The DOI matches its Crossref record; 49 of the 51 references it cites were found in a registry or an index.
Acetylation of the p53 DNA-binding domain regulates apoptosis induction.
Open accessAbstract
The ability of p53 to induce apoptosis plays an important role in tumor suppression. Here, we describe a previously unknown posttranslational modification of the DNA-binding domain of p53. This modification, acetylation of lysine 120 (K120), occurs rapidly after DNA damage and is catalyzed by the MYST family acetyltransferases hMOF and TIP60. Mutation of K120 to arginine, as occurs in human cancer, debilitates K120 acetylation and diminishes p53-mediated apoptosis without affecting cell-cycle arrest. The K120R mutation selectively blocks the transcription of proapoptotic target genes such as BAX and PUMA while the nonapoptotic targets p21 and hMDM2 remain unaffected. Consistent with this, depletion of hMOF and/or TIP60 inhibits the ability of p53 to activate BAX and PUMA transcription. Furthermore, the acetyllysine 120 (acetyl-K120) form of p53 specifically accumulates at proapoptotic target genes. These data suggest that K120 acetylation may help distinguish the cell-cycle arrest and apoptotic functions of p53.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“K120 resides within the p53 DNA-binding domain and its acetylation increases its binding affinity for the Bax and PUMA gene promoters, while simultaneously preventing binding to the promoter of p21 (Sykes et al., 2006; Tang Y. et al., 2006; Reed and Quelle, 2014).”
From USP7 Is a Master Regulator of Genome Stability (2020) · cites this paper as Sykes et al., 2006
Citations
Cites
WAF1, a potential mediator of p53 tumor suppression
El-Deiry, W. S., Tokino, T., Velculescu, V. E., Levy, D. B., Parsons, R., Trent, J. M., Lin, D., Mercer, W. E., Kinzler, K. W., & Vogelstein, B. (1993) · Cell · doi:10.1016/0092-8674(93)90500-p · Cited by 8,321
p53, the cellular gatekeeper for growth and division
Levine, A. J. (1997) · Cell · doi:10.1016/s0092-8674(00)81871-1 · Cited by 7,693
Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607 · cited 1×
“Alternatively, genes encoding other components of the p53 pathway can exhibit mutations (Vogelstein et al., 2000; Vousden and Lu, 2002).”
BackgroundEng, J. K., McCormack, A. L., & Yates, J. R. (1994) · Journal of the American Society for Mass Spectrometry · doi:10.1016/1044-0305(94)80016-2 · Cited by 6,484
Live or let die: the cell's response to p53
Vousden, K. H., & Lü, X. (2002) · Nature reviews. Cancer · doi:10.1038/nrc864 · Cited by 3,231
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
Crystal Structure of a p53 Tumor Suppressor-DNA Complex: Understanding Tumorigenic Mutations
Cho, Y., Gorina, S., Jeffrey, P. D., & Pavletich, N. P. (1994) · Science · doi:10.1126/science.8023157 · Cited by 2,559 · cited 2×
“Loss of K120 acetylation specifically inhibits p53-mediated apoptosis Lysine 120 lies within a region of the DNA binding domain of p53 termed the L1 loop (Cho et al., 1994).”
Backgroundp53- and Drug-Induced Apoptotic Responses Mediated by BH3-Only Proteins Puma and Noxa
Villunger, A., Michalak, E. M., Coultas, L., Müllauer, F., Böck, G., Ausserlechner, M. J., Adams, J. M., & Strasser, A. (2003) · Science · doi:10.1126/science.1090072 · Cited by 1,327
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
Oda, K., Arakawa, H., Tanaka, T., Matsuda, K., Tanikawa, C., Mori, T., Nishimori, H., Tamai, K., Tokino, T., Nakamura, Y., et al. (2000) · Cell · doi:10.1016/s0092-8674(00)00073-8 · Cited by 1,162
Flagged first, then by citations
2 of the 51 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 401–500 of 752
CHFR negatively regulates SIRT1 activity upon oxidative stress
Kim, M., Kwon, Y. E., Song, J. O., Bae, S. J., & Seol, J. H. (2016) · Scientific Reports · doi:10.1038/srep37578 · Cited by 24
CNPY2 promoted the proliferation of renal cell carcinoma cells and increased the expression of TP53
Taniguchi, H., Ito, S., Ueda, T., Morioka, Y., Kayukawa, N., Ueno, A., Nakagawa, H., Fujihara, A., Ushijima, S., Kanazawa, M., et al. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.02.095 · Cited by 24
Structure and function of histone acetyltransferase MOF
Chen, Q. Y., Costa, M., & Sun, H. (2015) · AIMS Biophysics · doi:10.3934/biophy.2015.4.555 · Cited by 28
Differential regulation of p53 target genes: it's (core promoter) elementary: Figure 1.Preprint
Gomes, N. P., & Espinosa, J. M. (2010) · Genes & Development · doi:10.1101/gad.1893610 · Cited by 24
Yu, T., Ding, C., Peng, J., Liang, G., Tang, Y., Zhao, J., & Li, Z. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07549-5 · Cited by 24
Interaction of the epigenetic integrator UHRF1 with the MYST domain of TIP60 inside the cell
Ashraf, W., Bronner, C., Zaayter, L., Ahmad, T., Richert, L., Alhosin, M., Ibrahim, A., Hamiche, A., Mély, Y., & Mousli, M. (2017) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-017-0659-1 · Cited by 23
The histone acetyltransferase Mof regulates Runx2 and Osterix for osteoblast differentiation
Chen, J., Liu, D., Chen, B., Yang, Y., Zhu, H., Li, D., Liu, K., Zhu, L., Liu, H., Li, M., et al. (2023) · Cell and Tissue Research · doi:10.1007/s00441-023-03791-5 · Cited by 23
Furgerson, M., Fechheimer, M., & Furukawa, R. (2012) · PLoS ONE · doi:10.1371/journal.pone.0044996 · Cited by 23
hMOF, a KAT(8) with Many Lives
Mellert, H. S., & McMahon, S. B. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.10.005 · Cited by 23
Self-citationIn vitro ischemia decreases histone H4K16 acetylation in neural cells
Dmitriev, R. I., & Papkovsky, D. B. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.11.038 · Cited by 24
Mechanistic Links Between ATM and Histone Methylation Codes During DNA Repair
Xu, Y., Xu, C., & Price, B. D. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-387665-2.00010-9 · Cited by 23
Lin, Y., & Wang, F.-F. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.10.017 · Cited by 26
Lee, S.-Y., Park, J., Jeong, S., Kim, B., Kang, Y., Xu, Y., & Chung, S. (2018) · Oncogene · doi:10.1038/s41388-018-0542-3 · Cited by 22
Histone acetyltransferase promotes fluoride toxicity in LS8 cells
Deng, H., Fujiwara, N., Cui, H., Whitford, G. M., Bartlett, J. D., & Suzuki, M. (2020) · Chemosphere · doi:10.1016/j.chemosphere.2020.125825 · Cited by 22
The pseudo-caspase FLIP(L) regulates cell fate following p53 activation
Lees, A., McIntyre, A. J., Crawford, N., Falcone, F., McCann, C. K., Holohan, C., Quinn, G. P., Roberts, J. Z., Sessler, T., Gallagher, P. F., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2001520117 · Cited by 22
ING Proteins: Tumour Suppressors or Oncoproteins
Jacquet, K., & Binda, O. (2021) · Cancers · doi:10.3390/cancers13092110 · Cited by 22
Li, J., Wang, J., Su, D., Nie, X., Liu, Y., Teng, L., Pang, J., Wu, H., & Liang, Z. (2021) · Gastroenterology Research and Practice · doi:10.1155/2021/2510195 · Cited by 22
PDCD5-Regulated Cell Fate Decision after Ultraviolet-Irradiation-Induced DNA Damage
Zhuge, C., Chang, Y., Li, Y., Chen, Y., & Lei, J. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.10.044 · Cited by 22
Plasmodium falciparumRuvB proteins
Ahmad, M., & Tuteja, R. (2012) · Communicative & Integrative Biology · doi:10.4161/cib.20005 · Cited by 22
Regulation of Tip60‐dependent p53 acetylation in cell fate decision
Wang, P., Bao, H., Zhang, X., Liu, F., & Wang, W. (2018) · FEBS Letters · doi:10.1002/1873-3468.13287 · Cited by 21
Soft-shell clam (Mya arenaria) p53: A structural and functional comparison to human p53
Holbrook, L. A. C., Butler, R. A., Cashon, R. E., & Beneden, R. J. V. (2008) · Gene · doi:10.1016/j.gene.2008.11.029 · Cited by 22
Nicotinamide adenine dinucleotide suppresses epileptogenesis at an early stage
Liu, J., Yang, B., Zhou, P., Kong, Y., Hu, W., Zhu, G., Ying, W., Li, W., Wang, Y., & Li, S. (2017) · Scientific Reports · doi:10.1038/s41598-017-07343-0 · Cited by 21
HDAC6 deficiency induces apoptosis in mesenchymal stem cells through p53 K120 acetylation
Park, S.-Y., Phorl, S., Jung, S., Korm, S., Lee, S.-I., Noh, S., Han, M., Naskar, R., Kim, J., Choi, Y., et al. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.10.087 · Cited by 21
CDK9‐mediated phosphorylation controls the interaction of TIP60 with the transcriptional machinery
Brauns‐Schubert, P., Schubert, F., Wissler, M., Weiß, M., Schlicher, L., Bessler, S., Safavi, M., Miething, C., Borner, C., Brummer, T., et al. (2018) · EMBO Reports · doi:10.15252/embr.201744311 · Cited by 20
Li, H., Lu, M., Zhang, H., Wang, S., Wang, F., Ma, X., Liu, J., Li, X., Yang, H., Shen, H., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04774-0 · Cited by 20
Global Effect of Inauhzin on Human p53-Responsive Transcriptome
Liao, J., Zeng, S. X., Zhou, X. Y., & Lu, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0052172 · Cited by 20
Romeo, M., Hutchison, T., Malu, A., White, A., Kim, J., Gardner, R., Smith, K., Nelson, K., Bergeson, R., McKee, R., et al. (2018) · Virology · doi:10.1016/j.virol.2018.02.010 · Cited by 20
Jiang, B.-H., Qian, Y.-C., Xie, Y.-X., Wang, C.-S., Shi, Z., Jiang, C., Tang, Y., Qian, X., & Wang, L. (2019) · Asian Journal of Andrology · doi:10.4103/aja.aja_76_19 · Cited by 20
Stress-Induced Cell-Cycle Activation in Tip60 Haploinsufficient Adult Cardiomyocytes
Fisher, J. B., Kim, M. S., Blinka, S. M., Ge, Z., Wan, T. C., Duris, C. B., Christian, D., Twaroski, K., North, P. E., Auchampach, J. A., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031569 · Cited by 20
Inhibition of the Single Downstream Target BAG1 Activates the Latent Apoptotic Potential of MYC
Zhang, X., Pfeiffer, H. K., Mellert, H. S., Stanek, T. J., Sussman, R. T., Kumari, A., Yu, D., Rigoutsos, I., Thomas‐Tikhonenko, A., Seidel, H. E., et al. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.06297-11 · Cited by 20
Self-citationSchirling, C., Heseding, C., Heise, F., Kesper, D. A., Klebes, A., Klein‐Hitpaß, L., Vortkamp, A., Hoffmann, D. E., Saumweber, H., & Ehrenhofer‐Murray, A. E. (2009) · Chromosoma · doi:10.1007/s00412-009-0247-z · Cited by 20
p73-Binding Partners and Their Functional Significance
Ozaki, T., Kubo, N., & Nakagawara, A. (2010) · International Journal of Proteomics · doi:10.1155/2010/283863 · Cited by 20
Integration of Apoptosis and MetabolismPreprint
Yi, C., Vakifahmetoglu-Norberg, H., & Yuan, J. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.010777 · Cited by 20
Pharmacological inhibition of the acetyltransferase Tip60 mitigates myocardial infarction injury
Wang, X., Wan, T. C., Harty, K. R., Lauth, A., Smith, B. C., Lough, J., & Auchampach, J. A. (2022) · Disease Models & Mechanisms · doi:10.1242/dmm.049786 · Cited by 19
Unbiased interrogation of functional lysine residues in human proteome
Bao, Y., Pan, Q., Xu, P., Liu, Z., Zhang, Z., Liu, Y., Xu, Y., Yu, Y., Zhou, Z. L., & Wei, W. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.10.033 · Cited by 19
Gogna, R., Madan, E., Kuppusamy, P., & Pati, U. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4103 · Cited by 20
The Histone Acetyltransferase hMOF is Overexpressed in Non-small Cell Lung Carcinoma
Song, J. S., Chun, S., Lee, J. Y., Kim, D. K., Kim, Y., & Jang, S. J. (2011) · Journal of Pathology and Translational Medicine · doi:10.4132/koreanjpathol.2011.45.4.386 · Cited by 19
Su, W., Ho, Y.-C., Wu, C.-K., Hsu, S.-H., Shiu, J.-L., Huang, J.-C., Chang, S., Chiu, W., Hung, J., Liu, T.-L., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-04223-5 · Cited by 19
Fang, X., Lu, G., Ha, K., Lin, H., Ye, D., Zuo, Q., Fu, Y., Zou, C., & Zhang, P. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.11.028 · Cited by 19
The genetic landscape of 5T models for multiple myeloma
Maes, K., Boeckx, B., Vlummens, P., Veirman, K. D., Menu, E., Vanderkerken, K., Lambrechts, D., & Bruyne, E. D. (2018) · Scientific Reports · doi:10.1038/s41598-018-33396-w · Cited by 20
TIP60 Represses Transcriptional Activity of p73β via an MDM2-bridged Ternary Complex
Kim, J.-W., Song, P. I., Jeong, M.-H., An, J., Lee, S., Jang, S., Song, K., Armstrong, C. A., & Choi, K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800161200 · Cited by 19
Ozaki, T., Nakamura, M., & Shimozato, O. (2015) · Biomolecules · doi:10.3390/biom5042854 · Cited by 18
The new frontier in cancer research: Deciphering cancer epigenetics
Lohrum, M. A. E., Stunnenberg, H. G., & Logie, C. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.03.011 · Cited by 19
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
MOF-mediated PRDX1 acetylation regulates inflammatory macrophage activation
Chen, H., Sun, Y., Mittler, G., Rumpf, T., Shvedunova, M., Grosschedl, R., & Akhtar, A. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114682 · Cited by 22
TIP60 up-regulates ΔNp63α to promote cellular proliferation
Stacy, A. J., Zhang, J., Craig, M. P., Hira, A., Dole, N., & Kadakia, M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010388 · Cited by 18
Histone lysine modifying enzymes and their critical roles in DNA double-strand break repair
Zhang, J., Lu, X., MoghaddamKohi, S., Shi, L., Xu, X., & Zhu, W. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103206 · Cited by 18
VprBP/DCAF1 regulates p53 function and stability through site-specific phosphorylation
Ghate, N. B., Kim, S., Mehmood, R., Shin, Y., Kim, K., & An, W. (2023) · Oncogene · doi:10.1038/s41388-023-02685-8 · Cited by 20
Advances in the mechanism of small nucleolar RNA and its role in DNA damage response
Shen, L., Zhang, W., Deng, J.-R., Qi, Z., Lin, Z.-W., & Wang, Z. (2024) · Military Medical Research · doi:10.1186/s40779-024-00553-4 · Cited by 22
RNAi screening identifies KAT8 as a key molecule important for cancer cell survival.
Zhang, S., Liu, X., Zhang, Y., Cheng, Y., & Li, Y. (2013) · Europe PMC (PubMed Central) · Cited by 18
Lysine methylation and the regulation of p53
Carr, S. M., Munro, S., & Thangue, N. B. L. (2012) · Essays in Biochemistry · doi:10.1042/bse0520079 · Cited by 18
Lysines in the tetramerization domain of p53 selectively modulate G1 arrest
Beckerman, R., Yoh, K. E., Mattia-Sansobrino, M., Zupnick, A., Laptenko, O., Karni-Schmidt, O., Ahn, J., Byeon, I. L., Keezer, S. M., & Prives, C. L. (2016) · Cell Cycle · doi:10.1080/15384101.2016.1170270 · Cited by 19
Wang, X., Wan, T. C., Lauth, A., Purdy, A. L., Harty, K. R., Patterson, M., Lough, J., & Auchampach, J. A. (2021) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2021.09.012 · Cited by 17
Cai, M., Xu, S., Jin, Y., Yu, J., Dai, S., Shi, X., & Guo, R. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01478-y · Cited by 18
Aspirin‐Mediated Acetylation of SIRT1 Maintains Intestinal Immune Homeostasis
Xie, L., Li, C., Wang, C., Wu, Z., Wang, C., Chen, C., Chen, X., Zhou, D., Zhou, Q., Lu, P., et al. (2024) · Advanced Science · doi:10.1002/advs.202306378 · Cited by 17
Activation of NFAT signal by p53‐K120R mutant
Shinmen, N., Koshida, T., Kumazawa, T., Sato, K., Shimada, H., Matsutani, T., Iwadate, Y., Takiguchi, M., & Hiwasa, T. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.04.041 · Cited by 17
An H4K16 histone acetyltransferase mediates decondensation of the X chromosome in C. elegans males
Lau, A. C., Zhu, K. P., Brouhard, E. A., Davis, M. B., & Csankovszki, G. (2016) · Epigenetics & Chromatin · doi:10.1186/s13072-016-0097-x · Cited by 17
Rivera-Colón, Y., Maguire, A., Liszczak, G., Olia, A. S., & Marmorstein, R. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.752220 · Cited by 17
Self-citationSilencers of HTLV-1 and HTLV-2: the pX-encoded latency-maintenance factors
Harrod, R. (2019) · Retrovirology · doi:10.1186/s12977-019-0487-9 · Cited by 17
Effect of lysine side chain length on histone lysine acetyltransferase catalysis
Proietti, G., Wang, Y., Rainone, G., & Mecinović, J. (2020) · Scientific Reports · doi:10.1038/s41598-020-69510-0 · Cited by 19
Class IIa HDACs inhibit cell death pathways and protect muscle integrity in response to lipotoxicity
Martin, S. D., Connor, T., Sanigorski, A., McEwen, K. A., Henstridge, D. C., Nijagal, B., De Souza, D., Tull, D. L., Meikle, P. J., Kowalski, G. M., et al. (2023) · Cell Death & Disease · doi:10.1038/s41419-023-06319-5 · Cited by 16
p53 as the main traffic controller of the cell signaling network
Sebastian, S. (2010) · Frontiers in bioscience · doi:10.2741/3669 · Cited by 16
Grass Carp (Ctenopharyngodon idella) KAT8 Inhibits IFN 1 Response Through Acetylating IRF3/IRF7
Li, M., Hu, J., Mao, H., Li, D., Jiang, Z., Sun, Z., Yu, T., Hu, C., & Xu, X. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2021.808159 · Cited by 16
New insights into the DNA repair pathway choice with NuA4/TIP60
Lashgari, A., Tchara, P.-E. K., Lambert, J., & Côté, J. (2022) · DNA repair · doi:10.1016/j.dnarep.2022.103315 · Cited by 17
Upregulation of SIRT1 Contributes to dmPGE2-dependent Radioprotection of Hematopoietic Stem Cells
Liu, L., Li, H., Patterson, A. M., Plett, P. A., Sampson, C. H., Mohammad, K. S., Capitano, M. L., Singh, P., Yao, C., Orschell, C. M., et al. (2022) · Stem Cell Reviews and Reports · doi:10.1007/s12015-022-10368-2 · Cited by 16
Wang, L., Yang, X., Zhao, K., Huang, S., Qin, Y., Chen, Z., Hu, X., Jin, G., & Zhou, Z. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.113908 · Cited by 16
Lysine and arginine methylation of transcription factors
Giaimo, B. D., Ferrante, F., & Borggrefe, T. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05531-6 · Cited by 17
Orphan Nuclear Receptor PNR/NR2E3 Stimulates p53 Functions by Enhancing p53 Acetylation
Wen, Z. H., Pyeon, D., Wang, Y., Lambert, P. F., Xu, W., & Ahlquist, P. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05513-11 · Cited by 16
Expression of the MOZ-TIF2 oncoprotein in mice represses senescence
Largeot, A., Pérez-Campo, F. M., Marinopoulou, E., Lie‐A‐Ling, M., Kouskoff, V., & Lacaud, G. (2016) · Experimental Hematology · doi:10.1016/j.exphem.2015.12.006 · Cited by 16
Regulation of Cellular Processes by SUMO: Understudied Topics
Enserink, J. M. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-50044-7_5 · Cited by 17
The “readers” of unacetylated p53 represent a new class of acidic domain proteins
Wang, D., Kon, N., Tavana, O., & Gu, W. (2017) · Nucleus · doi:10.1080/19491034.2017.1313939 · Cited by 16
Molecular mechanisms of cellular senescence and immortalization of human cells
Kiyono, T. (2007) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.11.12.1623 · Cited by 16
Choi, O. R., Ryu, M. S., & Lim, I. K. (2016) · Cellular Signalling · doi:10.1016/j.cellsig.2016.05.014 · Cited by 16
Therapeutic Role of Synthetic Lethality in ARID1A -Deficient Malignancies
Hein, K. Z., Stephen, B., & Fu, S. (2023) · Journal of Immunotherapy and Precision Oncology · doi:10.36401/jipo-22-37 · Cited by 17
The Janus Face of p53-Targeting Ubiquitin Ligases
Hao, Q., Chen, Y., & Zhou, X. Y. (2020) · Cells · doi:10.3390/cells9071656 · Cited by 16
Brénachot, X., Rigault, C., Nédélec, E., Laderrière, A., Khanam, T., Gouazé, A., Chaudy, S., Lemoine, A., Datiche, F., Gascuel, J., et al. (2014) · Molecular Metabolism · doi:10.1016/j.molmet.2014.05.006 · Cited by 15
Lora, V., Grings, A. O., Capp, E., Corleta, H. V. E., & Brum, I. S. (2012) · Archives of Gynecology and Obstetrics · doi:10.1007/s00404-012-2245-2 · Cited by 15
Fang, Q.-J., Chi, B., Lin, Q., Huang, C.-M., Jin, S.-W., Cai, J., Nan, K., Han, Y., Tao, Y., Cao, H., et al. (2020) · Europe PMC (PubMed Central) · Cited by 14
Millau, J., Bandele, O. J., Perron, J., Bastien, N., Bouchard, É. F., Gaudreau, L. R., Bell, D. A., & Drouin, R. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq1209 · Cited by 14
Regulation and function of histone acetyltransferase MOF
Yang, Y., Han, X., Guan, J., & Li, X. (2014) · Frontiers of Medicine · doi:10.1007/s11684-014-0314-6 · Cited by 14
Muzika, M., Muskat, N. H., Sarid, S., Ben‐David, O., Mehl, R. A., & Arbely, E. (2018) · RSC Advances · doi:10.1039/c8ra04359k · Cited by 14
Identification of New p53 Acetylation Sites in COS-1 Cells
Joubel, A., Chalkley, R. J., Medzihradszky, K. F., Hondermarck, H., & Burlingame, A. L. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800487-mcp200 · Cited by 15
Wu, Y. M., Zeng, K., Wang, C., Wang, S., Sun, H., Liu, W., Wang, X., Niu, J., Cong, S., Zhou, X., et al. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.10.090 · Cited by 13
Wang, X., Lupton, C., Lauth, A., Wan, T. C., Foster, P., Patterson, M., Auchampach, J. A., & Lough, J. (2021) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2021.02.005 · Cited by 13
TFIIS.h, a new target of p53, regulates transcription efficiency of pro-apoptotic bax gene
Liao, J., Cao, B., Deng, J., Zhou, X. Y., Strong, M. J., Zeng, S. X., Xiong, J., Flemington, E. K., & Lu, H. (2016) · Scientific Reports · doi:10.1038/srep23542 · Cited by 13
Mode of action of carboplatin via activating p53/miR‐145 axis in head and neck cancers
Kılıç, A., Barlak, N., Şanli, F., Aytatlı, A., Çapik, Ö., & Karataş, Ö. F. (2019) · The Laryngoscope · doi:10.1002/lary.28492 · Cited by 13
Zhu, Y., Xie, Z., Wang, J., Liu, Y., & Wang, J. (2012) · Gene · doi:10.1016/j.gene.2012.10.077 · Cited by 13
Crosstalk between site-specific modifications on p53 and histone H3
Warnock, L. J., Adamson, R., Lynch, C. J., & Milner, J. (2007) · Oncogene · doi:10.1038/sj.onc.1210787 · Cited by 13
Yapindi, L., Bowley, T. Y., Kurtaneck, N., Bergeson, R. L., James, K., Wilbourne, J., Harrod, C. K., Hernandez, B. Y., Emerling, B. E., Yates, C., et al. (2023) · Virology · doi:10.1016/j.virol.2023.05.004 · Cited by 15
A Novel Tumor suppressor network in squamous malignancies
Costa, C., Santos, M., Segrelles, C., Dueñas, M., Lara, M. F., Agirre, X., Prósper, F., García‐Escudero, R., & Paramio, J. M. (2012) · Scientific Reports · doi:10.1038/srep00828 · Cited by 12
Liu, H.-C., Ma, F., Shen, Y., Hu, Y., & Pan, S. (2015) · Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics · doi:10.3727/096504015x14424348426035 · Cited by 12
Retrotransposon‐derived p53 binding sites enhance telomere maintenance and genome protection
Lieberman, P. M. (2016) · BioEssays · doi:10.1002/bies.201600078 · Cited by 12
Cheng, Y., Li, S., Liu, Y., Li, J., Chen, Y., & Zhao, H. (2020) · Medical Science Monitor · doi:10.12659/msm.921250 · Cited by 12
The biology of papillomavirus PDZ associations: what do they offer papillomaviruses?
Thomas, M., & Banks, L. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.09.011 · Cited by 12
Mukherjee, S., Sarkar, R., Biswas, J., & Roy, M. (2012) · International Journal of Green Nanotechnology · doi:10.1080/19430892.2012.691799 · Cited by 12
Hu, S., Song, E., Tian, R., Ma, S., Yang, T., Mu, Y., Li, Y., Shao, C., Gao, S., & Gao, Y. (2009) · Cellular Physiology and Biochemistry · doi:10.1159/000233258 · Cited by 12
RETRACTED: High‐Resolution Imaging of Human Cancer Proteins Using Microprocessor Materials
Solares, M. J., Jonaid, G. M., Luqiu, W. Y., Berry, S., Khadela, J., Liang, Y., Evans, M. C., Pridham, K. J., Dearnaley, W. J., Sheng, Z., et al. (2022) · ChemBioChem · doi:10.1002/cbic.202200310 · Cited by 11
RetractedKim, H., Zheng, X., & Lee, E. N. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241311032 · Cited by 10
Liu, T., Zhao, Y.-M., Jin, K., Wang, J., & Zhao, X. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105704 · Cited by 11
Functional analysis of the acetylation of human p53 in DNA damage responses
Chung, S., Zhu, S., Xu, Y., & Fu, X. (2014) · Protein & Cell · doi:10.1007/s13238-014-0048-x · Cited by 11
Metadata
- Authors
- Sykes, S. M., Mellert, H. S., Holbert, M. A., Li, K., Marmorstein, R., Lane, W. S., & McMahon, S. B.
- Affiliations
- Thomas Jefferson University (US)
- The Wistar Institute (US)
- Harvard University (US)
- Corresponding author
- McMahon, Steven B.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2006-12
- Volume
- 24
- Issue
- 6
- Pages
- 841-851
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC1766330
- OpenAlex
- W2038324148
- Cited by
- 752
- References
- 51
- Citations by year
- 2026: 22 · 2025: 28 · 2024: 25 · 2023: 24 · 2022: 31 · 2021: 39 · 2020: 29 · 2019: 30 · 2018: 38 · 2017: 31 · 2016: 43 · 2015: 44 · 2014: 45 · 2013: 52 · 2012: 52
- FWCI
- 21.33
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (R01CA090465, CA090465, CA098172, R01CA098172)
- National Institute of General Medical Sciences (R01GM060293)
- 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 › Cell death mechanisms and regulation
- Keywords
- p53, DNA-binding domain, post-translational modification, apoptosis induction, hMOF, Tip60, p21, DNA damage response, tumor suppression, cell cycle arrest
- MeSH terms
- Lysine Acetyltransferase 5, Acetylation, Amino Acid Sequence, Binding Sites, Cell Cycle, Humans, Molecular Sequence Data, Promoter Regions, Genetic, Proto-Oncogene Proteins, Tumor Suppressor Protein p53, Apoptosis, Apoptosis Regulatory Proteins, bcl-2-Associated X Protein, Histone Acetyltransferases
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