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Chk2/hCds1 functions as a DNA damage checkpoint in G1by stabilizing p53
Open accessAbstract
Chk2/hcds1, the human homolog of the Saccharomyces cerevisiae RAD53/SPK1 and Schizosaccharomyces pombe cds1 DNA damage checkpoint genes, encodes a protein kinase that is post-translationally modified after DNA damage. Like its yeast homologs, the Chk2/hCds1 protein phosphorylates Cdc25C in vitro, suggesting that it arrests cells in G 2 in response to DNA damage. We expressed Chk2/hCds1 in human cells and analyzed their cell cycle profile. Wild-type, but not catalytically inactive, Chk2/hCds1 led to G 1 arrest after DNA damage. The arrest was inhibited by cotransfection of a dominant-negative p53 mutant, indicating that Chk2/hCds1 acted upstream of p53. In vitro, Chk2/hCds1 phosphorylated p53 on Ser-20 and dissociated preformed complexes of p53 with Mdm2, a protein that targets p53 for degradation. In vivo, ectopic expression of wild-type Chk2/hCds1 led to increased p53 stabilization after DNA damage, whereas expression of a dominant-negative Chk2/hCds1 mutant abrogated both phosphorylation of p53 on Ser-20 and p53 stabilization. Thus, in response to DNA damage, Chk2/hCds1 stabilizes the p53 tumor suppressor protein leading to cell cycle arrest in G 1.
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In the citing paper
“and hChk2, in turn, phosphorylates yet another amino-terminal Ser residue (Ser 20) in p53”
From Cell cycle checkpoint signaling through the ATM and ATR kinases (2001) · cites this paper as Chehab et al. 2000
In the citing paper
“These phosphorylation events contribute to disrupting the p53-Mdm2 (Chehab et al., 2000; Shieh et al., 2000), and Mdm2-DAXX (Tang et al., 2013) interactions, as well as to the degradation of Mdm2 and Mdm4 (Stommel and Wahl, 2004; Chen et al., 2005; Pereg et al., 2005, 2006; LeBron et al., 2006).”
From USP7 Is a Master Regulator of Genome Stability (2020) · cites this paper as Chehab et al., 2000
In the citing paper
“ATM also activates Chk2, which in turn phosphorylates p53 on serine 20 and inhibits MDM2 binding (Shieh et al, 1997;Banin et al, 1998;Chehab et al, 2000;Shieh et al, 2000).”
From ATM and Chk2-dependent phosphorylation of MDMX contribute to p53 activation after DNA damage (2005) · cites this paper as Chehab et al, 2000
In the citing paper
“Studies using Chk2-null mice, Chk2-null HCT116 cells, and Chk2 siRNA resulted in different conclusions (Zhang et al, 1998;Chehab et al, 2000;Shieh et al, 2000;Ahn et al, 2003; Jallepalli et al, 2003).”
From ATM and Chk2-dependent phosphorylation of MDMX contribute to p53 activation after DNA damage (2005) · cites this paper as Chehab et al, 2000
In the citing paper
“Although a role of ATM in p53 response is well established, the significance of Chk2 is still a matter of debate.”
From ATM and Chk2-dependent phosphorylation of MDMX contribute to p53 activation after DNA damage (2005) · cites this paper as Chehab et al, 2000
In the citing paper
“ATM also activates Chk2, which in turn phosphorylates p53 on S20, which is a part of the MDM2-binding site (Shieh et al, 1997(Shieh et al, , 2000;;Banin et al, 1998;Chehab et al, 2000).”
From ATM activates p53 by regulating MDM2 oligomerization and E3 processivity (2009) · cites this paper as Chehab et al, 2000
In the citing paper
“p53 is phosphorylated at Ser20 by the checkpoint kinase Chk2 after IR, which results in p53's dissociation from Mdm2 and its subsequent stabilization”
From USP10 Regulates p53 Localization and Stability by Deubiquitinating p53 (2010) · cites this paper as Chehab et al., 2000
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Citations
Cites
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
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
Participation of p53 protein in the cellular response to DNA damage.
Kastan, M. B., Onyekwere, O. C., Sidransky, D., Vogelstein, B., & Craig, R. W. (1991) · PubMed · Cited by 3,761
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 2×
“Stabilization of p53 in cells exposed to IR or UV light is due to dissociation from Mdm2 (Shieh et al. 1997), a protein that targets p53 for degradation through the ubiquitin pathway (Haupt et al. 1997; Kubbutat et al. 1997; Midgley and Lane 1997).”
BackgroundMomand, J., Zambetti, G. P., Olson, D. C., George, D., & Levine, A. J. (1992) · Cell · doi:10.1016/0092-8674(92)90644-r · Cited by 3,113
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
A Single Ataxia Telangiectasia Gene with a Product Similar to PI-3 Kinase
Savitsky, K., Bar-Shira, A., Gilad, S., Rotman, G., Ziv, Y., Vanagaite, L., Tagle, D. A., Smith, S., Uziel, T., Sfez, S., et al. (1995) · Science · doi:10.1126/science.7792600 · Cited by 2,785
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
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Lee, S. S., Vũ, T. T., Weiss, A. S., & Yeo, G. C. (2023) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2023.151331 · Cited by 43
Novel Insights into the Molecular Mechanisms Governing Mdm2 Ubiquitination and Destruction
Inuzuka, H., Fukushima, H., Shaik, S., & Wei, W. (2010) · Oncotarget · doi:10.18632/oncotarget.202 · Cited by 39
CHK2 stability is regulated by the E3 ubiquitin ligase SIAH2
García-Limones, C., Lara‐Chica, M., Jiménez‐Jiménez, C., Pérez, M., Moreno, P., Muñóz, E., & Calzado, M. A. (2016) · Oncogene · doi:10.1038/onc.2015.495 · Cited by 40
G1 and S-Phase Checkpoints, Chromosome Instability, and Cancer
Nojima, H. (2004) · Humana Press eBooks · doi:10.1385/1-59259-788-2:003 · Cited by 39
Characterization ofCHEK2 mutations in prostate cancer
Wu, X., Dong, X., Liu, W., & Chen, J. (2006) · Human Mutation · doi:10.1002/humu.20321 · Cited by 41
Lee, S. Y. (2003) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(03)00052-8 · Cited by 39
Jack, M. T., Woo, R. A., Motoyama, N., Takai, H., & Lee, P. W. K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309917200 · Cited by 39
Yong, K. J., Milenic, D. E., Baidoo, K. E., & Brechbiel, M. W. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17050736 · Cited by 38
Gene expression profiling assigns CHEK2 1100delC breast cancers to the luminal intrinsic subtypes
Nagel, J. H. A., Peeters, J. K., Smid, M., Sieuwerts, A. M., Wasielewski, M., de Weerd, V., Trapman-Jansen, A., van den Ouweland, A., Brüggenwirth, H. T., van IJcken, W. F. J., et al. (2011) · Breast Cancer Research and Treatment · doi:10.1007/s10549-011-1588-x · Cited by 39
Analysis of CHK2 in vulval neoplasia
Reddy, A., Yuille, M., Sullivan, A., Repellin, C. E., Bell, A., TIDY, J. A., Evans, D. J., Farrell, P. J., Gusterson, B. A., Gasco, M., et al. (2002) · British Journal of Cancer · doi:10.1038/sj.bjc.6600131 · Cited by 38
DNA damage-induced signalling in ataxia-telangiectasia and related syndromes
Lavin, M. F., & Kozlov, S. (2007) · Radiotherapy and Oncology · doi:10.1016/j.radonc.2007.04.032 · Cited by 40
Decision making of the p53 network: Death by integration
Li, Z., Ni, M., Li, J., Zhang, Y., Ouyang, Q., & Tang, C. (2010) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2010.11.041 · Cited by 39
Long Non-coding RNA Aerrie Controls DNA Damage Repair via YBX1 to Maintain Endothelial Cell Function
Pham, T. P., Bink, D. I., Stanicek, L., van Bergen, A. S., van Leeuwen, E., Tran, Y., Matic, L. P., Hedin, U., Wittig, I., Dimmeler, S., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.619079 · Cited by 37
Corp Regulates P53 in Drosophila melanogaster via a Negative Feedback Loop
Chakraborty, R., Li, Y., Zhou, L. J., & Golic, K. G. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005400 · Cited by 38
Alternative Splicing of CHEK2 and Codeletion with NF2 Promote Chromosomal Instability in Meningioma
Yang, H. W., Kim, T., Song, S. S., Shrinath, N., Park, R. W., Kalamarides, M., Park, P. J., Black, P. M., Carroll, R. S., & Johnson, M. D. (2012) · Neoplasia · doi:10.1593/neo.111574 · Cited by 37
Gupta, S. K., Guo, X., Durkin, S. S., Fryrear, K. A., Ward, M. D., & Semmes, O. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704110200 · Cited by 39
Mice with the CHEK2 *1100delC SNP are predisposed to cancer with a strong gender bias
Bahassi, E. M., Robbins, S. B., Yin, M., Boivin, G. P., Kuiper, R., STEEG, H. V., & Stambrook, P. J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909237106 · Cited by 38
Calenic, B., Yaegaki, K., Ishkitiev, N., Kumazawa, Y., Imai, T., & Tanaka, T. (2012) · Journal of Periodontal Research · doi:10.1111/jre.12011 · Cited by 37
Contribution of Growth and Cell Cycle Checkpoints to Radiation Survival in Drosophila
Jaklevic, B. R., Uyetake, L., Lemstra, W., Chang, J., Leary, W., Edwards, A., Vidwans, S. J., Sibon, O. C. M., & Su, T. T. (2006) · Genetics · doi:10.1534/genetics.106.064477 · Cited by 35
[Mitotic catastrophe: a special case of apoptosis].
Castedo, M., & Kroemer, G. (2004) · PubMed · Cited by 37
Yoshida, K., Oyaizu, N., Dutta, A., & Inoue, I. (2004) · Oncogene · doi:10.1038/sj.onc.1206987 · Cited by 37
The ATM regulated DNA damage response pathway as a chemo- and radiosensitisation target
Alao, J. P. (2009) · Expert Opinion on Drug Discovery · doi:10.1517/17460440902835475 · Cited by 36
Albert, E., & Laimins, L. A. (2020) · Viruses · doi:10.3390/v12070744 · Cited by 41
Regulation of the DNA Damage Response to DSBs by Post-Translational Modifications
Oberle, C., & Blattner, C. (2010) · Current Genomics · doi:10.2174/138920210791110979 · Cited by 37
Germline mutations in the CHEK2 kinase gene are associated with an increased risk of bladder cancer
Złowocka, E., Cybulski, C., Górski, B., Dębniak, T., Słojewski, M., Wokołorczyk, D., Serrano‐Fernández, P., Trubicka, J., van de Wetering, T., Sikorski, A., et al. (2007) · International Journal of Cancer · doi:10.1002/ijc.23099 · Cited by 36
DNA damage-induced cell-cycle phase regulation of p53 and p21waf1 in normal and ATM-defective cells
Delia, D., Fontanella, E., Ferrario, C., Chessa, L., & Mizutani, S. (2003) · Oncogene · doi:10.1038/sj.onc.1207086 · Cited by 36
Synthetic and Medicinal Chemistry Approaches Toward WEE1 Kinase Inhibitors and Its Degraders
Alli, V. J., Yadav, P., Suresh, V., & Jadav, S. S. (2023) · ACS Omega · doi:10.1021/acsomega.3c01558 · Cited by 35
Alterations of G1‐S checkpoint in chordoma
Naka, T., Boltze, C., Kuester, D., Schulz, T., Schneider‐Stock, R., Kellner, A., Samii, A., Herold, C., Ostertag, H., & Roessner, A. (2005) · Cancer · doi:10.1002/cncr.21296 · Cited by 35
The IGF-1R/AKT pathway determines cell fate in response to p53
Duan, L., & Maki, C. G. (2016) · Translational Cancer Research · doi:10.21037/tcr.2016.09.16 · Cited by 37
UVB-Induced p21 degradation promotes apoptosis of human keratinocytes
Lei, X., Liu, B., Han, W., Ming, M., & He, Y. (2010) · Photochemical & Photobiological Sciences · doi:10.1039/c0pp00244e · Cited by 34
Study of the cytolethal distending toxin (CDT)‐activated cell cycle checkpoint
Alby, F., Mazars, R., de Rycke, J., Guillou, E., Baldin, V., Darbon, J.-M., & Ducommun, B. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02205-0 · Cited by 38
Phenotype-Genotype Correlation in Familial Breast Cancer
Vargas, A. C., Reis-Filho, J. S., & Lakhani, S. R. (2011) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1007/s10911-011-9204-6 · Cited by 36
Involvement of dysregulated Wip1 in manganese-induced p53 signaling and neuronal apoptosis
Ma, X., Han, J., Wu, Q., Liu, H., Shi, S., Wang, C., Wang, Y., Xiao, J., Zhao, J., Jiang, J., et al. (2015) · Toxicology Letters · doi:10.1016/j.toxlet.2014.12.019 · Cited by 34
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
Sharma, S. K., & Münger, K. (2020) · mBio · doi:10.1128/mbio.01190-20 · Cited by 34
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
Yan, T., Seo, Y., Schupp, J. E., Zeng, X., Desai, A. B., & Kinsella, T. J. (2006) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-05-0364 · Cited by 34
Limited role of N-terminal phosphoserine residues in the activation of transcription by p53
Jackson, M. W., Agarwal, M. K., Agarwal, M. L., Agarwal, A. M., Stanhope-Baker, P., Williams, B. R. G., & Stark, G. R. (2004) · Oncogene · doi:10.1038/sj.onc.1207575 · Cited by 33
Analysis of the CHK2 Gene in Lymphoid Malignancies
Tavor, S., Takeuchi, S., Tsukasaki, K., Miller, C. W., Hofmann, W. K., Ikezoe, T., SAID, J. W., & Koeffler, H. P. (2001) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428190109064610 · 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
Hollingworth, R., Horniblow, R. D., Forrest, C., Stewart, G. S., & Grand, R. J. A. (2017) · Journal of Virology · doi:10.1128/jvi.00930-17 · Cited by 34
Teer, J. K., Machida, Y., Labit, H., Novac, O., Hyrien, O., Marheineke, K., Zannis‐Hadjopoulos, M., & Dutta, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m507150200 · Cited by 32
Low Frequency of CHEK2 Mutations in Familial Pancreatic Cancer
Bartsch, D. K., Krysewski, K., Sina‐Frey, M., Fendrich, V., Rieder, H., Langer, P., Kress, R., Schneider, M., Hahn, S. A., & Slater, E. P. (2006) · Familial Cancer · doi:10.1007/s10689-006-7850-4 · Cited by 33
Scott, S., O’Sullivan, M., Hafizi, S., Shapiro, L. M., & Bennett, M. R. (2002) · Circulation Research · doi:10.1161/hh0402.105900 · Cited by 33
Takagi, M. (2003) · Blood · doi:10.1182/blood-2003-01-0094 · Cited by 33
Matz, R. L., Erickson, B. W., Vaidyanathan, S., Kukowska‐Latallo, J. F., Baker, J. R., Orr, B. G., & Holl, M. M. B. (2013) · Molecular Pharmaceutics · doi:10.1021/mp300470d · Cited by 32
Effects of hyperthermia on p53 protein expression and activity
Guan, J., Stavridi, E. S., Leeper, D. B., & Iliakis, G. E. (2002) · Journal of Cellular Physiology · doi:10.1002/jcp.10069 · Cited by 30
Molecular interactions of polo-like kinase 1 in human cancers
Ng, W., Shin, J., Roberts, T. L., Wang, B., & Lee, C. S. (2016) · Journal of Clinical Pathology · doi:10.1136/jclinpath-2016-203656 · Cited by 33
Stability of Checkpoint Kinase 2 Is Regulated via Phosphorylation at Serine 456
Kass, E. M., Ahn, J., Tanaka, T., Freed-Pastor, W. A., Keezer, S. M., & Prives, C. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704642200 · Cited by 31
Growing and dividing: how O-GlcNAcylation leads the way
Saunders, H. I., Dias, W. B., & Slawson, C. M. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105330 · Cited by 30
Nucleotide excision repair- and p53-deficient mouse models in cancer research
Hoogervorst, E. M., STEEG, H. V., & de Vries, A. (2005) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2005.01.018 · Cited by 31
CHK2 kinase promotes pre-mRNA splicing via phosphorylating CDK11p110
Choi, H. J., Choi, H.-K., Jung, S. Y., Hyle, J. W., Kim, B., Yoon, K., Cho, E., Youn, H.-D., Lahti, J. M., Qin, J., et al. (2012) · Oncogene · doi:10.1038/onc.2012.535 · Cited by 32
Oishi, I., Iwai, K., Kagohashi, Y., Fujimoto, H., Kariya, K., Kataoka, T., Sawa, H., Okano, H., Otani, H., Yamamura, H., et al. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.4.1329-1335.2001 · Cited by 31
Contribution of the CHEK2 1100delC variant to risk of multiple colorectal adenoma and carcinoma
Lipton, L. R., Fleischmann, C., Sieber, O. M., Thomas, H. J. W., Hodgson, S. V., Tomlinson, I. P. M., & Houlston, R. S. (2003) · Cancer Letters · doi:10.1016/s0304-3835(03)00391-4 · Cited by 31
Stochastic and Deterministic Models of Cellular p53 Regulation
Leenders, G. B., & Tuszyński, J. A. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00064 · Cited by 28
Interplay Between the Cell Cycle and Double-Strand Break Response in Mammalian Cells
Beishline, K., & Azizkhan‐Clifford, J. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-0888-2_3 · Cited by 31
Kang, H., Lim, J. W., & Kim, H. (2018) · Journal of Ginseng Research · doi:10.1016/j.jgr.2018.08.003 · Cited by 30
Wang, N., Ding, H., Liu, C., Li, X., Wei, L., Yu, J., Liu, M., Ying, M., Gao, W., Jiang, H., et al. (2015) · Oncogene · doi:10.1038/onc.2014.443 · Cited by 28
Tian, H., Faje, A. T., Lee, S. L., & Jorgensen, T. J. (2002) · Neoplasia · doi:10.1038/sj.neo.7900219 · Cited by 30
Nishimura, K., Makino, S., Tanaka, Y., Kaneda, T., & Hashimoto, K. (2004) · Journal of Neuroendocrinology · doi:10.1111/j.1365-2826.2004.01131.x · Cited by 28
14‐3‐3 proteins integrate E2F activity with the DNA damage response
Milton, A. H., Khaire, N., Ingram, L., O'donnell, A. J., & Thangue, N. B. L. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7600999 · Cited by 29
Cordes, N., & Beuningen, D. V. (2004) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2003.09.069 · Cited by 29
Pike, B. L., Hammet, A., & Heierhorst, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009558200 · Cited by 28
Bean, L. J., & Stark, G. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108881200 · Cited by 29
p53 functional assays: detecting p53 mutations in both the germline and in sporadic tumours
Camplejohn, R. S., & Rutherford, J. (2001) · Cell Proliferation · doi:10.1046/j.1365-2184.2001.00193.x · Cited by 29
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
Zhao, X., Guo, X., Xing, L., Yue, W., Yin, H., He, M., Wang, J., Yang, J., & Chen, J. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0097-1 · Cited by 27
Synergism Through WEE1 and CHK1 Inhibition in Acute Lymphoblastic Leukemia
di Rorà, A. G. L., Bocconcelli, M., Ferrari, A., Terragna, C., Bruno, S., Imbrogno, E., Beeharry, N., Robustelli, V., Ghetti, M., Napolitano, R., et al. (2019) · Cancers · doi:10.3390/cancers11111654 · Cited by 29
RETRACTED: Oxaliplatin responses in colorectal cancer cells are modulated by CHK2 kinase inhibitors
Pires, I. M., Ward, T. H., & Dive, C. (2010) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00607.x · Cited by 29
RetractedNevirapine induces growth arrest and premature senescence in human cervical carcinoma cells
Stefanidis, K., Loutradis, D., Vassiliou, L. V., Anastasiadou, V., Kiapekou, E., Nikas, V., Patris, G., Vlachos, G. D., Rodolakis, A., & Antsaklis, A. J. (2008) · Gynecologic Oncology · doi:10.1016/j.ygyno.2008.08.006 · Cited by 28
Increased expression of CHK2 in human gastric carcinomas harboring p53 mutations
Shigeishi, H., Yokozaki, H., Oue, N., Kuniyasu, H., Kondo, T., Ishikawa, T., & Yasui, W. (2002) · International Journal of Cancer · doi:10.1002/ijc.10272 · Cited by 30
Running into problems: how cells cope with replicating damaged DNA
McGowan, C. H. (2003) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2003.08.011 · Cited by 28
The Transcriptional Program following p53 ActivationPreprint
Zhao, R., Gish, K., Murphy, M. E., Yin, Y., Notterman, D. A., HOFFMAN, W. H., Tom, E., Mack, D. H., & Levine, A. J. (2000) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2000.65.475 · Cited by 28
Chk2 Oligomerization Studied by Phosphopeptide Ligation
Li, J., Taylor, I. A., Lloyd, J., Clapperton, J. A., Howell, S. A., Macmillan, D., & Smerdon, S. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804075200 · Cited by 26
Wu, Q., Chen, Y., Fu, J., You, Q., Wang, S., Huang, X. S., Feng, X., & Zhang, S. (2014) · Cellular Oncology · doi:10.1007/s13402-014-0199-z · Cited by 27
Nagata, K., Izawa, I., & Inagaki, M. (2001) · Genes to Cells · doi:10.1046/j.1365-2443.2001.00454.x · Cited by 27
Kato, N., Fujimoto, H., Yoda, A., Oishi, I., Matsumura, N., Kondo, T., Tsukada, J., Tanaka, Y., Imamura, M., & Minami, Y. (2004) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401461 · Cited by 27
Dynamics of DNA Damage Induced Pathways to Cancer
Tian, K., Rajendran, R., Doddananjaiah, M., Krstic–Demonacos, M., & Schwartz, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072303 · Cited by 26
CHEK2 mutations in primary glioblastomas
Sallinen, S., konen, T., Haapasalo, H. K., & Schleutker, J. (2005) · Journal of Neuro-Oncology · doi:10.1007/s11060-005-5953-7 · Cited by 26
Barkley, L. R., Song, I. Y., Zou, Y., & Vaziri, C. (2009) · Cell Cycle · doi:10.4161/cc.8.10.8535 · Cited by 25
Ensuring the Stability of the Genome: DNA Damage Checkpoints
Latif, C., Harvey, S. H., & O'Connell, S. J. (2001) · The Scientific World JOURNAL · doi:10.1100/tsw.2001.297 · Cited by 26
Tischkowitz, M. D., Yılmaz, A. U., Chen, L. Q., Karyadi, D. M., Novak, D. J., Kirchhoff, T., Hamel, N., Tavtigian, S. V., Kolb, S., Bismar, T. A., et al. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.05.006 · Cited by 26
DNA replication blockade impairs p53-transactivation
Takimoto, R., & El‐Deiry, W. S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.3.781 · Cited by 26
The DNA Damage Checkpoint and Human CancerPreprint
Schultz, L. B., Chehab, N. H., Malikzay, A., DiTullio, R. A., Stavridi, E. S., & Halazonetis, T. D. (2000) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2000.65.489 · Cited by 26
Self-citationSanjiv, K., Su, T., Suman, S., Kakadiya, R., Lai, T., Wang, H.-W., Hsiao, M., & Lee, T. (2011) · International Journal of Cancer · doi:10.1002/ijc.26142 · Cited by 26
Myer, D. L., Robbins, S. B., Yin, M., Boivin, G. P., Liu, Y., Greis, K. D., Bahassi, E. M., & Stambrook, P. J. (2011) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2011.02.006 · Cited by 25
Rashid, M. U., Muhammad, N., Faisal, S., Amin, A., & Hamann, U. (2013) · BMC Cancer · doi:10.1186/1471-2407-13-312 · Cited by 26
Pharmacological inhibition of ATM by KU55933 stimulates ATM transcription
Khalil, H. S., Tummala, H., Hupp, T. R., & Zhelev, N. (2012) · Experimental Biology and Medicine · doi:10.1258/ebm.2012.011378 · Cited by 25
Chen, Y., Miao, Z., Zhao, W., & Ding, J. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.05.053 · Cited by 25
Essers, P., Pereboom, T. C., Goos, Y. J., Paridaen, J. T. M. L., & MacInnes, A. W. (2013) · Developmental Biology · doi:10.1016/j.ydbio.2013.10.029 · Cited by 25
Identification of CGI-121, a novel PRPK (p53-related protein kinase)-binding protein
Miyoshi, A., Kito, K., Aramoto, T., Abe, Y., Kobayashi, N., & Ueda, N. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00333-4 · Cited by 25
Chk2 splice variants express a dominant-negative effect on the wild-type Chk2 kinase activity
Berge, E. O., Staalesen, V., Straume, A. H., Lillehaug, J. R., & Lønning, P. E. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.01.005 · Cited by 27
Déry, U., & Masson, J. (2007) · DNA repair · doi:10.1016/j.dnarep.2006.12.009 · Cited by 27
Bahassi, E. M., Penner, C. G., Robbins, S. B., Tichy, E. D., Feliciano, E., Yin, M., Liang, L., Deng, L., Tischfield, J. A., & Stambrook, P. J. (2006) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2006.11.025 · Cited by 26
Regulation of p53 after Different Forms of Stress and at Different Cell Cycle StagesPreprint
Gottifredi, V., Shieh, S.-Y., & Prives, C. L. (2000) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2000.65.483 · Cited by 25
Tan, Y., Chen, Y., Yu, L., Zhu, H., Meng, X., Huang, X., Meng, L., Ding, M., Wang, Z., & Shan, L. (2010) · Cell Proliferation · doi:10.1111/j.1365-2184.2010.00699.x · Cited by 24
Ross, A. D. M., Cook, M. G., Chong, H., Hossain, M., Pandha, H., & Bennett, D. C. (2012) · Pigment Cell & Melanoma Research · doi:10.1111/pcmr.12060 · Cited by 27
Zhang, P., Gao, W., Li, H., Reed, E., & Chen, F. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.01.007 · Cited by 24
Zoppoli, G. M., Solier, S., Reinhold, W. C., Liu, H., Connelly, J. W., Monks, A. P., Shoemaker, R. H., Abaan, O. D., Davis, S. R., Meltzer, P. S., et al. (2011) · Oncogene · doi:10.1038/onc.2011.283 · Cited by 23
DNA damage response and hematological malignancy
Takagi, M. (2017) · International Journal of Hematology · doi:10.1007/s12185-017-2226-0 · Cited by 24
Metadata
- Authors
- Chehab, N. H., Malikzay, A., Appel, M., & Halazonetis, T. D.
- Affiliations
- The Wistar Institute (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2000-02-01
- Volume
- 14
- Issue
- 3
- Pages
- 278-288
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC316357
- OpenAlex
- W2131833681
- Cited by
- 805
- References
- 86
- Citations by year
- 2026: 8 · 2025: 5 · 2024: 8 · 2023: 11 · 2022: 19 · 2021: 17 · 2020: 18 · 2019: 11 · 2018: 11 · 2017: 10 · 2016: 25 · 2015: 16 · 2014: 28 · 2013: 27 · 2012: 29
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Cancer Society
- National Institutes of Health (CA-25874)
- National Cancer Institute (CA09171, CA-25874, CA-76367, R01CA076367, P01CA025874, T32CA009171)
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- Chk2, DNA damage checkpoint, p53 stabilization, MDM2, G1 cell cycle arrest, Cdc25C phosphorylation, post-translational modification, tumor suppressor proteins, dominant-negative mutant
- MeSH terms
- DNA Damage, Humans, Nuclear Proteins, Phosphorylation, Protein Kinases, Proto-Oncogene Proteins, Tumor Cells, Cultured, Tumor Suppressor Protein p53, G1 Phase, Protein Serine-Threonine Kinases, Schizosaccharomyces pombe Proteins, Proto-Oncogene Proteins c-mdm2, Checkpoint Kinase 2
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