Cell Type- and Promoter-specific Roles of Ser18 Phosphorylation in Regulating p53 Responses

p53 Mutations in Human Cancers

Hollstein, M., Sidransky, D., Vogelstein, B., & Harris, C. C. (1991) · Science · doi:10.1126/science.1905840 · Cited by 8,018

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

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

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

p53 is required for radiation-induced apoptosis in mouse thymocytes

Lowe, S. W., Schmitt, E. M., Smith, S. W., Osborne, B. A., & Jacks, T. (1993) · Nature · doi:10.1038/362847a0 · Cited by 2,864

p53: puzzle and paradigm.Preprint

Ko, L. J., & Prives, C. L. (1996) · Genes & Development · doi:10.1101/gad.10.9.1054 · Cited by 2,346

Thymocyte apoptosis induced by p53-dependent and independent pathways

Clarke, A. R., Purdie, C. A., Harrison, D. J., Morris, R. G., Bird, C. C., Hooper, M. L., & Wyllie, A. H. (1993) · Nature · doi:10.1038/362849a0 · Cited by 2,271

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

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

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

Modulation of the p53 family network by RNA-binding proteins

Lucchesi, C. A., Zhang, J., & Chen, X. (2016) · Translational Cancer Research · doi:10.21037/tcr.2016.08.30 · Cited by 17

Transcription activity is required for p53-dependent tumor suppression

Gaidarenko, O., & Xu, Y. (2009) · Oncogene · doi:10.1038/onc.2009.290 · Cited by 17

Delayed expression of apoptotic and cell-cycle control genes in carcinogen-exposed bladders of mice lacking p53.S389 phosphorylation

Bruins, W., Jonker, M. J., Bruning, O., Pennings, J. L. A., Schaap, M. M., Hoogervorst, E. M., STEEG, H. V., Breit, T. M., & de Vries, A. (2007) · Carcinogenesis · doi:10.1093/carcin/bgm041 · Cited by 13

Cell death in normal and abnormal development

Mirkes, P. E. (2008) · Congenital Anomalies · doi:10.1111/j.1741-4520.2007.00175.x · Cited by 14

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

Requirement for phosphorylation of P53 at Ser312 in suppression of chemical carcinogenesis

Slee, E. A., & Lü, X. (2013) · Scientific Reports · doi:10.1038/srep03105 · Cited by 10

Identification of a novel, transactivation-defective splicing variant of p53 gene in patients with chronic lymphocytic leukemia

Peková, Š., Čmejla, R., Smolej, L., Kozák, T., Špaček, M., & Průcha, M. (2007) · Leukemia Research · doi:10.1016/j.leukres.2007.06.022 · Cited by 10

TP53LNC-DB, the database of lncRNAs in the p53 signalling network

Khan, M. R., Bukhari, I., Khan, R., Hussain, H. M. J., Wu, M., Thorne, R. F., Li, J., & Liu, G. (2018) · Database · doi:10.1093/database/bay136 · Cited by 8

Comparison of quantitative faecal immunochemical tests for haemoglobin (FIT) for asymptomatic population screening

Fraser, C. G. (2016) · Translational Cancer Research · doi:10.21037/tcr.2016.10.22 · Cited by 8

Gatekeepers of the Guardian: p53 Regulation by Post-Translational Modification, MDM2 and MDMX

Wahl, G. M., Stommel, J. M., Krummel, K. A., & Wade, M. R. (2005) · Springer eBooks · doi:10.1007/978-1-4020-2922-6_4 · Cited by 9

Analysis of p53 Tumor Suppressor Pathway Genes in Chronic Lymphocytic Leukemia

Işın, M., Yenerel, M. N., Aktan, M., Buyru, N., & Dalay, N. (2011) · DNA and Cell Biology · doi:10.1089/dna.2011.1314 · Cited by 6

Allosteric changes in HDM2 by the ATM phosphomimetic S395D mutation: implications on HDM2 function

Uhrík, L., Wang, L., Hároníková, L., Medina‐Medina, I., Rebolloso‐Gómez, Y., Chen, S., Vojtěšek, B., Fåhræus, R., Hernychová, L., & Olivares‐Illana, V. (2019) · Biochemical Journal · doi:10.1042/bcj20190687 · Cited by 6

Regulation of p53 DNA Binding

McKinney, K. M., & Prives, C. L. (2005) · Springer eBooks · doi:10.1007/978-1-4020-2922-6_2 · Cited by 6

Tumor-suppressive or tumor-supportive: For p53, that is the question

Khan, M. R., Wu, M., & Liu, G. (2018) · Molecular & Cellular Oncology · doi:10.1080/23723556.2017.1408537 · Cited by 5

Loss of p53 Ser18 and Atm Results in Embryonic Lethality without Cooperation in Tumorigenesis

Armata, H. L., Shroff, P., Garlick, D., Penta, K. L., Tapper, A. R., & Sluss, H. K. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024813 · Cited by 4

Dysfunction of the Autophagy System and MDM2–p53 Axis Leads to the Accumulation of Amyloidogenic Proteins in Angelman Syndrome Models

de Almeida, J. F. M., Contestabile, M., Tonazzini, I., Cesari, C. D., Baroncelli, L., Martini, C., & Daniele, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262211032 · Cited by 3

Characterization of the E3 Ubiquitin Ligase Pirh2

Tai, E. (2010) · TSpace (University of Toronto) · Cited by 3

Regulation of p53 Activity and Associated Checkpoint Controls

Post, S. M., Quintás‐Cardama, A., & Lozano, G. (2009) · Humana Press eBooks · doi:10.1007/978-1-60761-178-3_11 · Cited by 2

The p53-Mdm2 Loop: A Critical Juncture of Stress Response

Levav-Cohen, Y., Goldberg, Z., Alsheich-Bartok, O., Zuckerman, V., Haupt, S., & Haupt, Y. (2010) · Molecular biology intelligence unit · doi:10.1007/978-1-4419-8231-5_5 · Cited by 2

p53: Point Mutations, SNPs and Cancer

Fang, M., Simeonova, I., & Toledo, F. (2012) · InTech eBooks · doi:10.5772/33715 · Cited by 1

Lessons on p53 from Mouse Models

Jiang, D., & Attardi, L. D. (2010) · Molecular biology intelligence unit · doi:10.1007/978-1-4419-8231-5_2 · Cited by 1

Dissecting the non-canonical functions of p53 through novel target identification and p53 acetylation

Wang, S.-J. (2014) · doi:10.7916/d85b00m3

Novel Roles of Replication Protein A Phosphorylation in the Cellular Response to DNA Damage

Serrano, M. A. (2013) · Digital Commons - East Tennessee State University (East Tennessee State University)

A novel phosphatase modulating the DNA damage response and the tumor suppressor p53

Marinoglou, K. (2011) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3254

Rb Inactivation Leads to E2F1-mediated DNA Double Strand Break Accumulation: A Dissertation

Pickering, M. (2006) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/h6jf-nf65

Oxidative Stress‐Mediated Signaling Pathways by Environmental Stressors

Sone, H., & Akanuma, H. (2011) · Wiley eBooks · doi:10.1002/9781118148143.ch13

To reactivate or not to reactivate : Control of KSHV lytic replication is essential for apoptosis in response to p53 restoration

Sarek, G. (2010) · Työväentutkimus Vuosikirja

DISSECTING THE P53 PATHWAY BY MEANS OF SMALL MOLECULE- MEDIATED REACTIVATION AND COMPUTATIONAL BIOLOGY

Enge, M. (2009) · Figshare

p53 and DNA damage checkpoint responses in the human prostate

af Hällström, T. (2007)

Identification of TGFβ signaling, p53, and actin stress fibers as targets of LKB1 tumor suppressor activity

Vaahtomeri, K. (2011) · Työväentutkimus Vuosikirja

The role of p53 in normal development and teratogen-induced apoptosis and birth defects in mouse embryos

Hosako, H. (2009) · OakTrust (Texas A&M University Libraries)

The accumulation of mutant p53 in human cancer cells

Bug, M. (2011) · doi:10.53846/goediss-3307

Faculty Opinions recommendation of Puma is required for p53-induced depletion of adult stem cells.

Kumar, S. (2010) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.5159956.5097054

Supplementary Figure Legends from Evidence for the Direct Binding of Phosphorylated p53 to Sites of DNA Breaks In vivo

Rashid, S. T. A., Dellaire, G., Cuddihy, A. R., Jalali, F., Vaid, M., Coackley, C. L., Folkard, M., Xu, Y., Chen, B. P. C., Chen, D. J., et al. (2023) · doi:10.1158/0008-5472.22364979

Effects of moderate - intensity exercise training on cardiac angiogenic capacity and fibrosis in middle-aged and aged rats

Mekrungruangwong, T., Patumraj, S., & Viboolvorakul, S. (2019) · doi:10.58837/chula.the.2019.368

Effets des dommages de l'ADN et du stress oxydant sur la dégénérescence des structures neuroépithéliales de la cochlée lors de l'intoxication au cisplatine et au cours du vieillissement.

Menardo, J. (2013) · theses.fr (ABES) · doi:10.70675/fe49b958za282z4b0bzad83z4b6038debf00

N-terminal isoforms of the p53 tumour suppressor protein : effects on p53 transcriptional activity and expression in cutaneous melanoma

Hafsi, H. (2012) · theses.fr (ABES) · doi:10.70675/636eb035zeb70z452ez8b98z0fdc80a752bb

Rôle de E4F1 dans la régulation de l'homéostasie des cellules cancéreuses

Houlès, T. (2015) · theses.fr (ABES) · doi:10.70675/e8fee4b0z4774z4e2cz8af0z6ec05b379c25

Mdm2-p53 Signaling in Tissue Homeostasis and the DNA Damage Response: A Dissertation

Gannon, H. (2012) · eScholarship@UMassChan · doi:10.13028/sfjc-xh51

Defining the Roles of p300/CBP (CREB Binding Protein) and S5a in p53 Polyubiquitination, Degradation and DNA Damage Responses: A Dissertation

Shi, D. (2010) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/hfsb-j486

DNA damage recognition in the normal epithelium of human prostate and seminal vesicles

Jäämaa, S. (2011) · Työväentutkimus Vuosikirja

Functional role of p53 N-terminal phosphorylation in regulating the p53 response to DNA damage

Chao, C. (2006) · eScholarship (California Digital Library)

Phosphorylation of murine p53 at Ser-18 regulates the p53 responses to DNA damage

Chao, C., Saito, S., Anderson, C. W., Appella, E., & Xu, Y. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.220252297 · Cited by 168

Phosphorylation of Serine 18 Regulates Distinct p53 Functions in Mice

Sluss, H. K., Armata, H., Gallant, J., & Jones, S. N. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.3.976-984.2004 · Cited by 152

Ser18 and 23 phosphorylation is required for p53‐dependent apoptosis and tumor suppression

Chao, C., Herr, D., Chun, J., & Xu, Y. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601167 · Cited by 158

Regulation of p53 antiproliferative function by transactivation domain phosphorylation at threonine 18 and serine 20

Jabbur, J. R. (2001) · Digital Commons-TMC (Texas Medical Center)