PUMA, a Novel Proapoptotic Gene, Is Induced by p53

Mitochondria and Apoptosis

Green, D. R., & Reed, J. C. (1998) · Science · doi:10.1126/science.281.5381.1309 · Cited by 8,998 · see citing works

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 · see citing works

Death Receptors: Signaling and Modulation

Ashkenazi, A., & Dixit, V. M. (1998) · Science · doi:10.1126/science.281.5381.1305 · Cited by 5,866 · see citing works

Tumor suppressor p53 is a direct transcriptional activator of the human bax gene

Toshiyuki, M., & Reed, J. C. (1995) · Cell · doi:10.1016/0092-8674(95)90412-3 · Cited by 4,063 · see citing works

Mice Lacking p21CIP1/WAF1 undergo normal development, but are defective in G1 checkpoint control

Deng, C., Zhang, P., Wade Harper, J., Elledge, S. J., & Leder, P. (1995) · Cell · doi:10.1016/0092-8674(95)90039-x · Cited by 2,113 · see citing works

Noxa, a BH3-Only Member of the Bcl-2 Family and Candidate Mediator of p53-Induced Apoptosis

Oda, E., Ohki, R., Murasawa, H., Nemoto, J., Shibue, T., Yamashita, T., Tokino, T., Taniguchi, T., & Tanaka, †. N. (2000) · Science · doi:10.1126/science.288.5468.1053 · Cited by 2,112 · see citing works

Apoptosis in cancer

Lowe, S. W., & Lin, A. W. (2000) · Carcinogenesis · doi:10.1093/carcin/21.3.485 · Cited by 1,867 · see citing works

Structural features in eukaryotic mRNAs that modulate the initiation of translation.

Kozak, M. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54860-2 · Cited by 1,826 · see citing works

PUMA Induces the Rapid Apoptosis of Colorectal Cancer Cells

Yu, J., Zhang, L., Hwang, P. M., Kinzler, K. W., & Vogelstein, B. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00213-1 · Cited by 1,282 · see citing works

tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome cPreprint

Wei, M. C., Lindsten, T., Mootha, V. K., Weiler, S., Gross, A., Ashiya, M., Thompson, C. B., & Korsmeyer, S. J. (2000) · Genes & Development · doi:10.1101/gad.14.16.2060 · Cited by 1,265 · see citing works

Radiation-induced cell cycle arrest compromised by p21 deficiency

Brugarolas, J., Chandrasekaran, C., Gordon, J. I., Beach, D., Jacks, T., & Hannon, G. J. (1995) · Nature · doi:10.1038/377552a0 · Cited by 1,242 · cited 1× · see citing works

p21 is necessary for the p53-mediated G1 arrest in human cancer cells.

Waldman, T. A., Kinzler, K. W., & Vogelstein, B. (1995) · PubMed · Cited by 1,203 · see citing works

The alternative product from the human CDKN2A locus, p14ARF, participates in a regulatory feedback loop with p53 and MDM2

Stott, F. J., Bates, S., James, M. C., McConnell, B. B., Starborg, M., Brookes, S., Palmero, I., Ryan, K. M., Hara, E., Vousden, K. H., et al. (1998) · The EMBO Journal · doi:10.1093/emboj/17.17.5001 · Cited by 1,165 · see citing works

p53AIP1, a Potential Mediator of p53-Dependent Apoptosis, and Its Regulation by Ser-46-Phosphorylated p53

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 · see citing works

KILLER/DR5 is a DNA damage–inducible p53–regulated death receptor gene

Wu, G. S., Burns, T. F., McDonald, E. R., Jiang, W., Meng, R., Krantz, I. D., Kao, G., Gan, D.-D., Zhou, J.-Y., Muschel, R. J., et al. (1997) · Nature Genetics · doi:10.1038/ng1097-141 · Cited by 1,081 · see citing works

Bcl-2 family proteins

Reed, J. C. (1998) · Oncogene · doi:10.1038/sj.onc.1202591 · Cited by 1,057 · 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 910 · see citing works

Death Signal-induced Localization of p53 Protein to Mitochondria

Marchenko, N. D., Zaika, A. I., & Moll, U. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.21.16202 · Cited by 902 · see citing works

Database of p53 gene somatic mutations in human tumors and cell lines.

Hollstein, M. C., Rice, K., Greenblatt, M. S., Soussi, T., Fuchs, R., Sørlie, T., Hovig, E. J., Smith‐Sørensen, B., Montesano, R., & Harris, C. C. (1994) · Europe PMC (PubMed Central) · Cited by 860 · see citing works

DNA Strand Breaks: the DNA Template Alterations That Trigger p53-Dependent DNA Damage Response Pathways

Nelson, W. G., & Kastan, M. B. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.3.1815 · Cited by 850 · see citing works

Regulation ofp53downstream genes

El‐Deiry, W. S. (1998) · Seminars in Cancer Biology · doi:10.1006/scbi.1998.0097 · Cited by 797 · see citing works

p53

Vousden, K. H. (2000) · Cell · doi:10.1016/s0092-8674(00)00171-9 · Cited by 785 · see citing works

Cell Surface Trafficking of Fas: A Rapid Mechanism of p53-Mediated Apoptosis

Bennett, M. R., Macdonald, K., Chan, S., Luzio, J. P., Simari, R. D., & Weissberg, P. L. (1998) · Science · doi:10.1126/science.282.5387.290 · Cited by 755 · see citing works

Wild-Type Human p53 and a Temperature-Sensitive Mutant Induce Fas/APO-1 Expression

Owen‐Schaub, L. B., Zhang, W. K., Cusack, J. C., Angelo, L. S., Santee, S. M., Fujiwara, T., Roth, J. A., Deisseroth, A., Zhang, W., Kruzel, E., et al. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.6.3032 · Cited by 731 · see citing works

Apaf-1 and Caspase-9 in p53-Dependent Apoptosis and Tumor Inhibition

Soengas, M. S., Alarcon, R. M., Yoshida, H., J., A., Giaccia, Hakem, R., Mak, T. W., & Lowe, S. W. (1999) · Science · doi:10.1126/science.284.5411.156 · Cited by 660 · see citing works

Bcl-2-family proteins: the role of the BH3 domain in apoptosis

Kelekar, A., & Thompson, C. B. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(98)01321-x · Cited by 654 · see citing works

Human papillomavirus 16 E6 expression disrupts the p53-mediated cellular response to DNA damage.

Kessis, T. D., Slebos, R. J. C., Nelson, W. G., Kastan, M. B., Plunkett, B., Han, S. M., Lorincz, A. T., Hedrick, L., & Cho, K. R. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.9.3988 · Cited by 525 · see citing works

Stress Signals Utilize Multiple Pathways To Stabilize p53

Ashcroft, M. A., Taya, Y., & Vousden, K. H. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.9.3224-3233.2000 · Cited by 356 · see citing works

Pidd, a new death-domain–containing protein, is induced by p53 and promotes apoptosis

Lin, Y., Ma, W., & Benchimol, S. (2000) · Nature Genetics · doi:10.1038/79102 · Cited by 353 · see citing works

Mechanisms of p53-mediated apoptosis

Bates, S., & Vousden, K. H. (1999) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050267 · Cited by 304 · see citing works

Specific loss of apoptotic but not cell‐cycle arrest function in a human tumor derived p53 mutant.

Rowan, S., Ludwig, R., Haupt, Y., Bates, S., Lü, X., Oren, M., & Vousden, K. H. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00418.x · Cited by 300 · see citing works

The p53-deficient mouse: a model for basic and applied cancer studies

Donehower, L. A. (1996) · Seminars in Cancer Biology · doi:10.1006/scbi.1996.0035 · Cited by 268 · see citing works

A ribonucleotide reductase gene is a transcriptional target of p53 and p73

Nakano, K., Bálint, É., Ashcroft, M. A., & Vousden, K. H. (2000) · Oncogene · doi:10.1038/sj.onc.1203774 · Cited by 231 · see citing works

TNF-α Signals Apoptosis through a Bid-Dependent Conformational Change in Bax that Is Inhibited by E1B 19K

Perez, D., & White, E. (2000) · Molecular Cell · doi:10.1016/s1097-2765(05)00013-4 · Cited by 195 · see citing works

Regulation and activation of p53 and its family members

Lohrum, M. A. E., & Vousden, K. H. (1999) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400625 · Cited by 90 · see citing works

Human Osteogenesis Involves Differentiation-Dependent Increases in the Morphogenically Active 3′ Alternative Splicing Variant of Acetylcholinesterase

Grisaru, D., Lev-Lehman, E., Shapira, M., et al. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.1.788 · Cited by 72 · see citing works

Nitric oxide-mediated apoptosis in human breast cancer cells requires changes in mitochondrial functions and is independent of CD95 (APO-1/Fas).

Umansky, V., Ushmorov, A., Ratter, F., et al. (2000) · International Journal of Oncology · doi:10.3892/ijo.16.1.109 · Cited by 41 · see citing works

Activation of p53 DNA binding activity by point mutation

Marston, N. J., Ludwig, R. L., & Vousden, K. H. (1998) · Oncogene · doi:10.1038/sj.onc.1201856 · Cited by 13 · see citing works

Cellular senescence and cancer

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

Cell Death

Danial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651 · see citing works

The Bcl2 family: regulators of the cellular life-or-death switch

Cory, S., & Adams, J. M. (2002) · Nature Reviews Cancer · doi:10.1038/nrc883 · Cited by 4,032 · see citing works

Reactive oxygen species, cellular redox systems, and apoptosis

Circu, M. L., & Aw, T. Y. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.12.022 · Cited by 3,340 · see citing works

Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy

Czabotar, P. E., Lessene, G., Strasser, A., & Adams, J. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3722 · Cited by 3,219 · 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

How does p53 induce apoptosis and how does this relate to p53-mediated tumour suppression

Aubrey, B. J., Kelly, G. L., Janic, A., Herold, M. J., & Strasser, A. (2018) · Cell Death & Differentiation · doi:10.1038/cdd.2017.169 · Cited by 1,395 · see citing works

DRAM, a p53-Induced Modulator of Autophagy, Is Critical for Apoptosis

Crighton, D., Wilkinson, S., O'Prey, J., Syed, N., Smith, P., Harrison, P. R., Gasco, M., Garrone, O., Crook, T., & Ryan, K. M. (2006) · Cell · doi:10.1016/j.cell.2006.05.034 · Cited by 1,380 · see citing works

p53- 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 · see citing works

Anoikis molecular pathways and its role in cancer progression

Paoli, P., Giannoni, E., & Chiarugi, P. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.06.026 · Cited by 1,160 · see citing works

Apoptosis - the p53 network

Haupt, S., Berger, M., Goldberg, Z., & Haupt, Y. (2003) · Journal of Cell Science · doi:10.1242/jcs.00739 · Cited by 1,136 · see citing works

Census and evaluation of p53 target genes

Fischer, M. (2017) · Oncogene · doi:10.1038/onc.2016.502 · Cited by 971 · see citing works

The role of BCL-2 family proteins in regulating apoptosis and cancer therapy

Qian, S., Wei, Z., Yang, W., Huang, J., Yang, Y., & Wang, J. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.985363 · Cited by 1,011 · see citing works

Targeting p53 pathways: mechanisms, structures, and advances in therapy

Wang, H., Guo, M., Wei, H., & Chen, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01347-1 · Cited by 1,016 · see citing works

Hierarchical regulation of mitochondrion-dependent apoptosis by BCL-2 subfamilies

Kim, H., Rafiuddin-Shah, M., Tu, H.-C., Jeffers, J. R., Zambetti, G. P., Hsieh, J. J.-D., & Cheng, E. H.-Y. (2006) · Nature Cell Biology · doi:10.1038/ncb1499 · Cited by 874 · see citing works

Thirty years of BCL-2: translating cell death discoveries into novel cancer therapies

Delbridge, A. R. D., Grabow, S., Strasser, A., & Vaux, D. L. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2015.17 · Cited by 752 · see citing works

Stressing the role of FoxO proteins in lifespan and disease

van der Horst, A., & Burgering, B. M. T. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2190 · Cited by 759 · see citing works

Mechanisms of Action of Bcl-2 Family Proteins

Shamas-Din, A., Kale, J., Leber, B., & Andrews, D. W. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008714 · Cited by 705 · see citing works

Bmf: A Proapoptotic BH3-Only Protein Regulated by Interaction with the Myosin V Actin Motor Complex, Activated by Anoikis

Puthalakath, H., Villunger, A., O'Reilly, L. A., Beaumont, J. G., Coultas, L., Cheney, R. E., Huang, D. C. S., & Strasser, A. (2001) · Science · doi:10.1126/science.1062257 · Cited by 656 · see citing works

Mitochondrial outer membrane permeabilization during apoptosis: the innocent bystander scenario

Chipuk, J. E., Bouchier-Hayes, L., & Green, D. R. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401963 · Cited by 631 · see citing works

The BCL2 Family: Key Mediators of the Apoptotic Response to Targeted Anticancer Therapeutics

Hata, A. N., Engelman, J. A., & Faber, A. C. (2015) · Cancer Discovery · doi:10.1158/2159-8290.cd-15-0011 · Cited by 619 · 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

p53 and E2f: partners in life and death

Polager, S., & Ginsberg, D. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2718 · Cited by 498 · see citing works

Small-Molecule Inhibitors of the MDM2–p53 Protein–Protein Interaction (MDM2 Inhibitors) in Clinical Trials for Cancer Treatment

Zhao, Y., Aguilar, A., Bernard, D., & Wang, S. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm501092z · Cited by 462 · see citing works

BID regulation by p53 contributes to chemosensitivity

Sax, J. K., Fei, P., Murphy, M. E., Bernhard, E., Korsmeyer, S. J., & El-Deiry, W. S. (2002) · Nature Cell Biology · doi:10.1038/ncb866 · Cited by 420 · see citing works

DNA damage responses and p53 in the aging process

Ou, H.-L., & Schumacher, B. (2018) · Blood · doi:10.1182/blood-2017-07-746396 · Cited by 377 · see citing works

p73 Induces apoptosis via PUMA transactivation and Bax mitochondrial translocation

Melino, G., Bernassola, F., Ranalli, M., Yee, K., Zong, W. X., Corazzari, M., Knight, R. A., Green, D. R., Thompson, C., & Vousden, K. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307469200 · Cited by 368 · see citing works

The intrinsic apoptosis pathway mediates the pro-longevity response to mitochondrial ROS in C. elegans

Yee, C., Yang, W., & Hekimi, S. (2014) · Cell · doi:10.1016/j.cell.2014.02.055 · Cited by 356 · see citing works

Mitochondria—Judges and Executioners of Cell Death Sentences

Bhola, P. D., & Letai, A. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.019 · Cited by 326 · see citing works

Influence of Induced Reactive Oxygen Species in p53-Mediated Cell Fate Decisions

Macip, S., Igarashi, M., Berggren, P., Yu, J., Lee, S. W., & Aaronson, S. A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.23.8576-8585.2003 · Cited by 331 · 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

Cell-to-cell variation in p53 dynamics leads to fractional killing.

Paek, A. L., Liu, J. C., Loewer, A., Forrester, W. C., & Lahav, G. (2016) · Cell · doi:10.1016/j.cell.2016.03.025 · Cited by 292 · see citing works

NEMO and RIP1 Control Cell Fate in Response to Extensive DNA Damage via TNF-α Feedforward Signaling

Biton, S., & Ashkenazi, A. (2011) · Cell · doi:10.1016/j.cell.2011.02.023 · Cited by 262 · see citing works

p53 in recombination and repair

Gatz, S. A., & Wiesmüller, L. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401903 · Cited by 242 · see citing works

The mitochondrial uncoupling protein-2 promotes chemoresistance in cancer cells

Derdak, Z., Mark, N. M., Beldi, G., Robson, S. C., Wands, J. R., & Baffy, G. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0053 · Cited by 229 · see citing works

Oncogenic Role of <i>miR-483-3p</i> at the <i>IGF2/483</i> Locus

Veronese, A., Lupini, L., Consiglio, J., Visone, R., Ferracin, M., Fornari, F., Zanesi, N., Alder, H., D'Elia, G., Gramantieri, L., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-4456 · Cited by 210 · see citing works

The ferredoxin reductase gene is regulated by the p53 family and sensitizes cells to oxidative stress-induced apoptosis

Liu, G., & Chen, X. (2002) · Oncogene · doi:10.1038/sj.onc.1205862 · Cited by 207 · see citing works

Intact p53-Dependent Responses in miR-34–Deficient Mice

Concepcion, C. P., Han, Y.-C., Mu, P., Bonetti, C., Yao, E., D'Andrea, A., Vidigal, J. A., Maughan, W. P., Ogrodowski, P., & Ventura, A. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002797 · Cited by 197 · see citing works

Regulation of AIF expression by p53

Stambolsky, P., Weisz, L., Shats, I., Klein, Y., Goldfinger, N., Oren, M., & Rotter, V (2006) · Cell Death &amp; Differentiation · doi:10.1038/sj.cdd.4401965 · Cited by 194 · see citing works

The Isoforms of the p53 Protein

Khoury, M. P., & Bourdon, J.-C. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000927 · Cited by 191 · see citing works

Deconstructing p53 transcriptional networks in tumor suppression

Bieging, K. T., & Attardi, L. D. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.10.006 · Cited by 194 · see citing works

APAF1 is a key transcriptional target for p53 in the regulation of neuronal cell death

Fortin, A., Cregan, S. P., MacLaurin, J. G., Kushwaha, N., Hickman, E. S., Thompson, C. S., Hakim, A., Albert, P. R., Cecconi, F., Helin, K., et al. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200105137 · Cited by 194 · see citing works

The metabolic life and times of a T‐cell

Michalek, R. D., & Rathmell, J. C. (2010) · Immunological Reviews · doi:10.1111/j.1600-065x.2010.00911.x · Cited by 186 · see citing works

ERK1/2‐dependent phosphorylation of BimEL promotes its rapid dissociation from Mcl‐1 and Bcl‐xL

Ewings, K. E., Hadfield‐Moorhouse, K., Wiggins, C. M., Wickenden, J. A., Balmanno, K., Gilley, R., Degenhardt, K., White, E., & Cook, S. J. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601723 · Cited by 176 · see citing works

MicroRNAs Enable mRNA Therapeutics to Selectively Program Cancer Cells to Self-Destruct

Jain, R., Frederick, J. P., Huang, E. Y., Burke, K. E., Mauger, D. M., Andrianova, E. A., Farlow, S. J., Siddiqui, S., Pimentel, J., Cheung-Ong, K., et al. (2018) · Nucleic Acid Therapeutics · doi:10.1089/nat.2018.0734 · Cited by 164 · see citing works

Genome Stability Requires p53

Eischen, C. M. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026096 · Cited by 161 · see citing works

The transcription factor p53: Not a repressor, solely an activator.

Fischer, M., Steiner, L., & Engeland, K. (2014) · Cell Cycle · doi:10.4161/15384101.2014.949083 · Cited by 153 · see citing works

The PP2A-Associated Protein α4 Is an Essential Inhibitor of Apoptosis

Kong, M., Fox, C. J., Mu, J., Solt, L., Xu, A., Cinalli, R. M., Birnbaum, M. J., Lindsten, T., & Thompson, C. B. (2004) · Science · doi:10.1126/science.1100537 · Cited by 149 · see citing works

Death Protein 5 and p53-Upregulated Modulator of Apoptosis Mediate the Endoplasmic Reticulum Stress–Mitochondrial Dialog Triggering Lipotoxic Rodent and Human β-Cell Apoptosis

Cunha, D. A., Igoillo-Esteve, M., Gurzov, E. N., Germano, C. M., Naamane, N., Marhfour, I., Fukaya, M., Vanderwinden, J.-M., Gysemans, C., Mathieu, C., et al. (2012) · Diabetes · doi:10.2337/db12-0123 · Cited by 130 · see citing works

The Biological Functions and Signaling Mechanisms of the p75 Neurotrophin Receptor

Kraemer, B. R., Yoon, S. O., & Carter, B. D. (2014) · Handbook of Experimental Pharmacology · doi:10.1007/978-3-642-45106-5_6 · Cited by 125 · see citing works

The DNA Damage Response in Neurons: Die by Apoptosis or Survive in a Senescence-Like State?

Fielder, E., von Zglinicki, T., & Jurk, D. (2017) · Journal of Alzheimer's Disease · doi:10.3233/jad-161221 · Cited by 126 · 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

USP7 Is a Master Regulator of Genome Stability

Valles, G. J., Bezsonova, I., Woodgate, R., & Ashton, N. W. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00717 · Cited by 114 · see citing works

Retinoic Acid Increases the Expression of p53 and Proapoptotic Caspases and Sensitizes Keratinocytes to Apoptosis

Mrass, P., Rendl, M., Mildner, M., Gruber, F., Lengauer, B., Ballaun, C., Eckhart, L., & Tschachler, E. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-1129 · Cited by 112 · see citing works

Regulation of the human AP-endonuclease (APE1/Ref-1) expression by the tumor suppressor p53 in response to DNA damage

Zaky, A., Busso, C., Izumi, T., Chattopadhyay, R., Bassiouny, A., Mitra, S., & Bhakat, K. K. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkm1173 · Cited by 111 · see citing works

Systems analysis of BCL2 protein family interactions establishes a model to predict responses to chemotherapy

Lindner, A. U., Concannon, C. G., Boukes, G. J., Cannon, M. D., Llambi, F., Ryan, D., Boland, K., Kehoe, J., McNamara, D. A., Murray, F., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-2269 · Cited by 105 · see citing works

DNA Polymerase η, the Product of the Xeroderma Pigmentosum Variant Gene and a Target of p53, Modulates the DNA Damage Checkpoint and p53 Activation

Liu, G., & Chen, X. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.4.1398-1413.2006 · Cited by 104 · see citing works

Noncanonical DNA Motifs as Transactivation Targets by Wild Type and Mutant p53

Jordan, J. J., Menendez, D., Inga, A., Nourredine, M., Bell, D., & Resnick, M. A. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000104 · Cited by 103 · see citing works

Apoptosis induced by proteasome inhibition in cancer cells: predominant role of the p53/PUMA pathway

Concannon, C. G., Koehler, B. F., Reimertz, C., Murphy, B. M., Bonner, C., Thurow, N., Ward, M. W., Villunger, A., Strasser, A., Kögel, D., et al. (2007) · Oncogene · doi:10.1038/sj.onc.1209974 · Cited by 95 · see citing works

Mutant p53 drives cancer chemotherapy resistance due to loss of function on activating transcription of PUMA

Huang, Y., Liu, N., Liu, J., Liu, Y., Zhang, C., Long, S., Luo, G., Zhang, L., & Zhang, Y. (2019) · Cell Cycle · doi:10.1080/15384101.2019.1688951 · Cited by 94 · see citing works

Crossing paths: interactions between the cell death machinery and growth factor survival signals

Brumatti, G., Salmanidis, M., & Ekert, P. G. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0288-8 · Cited by 85 · see citing works

Deubiquitination of Tip60 by USP7 determines the activity of the p53-dependent apoptotic pathway.

Dar, A., Shibata, E., & Dutta, A. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00358-13 · Cited by 83 · see citing works

Spontaneous Tumorigenesis in Mice Overexpressing the p53-Negative Regulator Mdm4

Xiong, S., Pant, V., Suh, Y.-A., Van Pelt, C. S., Wang, Y., Valentin-Vega, Y. A., Post, S. M., & Lozano, G. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-1457 · Cited by 82 · see citing works

Acetylation-dependent regulation of MDM2 E3 ligase activity dictates its oncogenic function.

Nihira, N. T., Ogura, K., Shimizu, K., North, B. J., Zhang, J., Gao, D., Inuzuka, H., & Wei, W. (2017) · Science Signaling · doi:10.1126/scisignal.aai8026 · Cited by 82 · see citing works

Regulation of Metabolic Activity by p53

Flöter, J., Kaymak, I., & Schulze, A. (2017) · Metabolites · doi:10.3390/metabo7020021 · Cited by 81 · see citing works

A positive feedback mechanism in the transcriptional activation of Apaf-1 by p53 and the coactivator Zac-1

Rozenfeld-Granot, G., Krishnamurthy, J., Kannan, K., Toren, A., Amariglio, N., Givol, D., & Rechavi, G. (2002) · Oncogene · doi:10.1038/sj.onc.1205218 · Cited by 72 · see citing works

DNA damage-induced cellular senescence is sufficient to suppress tumorigenesis: a mouse model

Van Nguyen, T., Puebla-Osorio, N., Pang, H., Dujka, M. E., & Zhu, C. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20062453 · Cited by 72 · see citing works

Redox-Dependent Translocation of p53 to Mitochondria or Nucleus in Human Melanocytes after UVA- and UVB-Induced Apoptosis

Wäster, P. K., & Öllinger, K. M. (2009) · Journal of Investigative Dermatology · doi:10.1038/jid.2008.421 · Cited by 72 · see citing works

DDB2 (damaged-DNA binding protein 2) in nucleotide excision repair and DNA damage response

Stoyanova, T., Roy, N., Kopanja, D., Raychaudhuri, P., & Bagchi, S. (2009) · Cell Cycle · doi:10.4161/cc.8.24.10109 · Cited by 70 · see citing works

De novo N-palmitoylsphingosine synthesis is the major biochemical mechanism of ceramide accumulation following p53 up-regulation

Panjarian, S., Kozhaya, L., Arayssi, S., Yehia, M., Bielawski, J., Bielawska, A., Usta, J., Hannun, Y. A., Obeid, L. M., & Dbaibo, G. S. (2008) · Prostaglandins &amp; Other Lipid Mediators · doi:10.1016/j.prostaglandins.2008.02.004 · Cited by 69 · see citing works

Brn-3a Transcription Factor Blocks p53-mediated Activation of Proapoptotic Target Genes Noxa and Bax in Vitro and in Vivo to Determine Cell Fate

Hudson, C. D., Morris, P. J., Latchman, D. S., & Budhram-Mahadeo, V. S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m408679200 · Cited by 68 · see citing works

ATM and MET kinases are synthetic lethal with nongenotoxic activation of p53

Sullivan, K. D., Padilla-Just, N., Henry, R. E., Porter, C. C., Kim, J., Tentler, J. J., Eckhardt, S. G., Tan, A. C., DeGregori, J., & Espinosa, J. M. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.965 · Cited by 67 · see citing works

Bcl-2 family in inter-organelle modulation of calcium signaling; roles in bioenergetics and cell survival

Lewis, A., Hayashi, T., Su, T.-P., & Betenbaugh, M. J. (2014) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-013-9527-7 · Cited by 66 · see citing works

Identification and Characterization of the Cytoplasmic Protein TRAF4 as a p53-regulated Proapoptotic Gene

Sax, J. K., & El-Deiry, W. S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303191200 · Cited by 60 · see citing works

Genotoxic stress/p53-induced DNAJB9 inhibits the pro-apoptotic function of p53

Lee, H. J., Kim, J. M., Kim, K. H., Heo, J. I., Kwak, S. J., & Han, J. A. (2015) · Cell Death &amp; Differentiation · doi:10.1038/cdd.2014.116 · Cited by 60 · see citing works

A mechanistic pan-cancer pathway model informed by multi-omics data interprets stochastic cell fate responses to drugs and mitogens

Bouhaddou, M., Barrette, A. M., Stern, A. D., Koch, R. J., DiStefano, M. S., Riesel, E. A., Santos, L. C., Tan, A. L., Mertz, A. E., & Birtwistle, M. R. (2018) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1005985 · Cited by 58 · see citing works

Loss of hepatocyte cell division leads to liver inflammation and fibrosis

Dewhurst, M. R., Ow, J. R., Zafer, G., van Hul, N. K. M., Wollmann, H., Bisteau, X., Brough, D., Choi, H., & Kaldis, P. (2020) · PLOS Genetics · doi:10.1371/journal.pgen.1009084 · Cited by 42 · see citing works

p53 directly regulates the glycosidase FUCA1 to promote chemotherapy-induced cell death

Baudot, A. D., Crighton, D., O'Prey, J., Somers, J., Sierra Gonzalez, P., & Ryan, K. M. (2016) · Cell Cycle · doi:10.1080/15384101.2016.1191714 · Cited by 31 · see citing works

Phosphorylation alters Bim‐mediated Mcl‐1 stabilization and priming

Conage‐Pough, J. E., & Boise, L. H. (2018) · The FEBS Journal · doi:10.1111/febs.14505 · Cited by 32 · 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

PUMA gene in cancer treatment

Luan, Q.-C., & Chen, Y. (2011) · Guoji zhongliuxue zazhi · doi:10.3760/cma.j.issn.1673-422x.2011.11.001

Pro-apoptotic Gene PUMA and Tumor Therapy

Wang, Y. (2012) · Medical Recapitulate

Effect and mechanism of PUMA on the apoptosis of mouse liver cell in vitro

Sheng, Y. (2009) · Di-Si Junyi Daxue xuebao

Promoting Apoptotic Effect of PUMA and Tumor Therapy

Yon, D. (2008) · Medical Recapitulate

PUMA Induces the Rapid Apoptosis of Colorectal Cancer Cells

Yu, J., Zhang, L., Hwang, P. M., Kinzler, K. W., & Vogelstein, B. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00213-1 · Cited by 1,282 · see citing works