The role of ubiquitin modification in the regulation of p53
Open accessAbstract
The p53 tumor suppressor protein is involved in regulating a wide variety of stress responses, from senescence and apoptosis to more recently discovered roles in allowing adaptation to metabolic and oxidative stress. After 34years of research, significant progress has been made in unraveling the complexity of the p53 network, and it is clear that the regulation of p53 protein stability is critical in the control of p53 activity. This article focuses on our current understanding of how the level and activity of p53 is controlled by this seemingly simple mechanism. This article is part of a Special Issue entitled: Ubiquitin-Proteasome System. Guest Editors: Thomas Sommer and Dieter H. Wolf.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
MDM2 can cooperate with MDMX to kinetically enhance p53 polyubiquitination, resulting in p53 stability and tumor occurrence.
“MDM2 can cooperate with MDMX (mouse double minute X) to kinetically enhance p53 polyubiquitination, resulting in p53 stability and the occurrence of tumors [11–13].”
From Targeting p53–MDM2 interaction by small-molecule inhibitors: learning from MDM2 inhibitors in clinical trials (2022) · cites this paper as [11]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
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
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
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
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
Self-citationBlinded 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
Self-citationSenescence and tumour clearance is triggered by p53 restoration in murine liver carcinomas
Xue, W., Zender, L., Miething, C., Dickins, R. A., Hernando, E., Krizhanovsky, V., Cordon-Cardo, C., & Lowe, S. W. (2007) · Nature · doi:10.1038/nature05529 · Cited by 2,473 · see citing works
RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
Hoege, C., Pfander, B., Moldovan, G., Pyrowolakis, G., & Jentsch, S. (2002) · Nature · doi:10.1038/nature00991 · Cited by 2,202 · 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
Restoration of p53 function leads to tumour regression in vivo
Ventura, A., Kirsch, D. G., McLaughlin, M. E., Tuveson, D. A., Grimm, J., Lintault, L., Newman, J., Reczek, E. E., Weissleder, R., & Jacks, T. (2007) · Nature · doi:10.1038/nature05541 · Cited by 1,820 · see citing works
Enhanced Phosphorylation of p53 by ATM in Response to DNA Damage
Banin, S., Moyal, L., Shieh, S.-Y., Taya, Y., Anderson, C. W., Chessa, L., Smorodinsky, N. I., Prives, C., Reiss, Y., Shiloh, Y., et al. (1998) · Science · doi:10.1126/science.281.5383.1674 · Cited by 1,797 · see citing works
Recognition of the polyubiquitin proteolytic signal
Thrower, J. S., Hoffman, L. M., Rechsteiner, M., & Pickart, C. M. (2000) · The EMBO Journal · doi:10.1093/emboj/19.1.94 · Cited by 1,718 · 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
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
MDM2, MDMX and p53 in oncogenesis and cancer therapy
Wade, M., Li, Y.-C., & Wahl, G. M. (2013) · Nature Reviews Cancer · doi:10.1038/nrc3430 · Cited by 1,279 · see citing works
Bond, G. L., Hu, W., Bond, E. E., Robins, H., Lutzker, S. G., Arva, N. C., Bargonetti, J., Bartel, F., Taubert, H., Wuerl, P., et al. (2004) · Cell · doi:10.1016/j.cell.2004.11.022 · Cited by 1,265 · see citing works
Myc signaling via the ARF tumor suppressor regulates p53-dependent apoptosis and immortalization
Zindy, F., Eischen, C. M., Randle, D. H., Kamijo, T., Cleveland, J. L., Sherr, C. J., & Roussel, M. F. (1998) · Genes & Development · doi:10.1101/gad.12.15.2424 · Cited by 1,245 · see citing works
Mayo, L. D., & Donner, D. B. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.181181198 · Cited by 1,230 · see citing works
Regulation of autophagy by cytoplasmic p53
Tasdemir, E., Maiuri, M. C., Galluzzi, L., Vitale, I., Djavaheri-Mergny, M., D'Amelio, M., Criollo, A., Morselli, E., Zhu, C., Harper, F., et al. (2008) · Nature Cell Biology · doi:10.1038/ncb1730 · Cited by 1,132 · 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 MDM2 gene amplification database
Momand, J. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.15.3453 · Cited by 982 · see citing works
p53 and Human Cancer: The First Ten Thousand Mutations
Hainaut, P. L., & Hollstein, M. C. (1999) · Advances in cancer research · doi:10.1016/s0065-230x(08)60785-x · Cited by 980 · see citing works
Shieh, S.-Y., Ahn, J., Tamai, K., Taya, Y., & Prives, C. (2000) · Genes & Development · doi:10.1101/gad.14.3.289 · Cited by 972 · see citing works
Involvement of linear polyubiquitylation of NEMO in NF-κB activation
Tokunaga, F., Sakata, S., Saeki, Y., Satomi, Y., Kirisako, T., Kamei, K., Nakagawa, T., Kato, M., Murata, S., Yamaoka, S., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1821 · Cited by 943 · see citing works
p14ARF links the tumour suppressors RB and p53
Bates, S., Phillips, A. C., Clark, P. A., Stott, F., Peters, G., Ludwig, R. L., & Vousden, K. H. (1998) · Nature · doi:10.1038/25867 · Cited by 918 · see citing works
Self-citationAcetylation Is Indispensable for p53 Activation
Tang, Y., Zhao, W., Chen, Y., Zhao, Y., & Gu, W. (2008) · Cell · doi:10.1016/j.cell.2008.03.025 · Cited by 838 · see citing works
Chk2/hCds1 functions as a DNA damage checkpoint in G<sub>1</sub>by 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
Mono- Versus Polyubiquitination: Differential Control of p53 Fate by Mdm2
Li, M., Brooks, C. L., Wu-Baer, F., Chen, D., Baer, R., & Gu, W. (2003) · Science · doi:10.1126/science.1091362 · Cited by 804 · see citing works
p53 regulates biosynthesis through direct inactivation of glucose-6-phosphate dehydrogenase
Jiang, P., Du, W., Wang, X., Mancuso, A., Gao, X., Wu, M., & Yang, X. (2011) · Nature Cell Biology · doi:10.1038/ncb2172 · Cited by 798 · see citing works
Non-Cell-Autonomous Tumor Suppression by p53
Lujambio, A., Akkari, L., Simon, J., Grace, D., Tschaharganeh, D. F., Bolden, J. E., Zhao, Z., Thapar, V., Joyce, J. A., Krizhanovsky, V., et al. (2013) · Cell · doi:10.1016/j.cell.2013.03.020 · Cited by 766 · see citing works
Small molecule RITA binds to p53, blocks p53–HDM-2 interaction and activates p53 function in tumors
Issaeva, N., Bozko, P. M., Enge, M., Protopopova, M., Verhoef, L. G. G. C., Masucci, M. G., Pramanik, A., & Selivanova, G. (2004) · Nature Medicine · doi:10.1038/nm1146 · Cited by 749 · 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
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
Atypical ubiquitylation — the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages
Kulathu, Y., & Komander, D. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3394 · Cited by 642 · see citing works
USP10 Regulates p53 Localization and Stability by Deubiquitinating p53
Yuan, J., Luo, K., Zhang, L., Cheville, J. C., & Lou, Z. (2010) · Cell · doi:10.1016/j.cell.2009.12.032 · Cited by 637 · 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
Self-citationRepression of p53 activity by Smyd2-mediated methylation
Huang, J. L., Perez-Burgos, L., Placek, B. J., Sengupta, R., Richter, M., Dorsey, J. A., Kubicek, S., Opravil, S., Jenuwein, T., & Berger, S. L. (2006) · Nature · doi:10.1038/nature05287 · Cited by 626 · see citing works
p19ARF links the tumour suppressor p53 to Ras
Palmero, I., Pantoja, C., & Serrano, M. (1998) · Nature · doi:10.1038/25870 · Cited by 617 · see citing works
Akt Enhances Mdm2-mediated Ubiquitination and Degradation of p53
Ogawara, Y., Kishishita, S., Obata, T., Isazawa, Y., Suzuki, T., Tanaka, K., Masuyama, N., & Gotoh, Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109745200 · Cited by 617 · see citing works
Modeling the Therapeutic Efficacy of p53 Restoration in Tumors
Martins, C. P., Brown-Swigart, L., & Evan, G. I. (2006) · Cell · doi:10.1016/j.cell.2006.12.007 · Cited by 600 · see citing works
Divorcing ARF and p53: an unsettled case
Sherr, C. J. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1954 · Cited by 595 · see citing works
Signaling to p53: ribosomal proteins find their way
Zhang, Y., & Lu, H. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.09.024 · Cited by 591 · see citing works
MDM2–HDAC1-mediated deacetylation of p53 is required for its degradation
Ito, A., Kawaguchi, Y., Lai, C., Kovacs, J. J., Higashimoto, Y., Appella, E., & Yao, T. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf616 · Cited by 570 · 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
Reifenberger, G., Liu, L., Ichimura, K., Schmidt, E., & Collins, V. P. (1993) · PubMed · Cited by 562 · see citing works
Reactivation of the p53 Tumor Suppressor Pathway by a Stapled p53 Peptide
Bernal, F., Tyler, A. F., Korsmeyer, S. J., Walensky, L. D., & Verdine, G. L. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0693587 · Cited by 559 · see citing works
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
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
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
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
Activation of p53 by conjugation to the ubiquitin‐like protein SUMO‐1
Gostissa, M., Hengstermann, A., Fogal, V., Sandy, P., Schwarz, S. E., Scheffner, M., & Sal, G. D. (1999) · The EMBO Journal · doi:10.1093/emboj/18.22.6462 · Cited by 512 · see citing works
Acetylation of p53 inhibits its ubiquitination by Mdm2
Li, M., Luo, J., Brooks, C. L., & Gu, W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200578200 · Cited by 503 · see citing works
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
Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability
Yang, W. H., Kim, J. E., Nam, H. W., Ju, J., Kim, H. S., Kim, Y. S., & Cho, J. W. (2006) · Nature Cell Biology · doi:10.1038/ncb1470 · Cited by 489 · see citing works
Querido, E., Blanchette, P., Yan, Q., Kamura, T., Morrison, M. R., Boivin, D., Kaelin, W. G., Conaway, R. C., Conaway, J. W., & Branton, P. E. (2001) · Genes & Development · doi:10.1101/gad.926401 · Cited by 480 · see citing works
MAGE-RING Protein Complexes Comprise a Family of E3 Ubiquitin Ligases
Doyle, J., Gao, J., Wang, J., Yang, M., & Potts, P. R. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.08.029 · Cited by 468 · see citing works
Modulation of p53 Function by SET8-Mediated Methylation at Lysine 382
Shi, X., Kachirskaia, I., Yamaguchi, H., West, L. E., Wen, H., Wang, E. W., Dutta, S. M., Appella, E., & Gozani, O. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.07.012 · Cited by 463 · see citing works
Dumaz, N., & Meek, D. W. (1999) · The EMBO Journal · doi:10.1093/emboj/18.24.7002 · 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
Involvement of PIAS1 in the Sumoylation of Tumor Suppressor p53
Kahyo, T., Nishida, T., & Yasuda, H. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00349-5 · Cited by 449 · see citing works
Yin Yang 1 Is a Negative Regulator of p53
Sui, G., Affar, E. B., Shi, Y. G., Brignone, C., Wall, N. R., Yin, P., Donohoe, M., Luke, M. P.-S., Calvo, D., Grossman, S. R., et al. (2004) · Cell · doi:10.1016/j.cell.2004.06.004 · Cited by 423 · see citing works
Kurki, S., Peltonen, K., Latonen, L., Kiviharju, T. M., Ojala, P. M., Meek, D. W., & Laiho, M. (2004) · Cancer Cell · doi:10.1016/s1535-6108(04)00110-2 · Cited by 416 · see citing works
p300/MDM2 complexes participate in MDM2-mediated p53 degradation
Grossman, S. R., Perez, M., Kung, A. L., Joseph, M., Mansur, C., Xiao, Z.-X., Kumar, S., Howley, P. M., & Livingston, D. M. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80140-9 · Cited by 414 · see citing works
c-Jun and p53 Activity Is Modulated by SUMO-1 Modification
Müller, S. P., Berger, M., Lehembre, F., Seeler, J.-S., Haupt, Y., & Dejean, A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.18.13321 · Cited by 399 · 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
NUMB controls p53 tumour suppressor activity
Colaluca, I. N., Tosoni, D., Nuciforo, P., Senic-Matuglia, F., Galimberti, V., Viale, G., Pece, S., & Di Fiore, P. P. (2008) · Nature · doi:10.1038/nature06412 · Cited by 385 · see citing works
The prolyl isomerase Pin1 is a regulator of p53 in genotoxic response
Zheng, H., You, H., Zhou, X. Z., Murray, S. A., Uchida, T., Wulf, G. M., Gu, L., Tang, X., Lu, K. P., & Xiao, Z. J. (2002) · Nature · doi:10.1038/nature01116 · Cited by 384 · see citing works
Nikolaev, A. Y., Li, M., Puskas, N., Qin, J., & Gu, W. J. (2003) · Cell · doi:10.1016/s0092-8674(02)01255-2 · Cited by 355 · see citing works
PML regulates p53 stability by sequestering Mdm2 to the nucleolus
Bernardi, R., Scaglioni, P. P., Bergmann, S., Horn, H. F., Vousden, K. H., & Pandolfi, P. P. (2004) · Nature Cell Biology · doi:10.1038/ncb1147 · Cited by 348 · see citing works
Self-citationMDM4 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
Fumagalli, S., Cara, A. D., Neb-Gulati, A., Natt, F., Schwemberger, S. J., Hall, J., Babcock, G. F., Bernardi, R., Pandolfi, P. P., & Thomas, G. (2009) · Nature Cell Biology · doi:10.1038/ncb1858 · Cited by 322 · 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
Self-citationBIRC7–E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer
Dou, H., Buetow, L., Sibbet, G. J., Cameron, K., & Huang, D. T. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2379 · Cited by 319 · see citing works
Lee, J. S., Galvin, K. M., See, R. H., Eckner, R., Livingston, D. M., Moran, E. M., & Shi, Y. (1995) · Genes & Development · doi:10.1101/gad.9.10.1188 · Cited by 311 · see citing works
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
Ribosome biogenesis surveillance: probing the ribosomal protein-Mdm2-p53 pathway
Deisenroth, C., & Zhang, Y. (2010) · Oncogene · doi:10.1038/onc.2010.189 · Cited by 303 · see citing works
Nutrient regulates Tor1 nuclear localization and association with rDNA promoter
Li, H., Tsang, C. K., Watkins, M. P., Bertram, P. G., & Zheng, X.-F. (2006) · Nature · doi:10.1038/nature05020 · Cited by 299 · see citing works
Feng, J., Tamaskovic, R., Yang, Z., Brazil, D. P., Merlo, A., Hess, D., & Hemmings, B. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404936200 · Cited by 294 · see citing works
Sur, S., Pagliarini, R. A., Bunz, F., Rago, C., Diaz, L. A., Kinzler, K. W., Vogelstein, B., & Papadopoulos, N. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0813333106 · Cited by 293 · see citing works
Trim24 targets endogenous p53 for degradation
Allton, K., Jain, A. K., Herz, H.-M., Tsai, W.-W., Jung, S. Y., Qin, J., Bergmann, A., Johnson, R. L., & Barton, M. C. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0813177106 · Cited by 292 · 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
Monoubiquitylation promotes mitochondrial p53 translocation
Marchenko, N. D., Wolff, S., Erster, S., Becker, K., & Moll, U. M. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601560 · Cited by 286 · 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
The Wip1 Phosphatase Acts as a Gatekeeper in the p53-Mdm2 Autoregulatory Loop
Lu, X., Ma, O., Nguyen, T., Jones, S. N., Oren, M., & Donehower, L. A. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.08.033 · Cited by 282 · see citing works
The deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2
Stevenson, L. F., Sparks, A., Allende‐Vega, N., Xirodimas, D. P., Lane, D. P., & Saville, M. K. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601567 · Cited by 280 · see citing works
Cytoplasmic destruction of p53 by the endoplasmic reticulum‐resident ubiquitin ligase ‘Synoviolin’
Yamasaki, S., Yagishita, N., Sasaki, T., Nakazawa, M., Kato, Y., Yamadera, T., Bae, E.-K., Toriyama, S., Ikeda, R., Zhang, L., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601490 · Cited by 275 · see citing works
Lauwers, E., Jacob, C., & André, B. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200810114 · Cited by 275 · see citing works
p38 Kinase Mediates UV-induced Phosphorylation of p53 Protein at Serine 389
Huang, C., Ma, W.-Y., Maxiner, A., Sun, Y., & Dong, Z. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.18.12229 · Cited by 274 · see citing works
Chen, D., Zhang, Z., Li, M., Wang, W., Li, Y., Rayburn, E. R., Hill, D. L., Wang, H., & Zhang, R. (2007) · Oncogene · doi:10.1038/sj.onc.1210327 · Cited by 265 · 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
The Chaperone-associated Ubiquitin Ligase CHIP Is Able to Target p53 for Proteasomal Degradation
Esser, C., Scheffner, M., & Höhfeld, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501574200 · Cited by 261 · see citing works
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
Structure of the Stapled p53 Peptide Bound to Mdm2
Baek, S., Kutchukian, P. S., Verdine, G. L., Huber, R., Holak, T. A., Lee, K. W., & Popowicz, G. M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja2090367 · Cited by 259 · see citing works
Mdm2 is critically and continuously required to suppress lethal p53 activity in vivo
Ringshausen, I., O'Shea, C. C., Finch, A. J., Swigart, L. B., & Evan, G. I. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.10.010 · Cited by 256 · 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
Itahana, K., Mao, H., Jin, A., Itahana, Y., Clegg, H. V., Lindström, M. S., Bhat, K. P., Godfrey, V. L., Evan, G. I., & Zhang, Y. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.09.007 · Cited by 245 · see citing works
(1997) · PubMed · Cited by 243 · see citing works
Cam, L. L., Linares, L. K., Paul, C., Julien, E., Lacroix, M., Hatchi, E., Triboulet, R., Bossis, G., Shmueli, A., Rodríguez, M. S., et al. (2006) · Cell · doi:10.1016/j.cell.2006.09.031 · Cited by 241 · see citing works
Mdm2 Regulates p53 mRNA Translation through Inhibitory Interactions with Ribosomal Protein L26
Ofir-Rosenfeld, Y., Boggs, K., Michael, D., Kastan, M. B., & Oren, M. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.08.031 · Cited by 240 · see citing works
Excess β‐catenin promotes accumulation of transcriptionally active p53
Damalas, A., Ben‐Ze'ev, A., Simcha, I., Shtutman, M. S., Martínez-Leal, J. F., Zhurinsky, J., Geiger, B., & Oren, M. (1999) · The EMBO Journal · doi:10.1093/emboj/18.11.3054 · Cited by 238 · see citing works
Basal Dynamics of p53 Reveal Transcriptionally Attenuated Pulses in Cycling Cells
Loewer, A., Batchelor, E., Gaglia, G., & Lahav, G. (2010) · Cell · doi:10.1016/j.cell.2010.05.031 · Cited by 234 · see citing works
Surf the Post-translational Modification Network of p53 Regulation
Gu, B., & Zhu, W. (2012) · International Journal of Biological Sciences · doi:10.7150/ijbs.4283 · Cited by 234 · see citing works
Activation of the p53 pathway by small-molecule-induced MDM2 and MDMX dimerization
Graves, B., Thompson, T., Xia, M., Janson, C., Lukacs, C., Deo, D., Di Lello, P., Fry, D., Garvie, C., Huang, K.-S., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1203789109 · Cited by 230 · see citing works
The oncoprotein gankyrin binds to MDM2/HDM2, enhancing ubiquitylation and degradation of p53
Higashitsuji, H., Higashitsuji, H., Itoh, K., Sakurai, T., Nagao, T., Sumitomo, H., Masuda, T., Dawson, S. P., Shimada, Y., Mayer, R. J., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.06.006 · Cited by 228 · see citing works
Onel, K., & Cordon‐Cardo, C. (2004) · Molecular Cancer Research · doi:10.1158/1541-7786.1.2.1 · Cited by 227 · see citing works
p53 Regulates Cell Cycle and MicroRNAs to Promote Differentiation of Human Embryonic Stem Cells
Jain, A. K., Allton, K. L., Iacovino, M., Mahen, E. M., Milczarek, R. J., Zwaka, T. P., Kyba, M., & Barton, M. C. (2012) · PLoS Biology · doi:10.1371/journal.pbio.1001268 · Cited by 226 · see citing works
Bursać, S., Brdovčak, M. C., Pfannkuchen, M. A., Oršolić, I., Golomb, L., Zhu, Y. Y., Katz, C., Daftuar, L., Grabušić, K., Vukelić, I., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218535109 · Cited by 226 · see citing works
C-terminal modifications regulate MDM2 dissociation and nuclear export of p53
Carter, S., Bischof, O., Dejean, A., & Vousden, K. H. (2007) · Nature Cell Biology · doi:10.1038/ncb1562 · Cited by 225 · see citing works
Self-citationZhang, J., Sun, Q., Zhang, Z., Ge, S., Han, Z.-G., & Chen, W.-T. (2012) · Oncogene · doi:10.1038/onc.2012.28 · Cited by 224 · see citing works
Reciprocal repression between P53 and TCTP
Amson, R. B., Pece, S., Lespagnol, A., Vyas, R., Mazzarol, G., Tosoni, D., Colaluca, I. N., Viale, G., Rodrigues-Ferreira, S., Wynendaele, J., et al. (2011) · Nature Medicine · doi:10.1038/nm.2546 · Cited by 223 · see citing works
Macias, E., Jin, A., Deisenroth, C., Bhat, K., Mao, H., Lindström, M. S., & Zhang, Y. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.08.007 · 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
Stapled Peptides with Improved Potency and Specificity That Activate p53
Brown, C. J., Quah, S. T., Jong, J., Goh, A. M., Chiam, P. C., Khoo, K. H., Choong, M. L., Lee, M. A., Yurlova, L., Zolghadr, K., et al. (2012) · ACS Chemical Biology · doi:10.1021/cb3005148 · Cited by 206 · see citing works
Inuzuka, H., Tseng, A., Gao, D., Zhai, B., Zhang, Q. H., Shaik, S., Wan, L., Cambronne, X. A., Mock, C. S., Yin, H., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.06.015 · Cited by 205 · see citing works
Poyurovsky, M. V., Priest, C., Kentsis, A., Borden, K. L., Pan, Z., Pavletich, N., & Prives, C. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601465 · Cited by 203 · see citing works
Activation of p53 by MDM2 Antagonists Can Protect Proliferating Cells from Mitotic Inhibitors
Carvajal, D. M., Tovar, C., Yang, H. S., Vu, B. T., Heimbrook, D. C., & Vassilev, L. T. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-3576 · Cited by 202 · see citing works
FBXO11 Promotes the Neddylation of p53 and Inhibits Its Transcriptional Activity
Abida, W. M., Nikolaev, A. Y., Zhao, W., Zhang, W., & Gu, W. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609001200 · Cited by 201 · 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
Positive regulation of p53 stability and activity by the deubiquitinating enzyme Otubain 1
Sun, X., Challagundla, K. B., & Dai, M. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.434 · Cited by 194 · see citing works
The 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
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
Topors Functions as an E3 Ubiquitin Ligase with Specific E2 Enzymes and Ubiquitinates p53
Rajendra, R., Malegaonkar, D., Pungaliya, P., Marshall, H., Rasheed, Z. A., Brownell, J. E., Liu, L. F., Lutzker, S. G., Saleem, A., & Rubin, E. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400300200 · Cited by 192 · see citing works
miR-605 joins p53 network to form a p53:miR-605:Mdm2 positive feedback loop in response to stress
Xiao, J., Lin, H., Luo, X., Luo, X., & Wang, Z. (2011) · The EMBO Journal · doi:10.1038/emboj.2010.347 · 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
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
Regulation of the MDM2-P53 pathway and tumor growth by PICT1 via nucleolar RPL11
Sasaki, M., Kawahara, K., Nishio, M., Mimori, K., Kogo, R., Hamada, K., Itoh, B., Wang, J., Komatsu, Y., Yang, Y. R., et al. (2011) · Nature Medicine · doi:10.1038/nm.2392 · Cited by 179 · see citing works
Ribosomal protein S14 unties the MDM2–p53 loop upon ribosomal stress
Zhou, X. Y., Hao, Q., Liao, J., Zhang, Q., & Lu, H. (2012) · Oncogene · doi:10.1038/onc.2012.63 · Cited by 176 · see citing works
Inactivation of HAUSP in vivo modulates p53 function.
Kon, N., Kobayashi, Y., Li, M., Brooks, C. L., Ludwig, T., & Gu, W. (2010) · Oncogene · doi:10.1038/onc.2009.427 · Cited by 176 · 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
Self-citationDifferent effects of p14ARF on the levels of ubiquitinated p53 and Mdm2 in vivo
Xirodimas, D., Saville, M. K., Edling, C., Lane, D. P., & Laín, S. (2001) · Oncogene · doi:10.1038/sj.onc.1204656 · Cited by 169 · see citing works
Gajjar, M. K., Candeias, M. M., Malbert-Colas, L., Mazars, A., Fujita, J., Olivares‐Illana, V., & Fåhræus, R. (2012) · Cancer Cell · doi:10.1016/j.ccr.2011.11.016 · Cited by 168 · see citing works
ATM activates p53 by regulating MDM2 oligomerization and E3 processivity
Cheng, Q., Chen, L., Li, Z., Lane, W. S., & Chen, J. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.294 · Cited by 165 · see citing works
Lu, H., Taya, Y., Ikeda, M., & Levine, A. J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6399 · Cited by 162 · see citing works
CBP and p300 are cytoplasmic E4 polyubiquitin ligases for p53
Shi, D., Pop, M. S., Kulikov, R., Love, I. M., Kung, A. L., & Grossman, S. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904305106 · Cited by 161 · see citing works
Transcription-independent ARF regulation in oncogenic stress-mediated p53 responses
Chen, D., Shan, J., Zhu, W.-G., Qin, J., & Gu, W. (2010) · Nature · doi:10.1038/nature08820 · Cited by 160 · see citing works
Ser18 and 23 phosphorylation is required for p53‐dependent apoptosis and tumor suppression
Chao, C., Herr, D., Chun, J., & Xu, Y. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601167 · Cited by 158 · see citing works
Caspase-2-Mediated Cleavage of Mdm2 Creates a p53-Induced Positive Feedback Loop
Oliver, T. G., Meylan, E., Chang, G. P., Xue, W., Burke, J. R., Humpton, T. J., Hubbard, D., Bhutkar, A. J., & Jacks, T. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.012 · Cited by 156 · see citing works
Promotion of CHIP-Mediated p53 Degradation Protects the Heart From Ischemic Injury
Naito, A. T., Okada, S., Minamino, T., Iwanaga, K., Liu, M.-L., Sumida, T. S., Nomura, S., Sahara, N., Mizoroki, T., Takashima, A., et al. (2010) · Circulation Research · doi:10.1161/circresaha.109.214346 · Cited by 152 · see citing works
USP4 inhibits p53 through deubiquitinating and stabilizing ARF‐BP1
Zhang, X., Berger, F. G., Yang, J., & Lu, X. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.125 · Cited by 152 · see citing works
Phosphorylation of Serine 18 Regulates Distinct p53 Functions in Mice
Sluss, H. K., Armata, H., Gallant, J., & Jones, S. N. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.3.976-984.2004 · Cited by 152 · see citing works
DNA damage induced p53 stabilization: no indication for an involvement of p53 phosphorylation
Blattner, C., Tobiasch, E., Litfen, M., Rahmsdorf, H. J., & Herrlich, P. (1999) · Oncogene · doi:10.1038/sj.onc.1202480 · Cited by 151 · 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
Lindström, M. S., Jin, A., Deisenroth, C., Wolf, G. W., & Zhang, Y. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01307-06 · Cited by 149 · see citing works
ATM-Dependent Downregulation of USP7/HAUSP by PPM1G Activates p53 Response to DNA Damage
Khoronenkova, S. V., Dianova, I. I., Ternette, N., Kessler, B. M., Parsons, J. L., & Dianov, G. L. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.01.021 · Cited by 146 · see citing works
MicroRNAs/TP53 feedback circuitry in glioblastoma multiforme
Suh, S.-S., Yoo, J. Y., Nuovo, G. J., Jeon, Y.-J., Kim, S., Lee, T. J., Kim, T., Bakàcs, A., Alder, H., Kaur, B., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1202465109 · Cited by 144 · see citing works
CAG expansion induces nucleolar stress in polyglutamine diseases
Tsoi, H., Lau, T. C., Tsang, S. Y., Lau, K., & Chan, H. Y. E. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1204089109 · Cited by 142 · 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
Cell Type- and Promoter-specific Roles of Ser18 Phosphorylation in Regulating p53 Responses
Chao, C., Hergenhahn, M., Kaeser, M. D., Wu, Z., Saito, S., Iggo, R., Hollstein, M., Appella, E., & Xu, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306938200 · Cited by 141 · see citing works
Liu, J., Chung, H., Vogt, M., Jin, Y., Malide, D., He, L., Dundr, M., & Levens, D. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.11 · Cited by 141 · see citing works
Xiong, X., Zhao, Y., He, H., & Sun, Y. (2010) · Oncogene · doi:10.1038/onc.2010.569 · Cited by 141 · see citing works
Cooperation between the ribosomal proteins L5 and L11 in the p53 pathway
Horn, H. F., & Vousden, K. H. (2008) · Oncogene · doi:10.1038/onc.2008.189 · Cited by 140 · see citing works
Self-citationImportin 7 and Exportin 1 Link c-Myc and p53 to Regulation of Ribosomal Biogenesis
Golomb, L., Bublik, D. R., Wilder, S., Nevo, R., Kiss, V., Grabusic, K., Volarevic, S., & Oren, M. (2012) · Molecular Cell · doi:10.1016/j.molcel.2011.11.022 · Cited by 137 · see citing works
The Mdm2 Oncoprotein Interacts with the Cell Fate Regulator Numb
Juven‐Gershon, T., Shifman, O., Unger, T., Elkeles, A., Haupt, Y., & Oren, M. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.7.3974 · Cited by 136 · see citing works
Ubiquitin-independent p53 proteasomal degradation
Tsvetkov, P., Reuven, N. B., & Shaul, Y. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.67 · Cited by 134 · see citing works
MDM2-ARF complex regulates p53 sumoylation
Chen, L., & Chen, J. (2003) · Oncogene · doi:10.1038/sj.onc.1206851 · Cited by 134 · 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
Glycogen synthase kinase 3-dependent phosphorylation of Mdm2 regulates p53 abundance
Kulikov, R., Boehme, K. A., & Blattner, C. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.16.7170-7180.2005 · Cited by 132 · see citing works
Functional analysis and intracellular localization of p53 modified by SUMO-1
Kwek, S. S., Derry, J. J., Tyner, A. L., Shen, Z., & Gudkov, A. V. (2001) · Oncogene · doi:10.1038/sj.onc.1204362 · Cited by 130 · see citing works
Regulation of p53 localization and transcription by the HECT domain E3 ligase WWP1
Laine, A., & Ronai, Z. A. (2006) · Oncogene · doi:10.1038/sj.onc.1209924 · Cited by 129 · see citing works
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
Cop1 constitutively regulates c-Jun protein stability and functions as a tumor suppressor in mice
Migliorini, D., Bogaerts, S., Defever, D., Vyas, R., Denecker, G., Radaelli, E., Zwolińska, A., Depaepe, V., Hochepied, T., Skarnes, W. C., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci45784 · Cited by 128 · see citing works
Banks, D., Wu, M., Higa, L. A., Gavrilova, N., Quan, J., Ye, T., Kobayashi, R., Sun, H., & Zhang, H. (2006) · Cell Cycle · doi:10.4161/cc.5.15.3150 · Cited by 127 · see citing works
Defective apoptosis and B-cell lymphomas in mice with p53 point mutation at Ser 23
MacPherson, D., Kim, J., Kim, T., Rhee, B. K., van Oostrom, C. T., DiTullio, R. A., Venere, M., Halazonetis, T. D., Bronson, R., de Vries, A., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600363 · Cited by 124 · see citing works
Regulation 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
Increased Sensitivity to UV Radiation in Mice with a p53 Point Mutation at Ser389
Bruins, W., Zwart, E., Attardi, L. D., Iwakuma, T., Hoogervorst, E. M., Beems, R. B., Miranda, B., van Oostrom, C. T. M., van den Berg, J., van den Aardweg, G. J., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.20.8884-8894.2004 · Cited by 121 · see citing works
Regulation of p53 stability and function by the deubiquitinating enzyme USP42
Hock, A. K., Vigneron, A. M., Carter, S., Ludwig, R. L., & Vousden, K. H. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.419 · Cited by 117 · see citing works
Self-citationUBE4B promotes Hdm2-mediated degradation of the tumor suppressor p53
Wu, H., Pomeroy, S. L., Ferreira, M., Teider, N., Mariani, J., Nakayama, K. I., Hatakeyama, S., Tron, V. A., Saltibus, L. F., Spyracopoulos, L., et al. (2011) · Nature Medicine · doi:10.1038/nm.2283 · Cited by 117 · 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
MdmX Protein Is Essential for Mdm2 Protein-mediated p53 Polyubiquitination
Wang, X., Wang, J., & Jiang, X. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.213868 · Cited by 115 · see citing works
A “Twist box” Code of p53 Inactivation: Twist box:p53 Interaction Promotes p53 Degradation
Piccinin, S., Tonin, E., Sessa, S., Demontis, S., Rossi, S., Pecciarini, L., Zanatta, L., Pivetta, F., Grizzo, A., Sonego, M., et al. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.08.003 · Cited by 112 · see citing works
Degradation of Phosphorylated p53 by Viral Protein-ECS E3 Ligase Complex
Sato, Y., Kamura, T., Shirata, N., Murata, T., Kudoh, A., Iwahori, S., Nakayama, S., Isomura, H., Nishiyama, Y., & Tsurumi, T. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000530 · Cited by 108 · see citing works
Expression of SUMO-2/3 Induced Senescence through p53- and pRB-mediated Pathways
Li, T., Santockyte, R., Shen, R., Tekle, E., Wang, G., Yang, D. C. H., & Chock, P. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608236200 · Cited by 107 · 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
Depletion of the Nucleolar Protein Nucleostemin Causes G1 Cell Cycle Arrest via the p53 Pathway
Ma, H., & Pederson, T. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-03-0244 · Cited by 106 · see citing works
Gannon, H. S., Woda, B. A., & Jones, S. N. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.04.011 · Cited by 105 · see citing works
Mutation of Mouse p53 Ser23 and the Response to DNA Damage
Wu, Z., Earle, J., Saito, S., Anderson, C. W., Appella, E., & Xu, Y. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.8.2441-2449.2002 · Cited by 103 · see citing works
Regulation of p53 Localization and Activity by Ubc13
Laine, A. M., Topisirović, I., Zhai, D., Reed, J. C., Borden, K. L. B., & Ronai, Z. A. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01156-06 · Cited by 101 · see citing works
Zwang, Y., Sas‐Chen, A., Drier, Y., Shay, T., Avraham, R., Lauriola, M., Shema, E., Nili, E. L., Jacob‐Hirsch, J., Amariglio, N., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.017 · Cited by 100 · 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
PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53
Cui, G., Park, S., Badeaux, A. I., Kim, D., Lee, J., Thompson, J. R., Yan, F., Kaneko, S., Yuan, Z., Botuyan, M. V., et al. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2353 · Cited by 99 · see citing works
MSL2 Promotes Mdm2-independent Cytoplasmic Localization of p53
Kruse, J.-P., & Gu, W. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805658200 · Cited by 99 · see citing works
Andrews, P., He, Y. J., & Xiong, Y. (2006) · Oncogene · doi:10.1038/sj.onc.1209490 · Cited by 95 · see citing works
P14ARF promotes accumulation of SUMO-1 conjugated (H)Mdm2
Xirodimas, D. P., Chisholm, J., Desterro, J. M. S., Lane, D. P., & Hay, R. T. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03310-0 · Cited by 94 · see citing works
Cul4A Physically Associates with MDM2 and Participates in the Proteolysis of p53
Nag, A., Bagchi, S., & Raychaudhuri, P. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-2598 · Cited by 94 · see citing works
Mdm2 facilitates the association of p53 with the proteasome
Kulikov, R., Letienne, J., Kaur, M., Grossman, S. R., Arts, J., & Blattner, C. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911716107 · Cited by 94 · see citing works
Wadgaonkar, R., & Collins, T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.20.13760 · Cited by 93 · 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
Kurki, S., Latonen, L., & Laiho, M. (2003) · Journal of Cell Science · doi:10.1242/jcs.00714 · Cited by 91 · see citing works
Molecular Mechanisms of Ubiquitin-Dependent Membrane Traffic
Hurley, J. H., & Stenmark, H. (2011) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-042910-155404 · Cited by 89 · see citing works
CARPs Are Ubiquitin Ligases That Promote MDM2-independent p53 and Phospho-p53ser20 Degradation
Yang, W., Rozan, L. M., McDonald, E. R., Navaraj, A., Liu, J. J., Matthew, E. M., Wang, W., Dicker, D. T., & El‐Deiry, W. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m610793200 · 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
Regulation of p53 family members by the ubiquitin-like SUMO system
Stehmeier, P., & Muller, S. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.01.002 · Cited by 83 · 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
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
Nie, J., Xie, P., Liu, L., Xing, G., Chang, Z., Yin, Y., Tian, C., He, F., & Zhang, L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.126920 · Cited by 79 · 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
JFK, a Kelch domain-containing F-box protein, links the SCF complex to p53 regulation
Sun, L., Shi, L., Li, W., Yu, W., Liang, J., Zhang, H., Yang, X., Wang, Y., Li, R., Yao, X., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901864106 · Cited by 79 · 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
Flagged first, then by citations
6 of the 275 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Autophagy in malignant transformation and cancer progression
Galluzzi, L., Pietrocola, F., Bravo‐San Pedro, J. M., Amaravadi, R. K., Baehrecke, E. H., Cecconi, F., Codogno, P., Debnath, J., Gewirtz, D. A., Karantza, V., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201490784 · Cited by 1,182 · see citing works
P53 in survival, death and metabolic health: a lifeguard with a licence to kill.
Kruiswijk, F., Labuschagne, C. F., & Vousden, K. H. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4007 · Cited by 1,080 · see citing works
Self-citationControl of protein stability by post-translational modifications
Lee, J. M., Hammarén, H. M., Savitski, M. M., & Baek, S. H. (2023) · Nature Communications · doi:10.1038/s41467-023-35795-8 · Cited by 822 · see citing works
Soussi, T., & Wiman, K. G. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2015.53 · Cited by 305 · see citing works
Therapeutic strategies to overcome taxane resistance in cancer
Das, T., Anand, U., Pandey, S. K., Ashby, C. R., Assaraf, Y. G., Chen, Z., & Dey, A. (2021) · Drug Resistance Updates · doi:10.1016/j.drup.2021.100754 · Cited by 254 · see citing works
The Regulation of Ferroptosis by Tumor Suppressor p53 and its Pathway
Liu, J., Zhang, C., Wang, J., Hu, W., & Feng, Z. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218387 · Cited by 249 · see citing works
Zhu, H., Gao, H., Ji, Y., Zhou, Q., Du, Z., Tian, L., Jiang, Y., Yao, K., & Zhou, Z. (2022) · Journal of Hematology & Oncology · doi:10.1186/s13045-022-01314-3 · Cited by 223 · see citing works
Control of metabolism by p53 – Cancer and beyond
Labuschagne, C. F., Zani, F., & Vousden, K. H. (2018) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2018.06.001 · Cited by 219 · see citing works
Self-citationImpaired ribosome biogenesis: mechanisms and relevance to cancer and aging
Turi, Z., Lacey, M., Mistrík, M., & Moudrý, P. (2019) · Aging · doi:10.18632/aging.101922 · Cited by 209 · see citing works
Pal, A., Young, M. A., & Donato, N. J. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-1211 · Cited by 198 · see citing works
Antioxidants and HNE in redox homeostasis
Łuczaj, W., Gęgotek, A., & Skrzydlewska, E. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.11.033 · Cited by 197 · see citing works
The relationship between the nucleolus and cancer: Current evidence and emerging paradigms
Oršolić, I., Jurada, D., Pullen, N., Oren, M., Eliopoulos, A. G., & Volarević, S. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.12.004 · Cited by 166 · see citing works
Limiting the power of p53 through the ubiquitin proteasome pathwayPreprint
Pant, V., & Lozano, G. (2014) · Genes & Development · doi:10.1101/gad.247452.114 · Cited by 165 · see citing works
Khan, H. Z., Reale, M., Ullah, H., Sureda, A., Tejada, S., Wang, Y., Zhang, Z., & Xiao, J. (2019) · Biotechnology Advances · doi:10.1016/j.biotechadv.2019.04.007 · Cited by 157 · see citing works
Activation of the tumor suppressor p53 upon impairment of ribosome biogenesis
Bursać, S., Brdovčak, M. C., Donati, G., & Volarević, S. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.08.014 · Cited by 154 · see citing works
Attenuating the p53 Pathway in Human Cancers: Many Means to the Same EndPreprint
Wasylishen, A. R., & Lozano, G. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026211 · Cited by 128 · see citing works
SCFFbxo22-KDM4A targets methylated p53 for degradation and regulates senescence
Johmura, Y., Sun, J. M., Kitagawa, K., Nakanishi, K., Kuno, T., Naiki‐Ito, A., Sawada, Y., Miyamoto, T., Okabe, A., Aburatani, H., et al. (2016) · Nature Communications · doi:10.1038/ncomms10574 · Cited by 119 · see citing works
Vergoni, B., Cornejo, P.-J., Gilleron, J., Djedaini, M., Ceppo, F., Jacquel, A., Bouget, G., Ginet, C., Gonzalez, T., Maillet, J., et al. (2016) · Diabetes · doi:10.2337/db16-0014 · Cited by 119 · see citing works
c-Myc inactivation of p53 through the pan-cancer lncRNA MILIP drives cancer pathogenesis
Feng, Y., Liu, X., Liu, T., Ji, Q., Wu, Y., Li, J., Gao, W., Zhang, Y. Y., La, T., Tabatabaee, H., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-18735-8 · Cited by 117 · see citing works
A comprehensive method for detecting ubiquitinated substrates using TR-TUBE
Yoshida, Y., Saeki, Y., Murakami, A., Kawawaki, J., Tsuchiya, H., Yoshihara, H., Shindo, M., & Tanaka, K. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1422313112 · Cited by 117 · see citing works
Role of the nucleus in apoptosis: signaling and execution
Prokhorova, E. A., Zamaraev, A. V., Kopeina, G. S., Zhivotovsky, B., & Lavrik, I. N. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2031-y · Cited by 115 · see citing works
Recognition of Client Proteins by the Proteasome
Yu, H., & Matouschek, A. T. (2017) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-070816-033719 · Cited by 109 · see citing works
p53 stability is regulated by diverse deubiquitinating enzymes
Kwon, S., Saindane, M., & Baek, K. (2017) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2017.08.001 · Cited by 110 · see citing works
Deregulation of UBE2C-mediated autophagy repression aggravates NSCLC progression
Guo, J., Wu, Y., Du, J., Yang, L., Chen, W., Gong, K., Dai, J., Miao, S., Jin, D., & Xi, S. (2018) · Oncogenesis · doi:10.1038/s41389-018-0054-6 · Cited by 113 · see citing works
The Cross Talk Between p53 and mTOR Pathways in Response to Physiological and Genotoxic Stresses
Cui, D., Qu, R., Liu, D., Xiong, X., Liang, T., & Zhao, Y. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.775507 · Cited by 106 · see citing works
C16-ceramide is a natural regulatory ligand of p53 in cellular stress response
Fekry, B., Jeffries, K. A., Esmaeilniakooshkghazi, A., Szulc, Z. M., Knagge, K. J., Kirchner, D. R., Horita, D. A., Krupenko, S. A., & Krupenko, N. I. (2018) · Nature Communications · doi:10.1038/s41467-018-06650-y · Cited by 102 · see citing works
Molecular Mechanisms of p53 Deregulation in Cancer: An Overview in Multiple Myeloma
Herrero, A. B., Rojas, E. A., Misiewicz-Krzemińska, I., Krzemiński, P., & Gutierrez, N. C. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17122003 · Cited by 99 · see citing works
The Interplay Between Tumor Suppressor p53 and Hypoxia Signaling Pathways in Cancer
Zhang, C., Liu, J., Wang, J., Zhang, T., Xu, D., Hu, W., & Feng, Z. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.648808 · Cited by 97 · see citing works
Ubiquitination and deubiquitination: Implications on cancer therapy
Dagar, G., Kumar, R., Yadav, K. K., Singh, M. K., & Pandita, T. K. (2023) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2023.194979 · Cited by 94 · see citing works
Delineating Crosstalk Mechanisms of the Ubiquitin Proteasome System That Regulate Apoptosis
Gupta, I., Singh, K., Varshney, N. K., & Khan, S. M. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00011 · Cited by 86 · see citing works
Prolyl isomerases in gene transcription
Hanes, S. D. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.10.028 · Cited by 87 · see citing works
Regulation of Mutant p53 Protein Expression
Vijayakumaran, R., Tan, K. H., Miranda, P. J., Haupt, S., & Haupt, Y. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00284 · Cited by 87 · see citing works
Hu, D., Su, C., Jiang, M., Shen, Y., Shi, A., Zhao, F., Chen, R., Shen, Z., Bao, J., & Tang, W. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.01.169 · Cited by 86 · see citing works
Killing by Degradation: Regulation of Apoptosis by the Ubiquitin-Proteasome-System
Abbas, R., & Larisch, S. (2021) · Cells · doi:10.3390/cells10123465 · Cited by 86 · see citing works
FBXW7 Confers Radiation Survival by Targeting p53 for Degradation
Cui, D., Xiong, X., Shu, J., Dai, X.-Q., Sun, Y., & Zhao, Y. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.12.032 · Cited by 81 · see citing works
Dynamics of p53: A Master Decider of Cell Fate
Luo, Q., Beaver, J. M., Liu, Y., & Zhang, Z. (2017) · Genes · doi:10.3390/genes8020066 · Cited by 78 · see citing works
A patent review of the ubiquitin ligase system: 2015–2018
Li, X., Ekinci, E., Rohondia, S. O., Wang, J., Liu, J., & Dou, Q. P. (2018) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2018.1549229 · Cited by 75 · see citing works
Pecháčková, S., Burdová, K., Benada, J., Kleiblová, P., Jeníková, G., & Macůrek, L. (2016) · Oncotarget · doi:10.18632/oncotarget.7363 · Cited by 75 · see citing works
Development of inhibitors in the ubiquitination cascade
Zhang, W., & Sidhu, S. S. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.11.003 · Cited by 73 · see citing works
Portman, N., Milioli, H. H., Alexandrou, S., Coulson, R. S., Yong, A., Fernandez, K. J., Chia, K. M., Halilovic, E., Segara, D., Parker, A., et al. (2020) · Breast Cancer Research · doi:10.1186/s13058-020-01318-2 · Cited by 65 · see citing works
Ceramide Signaling and p53 Pathways
Jeffries, K. A., & Krupenko, N. I. (2018) · Advances in cancer research · doi:10.1016/bs.acr.2018.04.011 · Cited by 64 · see citing works
Ovarian tumor domain-containing protein 1 deubiquitinates and stabilizes p53
Piao, S., Pei, H. Z., Huang, B., & Baek, S. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.02.011 · Cited by 65 · see citing works
Balamurugan, K., Sehareen, S., Sharan, S., Krishnamurthy, S., Tang, W., McKennett, L., Padmanaban, V., Czarra, K., Ewald, A. J., Ueno, N. T., et al. (2023) · JCI Insight · doi:10.1172/jci.insight.156057 · Cited by 62 · see citing works
Specificity and disease in the ubiquitin system
Chaugule, V. K., & Walden, H. (2016) · Biochemical Society Transactions · doi:10.1042/bst20150209 · Cited by 62 · see citing works
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
Ray, A., Rana, S., Banerjee, D., Mitra, A., Datta, R., Naskar, S., & Sarkar, S. (2015) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2015.11.011 · Cited by 58 · see citing works
The tumour suppressor CYLD regulates the p53 DNA damage response
Fernández‐Majada, V., Welz, P.-S., Ermolaeva, M., Schell, M. J., Adam, A. C., Dietlein, F., Komander, D., Büttner, R., Thomas, R. K., Schumacher, B., et al. (2016) · Nature Communications · doi:10.1038/ncomms12508 · Cited by 57 · see citing works
Generation and Validation of Intracellular Ubiquitin Variant Inhibitors for USP7 and USP10
Zhang, W., Sartori, M. A., Makhnevych, T., Federowicz, K., Dong, X., Liu, L., Nim, S., Dong, A., Yang, J., Li, Y., et al. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.05.025 · Cited by 56 · see citing works
Tumor suppressor p53 cross-talks with TRIM family proteins
Liu, J., Zhang, C., Wang, X. B., Hu, W., & Feng, Z. (2020) · Genes & Diseases · doi:10.1016/j.gendis.2020.07.003 · Cited by 55 · see citing works
Decision for cell fate: deubiquitinating enzymes in cell cycle checkpoint
Lim, K., Song, M.-H., & Baek, K. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2129-2 · Cited by 52 · see citing works
Recent advances on the intervention sites targeting USP7-MDM2-p53 in cancer therapy
Harakandi, C., Nininahazwe, L., Xu, H., Liu, B., He, C., Zheng, Y., & Zhang, H. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.105273 · Cited by 52 · see citing works
Rodríguez, J. A. (2014) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2014.03.005 · Cited by 46 · see citing works
Sparks, A., Dayal, S., Das, J., Robertson, P., Ménendez, S., & Saville, M. K. (2013) · Oncogene · doi:10.1038/onc.2013.413 · Cited by 47 · see citing works
Paclitaxel promotes lung cancer cell apoptosis via MEG3-P53 pathway activation
Xu, J., Su, C., Zhao, F., Tao, J., Hu, D., Shi, A., Pan, J., & Zhang, Y. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.08.142 · Cited by 46 · see citing works
Hock, A. K., Vigneron, A. M., & Vousden, K. H. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.589267 · Cited by 44 · see citing works
Self-citationSHARPIN Facilitates p53 Degradation in Breast Cancer Cells
Yang, H., Yu, S., Wang, W., Li, X., Hou, Y., Liu, Z., Shi, Y., Mu, K., Niu, G., Xu, J., et al. (2017) · Neoplasia · doi:10.1016/j.neo.2016.12.002 · Cited by 44 · see citing works
The regulation of radiosensitivity by p53 and its acetylation
Zhang, J., Shen, L., & Sun, L. (2015) · Cancer Letters · doi:10.1016/j.canlet.2015.04.015 · Cited by 44 · see citing works
Marcar, L., Ihrig, B., Hourihan, J. M., Bray, S. E., Quinlan, P., Jordan, L. B., Thompson, A. M., Hupp, T. R., & Meek, D. W. (2015) · PLoS ONE · doi:10.1371/journal.pone.0127713 · Cited by 42 · see citing works
Melatonin: Regulation of Biomolecular Condensates in Neurodegenerative Disorders
Loh, D., & Reiter, R. J. (2021) · Antioxidants · doi:10.3390/antiox10091483 · Cited by 43 · see citing works
Zhang, Z., Liu, P., Wang, J., Gong, T., Zhang, F., Ma, J., & Han, N. (2015) · Medical Oncology · doi:10.1007/s12032-015-0609-8 · Cited by 43 · see citing works
p53 regulation upon genotoxic stress: intricacies and complexities
Kumari, R., Kohli, S., & Das, S. (2014) · Molecular & Cellular Oncology · doi:10.4161/23723548.2014.969653 · Cited by 41 · see citing works
Swetzig, W. M., Wang, J., & Das, G. M. (2016) · Oncotarget · doi:10.18632/oncotarget.7533 · Cited by 42 · see citing works
OrfX, a Nucleomodulin Required for Listeria monocytogenes Virulence
Prokop, A., Gouin, E., Villiers, V., Nahori, M., Vincentelli, R., Duval, M., Cossart, P., & Dussurget, O. (2017) · mBio · doi:10.1128/mbio.01550-17 · Cited by 40 · see citing works
The Role of MDM2 in Promoting Genome Stability versus Instability
Saadatzadeh, M. R., Elmi, A. N., Pandya, P. H., Bijangi‐Vishehsaraei, K., Ding, J., Stamatkin, C. W., Cohen‐Gadol, A., & Pollok, K. E. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18102216 · Cited by 43 · see citing works
Anatomy of Mdm2 and Mdm4 in evolution
Tan, B. X., Liew, H. P., Chua, J. S., Ghadessy, F. J., Tan, Y. S., Lane, D. P., & Coffill, C. R. (2017) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjx002 · Cited by 40 · see citing works
New Insights Into the Role of Ubiquitylation of Proteins
McDowell, G. S., & Philpott, A. (2016) · International review of cytology · doi:10.1016/bs.ircmb.2016.02.002 · Cited by 37 · see citing works
Surmiak, E., Twarda‐Clapa, A., Żak, K. M., Musielak, B., Tomala, M. D., Kubica, K., Grudnik, P., Madej, M., Jabłoński, M., Potempa, J., et al. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00596 · Cited by 36 · see citing works
P53: Stability from the Ubiquitin–Proteasome System and Specific 26S Proteasome Inhibitors
do Patrocinio, A. B., Rodrigues, V., & Guidi Magalhães, L. (2022) · ACS Omega · doi:10.1021/acsomega.1c04726 · Cited by 36 · see citing works
An overview of the functions of p53 and drugs acting either on wild- or mutant-type p53
Huang, Y., Jiao, Z., Fu, Y., Hou, Y., Sun, J., Hu, F., Yu, S., Gong, K., Liu, Y., & Zhao, G. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116121 · Cited by 33 · see citing works
The p53-Mdm2 Loop: A Critical Juncture of Stress Response
Levav-Cohen, Y., Goldberg, Z., Tan, K. H., Alsheich-Bartok, O., Zuckerman, V., Haupt, S., & Haupt, Y. (2014) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-017-9211-0_9 · Cited by 36 · see citing works
Cruz, A., Ludovico, P., Torrado, E., Gama, J. B., Sousa, J., Gaifem, J., Appelberg, R., Rodrigues, F. J. S., Cooper, A. M., Pedrosa, J., et al. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00498 · Cited by 35 · see citing works
Two mammalian homologs of yeast Rad23, HR23A and HR23B, as multifunctional proteins
Yokoi, M., & Hanaoka, F. (2016) · Gene · doi:10.1016/j.gene.2016.10.027 · Cited by 34 · see citing works
Coffill, C. R., Lee, A., Siau, J. W., Chee, S. M. Q., Joseph, T. L., Tan, Y. S., Madhumalar, A., Tay, B.-H., Brenner, S., Verma, C. S., et al. (2016) · Genes & Development · doi:10.1101/gad.274118.115 · Cited by 34 · see citing works
FBXL6 degrades phosphorylated p53 to promote tumor growth
Li, Y., Cui, K., Zhang, Q., Lin, X., Lin, X., Tang, Y., Prochownik, E. V., & Li, Y. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-021-00739-6 · Cited by 34 · see citing works
Identification of small-molecule inhibitors of USP2a
Tomala, M. D., Magiera‐Mularz, K., Kubica, K., Krzanik, S., Zieba, B. J., Musielak, B., Pustuła, M., Popowicz, G. M., Sattler, M., Dubin, G., et al. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.03.009 · Cited by 32 · see citing works
Twarda‐Clapa, A., Krzanik, S., Kubica, K., Guzik, K., Łabuzek, B., Neochoritis, C. G., Khoury, K., Kowalska, K., Czub, M., Dubin, G., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00104 · Cited by 31 · see citing works
Quantitative Analysis of Ubiquitinated Proteins in Human Pituitary and Pituitary Adenoma Tissues
Qian, S., Zhan, X., Lu, M., Li, N., Long, Y., Li, X., Desiderio, D. M., & Zhan, X. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00328 · Cited by 31 · see citing works
Sun, Y., Cao, L., Sheng, X., Chen, J., Zhou, Y., Yang, C., Deng, T., Ma, H., Feng, P., Liu, J., et al. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.162 · Cited by 30 · see citing works
Román-Trufero, M., & Dillon, N. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1058751 · Cited by 29 · see citing works
Zanjirband, M., & Rahgozar, S. (2019) · Current Drug Targets · doi:10.2174/1389450120666190402120701 · Cited by 29 · see citing works
p53 Signaling Pathway Polymorphisms Associated With Emphysematous Changes in Patients With COPD
Mizuno, S., Ishizaki, T., Kadowaki, M., Akai, M., Shiozaki, K., Iguchi, M., Oikawa, T., Nakagawa, K., Osanai, K., Toga, H., et al. (2017) · CHEST Journal · doi:10.1016/j.chest.2017.03.012 · Cited by 29 · see citing works
Zhang, L., Li, L., Chen, X., Yuan, S., Xu, T., Zhao, W., Li, M., Wang, F., Hoffman, R. M., & Jia, L. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.154493 · Cited by 28 · see citing works
Andrews, J. L., Goodfellow, F. J., Matosin, N., Snelling, M., Newell, K. A., Huang, X., & Fernandez, F. (2017) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2017.01.009 · Cited by 27 · see citing works
Oral Papillomatosis: Its Relation with Human Papilloma Virus Infection and Local Immunity—An Update
ANDREI, E. C., Baniţă, I. M., Munteanu, M. C., Busuioc, C. J., Mateescu, G.-O., Mălin, R. D., & Pisoschi, C. G. (2022) · Medicina · doi:10.3390/medicina58081103 · Cited by 27 · see citing works
SIRT3 increases cisplatin sensitivity of small-cell lung cancer through apoptosis
Guo, R., Li, Y., Xue, Y., Chen, Y., Li, J., Deng, X. L., Su, J., Liu, Y., & Sun, L. (2020) · Gene · doi:10.1016/j.gene.2020.144629 · Cited by 27 · see citing works
Seo, S. U., Woo, S. M., Kim, S., Park, J., Lee, H., Bae, Y., Kim, S., Im, S., Seo, J. H., Min, K., et al. (2021) · Oncogene · doi:10.1038/s41388-021-02088-7 · Cited by 26 · see citing works
Isoforms of RNF128 Regulate the Stability of Mutant P53 in Barrett's Esophageal Cells
Ray, D., Ray, P., Ferrer-Torres, D., Wang, Z., Nancarrow, D. J., Yoon, H., Martinho, M. S., Hinton, T., Owens, S. R., Thomas, D. G., et al. (2019) · Gastroenterology · doi:10.1053/j.gastro.2019.10.040 · Cited by 25 · see citing works
Cao, J., Nie, G., Hu, H., Zhang, X., Ni, C., Huang, Z., Qiao, G., & Ouyang, L. (2022) · Journal of Gastrointestinal Oncology · doi:10.21037/jgo-22-516 · Cited by 25 · see citing works
Survivin expression modulates the sensitivity of A549 lung cancer cells resistance to vincristine
Zhou, C., Zhu, Y., Lu, B., Zhao, W., & Zhao, X. (2018) · Oncology Letters · doi:10.3892/ol.2018.9277 · Cited by 24 · see citing works
Zhang, Y., Duan, C., Yang, J., Chen, S., Liu, Q. L., Zhou, L., Huang, Z., Xu, Y., & Xu, G. (2018) · Biochemical Journal · doi:10.1042/bcj20180005 · Cited by 23 · see citing works
Lu, J., Li, Y., Wu, Y., Zhou, S., Duan, C., Dong, Z., Kang, T., & Tang, F. (2018) · Theranostics · doi:10.7150/thno.28228 · Cited by 22 · see citing works
RetractedThe Ins and Outs of HOPS/TMUB1 in biology and pathology
Fazia, M. A. D., Castelli, M., Piobbico, D., Pieroni, S., & Servillo, G. (2020) · FEBS Journal · doi:10.1111/febs.15539 · Cited by 21 · see citing works
Sengupta, S., Ghufran, S. M., Khan, A. A., Biswas, S., & Roychoudhury, S. (2022) · Cancer Cell International · doi:10.1186/s12935-022-02831-4 · Cited by 20 · see citing works
RNF125 is a Ubiquitin-Protein Ligase that Promotes p53 Degradation
Yang, L., Zhou, B., Li, X., Lu, Z., Li, W., Huo, X., & Miao, Z. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000369691 · Cited by 21 · see citing works
TP53 in Myelodysplastic Syndromes
Jiang, Y., Gao, S., Soubise, B., Douet‐Guilbert, N., Liu, Z., & Troadec, M. (2021) · Cancers · doi:10.3390/cancers13215392 · Cited by 21 · see citing works
Nakamura, M., Sugimoto, H., Ogata, T., Hiraoka, K., Yoda, H., Sang, M., Sang, M., Zhu, Y., Yu, M., Shimozato, O., et al. (2016) · Oncogenesis · doi:10.1038/oncsis.2016.40 · Cited by 20 · see citing works
Probing protein ubiquitination in live cells
Qin, W., Steinek, C., Kolobynina, K. G., Forné, I., Imhof, A., Cardoso, M. C., & Leonhardt, H. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac805 · Cited by 19 · see citing works
Tumour suppressors and cellular senescence
Chan, A. S. L., Mowla, S. N., Arora, P., & Jat, P. (2014) · IUBMB Life · doi:10.1002/iub.1335 · Cited by 17 · see citing works
Xu, Y., Gao, Q., Xue, Y., Li, X., Xu, L., Li, C., Qin, Y., & Fang, J. S. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.007181 · Cited by 17 · see citing works
Poly(ADP-ribosyl)ation of p53 Contributes to TPEN-Induced Neuronal Apoptosis
Kim, H.-L., Ra, H., Kim, K.-R., Lee, J.-M., Im, H., & Kim, Y. H. (2015) · Molecules and Cells · doi:10.14348/molcells.2015.2142 · Cited by 17 · see citing works
- Authors
- Hock, A. K., & Vousden, K. H.
- Affiliations
- Cancer Research UK Scotland Institute (GB)
- Corresponding author
- Vousden, Karen H.
- ORCID
- Vousden, Karen H.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2014-01
- Volume
- 1843
- Issue
- 1
- Pages
- 137-149
- ISSN
- 0167-4889 (ISSN-L)
- OpenAlex
- W2062976534
- Cited by
- 168
- References
- 275
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 5 · 2023: 9 · 2022: 12 · 2021: 27 · 2020: 9 · 2019: 9 · 2018: 15 · 2017: 17 · 2016: 18 · 2015: 19 · 2014: 15 · 2013: 3
- FWCI
- 1.94
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion)
- PubMed (publishedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
- Funders
- CR-UK
- 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
- p53, ubiquitin modification, protein stability, ubiquitin-proteasome system, tumor suppressor regulation, apoptosis, senescence, oxidative stress, metabolic stress, stress response
- MeSH terms
- Animals, Humans, Protein Processing, Post-Translational, Transcriptional Activation, Tumor Suppressor Protein p53, Ubiquitin, Proto-Oncogene Proteins c-mdm2, Ubiquitination, Protein Stability
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review