Cited by 124Cancer-related Molecular PathwaysCell death mechanisms and regulationHeat shock proteins research

The DOI matches its Crossref record; 48 of the 49 references it cites were found in a registry or an index.

Defective apoptosis and B-cell lymphomas in mice with p53 point mutation at Ser 23

Open access

MacPherson, David, Kim, Jungho, Kim, Teresa, Rhee, Byung Kirl, van Oostrom, Conny ThM, DiTullio, Richard A, Venere, Monica, Halazonetis, Thanos D, Bronson, Roderick, de Vries, Annemieke, Fleming, Mark, Jacks, Tyler·2004·The EMBO Journal

DOI 10.1038/sj.emboj.7600363PMC PMC517606

Open this paper in CoChat — free account Open PDF

Abstract

Phosphorylation of the p53 tumor suppressor at Ser20 (murine Ser23) has been proposed to be critical for disrupting p53 interaction with its negative regulator, MDM2, and allowing p53 stabilization. To determine the importance of Ser23 for the function of p53 in vivo, we generated a mouse in which the endogenous p53 locus was targeted to replace Ser23 with alanine. We show that, in mouse embryonic fibroblasts generated from Ser23 mutant mice, Ser23 mutation did not dramatically reduce IR-induced p53 protein stabilization or p53-dependent cell cycle arrest. However, in Ser23 mutant thymocytes and in the developing cerebellum, p53 stabilization following IR was decreased and resistance to apoptosis was observed. Homozygous Ser23 mutant animals had a reduced lifespan, but did not develop thymic lymphomas or sarcomas that are characteristic of p53-/- mice. Instead, Ser23 mutant animals died between 1 and 2 years with tumors that were most commonly of B-cell lineage. These data support an important role for Ser20/23 phosphorylation in p53 stabilization, apoptosis and tumor suppression.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1038/sj.emboj.7600363

Cites

48 of 48 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

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
Mice deficient for p53 are developmentally normal but susceptible to spontaneous tumours
Donehower, L. A., Harvey, M., Slagle, B. L., McArthur, M. J., Montgomery, C. A., Butel, J. S., & Bradley, A. (1992) · Nature · doi:10.1038/356215a0 · Cited by 4,649
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 · cited 1×
“The product of the p53 target gene MDM2 is involved in p53 ubiquitination and destruction via the proteasome, keeping p53 at low levels in unstressed cell (Haupt et al, 1997; Kubbutat et al, 1997).”
Background
A mammalian cell cycle checkpoint pathway utilizing p53 and GADD45 is defective in ataxia-telangiectasia
Kastan, M. B., Zhan, Q., El-Deiry, W. S., Carrier, F., Jacks, T., Walsh, W. V., Plunkett, B. S., Vogelstein, B., & Fornace, A. J. (1992) · Cell · doi:10.1016/0092-8674(92)90593-2 · Cited by 3,047
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
Self-citation
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
Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206
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
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

Show all 49 references

Sorted by citations

Modes of p53 regulation.
Kruse, J.-P., & Gu, W. (2009) · Cell · doi:10.1016/j.cell.2009.04.050 · Cited by 1,610
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
Tumour suppression by p53: a role for the DNA damage response?
Meek, D. W. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2716 · Cited by 625
Posttranslational Modification of p53: Cooperative Integrators of FunctionPreprint
Meek, D. W., & Anderson, C. W. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000950 · Cited by 510
The p53 orchestra: Mdm2 and Mdmx set the tone
Wade, M., Wang, Y. V., & Wahl, G. M. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.01.009 · Cited by 450
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
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
Regulation of the p53 response and its relationship to cancer
Meek, D. W. (2015) · Biochemical Journal · doi:10.1042/bj20150517 · Cited by 311
Acetylation of p53 at Lysine 373/382 by the Histone Deacetylase Inhibitor Depsipeptide Induces Expression of p21Waf1/Cip1
Zhao, Y., Lu, S., Wu, L., Chai, G., Wang, H., Chen, Y., Sun, J. T., Yu, Y., Zhou, W., Zheng, Q., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.7.2782-2790.2006 · Cited by 283
Mechanism of p53 stabilization by ATM after DNA damage
Cheng, Q., & Chen, J. (2010) · Cell Cycle · doi:10.4161/cc.9.3.10556 · Cited by 264
Taking the time to make important decisions: The checkpoint effector kinases Chk1 and Chk2 and the DNA damage response
Stracker, T. H., Usui, T., & Petrini, J. H. J. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.04.012 · Cited by 262
p53 alterations in human cancer: more questions than answers
Soussi, T. (2007) · Oncogene · doi:10.1038/sj.onc.1210280 · Cited by 236
How important are post-translational modifications in p53 for selectivity in target-gene transcription and tumour suppression?
Olsson, A., Manzl, C., Strasser, A., & Villunger, A. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402196 · Cited by 204
20 years studying p53 functions in genetically engineered mice
Donehower, L. A., & Lozano, G. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2731 · Cited by 196
p53-dependent Induction of PVT1 and miR-1204
Barsotti, A. M., Beckerman, R., Laptenko, O., Huppi, K. E., Caplen, N. J., & Prives, C. L. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.322875 · Cited by 189
Dysfunction of the TP53 tumor suppressor gene in lymphoid malignancies
Xu-Monette, Z. Y., Medeiros, L. J., Li, Y., Orlowski, R. Z., Andreeff, M., Bueso-Ramos, C., Greiner, T. C., McDonnell, T. J., & Young, K. H. (2012) · Blood · doi:10.1182/blood-2011-11-366062 · Cited by 190
The role of ubiquitin modification in the regulation of p53
Hock, A. K., & Vousden, K. H. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.05.022 · Cited by 168
ATM activates p53 by regulating MDM2 oligomerization and E3 processivity
Cheng, Q., Chen, L., Li, Z., Lane, W. S., & Chen, J. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.294 · Cited by 165
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
The regulation of p53 by phosphorylation: a model for how distinct signals integrate into the p53 pathway
MacLaine, N. J., & Hupp, T. R. (2009) · Aging · doi:10.18632/aging.100047 · Cited by 134
The p53 pathway in hematopoiesis: lessons from mouse models, implications for humans
Pant, V., Quintás-Cardama, A., & Lozano, G. (2012) · Blood · doi:10.1182/blood-2012-05-356014 · Cited by 129
New insights into p53 activation
Brooks, C. L., & Gu, W. (2010) · Cell Research · doi:10.1038/cr.2010.53 · Cited by 102
p53 N-terminal phosphorylation: a defining layer of complex regulation
Jenkins, L. M. M., Durell, S. R., Mazur, S. J., & Appella, E. (2012) · Carcinogenesis · doi:10.1093/carcin/bgs145 · Cited by 122
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. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-0729 · Cited by 107
p53 target gene AEN is a nuclear exonuclease required for p53-dependent apoptosis
Kawase, T., Ichikawa, H., Ohta, T., Nozaki, N., Tashiro, F., Ohki, R., & Taya, Y. (2008) · Oncogene · doi:10.1038/onc.2008.32 · Cited by 105
Mouse Models of p53 FunctionsPreprint
Lozano, G. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a001115 · Cited by 97
Monocytic Leukemia Zinc Finger (MOZ) Interacts with p53 to Induce p21 Expression and Cell-cycle Arrest
Rokudai, S., Aikawa, Y., Tagata, Y., Tsuchida, N., Taya, Y., & Kitabayashi, I. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805101200 · Cited by 95
In vivo analysis of p53 tumor suppressor function using genetically engineered mouse models
Brož, D. K., & Attardi, L. D. (2010) · Carcinogenesis · doi:10.1093/carcin/bgp331 · Cited by 92
A New Twist in the Feedback Loop: Stress-Activated MDM2 Destabilization is Required for p53 Activation
Stommel, J. M., & Wahl, G. M. (2005) · Cell Cycle · doi:10.4161/cc.4.3.1522 · Cited by 90
Regulation of Mutant p53 Protein Expression
Vijayakumaran, R., Tan, K. H., Miranda, P. J., Haupt, S., & Haupt, Y. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00284 · Cited by 87
What have animal models taught us about the p53 pathway?
Lozano, G., & Zambetti, G. P. (2005) · The Journal of Pathology · doi:10.1002/path.1704 · Cited by 78
Mutant TP53 Posttranslational Modifications: Challenges and Opportunities
Nguyen, T., Menéndez, D., Resnick, M. A., & Anderson, C. W. (2014) · Human Mutation · doi:10.1002/humu.22506 · Cited by 77
Cell and tissue responses to genotoxic stress
Coates, P. J., Lorimore, S. A., & Wright, E. G. (2005) · The Journal of Pathology · doi:10.1002/path.1701 · Cited by 77
Mitochondrially Targeted p53 Has Tumor Suppressor Activities In vivo
Talos, F., Petrenko, O., Mena, P., & Moll, U. M. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1084 · Cited by 74
Regulation of MDM2 E3 Ligase Activity by Phosphorylation after DNA Damage
Cheng, Q., Cross, B. L., Li, B., Chen, L., Li, Z., & Chen, J. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05553-11 · Cited by 78
Hyperproliferation, cancer, and inflammation in mice expressing a Δ133p53-like isoform
Slatter, T. L., Hung, N. A., Campbell, H. G., Rubio, C., Mehta, R., Renshaw, P., Williams, G., Wilson, M., Engelmann, A., Jeffs, A. R., et al. (2011) · Blood · doi:10.1182/blood-2010-11-321851 · Cited by 76
Inhibition of p53 DNA Binding Function by the MDM2 Protein Acidic Domain
Cross, B. L., Chen, L., Cheng, Q., Li, B., Yuan, Z.-M., & Chen, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.228981 · Cited by 72
Regulation of the Mdm2-p53 signaling axis in the DNA damage response and tumorigenesis
Carr, M. I., & Jones, S. N. (2016) · Translational Cancer Research · doi:10.21037/tcr.2016.11.75 · Cited by 71
The Ataxia Telangiectasia–Mutated Target Site Ser18 Is Required for p53-Mediated Tumor Suppression
Armata, H. L., Garlick, D. S., & Sluss, H. K. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-1610 · Cited by 69
Chk2 Suppresses the Oncogenic Potential of DNA Replication-Associated DNA Damage
Stracker, T. H., Couto, S. S., Cordon‐Cardo, C., Matos, T., & Petrini, J. H. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.04.028 · Cited by 64
p53–RNA interactions: New clues in an old mystery
Riley, K. J.-L., & Maher, L. J. (2007) · RNA · doi:10.1261/rna.673407 · Cited by 68
Mice Expressing a Mammary Gland–Specific R270H Mutation in the p53 Tumor Suppressor Gene Mimic Human Breast Cancer Development
Wijnhoven, S., Zwart, E., Speksnijder, E. N., Beems, R. B., Olive, K. P., Tuveson, D. A., Jonkers, J., Schaap, M. M., van den Berg, J., Jacks, T., et al. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1650 · Cited by 64
Mouse Mutants Reveal that Putative Protein Interaction Sites in the p53 Proline-Rich Domain Are Dispensable for Tumor Suppression
Toledo, F., Lee, C. J., Krummel, K. A., Rodewald, L.-W., Liu, C.-W., & Wahl, G. M. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00999-06 · Cited by 66
miRNA-126 Orchestrates an Oncogenic Program in B Cell Precursor Acute Lymphoblastic Leukemia
Nucera, S., Giustacchini, A., Boccalatte, F. E., Calabria, A., Fanciullo, C., Plati, T., Ranghetti, A., García-Manteiga, J. M., Cittaro, D., Benedicenti, F., et al. (2016) · Cancer Cell · doi:10.1016/j.ccell.2016.05.007 · Cited by 65
Crippling p53 activities via knock-in mutations in mouse models
Iwakuma, T., & Lozano, G. (2007) · Oncogene · doi:10.1038/sj.onc.1210278 · Cited by 66
PDHA1 Gene Knockout In Human Esophageal Squamous Cancer Cells Resulted In Greater Warburg Effect And Aggressive Features In Vitro And In Vivo
Liu, L., Cao, J., Zhao, J., Li, X., Suo, Z., & Li, H. (2019) · OncoTargets and Therapy · doi:10.2147/ott.s226851 · Cited by 61
Dissecting functional roles of p53 N‐terminal transactivation domains by microarray expression analysis
Ohki, R., Kawase, T., Ohta, T., Ichikawa, H., & Taya, Y. (2006) · Cancer Science · doi:10.1111/j.1349-7006.2006.00375.x · Cited by 64
Regulation of p53 by the 14-3-3 protein interaction network: new opportunities for drug discovery in cancer
Falcicchio, M., Ward, J. A., Macip, S., & Doveston, R. G. (2020) · Cell Death Discovery · doi:10.1038/s41420-020-00362-3 · Cited by 59
Illuminating p53 function in cancer with genetically engineered mouse models
Garcia, P. B., & Attardi, L. D. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2013.12.014 · Cited by 65
Cooperative functions of Chk1 and Chk2 reduce tumour susceptibility in vivo
Niida, H., Murata, K., Shimada, M., Ogawa, K., Ohta, K., Suzuki, K., Fujigaki, H., Khaw, A. K., Banerjee, B., Hande, M. P., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.218 · Cited by 56
The MDM2 Ubiquitination Signal in the DNA-Binding Domain of p53 Forms a Docking Site for Calcium Calmodulin Kinase Superfamily Members
Craig, A. L., Chrystal, J. A., Fraser, J. A., Sphyris, N., Lin, Y., Harrison, B. J., Scott, M. T., Dornreiter, I., & Hupp, T. R. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01595-06 · Cited by 52
MDM2 Chaperones the p53 Tumor Suppressor
Wawrzynów, B., Żylicz, M., Wallace, M., Hupp, T. R., & Żylicz, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702767200 · Cited by 53
Extended String Binding Mode of the Phosphorylated Transactivation Domain of Tumor Suppressor p53
Okuda, M., & Nishimura, Y. (2014) · Journal of the American Chemical Society · doi:10.1021/ja506351f · Cited by 54
A Central Role for CK1 in Catalyzing Phosphorylation of the p53 Transactivation Domain at Serine 20 after HHV-6B Viral Infection
MacLaine, N. J., Øster, B., Bundgaard, B. B., Fraser, J. A., Buckner, C., Lazo, P. A., Meek, D. W., Höllsberg, P., & Hupp, T. R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804433200 · Cited by 44
p53-mediated apoptosis prevents the accumulation of progenitor B cells and B-cell tumors
Slatter, T. L., Ganesan, P. L., Holzhauer, C., Mehta, R., Rubio‐Terres, C., Williams, G., Wilson, M., Royds, J. A., Baird, M. A., & Braithwaite, A. W. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.136 · Cited by 41
Simultaneous phosphorylation of p53 at serine 15 and 20 induces apoptosis in human glioma cells by increasing expression of pro-apoptotic genes
Amano, T., Nakamizo, A., Mishra, S. K., Gumin, J., Shinojima, N., Sawaya, R. A., & Lang, F. F. (2009) · Journal of Neuro-Oncology · doi:10.1007/s11060-009-9844-1 · Cited by 40
Switching on p53: an essential role for protein phosphorylation?
Loughery, J., & Meek, D. W. (2013) · Biodiscovery · doi:10.7750/biodiscovery.2013.8.1 · Cited by 39
Mouse bites dogma: how mouse models are changing our views of how P53 is regulated in vivo
Wahl, G. M. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401911 · Cited by 37
New insights into oncogenic stress
Haigis, K. M., & Sweet-Cordero, A. (2011) · Nature Genetics · doi:10.1038/ng0311-177 · Cited by 38
Identification of a Dominant Negative Functional Domain on DAPK-1 That Degrades DAPK-1 Protein and Stimulates TNFR-1-mediated Apoptosis
Lin, Y., Stevens, C., & Hupp, T. R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611559200 · Cited by 36
Zinc induces ERK-dependent cell death through a specific Ras isoform
Klein, C., Creach, K. M., Irintcheva, V., Hughes, K. J., Blackwell, P. L., Corbett, J. A., & Baldassare, J. J. (2006) · APOPTOSIS · doi:10.1007/s10495-006-0089-6 · Cited by 36
Correction: Phosphorylation of Daxx by ATM Contributes to DNA Damage-Induced p53 Activation
Tang, J., Agrawal, T., Cheng, Q., Qu, L., Brewer, M. D., Chen, J., & Yang, X. (2013) · PLoS ONE · doi:10.1371/annotation/032b026d-5bcf-4c1b-aa15-65c226a53818 · Cited by 36
The p53-Mdm2 Loop: A Critical Juncture of Stress Response
Levav-Cohen, Y., Goldberg, Z., Tan, K. H., Alsheich-Bartok, O., Zuckerman, V., Haupt, S., & Haupt, Y. (2014) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-017-9211-0_9 · Cited by 38
SMG7 is a critical regulator of p53 stability and function in DNA damage stress response
Luo, H., Cowen, L. E., Yu, G., Jiang, W. G., & Tang, Y. (2016) · Cell Discovery · doi:10.1038/celldisc.2015.42 · Cited by 33
Lack of p53 Ser389 Phosphorylation Predisposes Mice to Develop 2-Acetylaminofluorene–Induced Bladder Tumors but not Ionizing Radiation–Induced Lymphomas
Hoogervorst, E. M., Bruins, W., Zwart, E., van Oostrom, C. T. M., van den Aardweg, G. J., Beems, R. B., van den Berg, J., Jacks, T., STEEG, H. V., & de Vries, A. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-4328 · Cited by 34
The roles of MDM2 and MDMX phosphorylation in stress signaling to p53
Chen, J. (2012) · Genes & Cancer · doi:10.1177/1947601912454733 · Cited by 33
Phosphorylation of Thr18 and Ser20 of p53 in Ad-p53–induced apoptosis
Nakamizo, A., Amano, T., Zhang, W., Zhang, X.-Q., Ramdas, L., Liu, T.-J., Bekele, B. N., Shono, T., Sasaki, T., Benedict, W. F., et al. (2008) · Neuro-Oncology · doi:10.1215/15228517-2008-015 · Cited by 32
Activation of cAMP Signaling Interferes with Stress-Induced p53 Accumulation in ALL-Derived Cells by Promoting the Interaction between p53 and HDM2
Naderi, E. H., Jochemsen, A. G., Blomhoff, H. K., & Naderi, S. (2011) · Neoplasia · doi:10.1593/neo.11542 · Cited by 33
Insights into Wild-Type and Mutant p53 Functions Provided by Genetically Engineered Mice
Donehower, L. A. (2014) · Human Mutation · doi:10.1002/humu.22507 · Cited by 30
Phosphorylation of Daxx by ATM contributes to DNA damage-induced p53 activation.
Tang, J., Agrawal, T., Cheng, Q., Qu, L., Brewer, M. D., Chen, J., & Yang, X. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055813 · Cited by 28
A Novel p53 Phosphorylation Site within the MDM2 Ubiquitination Signal
Fraser, J. A., Madhumalar, A., Blackburn, E. A., Bramham, J., Walkinshaw, M. D., Verma, C. S., & Hupp, T. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.143107 · Cited by 29
A Novel p53 Phosphorylation Site within the MDM2 Ubiquitination Signal
Fraser, J. A., Vojtěšek, B., & Hupp, T. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.143099 · Cited by 28
On the Mechanism of Sequence-specific DNA-dependent Acetylation of p53: The Acetylation Motif is Exposed upon DNA Binding
Češková, P., Chichger, H., Wallace, M., Vojtesek, B., & Hupp, T. R. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.12.026 · Cited by 27
Role of Specific B-Cell Receptor Antigens in Lymphomagenesis
Thurner, L., Hartmann, S., Neumann, F., Hoth, M., Stilgenbauer, S., Küppers, R., Preuss, K., & Bewarder, M. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.604685 · Cited by 26
Tumor Susceptibility and Apoptosis Defect in a Mouse Strain Expressing a Human p53 Transgene
Dudgeon, C., Kek, C., Demidov, O. N., Saito, S., Fernandes, K., Diot, A., Bourdon, J., Lane, D. P., Appella, E., Fornace, A. J., et al. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-2063 · Cited by 25
CK2-site Phosphorylation of p53 is Induced in ΔNp63 Expressing Basal Stem Cells in UVB Irradiated Human Skin
Finlan, L. E., Nenutil, R., Ibbotson, S. H., Vojtesek, B., & Hupp, T. R. (2006) · Cell Cycle · doi:10.4161/cc.5.21.3393 · Cited by 24
Protein phosphatase 1 inhibits p53 signaling by dephosphorylating and stabilizing Mdmx
Lu, Z., Wan, G., Guo, H., Zhang, X., & Lu, X. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.12.014 · Cited by 25
Phosphorylation of Ser312 contributes to tumor suppression by p53 in vivo
Slee, E. A., Benassi, B., Goldin, R. D., Zhong, S., Ratnayaka, I., Blandino, G., & Lü, X. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1005165107 · Cited by 24
Tp53 deletion in B lineage cells predisposes mice to lymphomas with oncogenic translocations
Rowh, M. A. W., DeMicco, A., Horowitz, J. E., Yin, B., Yang-Iott, K. S., Fusello, A. M., Hobeika, E., Reth, M. G., & Bassing, C. H. (2011) · Oncogene · doi:10.1038/onc.2011.191 · Cited by 24
The Changing Face of HDAC Inhibitor Depsipeptide
Zhou, W., & Zhu, W. (2009) · Current Cancer Drug Targets · doi:10.2174/156800909787314039 · Cited by 23
The phenotype of MDM2 auto-degradation after DNA damage is due to epitope masking by phosphorylation
Cheng, Q., & Chen, J. (2011) · Cell Cycle · doi:10.4161/cc.10.7.15249 · Cited by 21
The role of the ubiquitin proteasome system in lymphoma
Suh, K. S., Tanaka, T., Sarojini, S., Nightingale, G., Gharbaran, R., Pecora, A. L., & Goy, A. H. (2013) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2013.02.005 · Cited by 20
Human herpesvirus 6B induces phosphorylation of p53 in its regulatory domain by a CK2- and p38-independent pathway
Øster, B., Bundgaard, B. B., Hupp, T. R., & Höllsberg, P. (2007) · Journal of General Virology · doi:10.1099/vir.0.83136-0 · Cited by 20
Serine 312 phosphorylation is dispensable for wild-type p53 functions in vivo
Lee, M. K., Tong, W., Wang, Z. Q., & Sabapathy, K. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.90 · Cited by 17
DNA repair-deficient Xpa/p53 knockout mice are sensitive to the non-genotoxic carcinogen cyclosporine A: escape of initiated cells from immunosurveillance?
van Kesteren, P. C. E., Beems, R. B., Luijten, M., Robinson, J. F., de Vries, A., & STEEG, H. V. (2009) · Carcinogenesis · doi:10.1093/carcin/bgp013 · Cited by 15
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
Modeling the Study of DNA Damage Responses in Mice
Specks, J., Nieto-Soler, M., Lopez-Contreras, A. J., & Fernández-Capetillo, Ó. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2297-0_21 · Cited by 13
Defining relative mutational difficulty to understand cancer formation
Shan, L., Yu, J., He, Z., Chen, S., Liu, M., Ding, H., Xu, L., Zhao, J., Yang, A. E., & Jiang, H. (2020) · Cell Discovery · doi:10.1038/s41421-020-0177-8 · Cited by 10
Induction of B-cell lymphoma by UVB Radiation in p53 Haploinsufficient Mice
Puebla‐Osorio, N., Miyahara, Y., Sreevidya, C. S., Limón-Flores, A. Y., Kazimi, N., Ullrich, S. E., & Zhu, C. (2011) · BMC Cancer · doi:10.1186/1471-2407-11-36 · 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
Multienzyme assembly of a p53 transcription complex
Hupp, T. R., & Walkinshaw, M. D. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1007-885 · Cited by 8
A Unique Spectrum of Spontaneous Tumors in Dino Knockout Mice Identifies Tissue-Specific Requirements for Tumor Suppression
Marney, C. B., Anderson, E. S., Baum, R., & Schmitt, A. M. (2022) · Cells · doi:10.3390/cells11111818 · Cited by 7
Bradykinin B2receptor null mice harboring a Ser23-to-Ala substitution in the p53 gene are protected from renal dysgenesis
El-Dahr, S. S., Aboudehen, K., & Dipp, S. (2008) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.90378.2008 · Cited by 7
Insuline-Like Growth Factor-2 (IGF2) and Hepatocyte Growth Factor (HGF) Promote Lymphomagenesis in p53-null Mice in Tissue-specific and Estrogen-signaling Dependent Manners
Huang, H.-S., Chu, S., Chen, P., Lee, M., Huang, C.-Y., Chou, H.-M., & Chu, T. (2021) · Journal of Cancer · doi:10.7150/jca.60120 · Cited by 6
Phosphorylation at Carboxyl-Terminal S373 and S375 Residues and 14-3-3 Binding Are Not Required for Mouse p53 Function
Lee, M. K., & Sabapathy, K. (2007) · Neoplasia · doi:10.1593/neo.07511 · Cited by 6
Mis-splicing drives loss of function of p53E224D point mutation
Lock, I. C., Leisenring, N. H., Floyd, W., Xu, E. S., Luo, L., Ma, Y., Mansell, E. C., Cardona, D. M., Lee, C., & Kirsch, D. G. (2025) · PLoS ONE · doi:10.1371/journal.pone.0318856 · Cited by 3
Dynamics of Delayed p53 Mutations in Mice Given Whole-Body Irradiation at 8 Weeks
Okazaki, R., Ootsuyama, A., Kakihara, H., Mabuchi, Y., Matsuzaki, Y., Michikawa, Y., Imai, T., & Norimura, T. (2010) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2010.07.022 · Cited by 4
DNA Damage Signaling Downstream of ATM
Bunz, F. (2011) · Springer eBooks · doi:10.1007/978-1-4419-8044-1_2 · Cited by 4
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

Authors: MacPherson, D., Kim, J., Kim, T., Rhee, B. K., van Oostrom, C. T., DiTullio, R. A., Venere, M., Halazonetis, T. D., Bronson, R., de Vries, A., Fleming, M., & Jacks, T.
Affiliations: Center for Cancer Research (US)
Sogang University (KR)
Massachusetts Institute of Technology (US)
The Wistar Institute (US)
Tufts University (US)
Boston Children's Hospital (US)
Howard Hughes Medical Institute (US)
Corresponding author: Jacks, Tyler
ORCID: MacPherson, David
Kim, Jungho
Kim, Teresa
Venere, Monica
Halazonetis, Thanos D
Bronson, Roderick
Fleming, Mark
Jacks, Tyler
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 2004-09-02
Volume: 23
Issue: 18
Pages: 3689-3699
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1038/sj.emboj.7600363
PMC: PMC517606
OpenAlex: W2158689768
Cited by: 124
References: 49
Citations by year: 2025: 1 · 2024: 1 · 2023: 3 · 2022: 1 · 2021: 1 · 2020: 4 · 2019: 2 · 2018: 1 · 2016: 3 · 2015: 4 · 2014: 8 · 2013: 8 · 2012: 6
FWCI: 4.81
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: The EMBO Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Rivm (National Institute for Public Health and the Environment) (submittedVersion)
Funders: Howard Hughes Medical Institute
University of Pennsylvania
Topics: Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Keywords: p53, MDM2, p53 stabilization, apoptosis resistance, B-cell lymphoma, thymocytes, cerebellar development, tumor suppression, mouse model, ionizing radiation, lifespan
MeSH terms: Animals, Cell Cycle, Cells, Cultured, Cerebellum, DNA Damage, Female, Fibroblasts, Homozygote, Infrared Rays, Male, Mice, Inbred C57BL, Phosphorylation, Serine, Thymus Gland, Survival Rate, Tumor Suppressor Protein p53, Lymphoma, B-Cell, Apoptosis, Point Mutation, Mice, Knockout, Mice

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

Defective apoptosis and B-cell lymphomas in mice with p53 point mutation at Ser 23

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks