Cited by 157Cancer-related Molecular PathwaysGenomics and Chromatin DynamicsNuclear Structure and Function

The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.

p53 represses ribosomal gene transcription

Budde, Andreja, Grummt, Ingrid·1999·Oncogene

DOI 10.1038/sj.onc.1202402

Open this paper in CoChat — free account

Abstract

Induction of the tumor suppressor protein p53 restricts cellular proliferation. Since actively growing cells require the ongoing synthesis of ribosomal RNA to sustain cellular biosynthesis, we studied the effect of p53 on ribosomal gene transcription by RNA polymerase I (Pol I). We have measured rDNA transcriptional activity in different cell lines which either lack or overexpress p53 and demonstrate that wild-type but not mutant p53 inhibits cellular pre-rRNA synthesis. Conversely, pre-rRNA levels are elevated both in cells which express mutant p53 and in fibroblasts from p53 knock-out mice. Transient transfection assays with a set of rDNA deletion mutants demonstrate that intergenic spacer sequences are dispensable and the minimal rDNA promoter is sufficient for p53-mediated repression of Pol I transcription. However, in a cell-free transcription system, recombinant p53 does not inhibit rDNA transcription, indicating that p53 does not directly interfere with the basal Pol I transcriptional machinery. Thus, repression of Pol I transcription by p53 may be a consequence of p53-induced growth arrest.

Integrity signals

Registry

Crossref · 10.1038/sj.onc.1202402

Cites

38 of 38 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
Dignam, J. D., Lebovitz, R. M., & Roeder, R. G. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.5.1475 · Cited by 11,262
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
The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases.
Wade Harper, J. (1993) · Cell · doi:10.1016/0092-8674(93)90499-g · Cited by 5,651
The retinoblastoma protein and cell cycle control
Weinberg, R. A. (1995) · Cell · doi:10.1016/0092-8674(95)90385-2 · Cited by 4,862
p21 is a universal inhibitor of cyclin kinases
Xiong, Y., Hannon, G., Zhang, H., Casso, D., Kobayashi, R., & Beach, D. (1993) · Nature · doi:10.1038/366701a0 · Cited by 3,691
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
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
Chromosome 17 Deletions and p53 Gene Mutations in Colorectal Carcinomas
Baker, S. J., Fearon, E. R., Nigro, J. M., Hamilton, S. R., Preisinger, A. C., Jessup, J. M., vanTuinen, P., Ledbetter, D. H., Barker, D. F., Nakamura, Y., et al. (1989) · Science · doi:10.1126/science.2649981 · Cited by 2,097
The p53 proto-oncogene can act as a suppressor of transformation
Finlay, C. A., Hinds, P. W., & Levine, A. J. (1989) · Cell · doi:10.1016/0092-8674(89)90045-7 · Cited by 1,987

Show all 37 references

Research works printed but not linked: 2

Grummt I . 1998 Prog. Nucl. Acid Res. Mol. Biol. in press.
Paule M . 1994 Transcription: Mechanism and Regulation. Conaway JW (ed). Raven Press: New York pp.83–106.

Sorted by citations

Census and evaluation of p53 target genes
Fischer, M. (2017) · Oncogene · doi:10.1038/onc.2016.502 · Cited by 971
Disruption of the nucleolus mediates stabilization of p53 in response to DNA damage and other stresses
Rubbi, C. P., & Milner, J. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg579 · Cited by 828
Divorcing ARF and p53: an unsettled case
Sherr, C. J. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1954 · Cited by 595
The cellular response to p53: the decision between life and death
Sionov, R. V., & Haupt, Y. (1999) · Oncogene · doi:10.1038/sj.onc.1203130 · Cited by 608
Transcriptional Regulation by P53
Beckerman, R., & Prives, C. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000935 · Cited by 569
Life on a planet of its own: Regulation of RNA polymerase I transcription in the nucleolus
Grummt, I. (2003) · Genes & Development · doi:10.1101/gad.1098503r · Cited by 540
Self-citation
mTOR-dependent activation of the transcription factor TIF-IA links rRNA synthesis to nutrient availabilityPreprint
Mayer, C., Zhao, J., Yuan, X., & Grummt, I. (2004) · Genes & Development · doi:10.1101/gad.285504 · Cited by 544
Self-citation
Transcriptional regulation by p53: one protein, many possibilities
Laptenko, O., & Prives, C. L. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401916 · Cited by 515
SURVEY AND SUMMARY Transcription by RNA polymerases I and III
Paule, M. R. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.6.1283 · Cited by 503
Ribosomal Protein L23 Activates p53 by Inhibiting MDM2 Function in Response to Ribosomal Perturbation but Not to Translation Inhibition
Dai, M., Zeng, S. X., Jin, Y., Sun, X., David, L. L., & Lu, H. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.17.7654-7668.2004 · Cited by 495
Chemotherapeutic Drugs Inhibit Ribosome Biogenesis at Various Levels
Burger, K., Mühl, B., Thomas, H., Michaela, R., Anastassia, M., Orban, M., Kellner, M., Anita, G.-E., Kremmer, E., Hölzel, M., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.074211 · Cited by 448
The RNA Polymerase I Transcription Machinery: An Emerging Target for the Treatment of Cancer
Drygin, D., Rice, W. G., & Grummt, I. (2010) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.010909.105844 · Cited by 439
Self-citation
Nuclear actin and myosin I are required for RNA polymerase I transcription
Philimonenko, V. V., Zhao, J., Iben, S., Dingová, H., Gaplovská-Kyselá, K., Kahle, M., Zentgraf, H., Hofmann, W. A., de Lanerolle, P., Hozák, P., et al. (2004) · Nature Cell Biology · doi:10.1038/ncb1190 · Cited by 398
Self-citation
RNA polymerases I and III, growth control and cancer
White, R. J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1551 · Cited by 342
A Targeting Modality for Destruction of RNA Polymerase I that Possesses Anticancer Activity
Peltonen, K., Colis, L. C., Liu, H., Trivedi, R. K., Moubarek, M. S., Moore, H. M., Bai, B., Rudek, M. A., Bieberich, C. J., & Laiho, M. (2014) · Cancer Cell · doi:10.1016/j.ccr.2013.12.009 · Cited by 327
A housekeeper with power of attorney: the rRNA genes in ribosome biogenesis
Moss, T., Langlois, F., Gagnon-Kugler, T., & Stefanovsky, V. Y. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-006-6278-1 · Cited by 310
Ribosome biogenesis surveillance: probing the ribosomal protein-Mdm2-p53 pathway
Deisenroth, C., & Zhang, Y. (2010) · Oncogene · doi:10.1038/onc.2010.189 · Cited by 301
Repression of RNA Polymerase I Transcription by the Tumor Suppressor p53
Zhai, W., & Comai, L. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.16.5930-5938.2000 · Cited by 289
Nucleolar Stress: hallmarks, sensing mechanism and diseases
Yang, K., Yang, J., & Yi, J. (2018) · Cell Stress · doi:10.15698/cst2018.06.139 · Cited by 302
Nucleolar Arf Tumor Suppressor Inhibits Ribosomal RNA Processing
Sugimoto, M., Kuo, M.-L., Roussel, M. F., & Sherr, C. J. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00057-1 · Cited by 273
Ribosomal protein S7 as a novel modulator of p53–MDM2 interaction: binding to MDM2, stabilization of p53 protein, and activation of p53 function
Chen, D., Zhang, Z., Li, M., Wang, W., Li, Y., Rayburn, E. R., Hill, D. L., Wang, H., & Zhang, R. (2007) · Oncogene · doi:10.1038/sj.onc.1210327 · Cited by 265
What the nucleolus says to a tumour pathologist
Derenzini, M., Montanaro, L., & Treré, D. (2009) · Histopathology · doi:10.1111/j.1365-2559.2008.03168.x · Cited by 271
ERK-Dependent Phosphorylation of the Transcription Initiation Factor TIF-IA Is Required for RNA Polymerase I Transcription and Cell Growth
Zhao, J., Yuan, X., Frödin, M., & Grummt, I. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00036-4 · Cited by 259
Self-citation
The nucleolus: an emerging target for cancer therapy
Hein, N., Hannan, K. M., George, A. J., Sanij, E., & Hannan, R. D. (2013) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2013.07.005 · Cited by 259
The Ribosome Biogenesis—Cancer Connection
Penzo, M., Montanaro, L., Treré, D., & Derenzini, M. (2019) · Cells · doi:10.3390/cells8010055 · Cited by 242
The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal gene promoter and represses RNA polymerase i transcription
Zhou, Y., Santoro, R., & Grummt, I. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf460 · Cited by 234
Self-citation
Ribosomal Proteins and Human Diseases: Pathogenesis, Molecular Mechanisms, and Therapeutic Implications
Wang, W., Nag, S. A., Zhang, X., Wang, M., Wang, H., Zhou, J., & Zhang, R. (2014) · Medicinal Research Reviews · doi:10.1002/med.21327 · Cited by 232
Dysregulation of the basal RNA polymerase transcription apparatus in cancer
Bywater, M. J., Pearson, R. B., McArthur, G. A., & Hannan, R. D. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3496 · Cited by 224
Dial 9-1-1 for p53: Mechanisms of p53 Activation by Cellular Stress
Ljungman, M. E. (2000) · Neoplasia · doi:10.1038/sj.neo.7900073 · Cited by 222
Mitotic occupancy and lineage-specific transcriptional control of rRNA genes by Runx2
Young, D. W., Hassan, M. Q., Pratap, J., Galindo, M. A., Zaidi, S. K., Lee, S.-H., Yang, X., Xie, R., Javed, A., Underwood, J. M., et al. (2007) · Nature · doi:10.1038/nature05473 · Cited by 220
Translating the genome in time and space: Specialized ribosomes, RNA regulons, and RNA-binding proteins
Shi, Z., & Barna, M. (2015) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100814-125346 · Cited by 205
RNA polymerases I and III, non-coding RNAs and cancer
White, R. J. (2008) · Trends in Genetics · doi:10.1016/j.tig.2008.10.003 · Cited by 190
Nucleolus: A Central Hub for Nuclear Functions
Iarovaia, O. V., Minina, E. P., Sheval, E. V., Onichtchouk, D., Dokudovskaya, S., Razin, S. V., & Vassetzky, Y. S. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.04.003 · Cited by 180
Single-cell RNA sequencing reveals intrinsic and extrinsic regulatory heterogeneity in yeast responding to stress
Gasch, A. P., Yu, F. B., Hose, J., Escalante, L. E., Place, M., Bacher, R. L., Kanbar, J. N., Ciobanu, D., Sandor, L., Grigoriev, I. V., et al. (2017) · PLoS Biology · doi:10.1371/journal.pbio.2004050 · Cited by 162
Stress-Dependent Nucleolin Mobilization Mediated by p53-Nucleolin Complex Formation
Daniely, Y., Dimitrova, D. D., & Borowiec, J. A. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.16.6014-6022.2002 · Cited by 174
Activation of RNA Polymerase I Transcription by Cockayne Syndrome Group B Protein and Histone Methyltransferase G9a
Yuan, X., Feng, W., Imhof, A., Grummt, I., & Zhou, Y. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.021 · Cited by 175
Self-citation
Discovery of CX-5461, the First Direct and Selective Inhibitor of RNA Polymerase I, for Cancer Therapeutics
Haddach, M., Schwaebe, M. K., Michaux, J., Nagasawa, J. Y., O’Brien, S., Whitten, J. P., Pierre, F., Kerdoncuff, P., Darjania, L., Stansfield, R. K., et al. (2012) · ACS Medicinal Chemistry Letters · doi:10.1021/ml300110s · Cited by 165
Regulation of NF‐κB and p53 through activation of ATR and Chk1 by the ARF tumour suppressor
Rocha, S., Garrett, M. D., Campbell, K. J., Schumm, K., & Perkins, N. D. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600608 · Cited by 161
Ribosomes and marrow failure: coincidental association or molecular paradigm?
Liu, J. M., & Ellis, S. R. (2006) · Blood · doi:10.1182/blood-2005-12-4831 · Cited by 159
The nucleolus and transcription of ribosomal genes
Raška, I., Koberna, K., Malínský, J., Fidlerová, H., & Mašata, M. (2004) · Biology of the Cell · doi:10.1016/j.biolcel.2004.04.015 · Cited by 165
The insulin-like growth factor-I receptor as a target for cancer therapy
Baserga, R. (2005) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.9.4.753 · Cited by 148
TFIIH Plays an Essential Role in RNA Polymerase I Transcription
Iben, S., Tschochner, H., Bier, M., Hoogstraten, D., Hozák, P., Egly, J., & Grummt, I. (2002) · Cell · doi:10.1016/s0092-8674(02)00729-8 · Cited by 145
Self-citation
MDMX regulation of p53 response to ribosomal stress
Gilkes, D. M., Chen, L., & Chen, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601424 · Cited by 142
The structure of NoRC‐associated RNA is crucial for targeting the chromatin remodelling complex NoRC to the nucleolus
Mayer, C., Neubert, M., & Grummt, I. (2008) · EMBO Reports · doi:10.1038/embor.2008.109 · Cited by 148
Self-citation
Importin 7 and Exportin 1 Link c-Myc and p53 to Regulation of Ribosomal Biogenesis
Golomb, L., Bublik, D. R., Wilder, S., Nevo, R., Kiss, V., Grabusic, K., Volarevic, S., & Oren, M. (2012) · Molecular Cell · doi:10.1016/j.molcel.2011.11.022 · Cited by 137
TIF‐IA, the factor mediating growth‐dependent control of ribosomal RNA synthesis, is the mammalian homolog of yeast Rrn3p
Bodem, J., Dobreva, G. D., Hoffmann‐Rohrer, U., Iben, S., Zentgraf, H., Delius, H., Vingron, M., & Grummt, I. (2000) · EMBO Reports · doi:10.1093/embo-reports/kvd032 · Cited by 133
Self-citation
The shared genomic architecture of human nucleolar organizer regionsPreprint
Floutsakou, I., Agrawal, S., Nguyen, T. T., Seoighe, C., Ganley, A. R. D., & McStay, B. (2013) · Genome Research · doi:10.1101/gr.157941.113 · Cited by 133
Cancer nucleus: Morphology and beyond
Dey, P. (2009) · Diagnostic Cytopathology · doi:10.1002/dc.21234 · Cited by 129
The role of translation in neoplastic transformation from a pathologist's point of view
Rosenwald, I. B. (2004) · Oncogene · doi:10.1038/sj.onc.1207552 · Cited by 125
The nucleolus as a fundamental regulator of the p53 response and a new target for cancer therapy
Woods, S. J., Hannan, K. M., Pearson, R. B., & Hannan, R. D. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.10.007 · Cited by 120
Exploiting the yeast stress-activated signaling network to inform on stress biology and disease signaling
Ho, Y., & Gasch, A. P. (2015) · Current Genetics · doi:10.1007/s00294-015-0491-0 · Cited by 110
p53 -Dependent and -Independent Nucleolar Stress Responses
Olausson, K. H., Nistér, M., & Lindström, M. S. (2012) · Cells · doi:10.3390/cells1040774 · Cited by 127
Human Nopp140, Which Interacts with RNA Polymerase I: Implications for rRNA Gene Transcription and Nucleolar Structural Organization
Chen, H.-K., Pai, C.-Y., Huang, J., & Yeh, N.-H. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.12.8536 · Cited by 111
Identification of ribosomal protein S25 (RPS25)–MDM2–p53 regulatory feedback loop
Zhang, X., Wang, W., Wang, H., Wang, M.-H., Xu, W., & Zhang, R. (2012) · Oncogene · doi:10.1038/onc.2012.289 · Cited by 106
Regulation of RNA Polymerase I Transcription in Development, Disease, and Aging
Sharifi, S., & Bierhoff, H. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-012612 · Cited by 108
LAS1L interacts with the mammalian Rix1 complex to regulate ribosome biogenesis
Castle, C. D., Cassimere, E. K., & Denicourt, C. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-06-0530 · Cited by 109
The intracrine hypothesis: An update
Ré, R. N., & Cook, J. L. (2005) · Regulatory Peptides · doi:10.1016/j.regpep.2005.09.012 · Cited by 101
Human rDNA: Evolutionary Patterns within the Genes and Tandem Arrays Derived from Multiple Chromosomes
Gonzalez, I. L., & Sylvester, J. E. (2001) · Genomics · doi:10.1006/geno.2001.6540 · Cited by 97
Multiple interactions between RNA polymerase I, TIF‐IA and TAFI subunits regulate preinitiation complex assembly at the ribosomal gene promoter
Yuan, X., Zhao, J., Zentgraf, H., Hoffmann‐Rohrer, U., & Grummt, I. (2002) · EMBO Reports · doi:10.1093/embo-reports/kvf212 · Cited by 96
Self-citation
Why should cancer biologists care about tRNAs? tRNA synthesis, mRNA translation and the control of growth
Grewal, S. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.12.005 · Cited by 97
Antiproliferative B cell translocation gene 2 protein is down-regulated post-transcriptionally as an early event in prostate carcinogenesis
Ficazzola, M. (2001) · Carcinogenesis · doi:10.1093/carcin/22.8.1271 · Cited by 93
Connecting the nucleolus to the cell cycle and human disease
Tsai, R. Y. L., & Pederson, T. (2014) · The FASEB Journal · doi:10.1096/fj.14-254680 · Cited by 98
p53 activation results in rapid dephosphorylation of the eIF4E-binding protein 4E-BP1, inhibition of ribosomal protein S6 kinase and inhibition of translation initiation
Horton, L. E., Bushell, M., Baus, D., Tilleray, V. J., Clemens, M. J., & Hensold, J. O. (2002) · Oncogene · doi:10.1038/sj.onc.1205662 · Cited by 94
The p53 Tumor Suppressor Causes Congenital Malformations in Rpl24-Deficient Mice and Promotes Their Survival
Barkić, M., Crnomarković, S., Grabušić, K., Bogetić, I., Panić, L., Tamarut, S., Brdovčak, M. C., Jerić, I., Vidak, S., & Volarević, S. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01588-08 · Cited by 92
Small Molecule BMH-Compounds That Inhibit RNA Polymerase I and Cause Nucleolar Stress
Peltonen, K., Colis, L. C., Liu, H., Jäämaa, S., Zhang, Z., af Hällström, T., Moore, H. M., Sirajuddin, P., & Laiho, M. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-14-0256 · Cited by 90
p53 Represses the Oncogenic Sno-MiR-28 Derived from a SnoRNA
Yu, F., Bracken, C. P., Pillman, K. A., Lawrence, D., Goodall, G. J., Callen, D. F., & Neilsen, P. M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0129190 · Cited by 92
p53, a translational regulator: contribution to its tumour-suppressor activity
Marcel, V., Catez, F., & Diaz, J. (2015) · Oncogene · doi:10.1038/onc.2015.25 · Cited by 94
Nucleolar Size and Activity Are Related to pRb and p53 Status in Human Breast Cancer
Treré, D., Ceccarelli, C., Montanaro, L., Tosti, E., & Derenzini, M. (2004) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.4a6454.2004 · Cited by 85
Integrated miRNA, mRNA and protein expression analysis reveals the role of post-transcriptional regulation in controlling CHO cell growth rate
Clarke, C., Henry, M. A., Doolan, P., Kelly, S., Aherne, S. T., Sanchez, N., Kelly, P. S., Kinsella, P., Breen, L., Madden, S. F., et al. (2012) · BMC Genomics · doi:10.1186/1471-2164-13-656 · Cited by 92
Runx2 deficiency and defective subnuclear targeting bypass senescence to promote immortalization and tumorigenic potential
Zaidi, S. K., Pande, S., Pratap, J., Gaur, T., Grigoriu, S., Ali, S. A., Stein, J. L., Lian, J. B., van Wijnen, A. J., & Stein, G. S. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709650104 · Cited by 82
Scission of the p53-MDM2 Loop by Ribosomal Proteins
Zhou, X. Y., Liao, J.-M., Liao, W.-J., & Lu, H. (2012) · Genes & Cancer · doi:10.1177/1947601912455200 · Cited by 82
Global Inhibition with Specific Activation: How p53 and MYC Redistribute the Transcriptome in the DNA Double-Strand Break Response
Porter, J. R., Fisher, B. E., Baranello, L., Liu, J. C., Kambach, D. M., Nie, Z., Koh, W. S., Luo, J., Stommel, J. M., Levens, D., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.07.028 · Cited by 79
Regulatory module involving FGF13, miR-504, and p53 regulates ribosomal biogenesis and supports cancer cell survival
Bublik, D. R., Bursać, S., Sheffer, M., Oršolić, I., Shalit, T., Tarcic, O., Kotler, E., Mouhadeb, O., Hoffman, Y., Fuchs, G., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1614876114 · Cited by 77
Las1L Is a Nucleolar Protein Required for Cell Proliferation and Ribosome Biogenesis
Castle, C. D., Cassimere, E. K., Lee, J., & Denicourt, C. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00358-10 · Cited by 75
Karyotypic dissection of Hodgkin's disease cell lines reveals ectopic subtelomeres and ribosomal DNA at sites of multiple jumping translocations and genomic amplification
MacLeod, R., Spitzer, D., Bar‐Am, I., Sylvester, J., Kaufmann, M., Wernich, A., & Drexler, H. G. (2000) · Leukemia · doi:10.1038/sj.leu.2401894 · Cited by 75
Non-activated p53 co-localizes with sites of transcription within both the nucleoplasm and the nucleolus
Rubbi, C. P., & Milner, J. (2000) · Oncogene · doi:10.1038/sj.onc.1203378 · Cited by 74
Overlapping Functions of the pRb Family in the Regulation of rRNA Synthesis
Ciarmatori, S., Scott, P., Sutcliffe, J. E., McLees, A., Alzuherri, H. M., Dannenberg, J., Riele, H. T., Grummt, I., Voit, R., & White, R. J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.17.5806-5814.2001 · Cited by 74
Self-citation
Ribosomal protein L4 is a novel regulator of the MDM2-p53 loop
He, X., Li, Y., Dai, M., & Sun, X. (2016) · Oncotarget · doi:10.18632/oncotarget.7479 · Cited by 73
Old Drug, New Target
Andrews, W. J., Panova, T. B., Normand, C., Gadal, O., Tikhonova, I. G., & Panov, K. I. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.411611 · Cited by 68
Human tumor suppressor p53 and DNA viruses
Collot-Teixeira, S., Bass, J., Denis, F., & Ranger‐Rogez, S. (2004) · Reviews in Medical Virology · doi:10.1002/rmv.431 · Cited by 69
Feedback Regulation of c-Myc by Ribosomal Protein L11
Dai, M., Sears, R. C., & Lu, H. (2007) · Cell Cycle · doi:10.4161/cc.6.22.4895 · Cited by 75
Topoisomerase IIα promotes activation of RNA polymerase I transcription by facilitating pre-initiation complex formation
Ray, S., Panova, T. B., Miller, G., Volkov, A., Porter, A. C. G., Russell, J., Panov, K. I., & Zomerdijk, J. C. B. M. (2013) · Nature Communications · doi:10.1038/ncomms2599 · Cited by 64
The chromatin remodeling complex NoRC and TTF-I cooperate in the regulation of the mammalian rRNA genes in vivo
Németh, A. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh732 · Cited by 64
Identification of DHX33 as a Mediator of rRNA Synthesis and Cell Growth
Zhang, Y., Forys, J. T., Miceli, A. P., Gwinn, A. S., & Weber, J. D. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05832-11 · Cited by 62
Nascent pre-rRNA overexpression correlates with an adverse prognosis in alveolar rhabdomyosarcoma
Williamson, D. S., Lu, Y., Fang, C., Pritchard‐Jones, K., & SHIPLEY, J. M. (2006) · Genes Chromosomes and Cancer · doi:10.1002/gcc.20347 · Cited by 63
The prognostic value of the AgNOR parameter in human breast cancer depends on the pRb and p53 status
Derenzini, M., Ceccarelli, C., Santini, D., Taffurelli, M., & Treré, D. (2004) · Journal of Clinical Pathology · doi:10.1136/jcp.2003.015917 · Cited by 62
40 Years of Research Put p53 in Translation
Marcel, V., Long, F. N. V., & Diaz, J. (2018) · Cancers · doi:10.3390/cancers10050152 · Cited by 61
Factors Responsible for Modulation of Ribosomal RNA Transcription
Wnuk, M., Słota, E., Kotylak, Z., & Bugno, M. (2006) · Folia Biologica · doi:10.3409/173491606777919184 · Cited by 60
Elevated expression of ribosomal protein genes L37, RPP-1, and S2 in the presence of mutant p53.
Loging, W., & Reisman, D. (1999) · PubMed · Cited by 58
The leukemogenic t(8;21) fusion protein AML1-ETO controls rRNA genes and associates with nucleolar-organizing regions at mitotic chromosomes
Bakshi, R., Zaidi, S. K., Pande, S., Hassan, M. Q., Young, D. W., Montecino, M. A., Lian, J. B., van Wijnen, A. J., Stein, J. L., & Stein, G. S. (2008) · Journal of Cell Science · doi:10.1242/jcs.033431 · Cited by 58
Function of basonuclin in increasing transcription of the ribosomal RNA genes during mouse oogenesis
Tian, Q., Kopf, G. S., Brown, R. S., & Tseng, H. (2001) · Development · doi:10.1242/dev.128.3.407 · Cited by 57
Nucleolar control of p53: a cellular Achilles’ heel and a target for cancer therapy
Vlatković, N., Boyd, M. T., & Rubbi, C. P. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1361-x · Cited by 54
Biological stoichiometry of tumor dynamics: Mathematical models and analysis
Kuang, Y., Nagy, J. D., & Elser, J. J. (2004) · Discrete and Continuous Dynamical Systems - B · doi:10.3934/dcdsb.2004.4.221 · Cited by 53
Expression of Eukaryotic Translation Initiation Factors 4E and 2 α Correlates with the Progression of Thyroid Carcinoma
Wang, S., Lloyd, R. V., Hutzler, M., Rosenwald, I. B., Safran, M., Patwardhan, N. A., & Khan, A. A. (2001) · Thyroid · doi:10.1089/10507250152740939 · Cited by 52
Different effects of ribosome biogenesis inhibition on cell proliferation in retinoblastoma protein‐ and p53‐deficient and proficient human osteosarcoma cell lines
Montanaro, L., Mazzini, G., Barbieri, S., Vici, M., Nardi-Pantoli, A., Govoni, M., Donati, G., Treré, D., & Derenzini, M. (2007) · Cell Proliferation · doi:10.1111/j.1365-2184.2007.00448.x · Cited by 50
Acetylation of UBF changes during the cell cycle and regulates the interaction of UBF with RNA polymerase I
Meraner, J. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl101 · Cited by 48
Bent bone dysplasia syndrome reveals nucleolar activity for FGFR2 in ribosomal DNA transcription.
Neben, C., Idoni, B., Salva, J. E., Tuzon, C. T., Rice, J., Krakow, D., & Merrill, A. E. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu282 · Cited by 35
Inhibition of the putative tumor suppressor gene TIMP-3 by tumor-derived p53 mutants and wild type p53
Loging, W., & Reisman, D. (1999) · Oncogene · doi:10.1038/sj.onc.1203135 · Cited by 41
P53-responsive genes and the potential for cancer diagnostics and therapeutics development
Xu, H. Y., & El-Gewely, M. R. (2001) · Biotechnology annual review · doi:10.1016/s1387-2656(01)07035-1 · Cited by 39
A Runx2-HDAC1 co-repressor complex regulates rRNA gene expression by modulating UBF acetylation
Ali, S. A., Dobson, J. R., Lian, J. B., Stein, J. L., van Wijnen, A. J., Zaidi, S. K., & Stein, G. S. (2012) · Journal of Cell Science · doi:10.1242/jcs.100909 · Cited by 41

Authors: Budde, A., & Grummt, I.
Affiliations: German Cancer Research Center (DE)
ORCID: Grummt, Ingrid
Venue: Oncogene
Publisher: Springer Science and Business Media LLC
Published: 1999-01-28
Volume: 18
Issue: 4
Pages: 1119-1124
ISSN: 0950-9232 (ISSN-L)
1476-5594
DOI: 10.1038/sj.onc.1202402
OpenAlex: W2076958652
Cited by: 157
References: 37
Citations by year: 2026: 2 · 2025: 3 · 2024: 1 · 2023: 1 · 2022: 1 · 2021: 5 · 2019: 6 · 2018: 6 · 2017: 5 · 2016: 5 · 2015: 4 · 2014: 13 · 2013: 10 · 2012: 7
FWCI: 2.97
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Oncogene (publishedVersion)
PubMed (publishedVersion)
Funders: Deutsche Forschungsgemeinschaft
Topics: Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
Keywords: p53, ribosomal DNA transcription, RNA polymerase I, pre-rRNA synthesis, transcriptional repression, tumor suppressor, growth arrest, mutant p53, p53 knockout mice, rDNA promoter, intergenic spacer, cell proliferation
MeSH terms: Animals, DNA, Ribosomal, RNA Polymerase I, RNA Precursors, Transcription, Genetic, Tumor Suppressor Protein p53, 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

p53 represses ribosomal gene transcription

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks