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

Surfing the p53 network

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

Mdm2 promotes the rapid degradation of p53

Haupt, Y., Maya, R., Kazaz, A., & Oren, M. (1997) · Nature · doi:10.1038/387296a0 · Cited by 4,506 · see citing works

Regulation of p53 stability by Mdm2

Kubbutat, M. H. G., Jones, S. N., & Vousden, K. H. (1997) · Nature · doi:10.1038/387299a0 · Cited by 3,312 · see citing works

The Transcriptional Coactivators p300 and CBP Are Histone Acetyltransferases

Ogryzko, V. V., Schiltz, R. L., Russanova, V., Howard, B. H., & Nakatani, Y. (1996) · Cell · doi:10.1016/s0092-8674(00)82001-2 · Cited by 2,952 · 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

p53: puzzle and paradigm.Preprint

Ko, L. J., & Prives, C. L. (1996) · Genes & Development · doi:10.1101/gad.10.9.1054 · Cited by 2,338 · 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

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

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

The CBP co-activator is a histone acetyltransferase

Bannister, A. J., & Kouzarides, T. (1996) · Nature · doi:10.1038/384641a0 · Cited by 1,824 · 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

Acetylation of Histones and Transcription-Related Factors

Sterner, D. E., & Berger, S. L. (2000) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.64.2.435-459.2000 · Cited by 1,766 · see citing works

The complexity of p53 modulation: emerging patterns from divergent signalsPreprint

Giaccia, A. J., & Kastan, M. B. (1998) · Genes & Development · doi:10.1101/gad.12.19.2973 · Cited by 1,303 · see citing works

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

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

DNA damage activates p53 through a phosphorylation–acetylation cascade

Sakaguchi, K., Herrera, J. E., Saito, S., Miki, T., Bustin, M., Vassilev, A., Anderson, C. W., & Appella, E. (1998) · Genes & Development · doi:10.1101/gad.12.18.2831 · Cited by 1,204 · 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

Involvement of the TIP60 Histone Acetylase Complex in DNA Repair and Apoptosis

Ikura, T., Ogryzko, V. V., Grigoriev, M., Groisman, R., Wang, J., Horikoshi, M., Scully, R., Qin, J., & Nakatani, Y. (2000) · Cell · doi:10.1016/s0092-8674(00)00051-9 · Cited by 1,029 · see citing works

Regulation of p53 in response to DNA damage

Lakin, N. D., & Jackson, S. P. (1999) · Oncogene · doi:10.1038/sj.onc.1203015 · Cited by 987 · see citing works

The human homologs of checkpoint kinases Chk1 and Cds1 (Chk2) phosphorylate p53 at multiple DNA damage-inducible sites.

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

Regulation of the specific DNA binding function of p53

Hupp, T. R., Meek, D. W., Midgley, C., & Lane, D. P. (1992) · Cell · doi:10.1016/0092-8674(92)90562-q · Cited by 905 · see citing works

Deacetylation of p53 modulates its effect on cell growth and apoptosis

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

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

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

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

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

The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins

McMahon, S. B., Van Buskirk, H. A., Dugan, K. A., Copeland, T. D., & Cole, M. D. (1998) · Cell · doi:10.1016/s0092-8674(00)81479-8 · Cited by 693 · see citing works

Transcriptional Regulation of the p21(WAF1/CIP1)Gene

Gartel, A. L., & Tyner, A. L. (1999) · Experimental Cell Research · doi:10.1006/excr.1998.4319 · Cited by 664 · see citing works

Analysis of Chromatin Structure byin VivoFormaldehyde Cross-Linking

Orlando, V., Strutt, H. L., & Paro, R. (1997) · Methods · doi:10.1006/meth.1996.0407 · Cited by 607 · see citing works

Histone acetylases and deacetylases in cell proliferation

Kouzarides, T. (1999) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(99)80006-9 · Cited by 602 · see citing works

Synergistic activation of transcription by CBP and p53

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

Human DNA-Activated Protein Kinase Phosphorylates Serines 15 and 37 in the Amino-Terminal Transactivation Domain of Human p53

Lees‐Miller, S. P., Sakaguchi, K., Ullrich, S. J., Appella, E., & Anderson, C. W. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.11.5041-5049.1992 · Cited by 487 · 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

Phosphorylation of p53 Serine 15 Increases Interaction with CBP

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

PERP, an apoptosis-associated target of p53, is a novel member of the PMP-22/gas3 familyPreprint

Attardi, L. D., Reczek, E. E., Cosmas, C., Demicco, E. G., McCurrach, M. E., Lowe, S. W., & Jacks, T. (2000) · Genes & Development · doi:10.1101/gad.14.6.704 · Cited by 394 · see citing works

Human STAGA Complex Is a Chromatin-Acetylating Transcription Coactivator That Interacts with Pre-mRNA Splicing and DNA Damage-Binding Factors In Vivo

Martinez, E., Palhan, V. B., Tjernberg, A., Lymar, E. S., Gamper, A. M., Kundu, T. K., Chait, B. T., & Roeder, R. G. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.20.6782-6795.2001 · Cited by 383 · see citing works

The many HATs of transcription coactivators

Brown, C. E., LECHNER, T., Howe, L. J., & Workman, J. L. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01516-9 · Cited by 348 · see citing works

Increased and altered DNA binding of human p53 by S and G2/M but not Gl cyclin-dependent kinases

Wang, Y., & Prives, C. (1995) · Nature · doi:10.1038/376088a0 · Cited by 336 · see citing works

The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition.

Ishov, A. M., & Maul, G. G. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.134.4.815 · Cited by 336 · 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

p53 transcriptional activity is essential for p53‐dependent apoptosis following DNA damage

Chao, C., Saito, S., Kang, J., Anderson, C. W., Appella, E., & Xu, Y. (2000) · The EMBO Journal · doi:10.1093/emboj/19.18.4967 · Cited by 253 · see citing works

Sequence-Specific Transcriptional Corepressor Function for BRCA1 through a Novel Zinc Finger Protein, ZBRK1

Zheng, L., Pan, H., Li, S., Flesken‐Nikitin, A., Chen, P., Boyer, T., & Lee, W. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00075-7 · Cited by 232 · see citing works

The DRIP Complex and SRC-1/p160 Coactivators Share Similar Nuclear Receptor Binding Determinants but Constitute Functionally Distinct Complexes

Rachez, C., Gamble, M. J., Chang, C.-P. B., Atkins, G. B., Lazar, M. A., & Freedman, L. P. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.8.2718-2726.2000 · Cited by 205 · see citing works

A transactivation-deficient mouse model provides insights into Trp53 regulation and function

Jimenez, G. S., Nistér, M., Stommel, J. M., Beeche, M., Barcarse, E. A., Zhang, X.-Q., O’Gorman, S., & Wahl, G. M. (2000) · Nature Genetics · doi:10.1038/79152 · Cited by 194 · see citing works

Wild‐type p53 adopts a ‘mutant’‐like conformation when bound to DNA.

Halazonetis, T. D., Davis, L. J., & Kandil, A. N. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05743.x · Cited by 193 · see citing works

CREB-binding protein and p300/CBP-associated factor are transcriptional coactivators of the p53 tumor suppressor protein.

Scolnick, D. M., Chehab, N. H., Stavridi, E. S., Lien, M. C., Caruso, L. C., Morán, E., Berger, S. L., & Halazonetis, T. D. (1997) · PubMed · Cited by 186 · see citing works

Kinetics of p53 Binding to Promoter Sites In Vivo

Szak, S. T., Mays, D. J., & Pietenpol, J. A. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.10.3375-3386.2001 · Cited by 178 · see citing works

p53 Is Phosphorylated by CDK7-Cyclin H in a p36MAT1-Dependent Manner

Ko, L. J., Shieh, S.-Y., Chen, X., Jayaraman, L., Tamai, K., Taya, Y., Prives, C. L., & Pan, Z. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.12.7220 · Cited by 171 · see citing works

The 400 kDa Subunit of the PCAF Histone Acetylase Complex Belongs to the ATM Superfamily

Vassilev, A. P., Yamauchi, J., Kotani, T., Prives, C. L., Avantaggiati, M. L., Qin, J., & Nakatani, Y. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80301-9 · Cited by 162 · see citing works

The dihedral symmetry of the p53 tetramerization domain mandates a conformational switch upon DNA binding.

Waterman, J. L. F., Shenk, J. L., & Halazonetis, T. D. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07027.x · Cited by 126 · see citing works

An engineered four-stranded coiled coil substitutes for the tetramerization domain of wild-type p53 and alleviates transdominant inhibition by tumor-derived p53 mutants.

Waterman, M. J. F., Waterman, J. L. F., & Halazonetis, T. D. (1996) · PubMed · Cited by 55 · see citing works

Substitutions that compromise the ionizing radiation-induced association of p53 with 14-3-3 proteins also compromise the ability of p53 to induce cell cycle arrest.

Stavridi, E. S., Chehab, N. H., Malikzay, A., & Halazonetis, T. D. (2001) · PubMed · Cited by 54 · see citing works

Change in oligomerization specificity of the p53 tetramerization domain by hydrophobic amino acid substitutions

Stavridi, E. S., Caruso, L. C., Chehab, N. H., & Halazonetis, T. D. (1999) · Protein Science · doi:10.1110/ps.8.9.1773 · Cited by 15 · see citing works

Cellular senescence and cancer

(1999) · doi:10.1002/(sici)1096-9896(199901)187:1

Untitled work

(1998) · doi:10.1002/(sici)1521-1878(199808)20:8

Transcriptional control of human p53-regulated genes

Riley, T., Sontag, E., Chen, P., & Levine, A. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2395 · Cited by 1,921 · see citing works

AMP-activated protein kinase induces a p53-dependent metabolic checkpoint

Jones, R. G., Plas, D. R., Kubek, S., Buzzai, M., Mu, J., Xu, Y., Birnbaum, M. J., & Thompson, C. B. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.03.027 · Cited by 1,619 · see citing works

Post-translational modification of p53 in tumorigenesis

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

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

Acetylation 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

Regulation and Destabilization of HIF-1α by ARD1-Mediated Acetylation

Jeong, J.-W., Bae, M.-K., Ahn, M.-Y., Kim, S.-H., Sohn, T.-K., Bae, M.-H., Yoo, M.-A., Song, E. J., Lee, K.-J., & Kim, K.-W. (2002) · Cell · doi:10.1016/s0092-8674(02)01085-1 · Cited by 716 · see citing works

The complexity of p53 stabilization and activation

Lavin, M. F., & Gueven, N. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401925 · Cited by 701 · see citing works

Structural and Functional Conservation of the NuA4 Histone Acetyltransferase Complex from Yeast to Humans

Doyon, Y., Selleck, W., Lane, W. S., Tan, S., & Côté, J. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.5.1884-1896.2004 · Cited by 597 · 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

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

The putative cancer stem cell marker USP22 is a subunit of the human SAGA complex required for activated transcription and cell-cycle progression

Zhang, X.-Y., Varthi, M., Sykes, S. M., Phillips, C., Warzecha, C., Zhu, W., Wyce, A., Thorne, A. W., Berger, S. L., & McMahon, S. B. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.12.015 · Cited by 427 · see citing works

RNA Binding to CBP Stimulates Histone Acetylation and Transcription

Bose, D. A., Donahue, G., Reinberg, D., Shiekhattar, R., Bonasio, R., & Berger, S. L. (2017) · Cell · doi:10.1016/j.cell.2016.12.020 · Cited by 426 · see citing works

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

Danovi, D., Meulmeester, E., Pasini, D., Migliorini, D., Capra, M., Frenk, R., de Graaf, P., Francoz, S., Gasparini, P., Gobbi, A., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.13.5835-5843.2004 · Cited by 310 · see citing works

Chromatin and Transcription in Yeast

Rando, O. J., & Winston, F. (2012) · Genetics · doi:10.1534/genetics.111.132266 · Cited by 269 · see citing works

DNA Damage Signaling and p53-dependent Senescence after Prolonged β-Interferon Stimulation

Moiseeva, O., Mallette, F. A., Mukhopadhyay, U. K., Moores, A., & Ferbeyre, G. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-09-0858 · Cited by 252 · see citing works

Functional Analysis of the Roles of Posttranslational Modifications at the p53 C Terminus in Regulating p53 Stability and Activity

Feng, L., Lin, T., Uranishi, H., Gu, W., & Xu, Y. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.13.5389-5395.2005 · Cited by 236 · see citing works

Double bromodomain‐containing gene <i>Brd2</i> is essential for embryonic development in mouse

Shang, E., Wang, X., Wen, D., Greenberg, D. A., & Wolgemuth, D. J. (2009) · Developmental Dynamics · doi:10.1002/dvdy.21911 · Cited by 156 · 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

Targeting the acetylation signaling pathway in cancer therapy

Dang, F., & Wei, W. (2022) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.03.001 · Cited by 109 · see citing works

Oxidative stress–CBP axis modulates MOB1 acetylation and activates the Hippo signaling pathway

Jin, J., Zhang, L., Li, X., Xu, W., Yang, S., Song, J., Zhang, W., Zhan, J., Luo, J., & Zhang, H. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac189 · Cited by 99 · 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

Impacts of transcriptional regulation on aging and senescence

Roy, A. K., Oh, T., Rivera, O., Mubiru, J., Song, C. S., & Chatterjee, B. (2002) · Ageing Research Reviews · doi:10.1016/s1568-1637(02)00006-5 · Cited by 72 · see citing works

Deciphering the acetylation code of p53 in transcription regulation and tumor suppression

Xia, Z., Kon, N., Gu, A. P., Tavana, O., & Gu, W. (2022) · Oncogene · doi:10.1038/s41388-022-02331-9 · Cited by 60 · see citing works

Epigenetically Down-Regulated Acetyltransferase PCAF Increases the Resistance of Colorectal Cancer to 5-Fluorouracil

Liu, T., Wang, X., Hu, W., Fang, Z., Jin, Y., Fang, X., & Miao, Q. R. (2019) · Neoplasia · doi:10.1016/j.neo.2019.03.011 · Cited by 41 · see citing works

Activation of p53 in Down Syndrome and in the Ts65Dn mouse brain is associated with a pro-apoptotic phenotype

Tramutola, A., Pupo, G., Di Domenico, F., Barone, E., Arena, A., Lanzillotta, C., Broekaart, D., Blarzino, C., Head, E., Butterfield, D. A., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-151105 · Cited by 40 · see citing works

CDK4 inhibition diminishes p53 activation by MDM2 antagonists

Sriraman, A., Dickmanns, A., Najafova, Z., Johnsen, S. A., & Dobbelstein, M. (2018) · Cell Death &amp; Disease · doi:10.1038/s41419-018-0968-0 · Cited by 40 · 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

Histone acetyltransferases are crucial regulators in NF-κB mediated inflammation

Ghizzoni, M., Haisma, H. J., Maarsingh, H., & Dekker, F. J. (2011) · Drug Discovery Today · doi:10.1016/j.drudis.2011.03.009 · Cited by 136 · see citing works

Modulation of cellular processes by histone and non-histone protein acetylation

Shvedunova, M., & Akhtar, A. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00441-y · Cited by 975 · see citing works

Modulation of Histone Deacetylase 6 (HDAC6) Nuclear Import and Tubulin Deacetylase Activity through Acetylation

Liu, Y., Peng, L., Seto, E., Huang, S., & Qiu, Y. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.371120 · Cited by 144 · see citing works

Acetylation of histone deacetylase 6 by p300 attenuates its deacetylase activity

Han, Y., Jeong, H. M., Jin, Y.-H., Kim, Y.-J., Jeong, H. G., Yeo, C., & Lee, K.-Y. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.03.147 · Cited by 58 · see citing works

Reversible Histone Acetylation Involved in Transcriptional Regulation of WT1 Gene

Shao, Y., Lü, J., Cao, C., et al. (2007) · Acta Biochimica et Biophysica Sinica · doi:10.1111/j.1745-7270.2007.00363.x · Cited by 12 · see citing works