Cited by 1,921Cancer-related Molecular PathwaysGenomics and Chromatin DynamicsDNA Repair Mechanisms

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Transcriptional control of human p53-regulated genes

Riley, Todd, Sontag, Eduardo, Chen, Patricia, Levine, Arnold·2008·Nature Reviews Molecular Cell Biology

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Abstract

The p53 protein regulates the transcription of many different genes in response to a wide variety of stress signals. Following DNA damage, p53 regulates key processes, including DNA repair, cell-cycle arrest, senescence and apoptosis, in order to suppress cancer. This Analysis article provides an overview of the current knowledge of p53-regulated genes in these pathways and others, and the mechanisms of their regulation. In addition, we present the most comprehensive list so far of human p53-regulated genes and their experimentally validated, functional binding sites that confer p53 regulation.

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Self-citation
Surfing the p53 network
Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607 · cited 1×
“These include several types of DNA damage: telomere shortening, hypoxia, mitotic spindle damage, heat or cold shock, unfolded proteins, improper ribosomal biogenesis, nutritional deprivation in a transformed cell, and even the activation of some oncogenes by mutatio”
BackgroundSelf-citation
Profile hidden Markov models
Eddy, S. R. (1998) · Bioinformatics · doi:10.1093/bioinformatics/14.9.755 · Cited by 5,515
Sequence logos: a new way to display consensus sequences
Schneider, T. D., & Stephens, R. M. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.20.6097 · Cited by 3,354
Biological Sequence Analysis
Durbin, R. M., Eddy, S. R., Krogh, A., & Mitchison, G. (1998) · Cambridge University Press eBooks · doi:10.1017/cbo9780511790492 · Cited by 3,255
Activation of p53 Sequence-Specific DNA Binding by Acetylation of the p53 C-Terminal Domain
Gu, W., & Roeder, R. G. (1997) · Cell · doi:10.1016/s0092-8674(00)80521-8 · Cited by 2,559
Crystal Structure of a p53 Tumor Suppressor-DNA Complex: Understanding Tumorigenic Mutations
Cho, Y., Gorina, S., Jeffrey, P. D., & Pavletich, N. P. (1994) · Science · doi:10.1126/science.8023157 · Cited by 2,559 · cited 1×
“On the basis of X-ray crystallography studies of the p53 DNA-binding core domain bound to a p53-RE DNA sequence, the most important bases for interactions with the p53 protein are the central RCWWGY, which come into close contact with the amino acids from the p53 core domai”
Background
Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
Minucci, S., & Pelicci, P. G. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1779 · Cited by 2,234
Wild-type p53 induces apoptosis of myeloid leukaemic cells that is inhibited by interleukin-6
Yonish-Rouach, E., Resnftzky, D., Lotem, J., Sachs, L., Kimchi, A., & Oren, M. (1991) · Nature · doi:10.1038/352345a0 · Cited by 2,079
Maximum Entropy Modeling of Short Sequence Motifs with Applications to RNA Splicing Signals
Yeo, G. W.-M., & Burge, C. B. (2004) · Journal of Computational Biology · doi:10.1089/1066527041410418 · Cited by 2,042

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Meek, D. W., & Hupp, T. R. (2010) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2009.10.005 · Cited by 76
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Lee, Y., Kim, N. H., Cho, E. S., Yang, J. H., Cha, Y. H., Kang, H. E., Yun, J. S., Cho, S. B., Lee, S.-H., Paclíková, P., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04757-w · Cited by 74
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Katoh (2009) · International Journal of Oncology · doi:10.3892/ijo_00000514 · Cited by 76
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Tebaldi, T., Zaccara, S., Alessandrini, F., Bisio, A., Ciribilli, Y., & Inga, A. (2015) · BMC Genomics · doi:10.1186/s12864-015-1643-9 · Cited by 72
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Chen, H., Yuan, Y., Zhang, C., Luo, A., Ding, F., Ma, J., Yang, S., Tian, Y., Tong, T., Zhan, Q., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.326975 · Cited by 73
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Authors: Riley, T., Sontag, E., Chen, P., & Levine, A.
Affiliations: Institute for Advanced Study (US)
Rutgers, The State University of New Jersey (US)
Corresponding author: Riley, Todd
ORCID: Sontag, Eduardo
Chen, Patricia
Levine, Arnold
Venue: Nature Reviews Molecular Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2008-05
Volume: 9
Issue: 5
Pages: 402-412
ISSN: 1471-0072 (ISSN-L)
1471-0080
DOI: 10.1038/nrm2395
OpenAlex: W1964719993
Cited by: 1,921
References: 201
Citations by year: 2026: 36 · 2025: 45 · 2024: 56 · 2023: 73 · 2022: 85 · 2021: 97 · 2020: 79 · 2019: 92 · 2018: 110 · 2017: 134 · 2016: 131 · 2015: 115 · 2014: 154 · 2013: 143 · 2012: 153
FWCI: 12.97
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Reviews Molecular Cell Biology (publishedVersion)
PubMed (publishedVersion)
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 › DNA Repair Mechanisms
Keywords: p53, transcriptional regulation, p53 target genes, DNA damage response, DNA repair, cell cycle arrest, senescence, apoptosis, tumor suppression, transcription factor binding sites, stress signaling
MeSH terms: Base Sequence, Binding Sites, Cell Transformation, Neoplastic, DNA Damage, Gene Expression Regulation, Humans, Markov Chains, Molecular Sequence Data, Regulatory Sequences, Nucleic Acid, Transcription, Genetic, Signal Transduction, Genes, p53, Tumor Suppressor Protein p53, Response Elements, Regulatory Elements, Transcriptional

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Transcriptional control of human p53-regulated genes

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