Cited by 1,705DNA Repair MechanismsCancer-related Molecular PathwaysUbiquitin and proteasome pathways

The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.

The DNA Damage Response: Ten Years After

Open access

Harper, J. Wade, Elledge, Stephen J.·2007·Molecular Cell

DOI 10.1016/j.molcel.2007.11.015

Open this paper in CoChat — free account Open PDF

Abstract

The DNA damage response (DDR), through the action of sensors, transducers, and effectors, orchestrates the appropriate repair of DNA damage and resolution of DNA replication problems, coordinating these processes with ongoing cellular physiology. In the past decade, we have witnessed an explosion in understanding of DNA damage sensing, signaling, and the complex interplay between protein phosphorylation and the ubiquitin pathway employed by the DDR network to execute the response to DNA damage. These findings have important implications for aging and cancer.

Integrity signals

Registry

Crossref · 10.1016/j.molcel.2007.11.015

Cites

44 of 44 references verified0 citation errors · 0 not checkable

Statistics

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

Claims the paper makes

We couldn’t retrieve this paper’s full text, 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?

DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139
Rogakou, E. P., Pilch, D. R., Orr, A. H., Ivanova, V. S., & Bonner, W. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.10.5858 · Cited by 5,438
DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation
Bakkenist, C. J., & Kastan, M. B. (2003) · Nature · doi:10.1038/nature01368 · Cited by 3,466
ATM and ATR Substrate Analysis Reveals Extensive Protein Networks Responsive to DNA Damage
Matsuoka, S., Ballif, B. A., Smogorzewska, A., McDonald, E. R., Hurov, K. E., Luo, J., Bakalarski, C. E., Zhao, Z., Solimini, N., Lerenthal, Y., et al. (2007) · Science · doi:10.1126/science.1140321 · Cited by 3,075
Self-citation
Sensing DNA Damage Through ATRIP Recognition of RPA-ssDNA Complexes
Zou, L., & Elledge, S. J. (2003) · Science · doi:10.1126/science.1083430 · Cited by 2,693
Self-citation
Cell Cycle Checkpoints: Preventing an Identity Crisis
Elledge, S. J. (1996) · Science · doi:10.1126/science.274.5293.1664 · Cited by 2,050
Self-citation
PCNA, the Maestro of the Replication Fork
Moldovan, G.-L., Pfander, B., & Jentsch, S. (2007) · Cell · doi:10.1016/j.cell.2007.05.003 · Cited by 1,796
ATM Activation by DNA Double-Strand Breaks Through the Mre11-Rad50-Nbs1 Complex
Lee, J.-H., & Paull, T. T. (2005) · Science · doi:10.1126/science.1108297 · Cited by 1,424
RNF8 Ubiquitylates Histones at DNA Double-Strand Breaks and Promotes Assembly of Repair Proteins
Mailand, N., Bekker‐Jensen, S., Kildegaard, H. F., Melander, F., Bártek, J., Lukas, C., & Lukas, J. (2007) · Cell · doi:10.1016/j.cell.2007.09.040 · Cited by 1,193
Molecular mechanism of nucleotide excision repair
de Laat, W. L., Jaspers, N. G. J., & Hoeijmakers, J. H. J. (1999) · Genes & Development · doi:10.1101/gad.13.7.768 · Cited by 1,122
Histone acetyltransferase complexes: one size doesn't fit all
Lee, K. K. W., & Workman, J. L. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2145 · Cited by 1,091

Flagged first, then by citations

Show all 44 references

Sorted by citations

Items 501–600 of 1,003

DNA damage repair pathway alterations in metastatic clear cell renal cell carcinoma and implications on systemic therapy
Ged, Y. M. A., Chaim, J. L., DiNatale, R. G., Knežević, A., Kotecha, R. R., Carlo, M. I., Lee, C., Foster, A., Feldman, D. R., Teo, M. Y., et al. (2020) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2019-000230 · Cited by 52
An ATM/TRIM37/NEMO Axis Counteracts Genotoxicity by Activating Nuclear-to-Cytoplasmic NF-κB Signaling
Wu, G., Song, L., Zhu, J., Hu, Y., Cao, L., Tan, Z., Zhang, S., Li, Z., & Li, J. (2018) · Cancer Research · doi:10.1158/0008-5472.can-18-2063 · Cited by 52
Epigenetic Alterations under Oxidative Stress in Stem Cells
Huang, M., Wu, Q., & Jiang, Z. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/6439097 · Cited by 50
Elevated Levels of the Polo Kinase Cdc5 Override the Mec1/ATR Checkpoint in Budding Yeast by Acting at Different Steps of the Signaling Pathway
Donnianni, R. A., Ferrari, M., Lazzaro, F., Clerici, M., Nachimuthu, B. T., Plevani, P., Muzi-Falconi, M., & Pellicioli, A. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1000763 · Cited by 50
Histone Post-Translational Modifications in DNA Damage Response
Méndez-Acuña, L., Tomaso, M. V. D., Palitti, F., & Martínez‐López, W. (2010) · Cytogenetic and Genome Research · doi:10.1159/000296275 · Cited by 49
BRCT domains: A little more than kin, and less than kind
Gerloff, D. L., Woods, N. T., Farago, A. A., & Monteiro, Á. N. A. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.05.005 · Cited by 51
Nutlins and Ionizing Radiation in Cancer Therapy
Impicciatore, G. G., Sancilio, S., Miscia, S., & Pietro, R. D. (2010) · Current Pharmaceutical Design · doi:10.2174/138161210791033932 · Cited by 50
Intrauterine programming of ageing
Fernández-Capetillo, Ó. (2009) · EMBO Reports · doi:10.1038/embor.2009.262 · Cited by 51
Noncanonical E2 Variant-Independent Function of UBC13 in Promoting Checkpoint Protein Assembly
Huen, M. S. Y., Huang, J., Yuan, J., Yamamoto, M., Akira, S., Ashley, C., Xiao, W., & Chen, J. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00987-08 · Cited by 49
MicroRNAs Used in Combination with Anti-Cancer Treatments Can Enhance Therapy Efficacy
Mognato, M., & Celotti, L. (2015) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557515666150709115355 · Cited by 50
Coordinated Activity of Y Family TLS Polymerases and EXO1 Protects Non-S Phase Cells from UV-Induced Cytotoxic Lesions
Sertic, S., Mollica, A., Campus, I., Roma, S., Tumini, E., Aguilera, A., & Muzi-Falconi, M. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.02.017 · Cited by 45
The Functions of DNA Damage Factor RNF8 in the Pathogenesis and Progression of Cancer
Zhou, T., Yi, F., Wang, Z., Guo, Q., Liu, J., Bai, N., Li, X., Dong, X. D., Ren, L., Cao, L., et al. (2019) · International Journal of Biological Sciences · doi:10.7150/ijbs.31972 · Cited by 49
ADP‐ribosylation of histone variant H2AX promotes base excision repair
Chen, Q., Bian, C., Wang, X., Liu, X., Kassab, M. A., Yu, Y., & Yu, X. (2020) · The EMBO Journal · doi:10.15252/embj.2020104542 · Cited by 49
Nemo-like kinase is critical for p53 stabilization and function in response to DNA damage
Zhang, H.-H., Li, S.-Z., Zhang, Z.-Y., Hu, X.-M., Hou, P.-N., Gao, L., Du, R.-L., & Zhang, X. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.78 · Cited by 47
ARTD2 activity is stimulated by RNA
Léger, K., Bär, D., Savić, N., Santoro, R., & Hottiger, M. O. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku131 · Cited by 47
UbcH7 regulates 53BP1 stability and DSB repair
Han, X., Zhang, L., Chung, J., Pozo, F. M., Tran, A. P., Seachrist, D. D., Jacobberger, J. W., Keri, R. A., Gilmore, H. L., & Zhang, Y. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1408538111 · Cited by 48
RETRACTED: Loss of CCDC6, the First Identified RET Partner Gene, Affects pH2AX S139 Levels and Accelerates Mitotic Entry upon DNA Damage
Merolla, F., Luise, C., Muller, M. T., Pacelli, R., Fusco, A., & Celetti, A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036177 · Cited by 48
Retracted
A screen for deubiquitinating enzymes involved in the G2/M checkpoint identifies USP50 as a regulator of HSP90-dependent Wee1 stability
Aressy, B., Jullien, D., Cazalès, M., Marcellin, M., Bugler, B., Burlet‐Schiltz, O., & Ducommun, B. (2010) · Cell Cycle · doi:10.4161/cc.9.18.13133 · Cited by 48
A Network of Conserved Damage Survival Pathways Revealed by a Genomic RNAi Screen
Ravi, D., Wiles, A. M., Selvaraj, B., Ruan, J., Leder, P., & Bishop, A. J. R. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000527 · Cited by 47
Guardian of the Human Genome: Host Defense Mechanisms against LINE-1 Retrotransposition
Ariumi, Y. (2016) · Frontiers in Chemistry · doi:10.3389/fchem.2016.00028 · Cited by 55
p53 and RAD9, the DNA Damage Response, and Regulation of Transcription Networks
Lieberman, H. B., Panigrahi, S. K., Hopkins, K. M., Wang, L., & Broustas, C. G. (2017) · Radiation Research · doi:10.1667/rr003cc.1 · Cited by 47
A20/TNFAIP3 Regulates the DNA Damage Response and Mediates Tumor Cell Resistance to DNA-Damaging Therapy
Yang, C., Zang, W., Tang, Z., Ji, Y., Xu, R., Yang, Y., Luo, A., Hu, B., Zhang, Z., Liu, Z., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-2143 · Cited by 50
The role of p38 MAPK pathway in p53 compromised state and telomere mediated DNA damage response
Roy, S., Roy, S., Rana, A., Akhter, Y., Hande, M. P., & Banerjee, B. (2018) · Mutation Research/Genetic Toxicology and Environmental Mutagenesis · doi:10.1016/j.mrgentox.2018.05.018 · Cited by 48
Cancer molecular biology and strategies for the design of cytotoxic gold( i ) and gold( iii ) complexes: a tutorial review
Westhuizen, D., Bezuidenhout, D. I., & Munro, O. Q. (2021) · Dalton Transactions · doi:10.1039/d1dt02783b · Cited by 49
Integrator3, a Partner of Single-stranded DNA-binding Protein 1, Participates in the DNA Damage Response
Zhang, F., Wu, J., & Yu, X. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.039404 · Cited by 51
Cryo-EM Structure of human ATR-ATRIP complex
Rao, Q., Liu, M., Tian, Y., Wu, Z., Wang, H., Wang, J., & Xu, Y. (2017) · Worldwide Protein Data Bank · doi:10.2210/pdb5yz0/pdb · Cited by 49
Pharmacological Targeting of Senescence with Senolytics as a New Therapeutic Strategy for Neurodegeneration
Richardson, M., & Richardson, D. R. (2023) · Molecular Pharmacology · doi:10.1124/molpharm.123.000803 · Cited by 48
Hypoxia Enhances the Radioresistance of Mouse Mesenchymal Stromal Cells
Sugrue, T., Lowndes, N. F., & Ceredig, R. (2014) · Stem Cells · doi:10.1002/stem.1683 · Cited by 49
Speckle-type POZ protein, SPOP, is involved in the DNA damage response
Zhang, D., Wang, H., Sun, M., Yang, J., Zhang, W., Han, S., & Xu, B. (2014) · Carcinogenesis · doi:10.1093/carcin/bgu022 · Cited by 48
Early steps of double-strand break repair in Bacillus subtilis
Alonso, J. C., Cárdenas, P. P., Sánchez, H., Hejna, J., Suzuki, Y., & Takeyasu, K. (2013) · DNA repair · doi:10.1016/j.dnarep.2012.12.005 · Cited by 52
The RSF1 Histone-Remodelling Factor Facilitates DNA Double-Strand Break Repair by Recruiting Centromeric and Fanconi Anaemia Proteins
Pessina, F., & Lowndes, N. F. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1001856 · Cited by 48
The Menin Tumor Suppressor Protein Is Phosphorylated in Response to DNA Damage
Francis, J. M., Lin, W., Rozenblatt–Rosen, O., & Meyerson, M. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016119 · Cited by 50
Targeting Nonhomologous End-Joining Through Epidermal Growth Factor Receptor Inhibition: Rationale and Strategies for Radiosensitization
Mukherjee, B., Choy, H., Nirodi, C. S., & Burma, S. (2010) · Seminars in Radiation Oncology · doi:10.1016/j.semradonc.2010.05.002 · Cited by 48
Prolonged pemetrexed pretreatment augments persistence of cisplatin-induced DNA damage and eliminates resistant lung cancer stem-like cells associated with EMT
Tièche, C. C., Peng, R., Dorn, P., Froment, L., Schmid, R. A., & Marti, T. M. (2016) · BMC Cancer · doi:10.1186/s12885-016-2117-4 · Cited by 47
Zscan4 Is Activated after Telomere Shortening in Mouse Embryonic Stem Cells
Nakai, Y., & Niwa, H. (2016) · Stem Cell Reports · doi:10.1016/j.stemcr.2016.02.010 · Cited by 47
Modulation of DNA double-strand break repair as a strategy to improve precise genome editing
Ray, U., & Raghavan, S. C. (2020) · Oncogene · doi:10.1038/s41388-020-01445-2 · Cited by 46
Pre-mRNA Processing Factors and Retinitis Pigmentosa: RNA Splicing and Beyond
Yang, C., Γεωργίου, Μ., Atkinson, R., Collin, J., Al-Aama, J. Y., Nagaraja‐Grellscheid, S., Johnson, C. A., Ali, R. R., Armstrong, L., Mozaffari‐Jovin, S., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.700276 · Cited by 49
Apalutamide, Darolutamide and Enzalutamide for Nonmetastatic Castration-Resistant Prostate Cancer (nmCRPC): A Critical Review
Cattrini, C., Caffo, O., Giorgi, U. D., Mennitto, A., Gennari, A., Olmos, D., & Castro, E. (2022) · Cancers · doi:10.3390/cancers14071792 · Cited by 47
ATR- and ATM-Mediated DNA Damage Response Is Dependent on Excision Repair Assembly during G1 but Not in S Phase of Cell Cycle
Ray, A., Blevins, C., Wani, G., & Wani, A. A. (2016) · PLOS ONE · doi:10.1371/journal.pone.0159344 · Cited by 44
Integrative Analysis of Cancer-Related Signaling Pathways
Keßler, T., Hache, H., & Wierling, C. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00124 · Cited by 54
DNA Damage-Induced Phosphorylation of TRF2 Is Required for the Fast Pathway of DNA Double-Strand Break Repair
Huda, N., Tanaka, H., Mendonca, M. S., & Gilley, D. P. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00944-08 · Cited by 46
Non-telomeric activities of telomerase
Majerská, J., Sýkorová, E., & Fajkus, J. (2011) · Molecular BioSystems · doi:10.1039/c0mb00268b · Cited by 47
Rtt107 Is Required for Recruitment of the SMC5/6 Complex to DNA Double Strand Breaks
Leung, G. P., Lee, L., Schmidt, T. I., Shirahige, K., & Kobor, M. S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.235200 · Cited by 46
PKC signaling prevents irradiation-induced apoptosis of primary human fibroblasts
Bluwstein, A., Kumar, N., Léger, K., Traenkle, J., van Oostrum, J., Rehrauer, H., Baudis, M., & Hottiger, M. O. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.15 · Cited by 47
Human INO80 chromatin-remodelling complex contributes to DNA double-strand break repair via the expression of Rad54B and XRCC3 genes
Park, E., Hur, S.-K., & Kwon, J. (2010) · Biochemical Journal · doi:10.1042/bj20100988 · Cited by 46
Making Epidermal Bladder Cells Bigger: Developmental- and Salinity-Induced Endopolyploidy in a Model Halophyte
Barkla, B. J., Rhodes, T., Tran, K.-N., Wijesinghege, C., Larkin, J. C., & Dassanayake, M. (2018) · PLANT PHYSIOLOGY · doi:10.1104/pp.18.00033 · Cited by 46
Regulating BRCA1 protein stability by cathepsin S-mediated ubiquitin degradation
Kim, S., Jin, H. K., Seo, H. R., Lee, H. J., & Lee, Y. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0153-0 · Cited by 47
BRCA2 deficiency is a potential driver for human primary ovarian insufficiency
Miao, Y., Wang, P., Xie, B., Yang, M., Li, S., Cui, Z., Fan, Y., Li, M., & Xiong, B. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1720-0 · Cited by 46
Targeting the DNA Damage Response for the Treatment of High Risk Neuroblastoma
Southgate, H. E. D., Chen, L., Curtin, N. J., & Tweddle, D. A. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00371 · Cited by 48
The Ku complex: recent advances and emerging roles outside of non-homologous end-joining
Abbasi, S., Parmar, G., Kelly, R. D., Balasuriya, N., & Schild‐Poulter, C. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03801-1 · Cited by 48
Mechanisms of ATR-mediated checkpoint signalling
Smits, V. A. J. (2010) · Frontiers in bioscience · doi:10.2741/3649 · Cited by 46
Wip1 phosphatase in breast cancer
Emelyanov, A., & Bulavin, D. V. (2014) · Oncogene · doi:10.1038/onc.2014.375 · Cited by 47
Proteolysis of Rad17 by Cdh1/APC regulates checkpoint termination and recovery from genotoxic stress
Zhang, L., Park, C.-H., Wu, J., Kim, H., Liu, W., Fujita, T., Balasubramani, M., Schreiber, E. M., Wang, X.-F., & Wan, Y. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.55 · Cited by 44
Chk1 suppressed cell death
Meuth, M. (2010) · Cell Division · doi:10.1186/1747-1028-5-21 · Cited by 44
PTIP Regulates 53BP1 and SMC1 at the DNA Damage Sites
Wu, J., Prindle, M. J., Dressler, G. R., & Yu, X. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.002527 · Cited by 46
DNA Polymerase η, a Key Protein in Translesion Synthesis in Human Cells
Cruet-Hennequart, S., Gallagher, K., Sokòl, A. M., Villalan, S., Prendergast, Á. M., & Carty, M. P. (2009) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-90-481-3471-7_10 · Cited by 47
Take your PIKK: tumour viruses and DNA damage response pathways
Pancholi, N. J., Price, A. M., & Weitzman, M. D. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0269 · Cited by 44
Staphylococcus aureus induces DNA damage in host cell
Deplanche, M., Mouhali, N., Nguyen, M., Cauty, C., Ezan, F., Diot, A., Raulin, L., Dutertre, S., Langouët, S., Legembre, P., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-44213-3 · Cited by 47
PKC-SWI6 signaling regulates asexual development, cell wall integrity, stress response, and lifestyle transition in the nematode-trapping fungus Arthrobotrys oligospora
Xie, M., Ma, N., Bai, N., Yang, L., Yang, X., Zhang, K., & Yang, J. (2022) · Science China Life Sciences · doi:10.1007/s11427-022-2118-0 · Cited by 45
Gefitinib radiosensitizes non-small cell lung cancer cells through inhibition of ataxia telangiectasia mutated
Park, S., Kim, Y. M., & Pyo, H. (2010) · Molecular Cancer · doi:10.1186/1476-4598-9-222 · Cited by 44
MCM6 is a critical transcriptional target of YAP to promote gastric tumorigenesis and serves as a therapeutic target
Wang, Y., Chen, H., Liu, W., Yan, H., Zhang, Y., Cheung, A. H. K., Zhang, J., Chen, B., Li, L., Zhou, Z., et al. (2022) · Theranostics · doi:10.7150/thno.75431 · Cited by 44
PD-1/PD-L1 and DNA Damage Response in Cancer
Kciuk, M., Kołat, D., Kałuzińska‐Kołat, Ż., Gawrysiak, M., Drozda, R., Çelik, İ., & Kontek, R. (2023) · Cells · doi:10.3390/cells12040530 · Cited by 46
Exploiting Synthetic Lethal Interactions Between DNA Damage Signaling, Checkpoint Control, and p53 for Targeted Cancer Therapy
Morandell, S., & Yaffe, M. B. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-387665-2.00011-0 · Cited by 45
Recruitment of the cohesin loading factor NIPBL to DNA double-strand breaks depends on MDC1, RNF168 and HP1γ in human cells
Oka, Y., Suzuki, K., Yamauchi, M., Mitsutake, N., & Yamashita, S. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.07.021 · Cited by 44
The Role of hnRPUL1 Involved in DNA Damage Response Is Related to PARP1
Hong, Z., Jiang, J., Ma, J., Dai, S., Xu, T., Li, H. Z., & Yasui, A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060208 · Cited by 45
The common fragile site FRA16D gene product WWOX: roles in tumor suppression and genomic stability
Aqeilan, R. I., Abu‐Remaileh, M., & Abu-Odeh, M. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1724-y · Cited by 45
Parvovirus Infection-Induced DNA Damage Response
Luo, Y., & Qiu, J. (2013) · Future Virology · doi:10.2217/fvl.13.5 · Cited by 46
Defective DNA double‐strand break repair in pediatric systemic lupus erythematosus
Davies, R. C., Pettijohn, K. J., Fike, F. M., Wang, J., Nahas, S., Tunuguntla, R., Hu, H., Gatti, R. A., & McCurdy, D. (2011) · Arthritis & Rheumatism · doi:10.1002/art.33334 · Cited by 44
DNA damage and DNA damage response in human bronchial epithelial BEAS-2B cells following exposure to 2-nitrobenzanthrone and 3-nitrobenzanthrone: role in apoptosis
Øya, E., Øvrevik, J., Arlt, V. M., Nagy, E., Phillips, D. H., & Holme, J. A. (2011) · Mutagenesis · doi:10.1093/mutage/ger035 · Cited by 46
Arenobufagin intercalates with DNA leading to G2 cell cycle arrest via ATM/ATR pathway
Deng, L., Peng, Q.-L., Wang, L.-H., Xu, J. H., Liu, J., Li, Y., Zhuo, Z., Bai, L., Hu, L., Chen, W., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.5545 · Cited by 44
The mitochondrial metabolic checkpoint and aging of hematopoietic stem cells
Mohrin, M., & Chen, D. (2016) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000244 · Cited by 46
MiR‐320b/RAD21 axis affects hepatocellular carcinoma radiosensitivity to ionizing radiation treatment through DNA damage repair signaling
Wang, J., Zhao, H. C., Yu, J., Xu, X., Jing, H., Li, N., Tang, Y., Wang, S., Li, Y., Cai, J., et al. (2020) · Cancer Science · doi:10.1111/cas.14751 · Cited by 43
TAK1 ubiquitination regulates doxorubicin-induced NF-κB activation
Liang, L., Fan, Y., Cheng, J., Cheng, D., Zhao, Y., Cao, B., Ma, L., An, L., Jia, W., Xu, S., et al. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.09.003 · Cited by 44
Identification of Signaling Pathways Mediating Cell Cycle Arrest and Apoptosis Induced by Porphyromonas gingivalis in Human Trophoblasts
Inaba, H., Kuboniwa, M., Sugita, H., Lamont, R. J., & Amano, A. (2012) · Infection and Immunity · doi:10.1128/iai.00258-12 · Cited by 46
Targeting Replication Stress and Chemotherapy Resistance with a Combination of Sacituzumab Govitecan and Berzosertib: A Phase I Clinical Trial
Abel, M. L., Takahashi, N., Peer, C. J., Redon, C. E., Nichols, S., Vilimas, R. J., Lee, M.-J., Lee, S., Shelat, M., Kattappuram, R., et al. (2023) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-23-0536 · Cited by 43
DNA damage response: The emerging role of c-Abl as a regulatory switch?
Maiani, E., Diederich, M. F., & Gonfloni, S. (2011) · Biochemical Pharmacology · doi:10.1016/j.bcp.2011.07.001 · Cited by 44
The significance of the alteration of 8-OHdG in serous ovarian carcinoma
Xu, X., Wang, Y., Guo, W., Zhou, Y., Lv, C., Chen, X., & Liu, K. (2013) · Journal of Ovarian Research · doi:10.1186/1757-2215-6-74 · Cited by 43
RhoB Promotes γH2AX Dephosphorylation and DNA Double-Strand Break Repair
Mamouni, K., Cristini, A., Guirouilh‐Barbat, J., Monferran, S., Lemarié, A., Faye, J., López, B. S., Favre, G., & Sordet, O. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01525-13 · Cited by 51
O6-Methylguanine DNA lesions induce an intra-S-phase arrest from which cells exit into apoptosis governed by early and late multi-pathway signaling network activation
Noonan, E. M., Shah, D., Yaffe, M. B., Lauffenburger, D. A., & Samson, L. D. (2012) · Integrative Biology · doi:10.1039/c2ib20091k · Cited by 41
Small-molecule drug repurposing to target DNA damage repair and response pathways
Brinkman, J. A., Liu, Y., & Kron, S. J. (2020) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2020.02.013 · Cited by 41
Literature review of the role of hydroxyl radicals in chemically-induced mutagenicity and carcinogenicity for the risk assessment of a disinfection system utilizing photolysis of hydrogen peroxide
Kanno, T., Nakamura, K., Ikai, H., Kikuchi, K., Sasaki, K., & Niwano, Y. (2012) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.11-105 · Cited by 44
BRCA1 deficiency in skin epidermis leads to selective loss of hair follicle stem cells and their progeny
Sotiropoulou, P. A., Karambelas, A. E., Debaugnies, M., Candi, A., Bouwman, P., Moers, V., Revenco, T., Rocha, A. S., Sekiguchi, K., Jonkers, J., et al. (2013) · Genes & Development · doi:10.1101/gad.206573.112 · Cited by 42
Aven‐mediated checkpoint kinase control regulates proliferation and resistance to chemotherapy in conventional osteosarcoma
Baranski, Z., Booij, T. H., Cleton-Jansen, A., Price, L., van de Water, B., Bovée, J. V. M. G., Hogendoorn, P. C. W., & Danen, E. H. J. (2015) · The Journal of Pathology · doi:10.1002/path.4528 · Cited by 42
DNA Damage Response and Repair: Insights Into Strategies for Radiation Sensitization of Gliomas
Kesari, S., Advani, S. J., Lawson, J. D., Kahle, K. T., Ng, K., Carter, B. S., & Chen, C. C. (2011) · Future Oncology · doi:10.2217/fon.11.111 · Cited by 41
CRL Ubiquitin Ligases and DNA Damage Response
Li, J.-M., & Jin, J. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00029 · Cited by 43
Doxorubicin induces the DNA damage response in cultured human mesenchymal stem cells
Cruet-Hennequart, S., Prendergast, Á. M., Shaw, G., Barry, F., & Carty, M. P. (2012) · International Journal of Hematology · doi:10.1007/s12185-012-1196-5 · Cited by 42
The ATM-Dependent DNA Damage Response Acts as an Upstream Trigger for Compensation in thefas1Mutation during Arabidopsis Leaf Development
Hisanaga, T., Ferjani, A., Horiguchi, G., Ishikawa, N., Fujikura, U., Kubo, M., Demura, T., Fukuda, H., Ishida, T., Sugimoto, K., et al. (2013) · PLANT PHYSIOLOGY · doi:10.1104/pp.113.216796 · Cited by 42
DNA Damage and Its Cellular Response in Mother and Fetus Exposed to Hyperglycemic Environment
Moreli, J. B., Santos, J. H., Rocha, C. R. R., Damasceno, D. C., Morceli, G., Rudge, M. V. C., Bevilacqua, E. M. A. F., & Calderon, I. D. M. P. (2014) · BioMed Research International · doi:10.1155/2014/676758 · Cited by 44
DNA Repair Inhibitors: The Next Major Step to Improve Cancer Therapy
Barakat, K., Gajewski, M. M., & Tuszyński, J. A. (2012) · Current Topics in Medicinal Chemistry · doi:10.2174/156802612801319070 · Cited by 41
Drosophila FMRP participates in the DNA damage response by regulating G2/M cell cycle checkpoint and apoptosis
Liu, W., Jiang, F., Bi, X., & Zhang, Y. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds307 · Cited by 38
Targeting argininosuccinate synthetase negative melanomas using combination of arginine degrading enzyme and cisplatin
Savaraj, N., Wu, C., Li, Y., Wangpaichitr, M., You, M., Bomalaski, J. S., He, W., Kuo, M. T., & Feun, L. G. (2015) · Oncotarget · doi:10.18632/oncotarget.3370 · Cited by 41
MicroRNAs and Cancer Drug Resistance
Gomes, B. C., Rueff, J., & Rodrigues, A. S. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3347-1_9 · Cited by 43
LKB1 is a DNA damage response protein that regulates cellular sensitivity to PARP inhibitors
Wang, Y.-S., Chen, J., Cui, F., Wang, H., Wang, S., Hang, W., Zeng, Q., Quan, C., Zhai, Y.-X., Wang, J.-W., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.12334 · Cited by 42
Ataxia Telangiectasia Mutated Protein Loss and Benefit From Oxaliplatin-based Chemotherapy in Colorectal Cancer
Sundar, R., Miranda, S., Rodrigues, D. N., Chénard-Poirier, M., Dolling, D. I., Clarke, M., Figueiredo, I., Bertan, C. M., Yuan, W., Ferreira, A., et al. (2018) · Clinical Colorectal Cancer · doi:10.1016/j.clcc.2018.05.011 · Cited by 41
SUMOylation stabilizes hSSB1 and enhances the recruitment of NBS1 to DNA damage sites
Zhou, L., Zheng, L., Hu, K., Wang, X., Zhang, R., Zou, Y., Zhong, L., Wang, S., Wu, Y., & Kang, T. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0172-4 · Cited by 41
AKTIP/Ft1, a New Shelterin-Interacting Factor Required for Telomere Maintenance
Burla, R., Carcuro, M., Raffa, G. D., Galati, A., Raimondo, D., Rizzo, A., Torre, M. L., Micheli, E., Ciapponi, L., Cenci, G., et al. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005167 · Cited by 42
Polo-like kinases and DNA damage checkpoint: beyond the traditional mitotic functions
Bahassi, E. M. (2011) · Experimental Biology and Medicine · doi:10.1258/ebm.2011.011011 · Cited by 42
Combination of gefitinib and olaparib versus gefitinib alone in EGFR mutant non-small-cell lung cancer (NSCLC): A multicenter, randomized phase II study (GOAL)
García‐Campelo, R., Arrieta, O. G., Massutí, B., Rodríguez‐Abreu, D., Granados, A. L. O., Majem, M., Vicente, D., LIANES, P., Bosch‐Barrera, J., Insa, A., et al. (2020) · Lung Cancer · doi:10.1016/j.lungcan.2020.09.018 · Cited by 41
High-LET-Radiation-Induced Persistent DNA Damage Response Signaling and Gastrointestinal Cancer Development
Kumar, K., Kumar, S., Datta, K., Fornace, A. J., & Suman, S. (2023) · Current Oncology · doi:10.3390/curroncol30060416 · Cited by 42
Atrazine Triggers DNA Damage Response and Induces DNA Double-Strand Breaks in MCF-10A Cells
Huang, P., Yang, J., Ning, J., Wang, M., & Song, Q. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160714353 · Cited by 43

Authors: Harper, J. W., & Elledge, S. J.
Affiliations: Brigham and Women's Hospital (US)
Corresponding author: Harper, J. Wade
Elledge, Stephen J.
ORCID: Harper, J. Wade
Elledge, Stephen J.
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2007-12
Volume: 28
Issue: 5
Pages: 739-745
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/j.molcel.2007.11.015
OpenAlex: W2042499074
Cited by: 1,705
References: 44
Citations by year: 2026: 39 · 2025: 50 · 2024: 51 · 2023: 51 · 2022: 86 · 2021: 70 · 2020: 79 · 2019: 69 · 2018: 77 · 2017: 78 · 2016: 92 · 2015: 116 · 2014: 107 · 2013: 133 · 2012: 147
FWCI: 7.79
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 2055 d)
Locations: Molecular Cell (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute on Aging (R01AG011085)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: DNA damage response, DNA damage recognition, DNA damage signaling, DNA repair, DNA replication, protein phosphorylation, ubiquitin pathway, aging, cancer
MeSH terms: Animals, DNA Damage, DNA Repair, Humans, Protein Processing, Post-Translational, Ubiquitin, Ubiquitin-Protein Ligase Complexes, Proteasome Endopeptidase Complex

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

The DNA Damage Response: Ten Years After

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