Post-translational modification of p53 in tumorigenesis

hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase

Vaziri, H., Dessain, S. K., Eaton, E. N., Imai, S., Frye, R. A., Pandita, T. K., Guarente, L., & Weinberg, R. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00527-x · Cited by 2,653 · see citing works

Activation of p53 Sequence-Specific DNA Binding by Acetylation of the p53 C-Terminal Domain

Gu, W., & Roeder, R. G. (1997) · Cell · doi:10.1016/s0092-8674(00)80521-8 · Cited by 2,559 · see citing works

The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53

Scheffner, M., Huibregtse, J. M., Vierstra, R. D., & Howley, P. M. (1993) · Cell · doi:10.1016/0092-8674(93)90384-3 · Cited by 2,387 · 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

Negative Control of p53 by Sir2α Promotes Cell Survival under Stress

Luo, J., Nikolaev, A. Y., Imai, S.-I., Chen, D., Su, F., Shiloh, A., Guarente, L., & Gu, W. (2001) · Cell · doi:10.1016/s0092-8674(01)00524-4 · Cited by 2,081 · 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

Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53

Honda, R., Tanaka, H., & Yasuda, H. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01480-4 · Cited by 1,951 · 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

p53 Has a Direct Apoptogenic Role at the Mitochondria

Mihara, M., Erster, S. H., Zaika, A. I., Petrenko, O., Chittenden, T. D., Pančoška, P., & Moll, U. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00050-9 · Cited by 1,771 · see citing works

p53 mutant mice that display early ageing-associated phenotypes

Tyner, S. D., Venkatachalam, S., Choi, J., Jones, S., Ghebranious, N., Igelmann, H., Lu, X., Soron, G., Cooper, B., Brayton, C., et al. (2002) · Nature · doi:10.1038/415045a · Cited by 1,459 · 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

A role for ATR in the DNA damage-induced phosphorylation of p53

Tibbetts, R. S., Brumbaugh, K. M., Williams, J. M., Sarkaria, J. N., Cliby, W. A., Shieh, S.-Y., Taya, Y., Prives, C., & Abraham, R. T. (1999) · Genes & Development · doi:10.1101/gad.13.2.152 · Cited by 1,046 · see citing works

Untitled work

(1999) · PubMed · Cited by 1,030 · 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

Human SIR2 deacetylates p53 and antagonizes PML/p53‐induced cellular senescence

Langley, E., Pearson, M., Faretta, M., Bauer, U., Frye, R. A., Minucci, S., Pelicci, P. G., & Kouzarides, T. (2002) · The EMBO Journal · doi:10.1093/emboj/21.10.2383 · Cited by 859 · see citing works

PML regulates p53 acetylation and premature senescence induced by oncogenic Ras

Pearson, M. A., Carbone, R., Sebastiani, C., Cioce, M., Fagioli, M., Saito, S., Higashimoto, Y., Appella, E., Minucci, S., Pandolfi, P. P., et al. (2000) · Nature · doi:10.1038/35018127 · Cited by 838 · see citing works

Pml Is Critical for Nd10 Formation and Recruits the Pml-Interacting Protein Daxx to This Nuclear Structure When Modified by Sumo-1

Ishov, A. M., Sotnikov, A. G., Negorev, D. G., Vladimirova, O. V., Neff, N. F., Kamitani, T., Yeh, E. T. H., Strauss, J. F., & Maul, G. G. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.2.221 · Cited by 825 · 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

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 · cited 1× · see citing works

p53 Sites Acetylated In Vitro by PCAF and p300 Are Acetylated In Vivo in Response to DNA Damage

Liu, L., Scolnick, D. M., Trievel, R. C., Zhang, H. B., Marmorstein, R., Halazonetis, T. D., & Berger, S. L. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.2.1202 · Cited by 776 · 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

A phylogenetically conserved NAD ⁺ -dependent protein deacetylase activity in the Sir2 protein family

Smith, J. S., Brachmann, C. B., Celic, I., Kenna, M. A., Muhammad, S., Starai, V. J., Avalos, J. L., Escalante-Semerena, J. C., Grubmeyer, C., Wolberger, C., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.12.6658 · Cited by 718 · 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

Acetylation of p53 Activates Transcription through Recruitment of Coactivators/Histone Acetyltransferases

Barlev, N. A., Liu, L., Chehab, N. H., Mansfield, K., Harris, K. G., Halazonetis, T. D., & Berger, S. L. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00414-2 · Cited by 710 · see citing works

Phosphorylation of human p53 by p38 kinase coordinates N‐terminal phosphorylation and apoptosis in response to UV radiation

Bulavin, D. V., Saito, S., Hollander, M. C., Sakaguchi, K., Anderson, C. W., Appella, E., & Fornace, A. J. (1999) · The EMBO Journal · doi:10.1093/emboj/18.23.6845 · 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

Homeodomain-interacting protein kinase-2 phosphorylates p53 at Ser 46 and mediates apoptosis

D’Orazi, G., Cecchinelli, B., Bruno, T., Manni, I., Higashimoto, Y., Saito, S., Gostissa, M., Coen, S., Marchetti, A., Sal, G. D., et al. (2001) · Nature Cell Biology · doi:10.1038/ncb714 · Cited by 682 · 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

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

THE GENETIC DEFECT IN ATAXIA-TELANGIECTASIA

Lavin, M. F., & Shiloh, Y. (1997) · Annual Review of Immunology · doi:10.1146/annurev.immunol.15.1.177 · Cited by 644 · see citing works

SUMO‐1 modification activates the transcriptional response of p53

Rodríguez, M. S., Desterro, J. M. P., Laı́n, S., Midgley, C., Lane, D. P., & Hay, R. T. (1999) · The EMBO Journal · doi:10.1093/emboj/18.22.6455 · Cited by 639 · see citing works

Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2

Hofmann, T. G., Möller, A., Sirma, H., Zentgraf, H., Taya, Y., Dröge, W., Will, H., & Schmitz, M. L. (2001) · Nature Cell Biology · doi:10.1038/ncb715 · Cited by 591 · see citing works

Phosphorylation by aurora kinase A induces Mdm2-mediated destabilization and inhibition of p53

Katayama, H. G., Sasai, K., Kawai, H., Yuan, Z.-M., Bondaruk, J. E., Suzuki, F., Fujii, S., Arlinghaus, R. B., Czerniak, B. A., & Sen, S. (2003) · Nature Genetics · doi:10.1038/ng1279 · 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

The transcriptional role of PML and the nuclear body

Zhong, S., Salomoni, P., & Pandolfi, P. P. (2000) · Nature Cell Biology · doi:10.1038/35010583 · Cited by 576 · 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

PML is induced by oncogenic <i>ras</i> and promotes premature senescence

Ferbeyre, G., de Stanchina, E., Querido, E., Baptiste, N., Prives, C., & Lowe, S. W. (2000) · Genes &amp; Development · doi:10.1101/gad.14.16.2015 · Cited by 536 · see citing works

MEKK1/JNK signaling stabilizes and activates p53

Fuchs, S. Y., Adler, V., Pincus, M. R., & Ronai, Z. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10541 · Cited by 521 · 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

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

The function of PML in p53-dependent apoptosis

Guo, A., Salomoni, P., Luo, J., Shih, A. H., Zhong, S., Gu, W., & Pandolfi, P. P. (2000) · Nature Cell Biology · doi:10.1038/35036365 · Cited by 466 · 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

p300 Transcriptional Repression Is Mediated by SUMO Modification

Girdwood, D., Bumpass, D. C., Vaughan, O. A., Thain, A., Anderson, L. A., Snowden, A. W., Garcia-Wilson, E., Perkins, N. D., & Hay, R. T. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00141-2 · Cited by 448 · see citing works

Transcriptional Regulation by p53 through Intrinsic DNA/Chromatin Binding and Site-Directed Cofactor Recruitment

Espinosa, J. M., & Emerson, B. M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00283-0 · Cited by 440 · see citing works

Acetylation of p53 augments its site-specific DNA binding both in vitro and in vivo

Luo, J., Li, M., Tang, Y., Laszkowska, M., Roeder, R. G., & Gu, W. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308762101 · Cited by 419 · see citing works

Histone Deacetylases Specifically Down-regulate p53-dependent Gene Activation

Juan, L.-J., Shia, W.-J., Chen, M.-H., Yang, W., Seto, E., Lin, Y.-S., & Wu, C.-W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000202200 · Cited by 415 · see citing works

COP9 signalosome‐specific phosphorylation targets p53 to degradation by the ubiquitin system

Bech‐Otschir, D., Kraft, R., Huang, X., Henklein, P., Kapelari, B., Pollmann, C., & Dubiel, W. (2001) · The EMBO Journal · doi:10.1093/emboj/20.7.1630 · Cited by 396 · see citing works

Resveratrol-induced activation of p53 and apoptosis is mediated by extracellular-signal-regulated protein kinases and p38 kinase.

She, Q., Bode, A. M., Ma, W., Chen, N. Y., & Dong, Z. (2001) · PubMed · Cited by 393 · 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

Critical role for Ser20 of human p53 in the negative regulation of p53 by Mdm2

Unger, T., Juven‐Gershon, T., Moallem, E., Berger, M., Sionov, R. V., Lozano, G., Oren, M., & Haupt, Y. (1999) · The EMBO Journal · doi:10.1093/emboj/18.7.1805 · Cited by 365 · see citing works

ERKs and p38 Kinase Phosphorylate p53 Protein at Serine 15 in Response to UV Radiation

She, Q., Chen, N., & Dong, Z. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001020200 · Cited by 345 · see citing works

JNK targets p53 ubiquitination and degradation in nonstressed cellsPreprint

Fuchs, S. Y., Adler, V., Buschmann, T., Yin, Z., Wu, X., Jones, S. N., & Ronai, Z. A. (1998) · Genes & Development · doi:10.1101/gad.12.17.2658 · Cited by 338 · see citing works

Resveratrol suppresses cell transformation and induces apoptosis through a p53-dependent pathway

Huang, C. (1999) · Carcinogenesis · doi:10.1093/carcin/20.2.237 · Cited by 338 · see citing works

Mutant p53 exerts a dominant negative effect by preventing wild-type p53 from binding to the promoter of its target genes

Willis, A. C., Jung, E. J., Wakefield, T., & Chen, X. (2004) · Oncogene · doi:10.1038/sj.onc.1207396 · Cited by 334 · see citing works

Role of p53 and NF-κB in epigallocatechin-3-gallate-induced apoptosis of LNCaP cells

Hastak, K., Gupta, S., Ahmad, N., Agarwal, M. K., Agarwal, M. L., & Mukhtar, H. (2003) · Oncogene · doi:10.1038/sj.onc.1206708 · Cited by 323 · see citing works

Pondering the Promyelocytic Leukemia Protein (PML) Puzzle: Possible Functions for PML Nuclear Bodies

Borden, K. L. B. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.15.5259-5269.2002 · 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

PML Is a Direct p53 Target that Modulates p53 Effector Functions

de Stanchina, E., Querido, E., Narita, M., Davuluri, R. V., Pandolfi, P. P., Ferbeyre, G., & Lowe, S. W. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00062-0 · Cited by 312 · see citing works

ATM Mediates Phosphorylation at Multiple p53 Sites, Including Ser46, in Response to Ionizing Radiation

Saito, S., Goodarzi, A. A., Higashimoto, Y., Noda, Y., Lees‐Miller, S. P., Appella, E., & Anderson, C. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200093200 · Cited by 302 · see citing works

Allosteric activation of latent p53 tetramers

Hupp, T. R., & Lane, D. P. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00195-0 · Cited by 300 · see citing works

A DNA Damage–Induced p53 Serine 392 Kinase Complex Contains CK2, hSpt16, and SSRP1

Keller, D. M., Zeng, X., Wang, Y., Zhang, Q. H., Kapoor, M., Shu, H., Goodman, R. H., Lozano, G., Zhao, Y., & Lu, H. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00176-9 · Cited by 297 · see citing works

Damage-mediated Phosphorylation of Human p53 Threonine 18 through a Cascade Mediated by a Casein 1-like Kinase

Sakaguchi, K., Saito, S., Higashimoto, Y., Roy, S., Anderson, C. W., & Appella, E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.13.9278 · Cited by 293 · see citing works

Jun NH 2 -Terminal Kinase Phosphorylation of p53 on Thr-81 Is Important for p53 Stabilization and Transcriptional Activities in Response to Stress

Buschmann, T., Potapova, O., Bar‐Shira, A., Ivanov, V. N., Fuchs, S. Y., Henderson, S. C., Fried, V. A., Minamoto, T., Alarcon-Vargas, D., Pincus, M. R., et al. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.8.2743-2754.2001 · Cited by 292 · 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

Characterization of the cDNA encoding human nucleophosmin and studies of its role in normal and abnormal growth

Chan, W., Liu, Q., Borjigin, J., Busch, H., Rennert, O. M., Tease, L. A., & Chan, P. K. (1989) · Biochemistry · doi:10.1021/bi00429a017 · Cited by 270 · see citing works

The p53 protein is an unusually shaped tetramer that binds directly to DNA.

Friedman, P. N., Chen, X., Bargonetti, J., & Prives, C. L. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.8.3319 · Cited by 264 · see citing works

Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depot

Negorev, D. G., & Maul, G. G. (2001) · Oncogene · doi:10.1038/sj.onc.1204764 · Cited by 258 · see citing works

Endoplasmic reticulum stress induces p53 cytoplasmic localization and prevents p53-dependent apoptosis by a pathway involving glycogen synthase kinase-3βPreprint

Qu, L.-K., Huang, S. H., Baltzis, D., Rivas-Estilla, A.-M., Pluquet, O., Hatzoglou, M., Koumenis, C., Taya, Y., Yoshimura, A., & Koromilas, A. E. (2004) · Genes & Development · doi:10.1101/gad.1165804 · Cited by 247 · see citing works

Phosphorylation of Serine 392 Stabilizes the Tetramer Formation of Tumor Suppressor Protein p53

Sakaguchi, K., Sakamoto, H., Lewis, M. S., Anderson, C. W., Erickson, J. W., Appella, E., & Xie, D. (1997) · Biochemistry · doi:10.1021/bi970759w · Cited by 247 · see citing works

TP53 mutation spectra and load: a tool for generating hypotheses on the etiology of cancer.

Olivier, M., Hussain, S. P., de Fromentel, C. C., Hainaut, P. L., & Harris, C. C. (2004) · PubMed · Cited by 243 · see citing works

Mdm2 association with p53 targets its ubiquitination

Fuchs, S. Y., Adler, V., Buschmann, T., Wu, X., & Ronai, Z. A. (1998) · Oncogene · doi:10.1038/sj.onc.1202200 · Cited by 235 · see citing works

Epigallocatechin-3-gallate Inhibits Epidermal Growth Factor Receptor Signaling Pathway

Sah, J. F., Balasubramanian, S., Eckert, R. L., & Rorke, E. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312333200 · Cited by 234 · see citing works

Deconstructing PML‐induced premature senescence

Bischof, O., Kirsh, O., Pearson, M. A., Itahana, K., Pelicci, P. G., & Dejean, A. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf341 · Cited by 229 · see citing works

Regulation of Transcription Functions of the p53 Tumor Suppressor by the mdm-2 Oncogene

Chen, J., Lin, J., & Levine, A. J. (1995) · Molecular Medicine · doi:10.1007/bf03401562 · Cited by 214 · see citing works

Resveratrol Induces Apoptosis in Thyroid Cancer Cell Lines via a MAPK- and p53-Dependent Mechanism

Shih, A., Davis, F. B., Lin, H., & Davis, P. J. (2002) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.87.3.8345 · Cited by 204 · see citing works

The double-stranded RNA activated protein kinase PKR physically associates with the tumor suppressor p53 protein and phosphorylates human p53 on serine 392 in vitro

Cuddihy, A. R., Hoi-Tao Wong, A., Wai Ning Tam, N., Li, S., & Koromilas, A. E. (1999) · Oncogene · doi:10.1038/sj.onc.1202620 · Cited by 203 · see citing works

Regulation of specific DNA binding by p53: evidence for a role for O-glycosylation and charged residues at the carboxy-terminus.

Shaw, P., Freeman, J., Bovey, R., & Iggo, R. D. (1996) · PubMed · Cited by 202 · 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

The AgNORs

Derenzini, M. (2000) · Micron · doi:10.1016/s0968-4328(99)00067-0 · Cited by 197 · see citing works

Activation of c- myc Gene Expression by Tumor-Derived p53 Mutants Requires a Discrete C-Terminal Domain

Frazier, M. W., He, X., Wang, J., Gu, Z., Cleveland, J. L., & Zambetti, G. P. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.7.3735 · Cited by 194 · 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

The Barrett’s Antigen Anterior Gradient-2 Silences the p53 Transcriptional Response to DNA Damage

Pöhler, E., Craig, A. L., Cotton, J. P., et al. (2004) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m300089-mcp200 · Cited by 192 · see citing works

The significance of stilbene phytoalexins in the Plasmopara viticola-grapevine interaction

Dercks, W., & Creasy, L. L. (1989) · Physiological and Molecular Plant Pathology · doi:10.1016/0885-5765(89)90043-x · Cited by 191 · see citing works

Preferential binding of ATR protein to UV-damaged DNA

Ünsal-Kaçmaz, K., Makhov, A. M., Griffith, J. D., & Sancar, A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.102167799 · Cited by 176 · see citing works

Metabolic-energy-dependent movement of PML bodies within the mammalian cell nucleus

Muratani, M., Gerlich, D. W., Janicki, S. M., Gebhard, M., Eils, R., & Spector, D. L. (2001) · Nature Cell Biology · doi:10.1038/ncb740 · Cited by 173 · see citing works

p53 is phosphorylated in vitro and in vivo by the delta and epsilon isoforms of casein kinase 1 and enhances the level of casein kinase 1 delta in response to topoisomerase-directed drugs

Knippschild, U., Milne, D., Campbell, L. E., DeMaggio, A. J., Christenson, E., Hoekstra, M. F., & Meek, D. W. (1997) · Oncogene · doi:10.1038/sj.onc.1201541 · Cited by 172 · see citing works

Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1

Kim, Y. H., Choi, C. Y., & Kim, Y. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.22.12350 · Cited by 161 · see citing works

How Many Mutant p53 Molecules Are Needed To Inactivate a Tetramer?

Chan, W. M., Siu, W. Y., Lau, A. W. S., & Poon, R. Y. C. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.8.3536-3551.2004 · Cited by 159 · see citing works

Hepatitis C virus core protein: intriguing properties and functional relevance

Ray, R. B., Ray, R. B., Ray, R., et al. (2001) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2001.tb10796.x · Cited by 153 · see citing works

Induction of apoptosis by caffeine is mediated by the p53, Bax, and caspase 3 pathways.

He, Z., Ma, W.-Y., Hashimoto, T., Bode, A. M., Yang, C. S., & Dong, Z. (2003) · PubMed · Cited by 152 · 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

Caffeine Inhibits Checkpoint Responses without Inhibiting the Ataxia-Telangiectasia-mutated (ATM) and ATM- and Rad3-related (ATR) Protein Kinases

Cortez, D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307088200 · Cited by 147 · see citing works

Green Tea Constituent (–)-Epigallocatechin-3-Gallate Inhibits Hep G2 Cell Proliferation and Induces Apoptosis through p53-Dependent and Fas-Mediated Pathways

Kuo, P., & Lin, C. (2003) · Journal of Biomedical Science · doi:10.1007/bf02256057 · Cited by 145 · see citing works

Hypophosphorylation of Mdm2 Augments p53 Stability

Blattner, C., Hay, T., Meek, D. W., & Lane, D. P. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.17.6170-6182.2002 · Cited by 144 · see citing works

Protein kinase CK1 is a p53‐threonine 18 kinase which requires prior phosphorylation of serine 15

Dumaz, N., Milne, D., & Meek, D. W. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01647-6 · Cited by 142 · see citing works

Inhibition of radiation-induced apoptosis in vitro by tumor promoters

Tomei, L., Kanter, P. M., & Wenner, C. E. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(88)81088-x · Cited by 136 · see citing works

The Promyelocytic Leukemia Protein Protects p53 from Mdm2-mediated Inhibition and Degradation

Louria‐Hayon, I., Grossman, T., Sionov, R. V., Alsheich-Bartok, O., Pandolfi, P. P., & Haupt, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301264200 · Cited by 135 · see citing works

Biogenesis of p53 Involves Cotranslational Dimerization of Monomers and Posttranslational Dimerization of Dimers

Nicholls, C. D., McLure, K. G., Shields, M. A., & Lee, P. W. K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108815200 · 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

Modulation of p53 transcription regulatory activity and post-translational modification by hepatitis C virus core protein

Kao, C.-F., Chen, S.-Y., Chen, J., & Lee, Y. W. (2004) · Oncogene · doi:10.1038/sj.onc.1207368 · Cited by 129 · see citing works

Human p53 Is Phosphorylated on Serines 6 and 9 in Response to DNA Damage-inducing Agents

Higashimoto, Y., Saito, S., Tong, X., Hong, A. L., Sakaguchi, K., Appella, E., & Anderson, C. W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002674200 · Cited by 128 · see citing works

Resveratrol inhibits cell proliferation and induces apoptosis of human breast carcinoma MCF-7 cells

Kim, Y., Choi, B. T., Lee, Y. S., et al. (2004) · Oncology Reports · doi:10.3892/or.11.2.441 · Cited by 123 · see citing works

Phosphorylation on Thr-55 by TAF1 Mediates Degradation of p53

Li, H.-H., Li, A. G., Sheppard, H. M., & Liu, X. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00123-6 · Cited by 118 · see citing works

Impairment of p53 acetylation, stability and function by an oncogenic transcription factor

Insinga, A., Monestiroli, S., Ronzoni, S., Carbone, R., Pearson, M. A., Pruneri, G., Viale, G., Appella, E., Pelicci, P. G., & Minucci, S. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600109 · Cited by 117 · see citing works

Caffeine Inhibits Cell Proliferation by G0/G1 Phase Arrest in JB6 Cells

Hashimoto, T., He, Z., Ma, W.-Y., Schmid, P. C., Bode, A. M., Yang, C. S., & Dong, Z. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-3453 · Cited by 115 · see citing works

Characterization of the oligomerization defects of two p53 mutants found in families with Li–Fraumeni and Li–Fraumeni-like syndrome

Davison, T. S., Yin, P., Nie, E., Kay, C. M., & Arrowsmith, C. H. (1998) · Oncogene · doi:10.1038/sj.onc.1202062 · Cited by 112 · see citing works

SUMO-1 and p53

Melchior, F., & Hengst, L. (2002) · Cell Cycle · doi:10.4161/cc.1.4.131 · Cited by 109 · see citing works

Inhibition of p53 degradation by Mdm2 acetylation

Wang, X., Taplick, J., Geva, N., & Oren, M. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00168-1 · Cited by 108 · see citing works

Induction of apoptosis in chronic lymphocytic leukemia cells and its prevention by phorbol ester

Forbes, I. J., Zalewski, P. D., Giannakis, C., et al. (1992) · Experimental Cell Research · doi:10.1016/0014-4827(92)90393-m · Cited by 106 · see citing works

Nucleophosmin Sets a Threshold for p53 Response to UV Radiation

Maiguel, D. A., Jones, L., Chakravarty, D., Yang, C., & Carrier, F. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.9.3703-3711.2004 · Cited by 105 · see citing works

Distinct pattern of p53 phosphorylation in human tumors

Minamoto, T., Buschmann, T., Habelhah, H., Matusevich, E., Tahara, H., Børresen‐Dale, A., Harris, C. C., Sidransky, D., & Ronai, Z. A. (2001) · Oncogene · doi:10.1038/sj.onc.1204458 · Cited by 96 · 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

Activation of the insulin-like growth factor II transcription by aflatoxin B1 induced p53 mutant 249 is caused by activation of transcription complexes; implications for a gain-of-function during the formation of hepatocellular carcinoma

Lee, Y. I., Lee, S., Das, G. C., Park, U. S., Park, S. M., & Lee, Y. I. (2000) · Oncogene · doi:10.1038/sj.onc.1203694 · Cited by 94 · see citing works

Phosphorylation at Ser-15 and Ser-392 in mutant p53 molecules from human tumors is altered compared to wild-type p53.

Ullrich, S. J., Sakaguchi, K., Lees‐Miller, S. P., Fiscella, M., Mercer, W. E., Anderson, C. W., & Appella, E. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.13.5954 · Cited by 93 · see citing works

Identification and Characterization of a Novel p300-mediated p53 Acetylation Site, Lysine 305

Wang, Y.-H., Tsay, Y.-G., Tan, B. C.-M., Lo, W.-Y., & Lee, S.-C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212574200 · Cited by 92 · see citing works

Altered Regulation of Cyclin G in Human Breast Cancer and Its Specific Localization at Replication Foci in Response to DNA Damage in p53+/+ Cells

Reimer, C., Borras, A. M., Kurdistani, S. K., Garreau, J. R., Chung, M., Aaronson, S. A., & Lee, S. W. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.16.11022 · Cited by 92 · see citing works

Stoichiometric Phosphorylation of Human p53 at Ser315Stimulates p53-dependent Transcription

Blaydes, J. P., Luciani, M. G., Pospı́šilová, Š., Ball, H. M.-L., Vojtesek, B., & Hupp, T. R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m003485200 · Cited by 90 · see citing works

Requirement of ATM in UVA-induced Signaling and Apoptosis

Zhang, Y., Ma, W., Kaji, A., Bode, A. M., & Dong, Z. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110245200 · Cited by 87 · see citing works

Ser392 Phosphorylation Regulates the Oncogenic Function of Mutant p53

Yap, D., Hsieh, J.-K., Zhong, S., Heath, V., Gusterson, B. A., Crook, T., & Lü, X. (2004) · Cancer Research · doi:10.1158/0008-5472.can-1305-2 · Cited by 84 · see citing works

Differential effects of theaflavin monogallates on cell growth, apoptosis, and Cox-2 gene expression in cancerous versus normal cells.

Lu, J., Ho, C., Ghai, G. R., & Chen, K. Y. (2000) · PubMed · Cited by 79 · see citing works

Inhibition of apoptosis in human tumour cells by okadaic acid

Song, Q., Baxter, G. D., Kovács, É., et al. (1992) · Journal of Cellular Physiology · doi:10.1002/jcp.1041530316 · Cited by 75 · see citing works

Role of MAP kinases in UVB-induced phosphorylation of p53 at serine 20

She, Q., Ma, W., & Dong, Z. (2002) · Oncogene · doi:10.1038/sj.onc.1205239 · Cited by 73 · see citing works

In vitro analysis of the dominant negative effect of p53 mutants

Chêne, P. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1897 · Cited by 72 · see citing works

p53 phosphorylation and association with murine double minute 2, c-Jun NH2-terminal kinase, p14ARF, and p300/CBP during the cell cycle and after exposure to ultraviolet irradiation.

Buschmann, T., Adler, V., Matusevich, E., Fuchs, S. Y., & Ronai, Z. A. (2000) · PubMed · Cited by 62 · see citing works

A decade of tyrosine kinases: from gene discovery to therapeutics

Craven, R. J., Lightfoot, H. M., & Cance, W. G. (2003) · Surgical Oncology · doi:10.1016/s0960-7404(03)00004-5 · Cited by 59 · see citing works

Inhibition of cell transformation by resveratrol and its derivatives: differential effects and mechanisms involved

She, Q., Ma, W., Wang, M., Kaji, A., Ho, C., & Dong, Z. (2003) · Oncogene · doi:10.1038/sj.onc.1206370 · Cited by 57 · see citing works

MDM2 Mediates p300/CREB-binding Protein-associated Factor Ubiquitination and Degradation

Jin, Y., Zeng, S. X., Lee, H., & Lu, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309916200 · Cited by 56 · see citing works

Resistance to UV‐induced apoptosis in human keratinocytes during accelerated senescence is associated with functional inactivation of p53

Chaturvedi, V., Qin, J.-Z., Stennett, L. S., Choubey, D., & Nickoloff, B. J. (2003) · Journal of Cellular Physiology · doi:10.1002/jcp.10392 · Cited by 56 · see citing works

Regulation of Ubiquitination and Degradation of p53 in Unstressed Cells through C-terminal Phosphorylation

Chernov, M. V., Bean, L. J., Lerner, N., & Stark, G. R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103170200 · Cited by 55 · see citing works

The Multistage Nature of Chemically Induced Hepatocarcinogenesis in the Rat

Pitot, H. C., & Dragan, Y. P. (1994) · Drug Metabolism Reviews · doi:10.3109/03602539409029792 · Cited by 55 · see citing works

Deacetylase inhibition in malignant melanomas: impact on cell cycle regulation and survival

Flørenes, V. A., Skrede, M. L., Jørgensen, K., & Nesland, J. M. (2004) · Melanoma Research · doi:10.1097/01.cmr.0000129576.49313.26 · Cited by 52 · see citing works

Mutant p53 is constitutively phosphorylated at Serine 15 in UV-induced mouse skin tumors: involvement of ERK1/2 MAP kinase

Melnikova, V. O., Santamaria, A. B., Bolshakov, S. V., & Ananthaswamy, H. N. (2003) · Oncogene · doi:10.1038/sj.onc.1206595 · Cited by 51 · see citing works

The negative role of cyclin G in ATM-dependent p53 activation

Ohtsuka, T., Jensen, M. R., Kim, H. G., Kim, K., & Lee, S. W. (2004) · Oncogene · doi:10.1038/sj.onc.1207693 · Cited by 50 · see citing works

p53 dephosphorylation and p21Cip1/Waf1 translocation correlate with caspase-3 activation in TGF-β1-induced apoptosis of HuH-7 cells

Fan, G., Ma, X., Wong, P., Rodrigues, C. M. P., & Steer, C. J. (2004) · APOPTOSIS · doi:10.1023/b:appt.0000018803.11260.02 · Cited by 45 · see citing works

Phosphorylation of Human p53 on Thr-55

Gatti, A. V., Li, H.-H., Traugh, J. A., et al. (2000) · Biochemistry · doi:10.1021/bi992454i · Cited by 45 · see citing works

Protein phosphatase 1, but not protein phosphatase 2A, dephosphorylates DNA‐damaging stress‐induced phospho‐serine 15 of p53

Haneda, M., Kojima, E., Nishikimi, A., Hasegawa, T., Nakashima, I., & Isobe, K. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.04.066 · Cited by 43 · see citing works

Nuclear Extracellular Signal-Regulated Kinase 2 Phosphorylates p53 at Thr55 in Response to Doxorubicin

Yeh, P.-Y., Chuang, S., Yeh, K., et al. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5043 · Cited by 33 · see citing works

p53 Activation in Chronic Radiation-Treated Breast Cancer Cells

Xia, L., Paik, A. S., & Li, J. J. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-0969 · Cited by 33 · see citing works

Identification and characterization of murine mHAUSP encoding a deubiquitinating enzyme that regulates the status of p53 ubiquitination

Lim, S.-K., Shin, J. A., Kim, Y., & Baek, K. (2004) · International Journal of Oncology · doi:10.3892/ijo.24.2.357 · Cited by 30 · see citing works

Frequent phosphorylation at serine 392 in overexpressed p53 protein due to missense mutation in carcinoma of the urinary tract

Furihata, M., Kurabayashl, A., Matsumoto, M., et al. (2002) · The Journal of Pathology · doi:10.1002/path.1082 · Cited by 26 · see citing works

Defective p53 Post-translational Modification Required for Wild Type p53 Inactivation in Malignant Epithelial Cells with mdm2 Gene Amplification

Knights, C. D., Liu, Y., Appella, E., & Kulesz-Martin, M. F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300279200 · Cited by 25 · see citing works

Mdm2 Regulates p53 Independently of p19ARF in Homeostatic Tissues

O’Leary, K. A., Mendrysa, S. M., Vaccaro, A. M., & Perry, M. E. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.24.1.186-191.2004 · Cited by 25 · see citing works

General Keynote: The Impact of Cancer Chemoprevention

Hong, W. K. (2003) · Gynecologic Oncology · doi:10.1006/gyno.2002.6685 · Cited by 22 · see citing works

Inhibition of B16BL6 tumor progression by coadministration of recombinant angiostatin K1-3 and endostatin genes with cationic liposomes

Kim, K. S., Kim, H. S., Park, J. S., Kwon, Y. G., & Park, Y. S. (2004) · Cancer Gene Therapy · doi:10.1038/sj.cgt.7700716 · Cited by 20 · see citing works

The gain of function of the p53 mutant Asp281Gly is dependent on its ability to form tetramers

Atema, A., & Chêne, P. (2002) · Cancer Letters · doi:10.1016/s0304-3835(02)00318-x · Cited by 15 · see citing works

Active transforming growth factor-β in human melanoma cell lines: No evidence for plasmin-related activation of latent TGF-β

Bízik, J., Felnerova, D., Grofova, M., & Vaheri, A. I. (1996) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(199607)62:1 · Cited by 10 · see citing works

ATP-citrate lyase links cellular metabolism to histone acetylation

Wellen, K. E., Hatzivassiliou, G., Sachdeva, U. M., Bui, T. V., Cross, J. R., & Thompson, C. B. (2009) · Science · doi:10.1126/science.1164097 · Cited by 2,298 · see citing works

Regulating the p53 pathway: in vitro hypotheses, in vivo veritas

Toledo, F., & Wahl, G. M. (2006) · Nature reviews. Cancer · doi:10.1038/nrc2012 · Cited by 1,286 · see citing works

The multiple mechanisms that regulate p53 activity and cell fate

Hafner, A., Bulyk, M. L., Jambhekar, A., & Lahav, G. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0110-x · Cited by 1,129 · see citing works

p53 Dynamics Control Cell Fate

Purvis, J. E., Karhohs, K. W., Mock, C., Batchelor, E., Loewer, A., & Lahav, G. (2012) · Science · doi:10.1126/science.1218351 · Cited by 770 · see citing works

Thioredoxin and Related Molecules–From Biology to Health and Disease

Lillig, C. H., & Holmgren, A. (2007) · Antioxidants &amp; Redox Signaling · doi:10.1089/ars.2007.9.25 · Cited by 724 · see citing works

Transcriptional Regulation by P53

Beckerman, R., & Prives, C. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000935 · Cited by 569 · see citing works

The expanding universe of p53 targets

Menendez, D., Inga, A., & Resnick, M. A. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2730 · Cited by 568 · see citing works

Coping with stress: multiple ways to activate p53

Horn, H. F., & Vousden, K. H. (2007) · Oncogene · doi:10.1038/sj.onc.1210263 · Cited by 522 · see citing works

Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell

Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436 · see citing works

Regulating tumor suppressor genes: post-translational modifications

Chen, L., Liu, S., & Tao, Y. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0196-9 · Cited by 449 · see citing works

AMPK, the metabolic syndrome and cancer

Luo, Z., Saha, A. K., Xiang, X., & Ruderman, N. B. (2005) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2004.12.011 · Cited by 426 · see citing works

p53 modifications: exquisite decorations of the powerful guardian

Liu, Y., Tavana, O., & Gu, W. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz060 · Cited by 392 · see citing works

Coordination and communication between the p53 and IGF-1–AKT–TOR signal transduction pathways

Levine, A. J., Feng, Z., Mak, T. W., You, H., & Jin, S. (2006) · Genes &amp; Development · doi:10.1101/gad.1363206 · Cited by 321 · see citing works

Distinct Regulatory Mechanisms and Functions for p53-Activated and p53-Repressed DNA Damage Response Genes in Embryonic Stem Cells

Li, M., He, Y., Dubois, W., Wu, X., Shi, J., & Huang, J. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.01.020 · Cited by 264 · 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

The nuclear-envelope protein and transcriptional repressor LAP2β interacts with HDAC3 at the nuclear periphery, and induces histone H4 deacetylation

Somech, R., Shaklai, S., Geller, O., Amariglio, N., Simon, A. J., Rechavi, G., & Gal-Yam, E. N. (2005) · Journal of Cell Science · doi:10.1242/jcs.02521 · Cited by 223 · see citing works

Cooperative regulation of p53 by modulation of ternary complex formation with CBP/p300 and HDM2

Ferreon, J. C., Lee, C. W., Arai, M., Martinez-Yamout, M. A., Dyson, H. J., & Wright, P. E. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811023106 · Cited by 210 · see citing works

Targeting histone deacetylases for cancer therapy: Trends and challenges

Liang, T., Wang, F., Elhassan, R. M., Cheng, Y., Tang, X., Chen, W., Fang, H., & Hou, X. (2023) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2023.02.007 · Cited by 222 · see citing works

Levels of HdmX expression dictate the sensitivity of normal and transformed cells to Nutlin-3

Patton, J. T., Mayo, L. D., Singhi, A. D., Gudkov, A. V., Stark, G. R., & Jackson, M. W. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3832 · Cited by 189 · see citing works

Protein neddylation and its role in health and diseases

Zhang, S., Yu, Q., Li, Z., Zhao, Y., & Sun, Y. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01800-9 · Cited by 171 · see citing works

Suppression of p53 by Notch in lymphomagenesis: implications for initiation and regression

Beverly, L. J., Felsher, D. W., & Capobianco, A. J. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1664 · Cited by 157 · see citing works

Division and apoptosis of E2f-deficient retinal progenitors

Chen, D., Pacal, M., Wenzel, P., Knoepfler, P. S., Leone, G., & Bremner, R. (2009) · Nature · doi:10.1038/nature08544 · Cited by 144 · see citing works

The UMD TP53 database and website: update and revisions

Hamroun, D., Kato, S., Ishioka, C., Claustres, M., Béroud, C., & Soussi, T. (2006) · Human Mutation · doi:10.1002/humu.20269 · Cited by 140 · see citing works

L2DTL/CDT2 and PCNA interact with p53 and regulate p53 polyubiquitination and protein stability through MDM2 and CUL4A/DDB1 complexes

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

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

Coffee Phenolic Phytochemicals Suppress Colon Cancer Metastasis by Targeting MEK and TOPK

Kang, N. J., Lee, K. W., Kim, B. H., Bode, A. M., Lee, H.-J., Heo, Y.-S., Boardman, L., Limburg, P., Lee, H. J., & Dong, Z. (2011) · Carcinogenesis · doi:10.1093/carcin/bgr022 · Cited by 123 · see citing works

Current status and new treatment approaches in TP53 mutated AML

Hunter, A. M., & Sallman, D. A. (2019) · Best Practice &amp; Research Clinical Haematology · doi:10.1016/j.beha.2019.05.004 · Cited by 102 · see citing works

Autophagy promotes mammalian survival by suppressing oxidative stress and p53

Yang, Y., Karsli-Uzunbas, G., Poillet-Perez, L., Sawant, A., Hu, Z. S., Zhao, Y., Moore, D., Hu, W., & White, E. (2020) · Genes &amp; Development · doi:10.1101/gad.335570.119 · 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

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

Expanding the p53 regulatory network: LncRNAs take up the challenge

Grossi, E., Sánchez, Y., & Huarte, M. (2016) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2015.07.011 · Cited by 78 · see citing works

Translational approaches targeting the p53 pathway for anti‐cancer therapy

Essmann, F., & Schulze‐Osthoff, K. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01570.x · Cited by 77 · see citing works

Regulation of the p53 Family Proteins by the Ubiquitin Proteasomal Pathway

Bang, S., Kaur, S., & Kurokawa, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms21010261 · Cited by 69 · see citing works

Molecular events in kidney ageing

Famulski, K. S., & Halloran, P. F. (2005) · Current Opinion in Nephrology and Hypertension · doi:10.1097/01.mnh.0000165890.60254.4e · Cited by 53 · see citing works

Cooperation of Nutlin-3a and a Wip1 inhibitor to induce p53 activity

Sriraman, A., Radovanovic, M., Wienken, M., Najafova, Z., Li, Y., & Dobbelstein, M. (2016) · Oncotarget · doi:10.18632/oncotarget.9302 · Cited by 44 · see citing works

Modification of Drosophila p53 by SUMO Modulates Its Transactivation and Pro-apoptotic Functions

Mauri, F., McNamee, L. M., Lunardi, A., Chiacchiera, F., Del Sal, G., Brodsky, M. H., & Collavin, L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710186200 · Cited by 33 · see citing works

Estimating the Distribution of Protein Post-Translational Modification States by Mass Spectrometry

Compton, P. D., Kelleher, N. L., & Gunawardena, J. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00150 · Cited by 30 · see citing works

Functional investigations of p53 acetylation enabled by heterobifunctional molecules

Chen, L.-Y., Singha Roy, S. J., Jadhav, A. M., Wang, W. W., Chen, P.-H., Bishop, T., Erb, M. A., & Parker, C. G. (2024) · ACS Chemical Biology · doi:10.1021/acschembio.4c00438 · Cited by 18 · see citing works

Susceptibility to metanephric apoptosis in bradykinin B2 receptor null mice via the p53-Bax pathway

Fan, H., Stefkova, J., & El-Dahr, S. S. (2006) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00037.2006 · Cited by 13 · see citing works

[Role of the tumor suppressor ARF in oncogenesis].

Pimkina, I. S., & Ae, D. (2009) · PubMed

Inactivation of the p53 tumor suppressor gene and activation of the Ras oncogene: cooperative events in tumorigenesis.

Solomon, H., Brosh, R., Buganim, Y., & Rotter, V. (2010) · PubMed · Cited by 40 · see citing works

The Diverse Functions of Mutant 53, Its Family Members and Isoforms in Cancer

Hall, C., & Muller, P. A. J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20246188 · Cited by 17 · see citing works

Mutant p53: One, No One, and One Hundred Thousand

Walerych, D., Lisek, K., & Sal, G. D. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00289 · Cited by 92 · see citing works

GOF Mutant p53 in Cancers: A Therapeutic Challenge

Dolma, L., & Muller, P. A. J. (2022) · Cancers · doi:10.3390/cancers14205091 · Cited by 27 · see citing works