citing works

Germ Line p53 Mutations in a Familial Syndrome of Breast Cancer, Sarcomas, and Other Neoplasms

Malkin, D., Li, F. P., Strong, L. C., Fraumeni, J. F., Nelson, C. E., Kim, D. H., Kassel, J., Gryka, M. A., Bischoff, F. Z., Tainsky, M. A., et al. (1990) · Science · doi:10.1126/science.1978757 · Cited by 3,765 · see citing works

Mechanisms Underlying Ubiquitination

Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,731 · see citing works

Mutations in the p53 tumor suppressor gene: clues to cancer etiology and molecular pathogenesis.

Greenblatt, M. S., Bennett, W. P., Hollstein, M., & Harris, C. C. (1994) · PubMed · Cited by 3,463 · 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 · see citing works

Live 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

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 · see citing works

A human DNA segment with properties of the gene that predisposes to retinoblastoma and osteosarcoma

Friend, S. H., Bernards, R., Rogelj, S., Weinberg, R. A., Rapaport, J. M., Albert, D. M., & Dryja, T. P. (1986) · Nature · doi:10.1038/323643a0 · Cited by 2,948 · see citing works

Serine Phosphorylation of Death Agonist BAD in Response to Survival Factor Results in Binding to 14-3-3 Not BCL-XL

Zha, J., Harada, H., Yang, E., Jockel, J., & Korsmeyer, S. J. (1996) · Cell · doi:10.1016/s0092-8674(00)81382-3 · Cited by 2,578 · see citing works

Crystal Structure of a p53 Tumor Suppressor-DNA Complex: Understanding Tumorigenic Mutations

Cho, Y., Gorina, S., Jeffrey, P. D., & Pavletich, N. P. (1994) · Science · doi:10.1126/science.8023157 · Cited by 2,559 · see citing works

T antigen is bound to a host protein in SY40-transformed cells

Lane, D. P., & Crawford, L. V. (1979) · Nature · doi:10.1038/278261a0 · Cited by 2,443 · see citing works

PUMA, a Novel Proapoptotic Gene, Is Induced by p53

Nakano, K., & Vousden, K. H. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00214-3 · Cited by 2,315 · see citing works

Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain

Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206 · see citing works

Tumor suppressor p53 is a regulator of bcl-2 and bax gene expression in vitro and in vivo.

Miyashita, T., Krajewski, S., Krajewska, M., Wang, H., Lin, H., Liebermann, D. A., Hoffman‐Liebermann, B., & Reed, J. C. (1994) · PubMed · Cited by 2,143 · see citing works

Noxa, a BH3-Only Member of the Bcl-2 Family and Candidate Mediator of p53-Induced Apoptosis

Oda, E., Ohki, R., Murasawa, H., Nemoto, J., Shibue, T., Yamashita, T., Tokino, T., Taniguchi, T., & Tanaka, †. N. (2000) · Science · doi:10.1126/science.288.5468.1053 · Cited by 2,112 · see citing works

DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2

Shieh, S.-Y., Ikeda, M., Taya, Y., & Prives, C. (1997) · Cell · doi:10.1016/s0092-8674(00)80416-x · Cited by 2,100 · see citing works

Wild-type p53 induces apoptosis of myeloid leukaemic cells that is inhibited by interleukin-6

Yonish-Rouach, E., Resnftzky, D., Lotem, J., Sachs, L., Kimchi, A., & Oren, M. (1991) · Nature · doi:10.1038/352345a0 · Cited by 2,079 · see citing works

Activation of the ATM Kinase by Ionizing Radiation and Phosphorylation of p53

Canman, C. E., Lim, D.-S., Cimprich, K. A., Taya, Y., Tamai, K., Sakaguchi, K., Appella, E., Kastan, M. B., & Siliciano, J. D. (1998) · Science · doi:10.1126/science.281.5383.1677 · Cited by 2,042 · see citing works

The p53 pathway: positive and negative feedback loops

Harris, S. L., & Levine, A. J. (2005) · Oncogene · doi:10.1038/sj.onc.1208615 · Cited by 1,967 · see citing works

Cell cycle checkpoint signaling through the ATM and ATR kinases

Abraham, R. T. (2001) · Genes & Development · doi:10.1101/gad.914401 · Cited by 1,966 · 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

Characterization of a 54K Dalton cellular SV40 tumor antigen present in SV40-transformed cells and uninfected embryonal carcinoma cells

Linzer, D. I. H., & Levine, A. J. (1979) · Cell · doi:10.1016/0092-8674(79)90293-9 · Cited by 1,814 · 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

An Adenovirus Mutant That Replicates Selectively in p53- Deficient Human Tumor Cells

Bischoff, J. R., Kirn, D. H., Williams, A., Heise, C. C., Horn, S. T., Muna, M., Ng, L., Nye, J. A., Sampson-Johannes, A., Fattaey, A., et al. (1996) · Science · doi:10.1126/science.274.5286.373 · Cited by 1,753 · see citing works

Suppression of Human Colorectal Carcinoma Cell Growth by Wild-Type p53

Baker, S. J., Markowitz, S. D., Fearon, E. R., Willson, J. K. V., & Vogelstein, B. (1990) · Science · doi:10.1126/science.2144057 · Cited by 1,742 · see citing works

UBIQUITIN-DEPENDENT PROTEIN DEGRADATION

Hochstrasser, M. (1996) · Annual Review of Genetics · doi:10.1146/annurev.genet.30.1.405 · Cited by 1,695 · see citing works

ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways

Zhang, Y., Xiong, Y., & Yarbrough, W. G. (1998) · Cell · doi:10.1016/s0092-8674(00)81401-4 · Cited by 1,626 · see citing works

The Structural Basis for 14-3-3:Phosphopeptide Binding Specificity

Yaffe, M. B., Rittinger, K., Volinia, S., Caron, P. R., Aitken, A., Leffers, H. C. B., Gamblin, S. J., Smerdon, S. J., & Cantley, L. C. (1997) · Cell · doi:10.1016/s0092-8674(00)80487-0 · Cited by 1,604 · see citing works

14-3-3 Proteins: Structure, Function, and Regulation

Fu, H., Subramanian, R. R., & Masters, S. C. (2000) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.40.1.617 · Cited by 1,569 · see citing works

The Ink4a tumor suppressor gene product, p19Arf, interacts with MDM2 and neutralizes MDM2’s inhibition of p53

Pomerantz, J., Schreiber-Agus, N., Liégeois, N. J., Silverman, A., Alland, L., Chin, L., Potes, J., Chen, K., Orlow, I., Lee, H.-W., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)81400-2 · Cited by 1,521 · see citing works

Chk1 and Chk2 kinases in checkpoint control and cancer

Bartek, J., & Lukas, J. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00110-7 · Cited by 1,513 · see citing works

The Proteasome: Paradigm of a Self-Compartmentalizing Protease

Baumeister, W. P., Walz, J., Zühl, F., & Seemüller, E. (1998) · Cell · doi:10.1016/s0092-8674(00)80929-0 · Cited by 1,497 · see citing works

Bid, Bax, and Lipids Cooperate to Form Supramolecular Openings in the Outer Mitochondrial Membrane

Kuwana, T., Mackey, M. R., Perkins, G. A., Ellisman, M. H., Latterich, M., Schneiter, R., Green, D. R., & Newmeyer, D. D. (2002) · Cell · doi:10.1016/s0092-8674(02)01036-x · Cited by 1,480 · see citing works

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 1,447 · 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 · see citing works

mdm2 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

DNA Damage-Induced Activation of p53 by the Checkpoint Kinase Chk2

Hirao, A., Kong, Y., Matsuoka, S., Wakeham, A. C., Ruland, J., Yoshida, H., Liu, D., Elledge, S. J., & Mak, T. W. (2000) · Science · doi:10.1126/science.287.5459.1824 · Cited by 1,288 · 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 · see citing works

Post-translational modification of p53 in tumorigenesis

Bode, A. M., & Dong, Z. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1455 · Cited by 1,270 · see citing works

Is a p53-Regulated Inhibitor of G2/M Progression

Hermeking, H., Lengauer, C., Polyak, K., He, T.-C., Zhang, L., Thiagalingam, S., Kinzler, K. W., & Vogelstein, B. (1997) · Molecular Cell · doi:10.1016/s1097-2765(00)80002-7 · Cited by 1,251 · see citing works

Germ-line transmission of a mutated p53 gene in a cancer-prone family with Li–Fraumeni syndrome

Srivastava, S. K., Zou, Z., Pirollo, K. F., Blattner, W. A., & Chang, E. H. (1990) · Nature · doi:10.1038/348747a0 · Cited by 1,210 · see citing works

The alternative product from the human CDKN2A locus, p14ARF, participates in a regulatory feedback loop with p53 and MDM2

Stott, F. J., Bates, S., James, M. C., McConnell, B. B., Starborg, M., Brookes, S., Palmero, I., Ryan, K. M., Hara, E., Vousden, K. H., et al. (1998) · The EMBO Journal · doi:10.1093/emboj/17.17.5001 · Cited by 1,165 · see citing works

Ca 2+ -Induced Apoptosis Through Calcineurin Dephosphorylation of BAD

Wang, H., Pathan, N., Ethell, I. M., Krajewski, S., Yamaguchi, Y., Shibasaki, F., McKeon, F., Bobo, T., Franke, T. F., & Reed, J. C. (1999) · Science · doi:10.1126/science.284.5412.339 · Cited by 1,132 · see citing works

KILLER/DR5 is a DNA damage–inducible p53–regulated death receptor gene

Wu, G. S., Burns, T. F., McDonald, E. R., Jiang, W., Meng, R., Krantz, I. D., Kao, G., Gan, D.-D., Zhou, J.-Y., Muschel, R. J., et al. (1997) · Nature Genetics · doi:10.1038/ng1097-141 · Cited by 1,081 · see citing works

Post‐translational modifications and activation of p53 by genotoxic stresses

Appella, E., & Anderson, C. W. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02225.x · Cited by 1,071 · see citing works

Mdm2 Is a RING Finger-dependent Ubiquitin Protein Ligase for Itself and p53

Fang, S., Jensen, J. P., Ludwig, R. L., Vousden, K. H., & Weissman, A. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.8945 · Cited by 1,044 · see citing works

Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization

Li, M., Chen, D., Shiloh, A., Luo, J., Nikolaev, A. Y., Qin, J., & Gu, W. J. (2002) · Nature · doi:10.1038/nature737 · Cited by 1,027 · see citing works

The INK4a/ARF network in tumour suppression

Sherr, C. J. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35096061 · Cited by 984 · see citing works

ONYX-015, an E1B gene-attenuated adenovirus, causes tumor-specific cytolysis and antitumoral efficacy that can be augmented by standard chemotherapeutic agents

Heise, C. C., Sampson-Johannes, A., Williams, A., McCormick, F. P., Hoff, D. D. V., & Kirn, D. H. (1997) · Nature Medicine · doi:10.1038/nm0697-639 · Cited by 941 · see citing works

Nucleolar Arf sequesters Mdm2 and activates p53

Weber, J. D., Taylor, L. J., Roussel, M. F., Sherr, C. J., & Bar-Sagi, D. (1999) · Nature Cell Biology · doi:10.1038/8991 · Cited by 940 · see citing works

Functional and physical interactions of the ARF tumor suppressor with p53 and Mdm2

Kamijo, T., Weber, J. D., Zambetti, G., Zindy, F., Roussel, M. F., & Sherr, C. J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.14.8292 · Cited by 899 · see citing works

p53 Activates the CD95 (APO-1/Fas) Gene in Response to DNA Damage by Anticancer Drugs

Müller, M., Wilder, S., Bannasch, D., Israeli, D., Lehlbach, K., Li-Weber, M., Friedman, S. L., Galle, P. R., Stremmel, W., Oren, M., et al. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.188.11.2033 · Cited by 878 · see citing works

Deacetylation of p53 modulates its effect on cell growth and apoptosis

Luo, J., Su, F., Chen, D., Shiloh, A., & Gu, W. J. (2000) · Nature · doi:10.1038/35042612 · Cited by 818 · see citing works

Chk2/hCds1 functions as a DNA damage checkpoint in G₁by stabilizing p53

Chehab, N. H., Malikzay, A., Appel, M., & Halazonetis, T. D. (2000) · Genes & Development · doi:10.1101/gad.14.3.278 · Cited by 805 · see citing works

Regulation ofp53downstream genes

El‐Deiry, W. S. (1998) · Seminars in Cancer Biology · doi:10.1006/scbi.1998.0097 · Cited by 797 · see citing works

The many substrates and functions of ATM.

Kastan, M. B., & Lim, D.-S. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35043058 · Cited by 779 · see citing works

A leucine-rich nuclear export signal in the p53 tetramerization domain: regulation of subcellular localization and p53 activity by NES masking

Stommel, J. M., Marchenko, N. D., Jimenez, G. S., Moll, U. M., Hope, T. J., & Wahl, G. M. (1999) · The EMBO Journal · doi:10.1093/emboj/18.6.1660 · Cited by 738 · see citing works

Wild-Type Human p53 and a Temperature-Sensitive Mutant Induce Fas/APO-1 Expression

Owen‐Schaub, L. B., Zhang, W. K., Cusack, J. C., Angelo, L. S., Santee, S. M., Fujiwara, T., Roth, J. A., Deisseroth, A., Zhang, W., Kruzel, E., et al. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.6.3032 · Cited by 731 · see citing works

Detection of a transformation-related antigen in chemically induced sarcomas and other transformed cells of the mouse.

DeLeo, A. B., Jay, G. D., Appella, E., DuBois, G. C., Law, L. W., & Old, L. J. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.5.2420 · Cited by 721 · see citing works

Pirh2, 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

Tumorigenic potential associated with enhanced expression of a gene that is amplified in a mouse tumor cell line.

Fakharzadeh, S. S., Trusko, S. P., & George, D. L. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07676.x · Cited by 704 · 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

Binding and modulation of p53 by p300/CBP coactivators

Lill, N. L., Grossman, S. R., Ginsberg, D., DeCaprio, J. A., & Livingston, D. M. (1997) · Nature · doi:10.1038/42981 · Cited by 693 · see citing works

Mapping of the p53 and mdm-2 Interaction Domains

Chen, J., Maréchal, V., & Levine, A. J. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.7.4107 · Cited by 689 · 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

Oncogenic mutations of the p53 tumor suppressor: the demons of the guardian of the genome.

Sigal, A., & Rotter, V. (2000) · PubMed · Cited by 669 · see citing works

Regulating Access to the Genome

Weis, K. (2003) · Cell · doi:10.1016/s0092-8674(03)00082-5 · Cited by 668 · see citing works

Recruitment of p300/CBP in p53-Dependent Signal Pathways

Avantaggiati, M. L., Ogryzko, V. V., Gardner, K., Giordano, A., Levine, A. S., & Kelly, K. (1997) · Cell · doi:10.1016/s0092-8674(00)80304-9 · Cited by 668 · see citing works

14-3-3 Proteins and Survival Kinases Cooperate to Inactivate BAD by BH3 Domain Phosphorylation

Datta, S. R., Katsov, A., Hu, L. S., Petros, A. M., Fesik, S. W., Yaffe, M. B., & Greenberg, M. E. (2000) · Molecular Cell · doi:10.1016/s1097-2765(05)00012-2 · Cited by 663 · see citing works

Several hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 E1B 55-kD protein.Preprint

Lin, J., Chen, J., Elenbaas, B., & Levine, A. J. (1994) · Genes & Development · doi:10.1101/gad.8.10.1235 · Cited by 652 · 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

Regulation of HDM2 activity by the ribosomal protein L11

Lohrum, M. A. E., Ludwig, R. L., Kubbutat, M. H. G., Hanlon, M., & Vousden, K. H. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00134-x · Cited by 626 · see citing works

Nucleo‐cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein

Roth, J., Dobbelstein, M., Freedman, D. A., Shenk, T., & Levine, A. J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.2.554 · Cited by 610 · see citing works

Synergistic activation of transcription by CBP and p53

Gu, W., Shi, X.-L., & Roeder, R. G. (1997) · Nature · doi:10.1038/42972 · Cited by 596 · see citing works

Inactivation 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

Interaction between the retinoblastoma protein and the oncoprotein MDM2

Xiao, Z.-X., Chen, J., Levine, A. J., Modjtahedi, N., Xing, J. W., Sellers, W. R., & Livingston, D. M. (1995) · Nature · doi:10.1038/375694a0 · Cited by 586 · see citing works

Phosphorylation of Ser-20 mediates stabilization of human p53 in response to DNA damage.

Chehab, N. H., Malikzay, A., Stavridi, E. S., & Halazonetis, T. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.13777 · Cited by 583 · see citing works

p300/CBP‐mediated p53 acetylation is commonly induced by p53‐activating agents and inhibited by MDM2

Ito, A., Lai, C.-H., Zhao, X., Saito, S., Hamilton, M. H., Appella, E., & Yao, T. (2001) · The EMBO Journal · doi:10.1093/emboj/20.6.1331 · Cited by 582 · see citing works

Mdm2-Mediated NEDD8 Conjugation of p53 Inhibits Its Transcriptional Activity

Xirodimas, D. P., Saville, M. K., Bourdon, J.-C., Hay, R. T., & Lane, D. P. (2004) · Cell · doi:10.1016/j.cell.2004.06.016 · Cited by 570 · see citing works

14-3-3 transits to the nucleus and participates in dynamic nucleocytoplasmic transport

Brunet, A., Kanai, F., Stehn, J. R., Xu, J., Sarbassova, D. A., Frangioni, J. V., Dalal, S. N., DeCaprio, J. A., Greenberg, M. E., & Yaffe, M. B. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200112059 · Cited by 562 · see citing works

Inhibition of p53 transactivation required for transformation by adenovirus early 1B protein

Yew, P. R., & Berk, A. J. (1992) · Nature · doi:10.1038/357082a0 · Cited by 557 · see citing works

Ribosomal Protein L11 Negatively Regulates Oncoprotein MDM2 and Mediates a p53-Dependent Ribosomal-Stress Checkpoint Pathway

Zhang, Y., Wolf, G. W., Bhat, K., Jin, A., Allio, T., Burkhart, W., & Xiong, Y. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.23.8902-8912.2003 · Cited by 556 · see citing works

Inhibition of MDM2-mediated p53 Ubiquitination and Degradation by Ribosomal Protein L5

Dai, M., & Lu, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403722200 · Cited by 536 · see citing works

Nucleophosmin regulates the stability and transcriptional activity of p53

Colombo, E., Marine, J., Danovi, D., Falini, B., & Pelicci, P. G. (2002) · Nature Cell Biology · doi:10.1038/ncb814 · Cited by 528 · see citing works

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

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

Nuclear Export Is Required for Degradation of Endogenous p53 by MDM2 and Human Papillomavirus E6

Freedman, D. A., & Levine, A. J. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.12.7288 · Cited by 513 · see citing works

Untitled work

(1994) · PubMed · Cited by 509 · see citing works

p63 and p73: p53 mimics, menaces and more

Yang, A., & McKeon, F. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35043127 · Cited by 504 · see citing works

Wild-type p53 binds to the TATA-binding protein and represses transcription.

Seto, E., Usheva, A., Zambetti, G. P., Momand, J. A., Horikoshi, N., Weinmann, R. S., Levine, A. J., & Shenk, T. E. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.24.12028 · Cited by 504 · see citing works

14-3-3 proteins: a highly conserved, widespread family of eukaryotic proteins

Aitken, A., Collinge, D. B., van Heusden, B. P. H., Isobe, T., Roseboom, P. H., Rosenfeld, G. C., & Soll, J. (1992) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(92)90339-b · Cited by 496 · see citing works

Ribosomal Protein L23 Activates p53 by Inhibiting MDM2 Function in Response to Ribosomal Perturbation but Not to Translation Inhibition

Dai, M., Zeng, S. X., Jin, Y., Sun, X., David, L. L., & Lu, H. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.17.7654-7668.2004 · Cited by 495 · see citing works

A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity

Tzivion, G., Luo, Z., & Avruch, J. (1998) · Nature · doi:10.1038/27938 · Cited by 482 · see citing works

ATM associates with and phosphorylates p53: mapping the region of interaction

Khanna, K. K., Keating, K. E., Kozlov, S., Scott, S. P., Gatei, M. H., Hobson, K., Taya, Y., Gabrielli, B. G., Chan, D. W., Lees‐Miller, S. P., et al. (1998) · Nature Genetics · doi:10.1038/3882 · Cited by 481 · see citing works

ATM-dependent activation of p53 involves dephosphorylation and association with 14-3-3 proteins

Waterman, M. J. F., Stavridi, E. S., Waterman, J. L. F., & Halazonetis, T. D. (1998) · Nature Genetics · doi:10.1038/542 · Cited by 457 · see citing works

Serine 15 phosphorylation stimulates p53 transactivation but does not directly influence interaction with HDM2

Dumaz, N., & Meek, D. W. (1999) · The EMBO Journal · doi:10.1093/emboj/18.24.7002 · Cited by 455 · see citing works

IARC Database of p53 gene mutations in human tumors and cell lines: updated compilation, revised formats and new visualisation tools

Hainaut, P. L. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.1.205 · Cited by 446 · see citing works

High frequency of hypermethylation at the 14-3-3 σ locus leads to gene silencing in breast cancer

Ferguson, A. T., Evron, E., Umbricht, C. B., Pandita, T. K., Chan, T. A.-T., Hermeking, H., Marks, J. R., Lambers, A. R., Futreal, P. A., Stampfer, M. R., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.100566997 · Cited by 444 · see citing works

INK4a/ARF: A multifunctional tumor suppressor locus

Sharpless, N. E. (2005) · Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis · doi:10.1016/j.mrfmmm.2004.08.021 · Cited by 442 · cited 2× · see citing works

Chk2‐deficient mice exhibit radioresistance and defective p53‐mediated transcription

Takai, H., Naka, K., Okada, Y., Watanabe, M., Harada, N., Saito, S., Anderson, C. W., Appella, E., Nakanishi, M., Suzuki, H., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf506 · Cited by 435 · see citing works

The 14-3-3 cancer connection

Hermeking, H. (2003) · Nature reviews. Cancer · doi:10.1038/nrc1230 · Cited by 434 · see citing works

Phosphorylation of p53 Serine 15 Increases Interaction with CBP

Lambert, P. F., Kashanchi, F., Radonovich, M. F., Shiekhattar, R., & Brady, J. N. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.49.33048 · Cited by 423 · see citing works

Chk2 Is a Tumor Suppressor That Regulates Apoptosis in both an Ataxia Telangiectasia Mutated (ATM)-Dependent and an ATM-Independent Manner

Hirao, A., Cheung, A., Duncan, G. S., Girard, P.-M., Elia, A., Wakeham, A. C., Okada, H., Sarkissian, T., Wong, J. A., Sakai, T., et al. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.18.6521-6532.2002 · Cited by 404 · see citing works

Chk2 kinase — a busy messenger

Bártek, J., Falck, J., & Lukas, J. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35103059 · Cited by 400 · see citing works

Threonine 68 phosphorylation by ataxia telangiectasia mutated is required for efficient activation of Chk2 in response to ionizing radiation.

Ahn, J. Y., Schwarz, J. K., Piwnica-Worms, H. M., & Canman, C. E. (2000) · PubMed · Cited by 396 · see citing works

Crystal Structure of the 14-3-3ζ:Serotonin N-Acetyltransferase Complex

Obšil, T., Ghirlando, R., Klein, D. C., Ganguly, S., & Dyda, F. (2001) · Cell · doi:10.1016/s0092-8674(01)00316-6 · Cited by 389 · see citing works

Overexpression of Mdm2 in mice reveals a p53-independent role for Mdm2 in tumorigenesis

Jones, S. N., Hancock, A. R., Vogel, H., Donehower, L. A., & Bradley, A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.26.15608 · Cited by 386 · see citing works

Multiple C-Terminal Lysine Residues Target p53 for Ubiquitin-Proteasome-Mediated Degradation

Rodríguez, M. S., Desterro, J. M. P., Laı́n, S., Lane, D. P., & Hay, R. T. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.22.8458-8467.2000 · Cited by 386 · see citing works

The Human Myt1 Kinase Preferentially Phosphorylates Cdc2 on Threonine 14 and Localizes to the Endoplasmic Reticulum and Golgi Complex

Liu, F., Stanton, J. J., Wu, Z., & Piwnica-Worms, H. M. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.2.571 · Cited by 378 · see citing works

Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase

Honda, R., & Yasuda, H. (2000) · Oncogene · doi:10.1038/sj.onc.1203464 · Cited by 376 · see citing works

Functional inactivation but not structural mutation of p53 causes liver cancer

Ueda, H., Ullrich, S. J., Gangemi, J. D., Kappel, C. A., Ngo, L. T., Feitelson, M. A., & Jay, G. (1995) · Nature Genetics · doi:10.1038/ng0195-41 · 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

Inhibition of HDM2 and Activation of p53 by Ribosomal Protein L23

Jin, A., Itahana, K., O’Keefe, K. J., & Zhang, Y. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.17.7669-7680.2004 · Cited by 356 · see citing works

Molecular analysis and chromosomal mapping of amplified genes isolated from a transformed mouse 3T3 cell line

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

Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53

Tao, W., & Levine, A. J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3077 · Cited by 355 · see citing works

Intracellular localization of proteasomes

Wójcik, C., & Demartino, G. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(02)00380-1 · Cited by 354 · see citing works

Pidd, a new death-domain–containing protein, is induced by p53 and promotes apoptosis

Lin, Y., Ma, W., & Benchimol, S. (2000) · Nature Genetics · doi:10.1038/79102 · Cited by 353 · see citing works

STAT3 nuclear import is independent of tyrosine phosphorylation and mediated by importin-α3

Liu, L., McBride, K. M., & Reich, N. C. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501643102 · Cited by 348 · see citing works

Mutations in Human ARF Exon 2 Disrupt Its Nucleolar Localization and Impair Its Ability to Block Nuclear Export of MDM2 and p53

Zhang, Y., & Xiong, Y. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80351-2 · Cited by 347 · see citing works

14-3-3 Interacts Directly with and Negatively Regulates Pro-apoptotic Bax

Nomura, M., Shimizu, S., Sugiyama, T., Narita, M., Ito, T., Matsuda, H., & Tsujimoto, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m207880200 · Cited by 345 · see citing works

14-3-3ζ Binds a Phosphorylated Raf Peptide and an Unphosphorylated Peptide via Its Conserved Amphipathic Groove

Petosa, C., Masters, S. C., Bankston, L. A., Pohl, J., Wang, B., Fu, H., & Liddington, R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.26.16305 · Cited by 345 · see citing works

The p53 response to DNA damage

Meek, D. W. (2004) · DNA Repair · doi:10.1016/j.dnarep.2004.03.027 · Cited by 329 · see citing works

Regulation of mdm2 expression by p53: alternative promoters produce transcripts with nonidentical translation potential.

Barak, Y., Gottlieb, E., Juven-Gershon, T., & Oren, M. (1994) · Genes & Development · doi:10.1101/gad.8.15.1739 · Cited by 328 · see citing works

MDM2 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

Small molecule inhibitors of HDM2 ubiquitin ligase activity stabilize and activate p53 in cells

Yang, Y., Ludwig, R. L., Jensen, J. P., Pierre, S. A., Medaglia, M. V., Davydov, I. V., Safiran, Y. J., Oberoi, P., Kenten, J. H., Phillips, A. C., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.04.029 · Cited by 321 · see citing works

Hypoxia Links ATR and p53 through Replication Arrest

Hammond, E. M., Denko, N. C., Dorie, M. J., Abraham, R. T., & Giaccia, A. J. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.6.1834-1843.2002 · Cited by 321 · see citing works

The Ribosomal L5 Protein Is Associated with mdm-2 and mdm-2-p53 Complexes

Maréchal, V., Elenbaas, B., Piette, J., Nicolas, J. C., & Levine, A. J. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.11.7414 · Cited by 318 · see citing works

Involvement of 14‐3‐3 proteins in nuclear localization of telomerase

Seimiya, H., Sawada, H., Muramatsu, Y., Shimizu, M., Ohko, K., Yamane, K., & Tsuruo, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.11.2652 · Cited by 314 · see citing works

Mdm4 (Mdmx) regulates p53-induced growth arrest and neuronal cell death during early embryonic mouse development

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

The mdm-2 oncogene can overcome wild-type p53 suppression of transformed cell growth.

Finlay, C. A. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.1.301 · Cited by 311 · see citing works

Amplification of <i>Mdmx</i> (or <i>Mdm4</i> ) Directly Contributes to Tumor Formation by Inhibiting p53 Tumor Suppressor Activity

Danovi, 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

14-3-3 proteins; bringing new definitions to scaffolding

Tzivion, G., Shen, Y. H., & Zhu, J. (2001) · Oncogene · doi:10.1038/sj.onc.1204777 · Cited by 300 · see citing works

Database of p53 gene somatic mutations in human tumors and cell lines: updated compilation and future prospects

Hainaut, P. L., Soussi, T., Shomer, B., Hollstein, M. C., Greenblatt, M. S., Hovig, E. J., Harris, C. C., & Montesano, R. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.1.151 · Cited by 299 · see citing works

Pharmacologic activation of p53 elicits Bax-dependent apoptosis in the absence of transcription

Chipuk, J. E., Maurer, U., Green, D. R., & Schüler, M. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00272-1 · Cited by 297 · see citing works

The human MDM-2 oncogene is overexpressed in leukemias

Bueso-Ramos, C., Yang, Y. S., deLeon, E., McCown, P., Stass, S. A., & Albitar, M. X. (1993) · Blood · doi:10.1182/blood.v82.9.2617.bloodjournal8292617 · Cited by 292 · see citing works

Nucleophosmin (B23) Targets ARF to Nucleoli and Inhibits Its Function

Korgaonkar, C. K., Hagen, J., Tompkins, V. S., Frazier, A. A., Allamargot, C., Quelle, F. W., & Quelle, D. E. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.4.1258-1271.2005 · Cited by 290 · 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

Isoforms of 14‐3‐3 protein can form homo‐ and heterodimers in vivo and in vitro: implications for function as adapter proteins

Jones, D. H., Ley, S. C., & Aitken, A. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00598-4 · Cited by 279 · see citing works

Repression of p53-mediated transcription by MDM2: a dual mechanism

Thut, C. J., Goodrich, J. A., & Tjian, R. (1997) · Genes &amp; Development · doi:10.1101/gad.11.15.1974 · Cited by 272 · see citing works

Small-Molecule Antagonists of p53-MDM2 Binding: Research Tools and Potential Therapeutics

Vassilev, L. T. (2004) · Cell Cycle · doi:10.4161/cc.3.4.801 · Cited by 271 · 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

Loss of HAUSP-mediated deubiquitination contributes to DNA damage-induced destabilization of Hdmx and Hdm2.

Meulmeester, 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

ATM 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

Effects of genetic background on tumorigenesis in <i>p53</i>‐deficient mice

Donehower, L. A., Harvey, M., Vogel, H., McArthur, M. J., Montgomery, C. A., Park, S. H., Thompson, T., Ford, R. J., & Bradley, A. (1995) · Molecular Carcinogenesis · doi:10.1002/mc.2940140105 · Cited by 252 · see citing works

14-3-3 Proteins—a focus on cancer and human disease

Wilker, E., & Yaffe, M. B. (2004) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2004.04.015 · Cited by 251 · see citing works

An ATR- and Chk1-Dependent S Checkpoint Inhibits Replicon Initiation following UVC-Induced DNA Damage

Heffernan, T. P., Simpson, D. A., Frank, A. R., Heinloth, A. N., Paules, R. S., Cordeiro-Stone, M., & Kaufmann, W. K. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.24.8552-8561.2002 · Cited by 251 · see citing works

Regulation of apoptosis: the ubiquitous way

Yang, Y., & Xiao-dan, Y. (2003) · The FASEB Journal · doi:10.1096/fj.02-0654rev · Cited by 249 · see citing works

Essential role of ribosomal protein L11 in mediating growth inhibition‐induced p53 activation

Bhat, K., Itahana, K., Jin, A., & Zhang, Y. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600247 · Cited by 249 · see citing works

Mapping of the p53 and mdm-2 Interaction Domains

Chen, J., Maréchal, V., & Levine, A. J. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.7.4107-4114.1993 · 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 3× · see citing works

Untitled work

(1997) · PubMed · Cited by 243 · see citing works

p53 in recombination and repair

Gatz, S. A., & Wiesmüller, L. (2006) · Cell Death &amp; Differentiation · doi:10.1038/sj.cdd.4401903 · Cited by 242 · see citing works

MDMX overexpression prevents p53 activation by the MDM2 inhibitor Nutlin

Hu, B., Gilkes, D. M., Farooqi, B., Sebti, S. M., & Chen, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c600147200 · Cited by 236 · see citing works

Targeted expression of MDM2 uncouples S phase from mitosis and inhibits mammary gland development independent of p53.

Lundgren, K., Montes de Oca Luna, R., McNeill, Y. B., Emerick, E. P., Spencer, B., Barfield, C. R., Lozano, G., Rosenberg, M. P., & Finlay, C. A. (1997) · Genes &amp; Development · doi:10.1101/gad.11.6.714 · Cited by 235 · see citing works

Mdmx 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

14-3-3σ Positively Regulates p53 and Suppresses Tumor Growth

Yang, H.-Y., Wen, Y.-Y., Chen, C.-H., Lozano, G., & Lee, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.20.7096-7107.2003 · Cited by 229 · see citing works

Tissue and cell-specific expression of the p53-target genes: bax, fas, mdm2 and waf1/p21, before and following ionising irradiation in mice

Bouvard, V., Zaitchouk, T., Vacher, M., Duthu, A., Canivet, M., Choisy, C., Nieruchalski, M., & May, E. (2000) · Oncogene · doi:10.1038/sj.onc.1203366 · Cited by 219 · see citing works

14-3-3 proteins as potential oncogenes

Tzivion, G., Gupta, V. S., Kaplun, L., & Balan, V. (2006) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2006.03.004 · Cited by 218 · see citing works

Regulation of p53 localization

Liang, S., & Clarke, M. F. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02227.x · Cited by 216 · 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 5× · see citing works

Tumor suppression and normal aging in mice with constitutively high p53 activity

Mendrysa, S. M., O'Leary, K. A., McElwee, M. K., Michalowski, J., Eisenman, R. N., Powell, D. A., & Perry, M. E. (2006) · Genes &amp; Development · doi:10.1101/gad.1378506 · Cited by 210 · see citing works

Multiple Lysine Mutations in the C-Terminal Domain of p53 Interfere with MDM2-Dependent Protein Degradation and Ubiquitination

Nakamura, S., Roth, J. A., & Mukhopadhyay, T. K. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.24.9391-9398.2000 · Cited by 198 · see citing works

14-3-3 (ϵ) Interacts with the Insulin-like Growth Factor I Receptor and Insulin Receptor Substrate I in a Phosphoserine-dependent Manner

Craparo, A., Freund, R., & Gustafson, T. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.17.11663 · Cited by 196 · see citing works

MDM2 inhibits p300-mediated p53 acetylation and activation by forming a ternary complex with the two proteins

Kobet, E., Zeng, X., Zhu, Y., Keller, D., & Lu, H. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.23.12547 · Cited by 193 · see citing works

mdmx 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

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

HAUSP is Required for p53 Destabilization

Cummins, J. M., & Vogelstein, B. (2004) · Cell Cycle · doi:10.4161/cc.3.6.924 · Cited by 188 · see citing works

Identification of a cryptic nucleolar-localization signal in MDM2

Lohrum, M. A. E., Ashcroft, M. A., Kubbutat, M. H. G., & Vousden, K. H. (2000) · Nature Cell Biology · doi:10.1038/35004057 · Cited by 186 · see citing works

The SV40 a gene product is required for the production of a 54,000 MW cellular tumor antigen

Linzer, D. I. H., Maltzman, W., & Levine, A. J. (1979) · Virology · doi:10.1016/0042-6822(79)90554-3 · Cited by 184 · see citing works

Identification of novel mdm2 binding peptides by phage display.

Böttger, V., Böttger, A., Howard, S. F., Picksley, S. M., Chêne, P., Garcı́a-Echeverrı́a, C., Hochkeppel, H. K., & Lane, D. P. (1996) · PubMed · Cited by 182 · see citing works

Phosphorylation 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

Inhibition of MDM2 by hsp90 Contributes to Mutant p53 Stabilization

Peng, Y., Chen, L., Li, C., Lu, W., & Chen, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102817200 · Cited by 180 · see citing works

Control of p53 ubiquitination and nuclear export by MDM2 and ARF.

Zhang, Y., & Xiong, Y. (2001) · PubMed · Cited by 176 · see citing works

Mutant p53-dependent growth suppression distinguishes PRIMA-1 from known anticancer drugs: a statistical analysis of information in the National Cancer Institute database

Bykov, V. J. N. (2002) · Carcinogenesis · doi:10.1093/carcin/23.12.2011 · Cited by 172 · see citing works

p53 Activation by Small Molecules: Application in Oncology

Vassilev, L. T. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm058174k · Cited by 172 · see citing works

ATM-Mediated Phosphorylations Inhibit Mdmx/Mdm2 Stabilization by HAUSP in Favor of p53 Activation

Meulmeester, E., Pereg, Y., Shiloh, Y., & Jochemsen, A. G. (2005) · Cell Cycle · doi:10.4161/cc.4.9.1981 · Cited by 166 · see citing works

The role of RB in cell cycle control

Hatakeyama, M., & Weinberg, R. A. (1995) · Springer eBooks · doi:10.1007/978-1-4615-1809-9_2 · Cited by 164 · 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

Identification of the p53 protein domain involved in formation of the simian virus 40 large T-antigen-p53 protein complex

Tan, T., Wallis, J., & Levine, A. J. (1986) · Journal of Virology · doi:10.1128/jvi.59.3.574-583.1986 · Cited by 159 · see citing works

Synergistic 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

The G2/M Regulator 14-3-3ς Prevents Apoptosis through Sequestration of Bax

Samuel, T., Weber, H. O., Rauch, P., Verdoodt, B., Eppel, J.-T., McShea, A., Hermeking, H., & Funk, J. O. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106427200 · Cited by 155 · see citing works

Mammalian and yeast 14-3-3 isoforms form distinct patterns of dimers in vivo

Chaudhri, M., Scarabel, M., & Aitken, A. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02902-9 · Cited by 154 · see citing works

The Chk2 Tumor Suppressor Is Not Required for p53 Responses in Human Cancer Cells

Jallepalli, P. V., Lengauer, C., Vogelstein, B., & Bunz, F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213159200 · Cited by 154 · 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

Tissue-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

Regulation of Chk1 Includes Chromatin Association and 14-3-3 Binding following Phosphorylation on Ser-345

Jiang, K., Pereira, E., Maxfield, M. D., Russell, B., Goudelock, D. M., & Sánchez, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300070200 · Cited by 147 · see citing works

Hdmx Stabilizes Mdm2 and p53

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

Hdmx 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

MDMX regulation of p53 response to ribosomal stress

Gilkes, D. M., Chen, L., & Chen, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601424 · Cited by 142 · see citing works

Phosphorylation of β-Catenin by AKT Promotes β-Catenin Transcriptional Activity*

Fang, D.-X., Hawke, D., Zheng, Y., Xia, Y., Meisenhelder, J., Nika, H., Mills, G., Kobayashi, R., Hunter, T., & Lu, Z. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611871200 · Cited by 774 · see citing works

CHK2 kinase in the DNA damage response and beyond

Zannini, L., Delia, D., & Buscemi, G. (2014) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mju045 · Cited by 455 · 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

The dynamic and stress-adaptive signaling hub of 14-3-3: emerging mechanisms of regulation and context-dependent protein–protein interactions

Pennington, K. L., Ty, C., Torres, M. P., & Andersen, J. (2018) · Oncogene · doi:10.1038/s41388-018-0348-3 · Cited by 365 · see citing works

Regulation 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

Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans

Linke, K., Mace, P. D., Smith, C. A., Vaux, D. L., Silke, J., & Day, C. L. (2008) · Cell Death &amp; Differentiation · doi:10.1038/sj.cdd.4402309 · Cited by 288 · see citing works

CHK2 kinase: cancer susceptibility and cancer therapy – two sides of the same coin?

Antoni, L., Sodha, N., Collins, I., & Garrett, M. D. (2007) · Nature reviews. Cancer · doi:10.1038/nrc2251 · Cited by 287 · see citing works

Mechanism of p53 stabilization by ATM after DNA damage

Cheng, Q., & Chen, J. (2010) · Cell Cycle · doi:10.4161/cc.9.3.10556 · Cited by 248 · see citing works

Taking the time to make important decisions: The checkpoint effector kinases Chk1 and Chk2 and the DNA damage response

Stracker, T. H., Usui, T., & Petrini, J. H. J. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.04.012 · Cited by 245 · see citing works

MDMX overexpression prevents p53 activation by the MDM2 inhibitor Nutlin

Hu, B., Gilkes, D. M., Farooqi, B., Sebti, S. M., & Chen, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c600147200 · Cited by 236 · see citing works

MDMX: from bench to bedside

Marine, J.-C. W., Dyer, M. A., & Jochemsen, A. G. (2007) · Journal of Cell Science · doi:10.1242/jcs.03362 · Cited by 228 · see citing works

Efficient p53 Activation and Apoptosis by Simultaneous Disruption of Binding to MDM2 and MDMX

Hu, B., Gilkes, D. M., & Chen, J. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-1140 · Cited by 214 · 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

14-3-3ζ Cooperates with ErbB2 to Promote Ductal Carcinoma In Situ Progression to Invasive Breast Cancer by Inducing Epithelial-Mesenchymal Transition

Lü, J., Guo, H., Treekitkarnmongkol, W., Li, P., Zhang, J., Shi, B., Ling, C., Zhou, X., Chen, T., Chiao, P. J., et al. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.08.010 · Cited by 193 · see citing works

An essential function of the extreme C-terminus of MDM2 can be provided by MDMX

Uldrijan, S., Pannekoek, W., & Vousden, K. H. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601469 · Cited by 170 · see citing works

The role of ubiquitin modification in the regulation of p53

Hock, A. K., & Vousden, K. H. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.05.022 · Cited by 168 · see citing works

Hdmx modulates the outcome of p53 activation in human tumor cells

Wade, M., Wong, E. T., Tang, M., Stommel, J. M., & Wahl, G. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605405200 · Cited by 163 · see citing works

MDMX regulation of p53 response to ribosomal stress

Gilkes, D. M., Chen, L., & Chen, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601424 · Cited by 142 · see citing works

Regulation of p53: a collaboration between Mdm2 and MdmX

Pei, D., Zhang, Y., & Zheng, J. (2012) · Oncotarget · doi:10.18632/oncotarget.443 · Cited by 140 · see citing works

Chibby cooperates with 14-3-3 to regulate β-catenin subcellular distribution and signaling activity

Li, F., Mofunanya, A., Harris, K., & Takemaru, K. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200709091 · Cited by 140 · see citing works

The regulated assembly of a PKCɛ complex controls the completion of cytokinesis

Saurin, A. T., Durgan, J., Cameron, A. J. M., Faisal, A., Marber, M. S., & Parker, P. J. (2008) · Nature Cell Biology · doi:10.1038/ncb1749 · Cited by 128 · see citing works

MDM2 and MDMX: Alone and together in regulation of p53.

Shadfan, M., Lopez-Pajares, V., & Yuan, Z.-M. (2012) · PubMed · Cited by 125 · see citing works

The multiple checkpoint functions of CHK1 and CHK2 in maintenance of genome stability.

Chen, Y., & Poon, R. Y. C. (2008) · PubMed · doi:10.2741/3060 · Cited by 119 · see citing works

USP7 Is a Master Regulator of Genome Stability

Valles, G. J., Bezsonova, I., Woodgate, R., & Ashton, N. W. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00717 · Cited by 114 · see citing works

Quantitative analyses reveal the importance of regulated Hdmx degradation for p53 activation

Wang, Y. V., Wade, M., Wong, E., Li, Y.-C., Rodewald, L. W., & Wahl, G. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701497104 · Cited by 116 · see citing works

Mdm2 and MdmX partner to regulate p53

Wang, X., & Jiang, X. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.02.049 · Cited by 111 · see citing works

Regulation of the p53-MDM2 pathway by 14-3-3 σ and other proteins

Lee, M., & Lozano, G. (2006) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2006.03.009 · Cited by 108 · see citing works

AMP-Activated Protein Kinase Induces p53 by Phosphorylating MDMX and Inhibiting Its Activity

He, G., Zhang, Y.-W., Lee, J., Zeng, S. X., Wang, Y. V., Luo, Z., Dong, X. C., Viollet, B., Wahl, G. M., & Lu, H. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00670-13 · Cited by 105 · see citing works

EEF1A2 Inactivates p53 by Way of PI3K/AKT/mTOR-Dependent Stabilization of MDM4 in Hepatocellular Carcinoma

Pellegrino, R., Calvisi, D. F., Neumann, O., Kolluru, V., Wesely, J., Chen, X., Wang, C., Wüestefeld, T., Ladu, S., Elgohary, N., et al. (2013) · Hepatology · doi:10.1002/hep.26954 · Cited by 99 · 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

Phosphatases in the cellular response to DNA damage

Freeman, A. K., & Monteiro, Á. N. A. (2010) · Cell Communication and Signaling · doi:10.1186/1478-811x-8-27 · Cited by 93 · see citing works

hnRNPA1 couples nuclear export and translation of specific mRNAs downstream of FGF-2/S6K2 signalling

Roy, R., Durie, D., Li, H. Z., Liu, B., Skehel, J. M., Mauri, F. A., Cuorvo, L. V., Barbareschi, M., Guo, L., Holčı́k, M., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku953 · Cited by 91 · see citing works

Balance of Yin and Yang: Ubiquitylation-Mediated Regulation of p53 and c-Myc

Dai, M., Jin, Y., Gallegos, J. R., & Lu, H. (2006) · Neoplasia · doi:10.1593/neo.06334 · Cited by 83 · see citing works

MDMX (MDM4), a Promising Target for p53 Reactivation Therapy and BeyondPreprint

Marine, J., & Jochemsen, A. G. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026237 · Cited by 81 · see citing works

Regulation of MDMX Expression by Mitogenic Signaling

Gilkes, D. M., Pan, Y., Coppola, D., Yeatman, T., Reuther, G. W., & Chen, J. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01633-07 · Cited by 82 · see citing works

Phosphorylation of MDMX Mediated by Akt Leads to Stabilization and Induces 14-3-3 Binding

Lopez-Pajares, V., Kim, M. M., & Yuan, Z.-M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710030200 · Cited by 79 · see citing works

MDM4 (MDMX) localizes at the mitochondria and facilitates the p53‐mediated intrinsic‐apoptotic pathway

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

Increased Radioresistance and Accelerated B Cell Lymphomas in Mice with Mdmx Mutations that Prevent Modifications by DNA-Damage-Activated Kinases

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

MDMX Promotes Proteasomal Turnover of p21 at G1 and Early S Phases Independently of, but in Cooperation with, MDM2

Jin, Y., Zeng, S. X., Sun, X., Lee, H., Blattner, C., Xiao, Z. J., & Lu, H. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01198-07 · Cited by 79 · see citing works

The regulation of MDM2 by multisite phosphorylation—opportunities for molecular-based intervention to target tumours?

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

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

The long and the short of it: the MDM4 tail so far

Haupt, S., Mejía-Hernández, J. O., Vijayakumaran, R., Keam, S. P., & Haupt, Y. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz007 · 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

Regulation of the Mdm2-p53 signaling axis in the DNA damage response and tumorigenesis

Carr, M. I., & Jones, S. N. (2016) · Translational Cancer Research · doi:10.21037/tcr.2016.11.75 · Cited by 70 · see citing works

Activation and stabilization of human tryptophan hydroxylase 2 by phosphorylation and 14-3-3 binding

Winge, I., McKinney, J. A., Ying, M., D’Santos, C. S., Kleppe, R., Knappskog, P. M., & Haavik, J. (2008) · Biochemical Journal · doi:10.1042/bj20071033 · Cited by 68 · see citing works

Attenuation of T Cell Receptor Signaling by Serine Phosphorylation-mediated Lysine 30 Ubiquitination of SLP-76 Protein

Wang, X., Li, J.-P., Chiu, L.-L., Lan, J., Chen, D.-Y., Boomer, J. S., & Tan, T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.371062 · Cited by 67 · see citing works

Regulation of p53 by the 14-3-3 protein interaction network: new opportunities for drug discovery in cancer

Falcicchio, M., Ward, J. A., Macip, S., & Doveston, R. G. (2020) · Cell Death Discovery · doi:10.1038/s41420-020-00362-3 · Cited by 58 · see citing works

HDMX-L Is Expressed from a Functional p53-responsive Promoter in the First Intron of the HDMX Gene and Participates in an Autoregulatory Feedback Loop to Control p53 Activity

Phillips, A., Teunisse, A., Lam, S., Lodder, K., Darley, M., Emaduddin, M., Wolf, A., Richter, J., de Lange, J., Verlaan-de Vries, M., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.129726 · Cited by 55 · see citing works

Deubiquitinating enzyme regulation of the p53 pathway: A lesson from Otub1

Sun, X. (2014) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v5.i2.75 · Cited by 55 · see citing works

A Critical Role for Noncoding 5S rRNA in Regulating Mdmx Stability

Li, M., & Gu, W. J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.020 · Cited by 50 · see citing works

Autoinhibition of MDMX by intramolecular p53 mimicry

Chen, L., Borcherds, W. M., Wu, S., Becker, A., Schönbrunn, E., Daughdrill, G. W., & Chen, J. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1420833112 · Cited by 49 · see citing works

Casein Kinase 1α Regulates an MDMX Intramolecular Interaction To Stimulate p53 Binding

Wu, S., Chen, L., Becker, A., Schönbrunn, E., & Chen, J. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00851-12 · Cited by 48 · see citing works

The DNA damage response pathway in normal hematopoiesis and malignancies

Delia, D., & Mizutani, S. (2017) · International Journal of Hematology · doi:10.1007/s12185-017-2300-7 · Cited by 47 · see citing works

DNA Damage-Induced Cell Cycle Regulation and Function of Novel Chk2 Phosphoresidues

Buscemi, G., Carlessi, L., Zannini, L., Lisanti, S., Fontanella, E., Canevari, S., & Delia, D. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00534-06 · Cited by 44 · see citing works

Competitive ubiquitination activates the tumor suppressor p53

Li, X., Guo, M., Cai, L., Du, T., Liu, Y., Ding, H., Wang, H., Zhang, J., Chen, X., & Yan, C. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0463-x · Cited by 41 · see citing works

MDM4 (MDMX) and its Transcript Variants

Mancini, F., Conza, G. D., & Moretti, F. (2009) · Current Genomics · doi:10.2174/138920209787581280 · Cited by 39 · see citing works

Inhibition of MELK produces potential anti‐tumour effects in bladder cancer by inducing G1/S cell cycle arrest via the ATM/CHK2/p53 pathway

Chen, S., Zhou, Q., Guo, Z., Wang, Y., Wang, L., Liu, X., Lü, M., Ju, L., Xiao, Y., & Wang, X. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14878 · Cited by 37 · see citing works

MDM2 and MDMX in Cancer and Development

Marine, J. (2011) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/b978-0-12-380916-2.00003-6 · Cited by 38 · see citing works

Switching on p53: an essential role for protein phosphorylation?

Loughery, J., & Meek, D. W. (2013) · Biodiscovery · doi:10.7750/biodiscovery.2013.8.1 · Cited by 38 · see citing works

Functions of MDMX in the Modulation of the p53‐Response

Lenos, K., & Jochemsen, A. G. (2011) · BioMed Research International · doi:10.1155/2011/876173 · Cited by 38 · see citing works

Dual Phosphorylation of Btk by Akt/Protein Kinase B Provides Docking for 14-3-3ζ, Regulates Shuttling, and Attenuates both Tonic and Induced Signaling in B Cells

Mohammad, D. K., Nore, B. F., Hussain, A., Gustafsson, M. O., Mohamed, A. J., & Smith, C. I. E. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00247-13 · Cited by 37 · see citing works

Identification of a Suppressive Mechanism for Hedgehog Signaling through a Novel Interaction of Gli with 14-3-3

Asaoka, Y., Kanai, F., Ichimura, T., Tateishi, K., Tanaka, Y., Ohta, M., Seto, M., Tada, M., Ijichi, H., Ikenoue, T., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.038232 · Cited by 36 · see citing works

SMG7 is a critical regulator of p53 stability and function in DNA damage stress response

Luo, H., Cowen, L. E., Yu, G., Jiang, W. G., & Tang, Y. (2016) · Cell Discovery · doi:10.1038/celldisc.2015.42 · Cited by 33 · see citing works

The roles of MDM2 and MDMX phosphorylation in stress signaling to p53

Chen, J. (2012) · Genes &amp; Cancer · doi:10.1177/1947601912454733 · Cited by 33 · see citing works

The p53 inhibitor Mdm4 cooperates with multiple genetic lesions in tumourigenesis

Xiong, S., Pant, V., Zhang, Y., Aryal, N. K., You, M. J., Kusewitt, D. F., & Lozano, G. (2016) · The Journal of Pathology · doi:10.1002/path.4854 · Cited by 32 · see citing works

A polymorphic variant in human MDM4 associates with accelerated age of onset of estrogen receptor negative breast cancer

Kulkarni, D. A., Vázquez, A., Haffty, B. G., Bandera, E. V., Hu, W., Sun, Y., Toppmeyer, D., Levine, A. J., & Hirshfield, K. M. (2009) · Carcinogenesis · doi:10.1093/carcin/bgp224 · Cited by 32 · see citing works

Stochastic and Deterministic Models of Cellular p53 Regulation

Leenders, G. B., & Tuszyński, J. A. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00064 · Cited by 28 · see citing works

c-Abl Phosphorylation of Mdm2 Facilitates Mdm2-Mdmx Complex Formation

Waning, D. L., Lehman, J. A., Batuello, C. N., & Mayo, L. D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.183012 · Cited by 30 · see citing works

Controlling the Mdm2-Mdmx-p53 Circuit

Waning, D. L., Lehman, J. A., Batuello, C. N., & Mayo, L. D. (2010) · Pharmaceuticals · doi:10.3390/ph3051576 · Cited by 30 · see citing works

Mechanisms of TP53 Pathway Inactivation in Embryonic and Somatic Cells—Relevance for Understanding (Germ Cell) Tumorigenesis

Timmerman, D. M., Remmers, T. L., Hillenius, S., & Looijenga, L. H. J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22105377 · Cited by 26 · see citing works

Hypoxia Activates Tumor Suppressor p53 by Inducing ATR-Chk1 Kinase Cascade-mediated Phosphorylation and Consequent 14-3-3γ Inactivation of MDMX Protein

Lee, J.-H., Jin, Y., He, G., Zeng, S. X., Wang, Y. V., Wahl, G. M., & Lu, H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.336875 · Cited by 25 · see citing works

RBM10, a New Regulator of p53

Jung, J. H., Lee, H., Zeng, S. X., & Lu, H. (2020) · Cells · doi:10.3390/cells9092107 · Cited by 26 · see citing works

Drosophila Chk2 and p53 proteins induce stage-specific cell death independently during oogenesis

Bakhrat, A., Pritchett, T. L., Peretz, G., McCall, K., & Abdu, U. (2010) · APOPTOSIS · doi:10.1007/s10495-010-0539-z · Cited by 26 · see citing works

14-3-3γ Inhibition of MDMX-mediated p21 Turnover Independent of p53

Lee, J., & Lu, H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.190470 · Cited by 22 · see citing works

Regulation of MDM4

Markey, M. P. (2010) · Frontiers in bioscience · doi:10.2741/3780 · Cited by 24 · see citing works

Alternative UPS drug targets upstream the 26S proteasome

Hjerpe, R., & Rodríguez, M. S. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.11.021 · Cited by 24 · see citing works

Inauhzin Sensitizes p53-Dependent Cytotoxicity and Tumor Suppression of Chemotherapeutic Agents

Zhang, Y., Zhang, Q., Zeng, S. X., Hao, Q., & Lu, H. (2013) · Neoplasia · doi:10.1593/neo.13142 · Cited by 23 · see citing works

Phosphorylation and ubiquitination-dependent degradation of CABIN1 releases p53 for transactivation upon genotoxic stress

Choi, S., Jang, H., Roe, J., Kim, S., Cho, E., & Youn, H. (2013) · Nucleic Acids Research · doi:10.1093/nar/gks1319 · Cited by 21 · see citing works

Protecting the genome from mdm2 and mdmx

Melo, A. N., & Eischen, C. M. (2012) · Genes &amp; Cancer · doi:10.1177/1947601912454139 · Cited by 20 · see citing works

Mouse modelling of the MDM2/MDMX−p53 signalling axis

Tackmann, N. R., & Zhang, Y. (2017) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjx006 · Cited by 21 · see citing works

MDM4 alternative splicing and implication in MDM4 targeted cancer therapies.

Wu, J., Lu, G., & Wang, X. (2021) · PubMed Central · Cited by 19 · see citing works

Feeder-free culture of human pluripotent stem cells drives MDM4-mediated gain of chromosome 1q

Stavish, D., Price, C. J., Gelezauskaite, G., Alsehli, H., Leonhard, K. A., Taapken, S. M., McIntire, E. M., Laing, O., James, B. M., Riley, J. J., et al. (2024) · Stem Cell Reports · doi:10.1016/j.stemcr.2024.06.003 · Cited by 19 · see citing works

Chek2 DNA Damage Response Pathway and Inherited Breast Cancer Risk

Tung, N., & Silver, D. P. (2011) · Journal of Clinical Oncology · doi:10.1200/jco.2011.37.1476 · Cited by 17 · see citing works

Profiling the proteome dynamics during the cell cycle of human hepatoma cells

Hsieh, S., Zhuang, F., Wu, Y., Chen, J., & Lee, Y. (2008) · PROTEOMICS · doi:10.1002/pmic.200800196 · Cited by 18 · see citing works

Regulation of MDM4 (MDMX) function by p76MDM2: a new facet in the control of p53 activity

Giglio, S., Mancini, F., Pellegrino, M., Conza, G. D., Puxeddu, E., Sacchi, A., Pontecorvi, A., & Moretti, F. (2010) · Oncogene · doi:10.1038/onc.2010.324 · Cited by 16 · see citing works

The key vulnerabilities and therapeutic opportunities in the USP7-p53/MDM2 axis in cancer

Saha, G., & Ghosh, M. K. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2025.119908 · Cited by 17 · see citing works

Understanding the interaction of 14‐3‐3 proteins with h DMX and h DM2: a structural and biophysical study

Srdanović, S., Wolter, M., Trinh, C. H., Ottmann, C., Warriner, S. L., & Wilson, A. J. (2022) · FEBS Journal · doi:10.1111/febs.16433 · Cited by 12 · see citing works

Rare MDM4 gene amplification in colorectal cancer: The principle of a mutually exclusive relationship between MDM alteration and TP53 inactivation is not applicable

Miyagi, Y. (2011) · Oncology Reports · doi:10.3892/or.2011.1270 · Cited by 10 · see citing works

Dichlorvos‐induced cell cycle arrest and DNA damage repair activation in primary rat microglial cells

Sunkaria, A., Wani, W. Y., Sharma, D. R., & Gill, K. D. (2012) · Journal of Neuroscience Research · doi:10.1002/jnr.23173 · Cited by 9 · see citing works

GSTpi reduces DNA damage and cell death by regulating the ubiquitination and nuclear translocation of NBS1

Zhou, J., Gu, L., Shi, Y., Huang, T. H., Fan, X., Bi, X., Lü, S., Liang, J., Luo, L., Cao, P., et al. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-04057-5 · Cited by 8 · see citing works

Estrogens Counteract Platinum-Chemosensitivity by Modifying the Subcellular Localization of MDM4

Lucà, R., di Blasio, G., Gallo, D., Monteleone, V., Manni, I., Fici, L., Buttarelli, M., Ciolli, G., Pellegrino, M., Teveroni, E., et al. (2019) · Cancers · doi:10.3390/cancers11091349 · Cited by 8 · see citing works

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 · see citing works

Chk2 Protects against Radiation-Induced Genomic Instability

MacLaren, A., Slavin, D. A., & McGowan, C. H. (2009) · Radiation Research · doi:10.1667/rr1603.1 · Cited by 6 · see citing works

The fate of murine double minute X (MdmX) is dictated by distinct signaling pathways through murine double minute 2 (Mdm2)

Hauck, P. M., Wolf, E. R., Olivos, D. J., McAtarsney, C. P., & Mayo, L. D. (2017) · Oncotarget · doi:10.18632/oncotarget.22320 · Cited by 6 · see citing works

Intra molecular interactions in the regulation of p53 pathway

Chen, J. (2016) · Translational Cancer Research · doi:10.21037/tcr.2016.09.23 · Cited by 5 · see citing works

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 · see citing works

Cortical recruitment of centralspindlin and RhoA effectors during meiosis I of Caenorhabditis elegans primary spermatocytes

Wang, X., Zhang, D., Zheng, C., Wu, S., Glotzer, M., & Tse, Y. C. (2021) · Journal of Cell Science · doi:10.1242/jcs.238543 · Cited by 3 · see citing works

EEF1A2 inhibiert über eine PI3K/AKT/mTOR-abhängige Stabilisierung von MDM4 die p53-Funktion im Leberzellkarzinom

Longerich, T. (2014) · Der Pathologe · doi:10.1007/s00292-014-2007-y · Cited by 2 · see citing works

Reduction of lymphotoxin beta receptor induces cellular senescence via the MDMX-p53 pathway

Kim, S. Y., Lee, B., Lee, J., Kwak, M. S., Rhee, W. J., Park, I. H., & Shin, J. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02708-1 · Cited by 2 · see citing works

DNA Damage-Induced Phosphorylation of MdmX at Serine 367 Activates p53 by Targeting MdmX for Mdm2-Dependent Degradation

Okamoto, 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

ATM 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

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

DNA Damage-Induced Phosphorylation of MdmX at Serine 367 Activates p53 by Targeting MdmX for

Jochemsen, A. G., & Taya, Y. (2005)

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