The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
DNA processing is not required for ATM-mediated telomere damage response after TRF2 deletion
Abstract
Telomere attrition and other forms of telomere damage can activate the ATM kinase pathway. What generates the DNA damage signal at mammalian chromosome ends or at other double-strand breaks is not known. Telomere dysfunction is often accompanied by disappearance of the 3' telomeric overhang, raising the possibility that DNA degradation could generate the structure that signals. Here we address these issues by studying telomere structure after conditional deletion of mouse TRF2, the protective factor at telomeres. Upon removal of TRF2 from TRF2(F/-) p53-/- mouse embryo fibroblasts, a telomere damage response is observed at most chromosome ends. As expected, the telomeres lose the 3' overhang and are processed by the non-homologous end-joining pathway. Non-homologous end joining of telomeres was abrogated in DNA ligase IV-deficient (Lig4-/-) cells. Unexpectedly, the telomeres of TRF2-/- Lig4-/- p53-/- cells persisted in a free state without undergoing detectable DNA degradation. Notably, the telomeres retained their 3' overhangs, but they were recognized as sites of DNA damage, accumulating the DNA damage response factors 53BP1 and gamma-H2AX, and activating the ATM kinase. Thus, activation of the ATM kinase pathway at chromosome ends does not require overhang degradation or other overt DNA processing.
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“By contrast, when telomeres are compromised through the loss of TRF2, their repair is carried out by c-NHEJ80–82.”
From Telomeres in cancer: tumour suppression and genome instability (2017) · cites this paper as [81]
In the citing paper
“Similarly, acute telomere deprotection by inactivation of the shelterin protein TRF2 leads to robust telomeric ATM signaling, NHEJ-dependent telomere end-to-end fusion, and rapid cell cycle arrest [71,95].”
From Mechanisms and Regulation of Cellular Senescence (2021) · cites this paper as [95]
In the citing paper
“TRF2 is critical for telomere end protection and can facilitate formation of the t-loop conformation.”
From Telomeres and telomerase in cancer (2010) · cites this paper as [4]
In the citing paper
“Disruption of TRF2 through overexpression of a dominant-negative form or through deletion in TRF2-knockout mouse embryo fibroblasts leads to loss of the protective capped structure, characterized by processing of the 3# overhang and ligation of chromosome ends (3,4).”
From Telomeres and telomerase in cancer (2010) · cites this paper as [4]
Citations
Cites
A biomarker that identifies senescent human cells in culture and in aging skin in vivo.
Dimri, G. P., Lee, X., Basile, G., Acosta, M., Scott, G., Roskelley, C., Medrano, E. E., Linskens, M., Rubelj, I., & Pereira-Smith, O. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.20.9363 · Cited by 7,477
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
A DNA damage checkpoint response in telomere-initiated senescence
Fagagna, F. D. D., Reaper, P. M., Clay-Farrace, L., Fiegler, H., Carr, P., von Zglinicki, T., Saretzki, G., Carter, N. P., & Jackson, S. P. (2003) · Nature · doi:10.1038/nature02118 · Cited by 2,917
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
Mammalian Telomeres End in a Large Duplex Loop
Griffith, J. D., Comeau, L., Rosenfield, S., Stansel, R. M., Bianchi, A., Moss, H., & de Lange, T. (1999) · Cell · doi:10.1016/s0092-8674(00)80760-6 · Cited by 2,447
Tumor spectrum analysis in p53-mutant mice
Jacks, T., Remington, L., Williams, B. O., Schmitt, E. M., Halachmi, S., Bronson, R. T., & Weinberg, R. A. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00002-6 · Cited by 2,051
TRF2 Protects Human Telomeres from End-to-End Fusions
van Steensel, B., Smogorzewska, A., & de Lange, T. (1998) · Cell · doi:10.1016/s0092-8674(00)80932-0 · Cited by 1,709
DNA Damage Foci at Dysfunctional Telomeres
Takai, H., Smogorzewska, A., & de Lange, T. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00542-6 · Cited by 1,409
Herbig, U., Jobling, W. A., Chen, B. P. C., Chen, D. J., & Sedivy, J. M. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00256-4 · Cited by 1,344
Ma, Y., Pannicke, U., Schwarz, K., & Lieber, M. R. (2002) · Cell · doi:10.1016/s0092-8674(02)00671-2 · Cited by 1,166
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Telomere Length in Renal Cell Carcinoma: The Jekyll and Hyde Biomarker of Ageing of the Kidney
Morais, M., Dias, F., Teixeira, A. L., & Medeiros, R. (2020) · Cancer Management and Research · doi:10.2147/cmar.s211225 · Cited by 16
Zhang, Y., Zhang, Z., Miao, Z., & Ding, J. (2007) · Molecular Pharmacology · doi:10.1124/mol.107.039081 · Cited by 16
Telomere Repeat-Binding Factor 2 Is Responsible for the Telomere Attachment to the Nuclear Membrane
Ilicheva, N. V., Podgornaya, O. I., & Voronin, A. P. (2015) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2015.06.009 · Cited by 16
The long and the short of TRF2 in neurogenesis
Grammatikakis, I., Zhang, P., Mattson, M. P., & Gorospe, M. (2016) · Cell Cycle · doi:10.1080/15384101.2016.1222339 · Cited by 15
Rai, R., Biju, K., Sun, W., Sodeinde, T., Al-Hiyasat, A., Morgan, J. E., Ye, X., Li, X., Chen, Y., & Chang, S. S. (2023) · Nature Communications · doi:10.1038/s41467-023-37761-w · Cited by 14
Sande, C. M., Chen, S., Mitchell, D. V., Lin, P., Abraham, D. M., Cheng, J. M., Gebhard, T., Deolikar, R. J., Freeman, C. M., Zhou, M., et al. (2025) · Journal of Clinical Investigation · doi:10.1172/jci181659 · Cited by 15
Li, B. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.699639 · Cited by 14
Hübner, B., von Otter, E., Ahsan, B., Wee, M. L., Henriksson, S., Ludwig, A., & Sandin, S. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac309 · Cited by 14
Nuclear imaging in three dimensions: A unique tool in cancer research
Klonisch, T. C., Wark, L., Hombach‐Klonisch, S., & Mai, S. (2010) · Annals of Anatomy - Anatomischer Anzeiger · doi:10.1016/j.aanat.2010.07.007 · Cited by 15
Mitchell, T. R. H., & Zhu, X. (2014) · Aging · doi:10.18632/aging.100650 · Cited by 15
Telomere capping and cellular checkpoints: clues from fruit flies
Ciapponi, L., & Cenci, G. (2008) · Cytogenetic and Genome Research · doi:10.1159/000167824 · Cited by 14
Telomerase and the endocrine system
Pacini, F., Cantara, S., Capezzone, M., & Marchisotta, S. (2011) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2011.52 · Cited by 14
Telomere uncapping at the crossroad between cell cycle arrest and carcinogenesis
Gobbini, E., Trovesi, C., Cassani, C., & Longhese, M. P. (2014) · Molecular & Cellular Oncology · doi:10.4161/mco.29901 · Cited by 15
Kishi, S. (2011) · Birth Defects Research Part C Embryo Today Reviews · doi:10.1002/bdrc.20217 · Cited by 16
Structural biology of shelterin and telomeric chromatin: the pieces and an unfinished puzzle
Hu, H., Yan, H. L., & Nguyen, T. H. D. (2024) · Biochemical Society Transactions · doi:10.1042/bst20230300 · Cited by 12
Her, J., Jeong, Y. Y., & Chung, I. K. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.09.030 · Cited by 14
Tumor viruses and replicative immortality – Avoiding the telomere hurdle
Chen, X., Kamranvar, S. A., & Masucci, M. G. (2014) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2014.01.006 · Cited by 14
Li, B., & Zhao, Y. (2021) · Pathogens · doi:10.3390/pathogens10080967 · Cited by 13
Stock, A. J., McDevitt, R. A., Puligilla, C., Wang, Y., Zhang, Y., Wang, K., Sun, C., Becker, K. G., Lehrmann, E., Wood, W. H., et al. (2022) · PLoS Genetics · doi:10.1371/journal.pgen.1010506 · Cited by 12
A siRNA-Based Screen for Genes Involved in Chromosome End Protection
Lackner, D. H., Durocher, D., & Karlseder, J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021407 · Cited by 13
In Vitro Nonhomologous DNA End Joining System
Ma, Y., & Lieber, M. R. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(06)08031-1 · Cited by 13
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Barry, R. M., Sacco, O., Mameri, A., Stojaspal, M., Kartsonis, W., Shah, P., Ioannes, P. D., Hofr, C., Côté, J., & Sfeir, A. J. (2022) · Genes & Development · doi:10.1101/gad.349039.121 · Cited by 13
Multi-omics and single cell characterization of cancer immunosenescence landscape
Wei, Q., Chen, R., He, X., Qu, Y., Yan, C., Liu, X., Liu, J., Luo, J., Yu, Z., Hu, W., et al. (2024) · Scientific Data · doi:10.1038/s41597-024-03562-z · Cited by 13
Genetic and Epigenetic Inheritance at Telomeres
Lister‐Shimauchi, E. H., McCarthy, B., Lippincott, M. J., & Ahmed, S. C. (2022) · Epigenomes · doi:10.3390/epigenomes6010009 · Cited by 13
Shelterin dysfunction promotes CD4+ T cell senescence in Behçet’s disease
Shi, J., Zhang, M., Zhang, L., Yu, X., Sun, L., Liu, J., Zhao, Y., & Zheng, W. (2023) · Rheumatology · doi:10.1093/rheumatology/kead703 · Cited by 13
Hartwig, F. P., & Collares, T. V. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2013.03.003 · Cited by 11
RETRACTED: A subset of PARP inhibitors induces lethal telomere fusion in ALT-dependent tumor cells
Mukherjee, J., Pandita, A., Chatla, K., Johannessen, T.-C. A., Ohba, S., Tang, Y., Ore, C. L. D., Bjerkvig, R., & Pieper, R. O. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abc7211 · Cited by 12
RetractedGarrobo, I., Marión, R. M., Domı́nguez, O., Pisano, D. G., & Blasco, M. A. (2014) · Cell Cycle · doi:10.4161/15384101.2014.965044 · Cited by 12
Bojović, B., Ho, H.-Y., Wu, J., & Crowe, D. L. (2012) · Oncogene · doi:10.1038/onc.2012.555 · Cited by 14
Trf1 Is Not Required for Proliferation or Functional Telomere Maintenance in Chicken DT40 Cells
Cooley, C., Baird, K. M., Faure, V., Wenner, T., Stewart, J. L., Modino, S., Slijepčević, P., Farr, C. J., & Morrison, C. G. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-10-1019 · Cited by 11
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Zhang, Y., Hou, K., Tong, J., Zhang, H., Xiong, M., Liu, J., & Jia, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242316830 · Cited by 11
In vivo role of checkpoint kinase 2 in signaling telomere dysfunction
Beccaria, M. G., Martínez, P., Flores, J. M., & Blasco, M. A. (2014) · Aging Cell · doi:10.1111/acel.12237 · Cited by 11
Lagunas, A. M., Wu, J., & Crowe, D. L. (2017) · Oncotarget · doi:10.18632/oncotarget.20960 · Cited by 11
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Sheppard, S. A., Savinova, T., & Loayza, D. (2011) · Cell Cycle · doi:10.4161/cc.10.11.15676 · Cited by 11
Genome stability in Arabidopsis cells exhibiting alternative lengthening of telomeres
Akimcheva, S., Zellinger, B., & Riha, K. (2008) · Cytogenetic and Genome Research · doi:10.1159/000167827 · Cited by 11
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Nassour, J., & Karlseder, J. (2025) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041688 · Cited by 16
Chromosome instability induced by a single defined sister chromatid fusion
Kagaya, K., Noma-Takayasu, N., Yamamoto, I., Tashiro, S., Ishikawa, F., & Hayashi, M. (2020) · Life Science Alliance · doi:10.26508/lsa.202000911 · Cited by 11
Telomeres cooperate with the nuclear envelope to maintain genome stability
Rai, R., Sodeinde, T., Boston, A. M., & Chang, S. S. (2023) · BioEssays · doi:10.1002/bies.202300184 · Cited by 9
Cipressa, F., & Cenci, G. (2013) · PubMed · Cited by 10
Bridger, J. M., & Foster, H. A. (2020) · Springer eBooks · doi:10.1007/978-3-030-62532-0_5 · Cited by 10
Silvestre, D. C., & Londoño‐Vallejo, A. (2012) · Genome dynamics · doi:10.1159/000337128 · Cited by 11
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Tan, R., & Lan, L. (2016) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmw040 · Cited by 10
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Wu, R.-C., Zhang, J.-M., Huang, X., Li, Q.-M., Zhou, Z. P., Liang, H., Tan, M., & Qin, Q. (2025) · New Journal of Chemistry · doi:10.1039/d4nj04292a · Cited by 10
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Wu, J., & Crowe, D. L. (2020) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-19-1129 · Cited by 9
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Wondimagegnhu, B., Ma, W., Paul, T., Liao, T.-W., Lee, C. Y., Sanford, S. L., Opresko, P. L., & Myong, S. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae732 · Cited by 9
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Lichterfeld, M., Cung, T., Seiss, K., Rosenberg, E. S., Pereyra, F., & Yu, X. G. (2012) · Journal of Virology · doi:10.1128/jvi.00196-12 · Cited by 9
Dewar, J. M., & Lydall, D. A. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-998-3_24 · Cited by 9
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Iurato, G., & Igamberdiev, A. U. (2022) · Biosystems · doi:10.1016/j.biosystems.2022.104774 · Cited by 9
Begemann, S., Galimi, F., & Karlseder, J. (2009) · Aging · doi:10.18632/aging.100015 · Cited by 11
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Advances in biomarkers and diagnostic significance of organ aging
Chen, Y., Li, J., Liu, X., Geng, Z., Xu, K., & Su, J. (2023) · Fundamental Research · doi:10.1016/j.fmre.2023.03.009 · Cited by 9
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Xie, Y., Yang, D., He, Q., & Songyang, Z. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016440 · Cited by 8
Faure, V., Wenner, T., Cooley, C., Bourke, E., Farr, C. J., Takeda, S., & Morrison, C. G. (2008) · DNA repair · doi:10.1016/j.dnarep.2008.01.008 · Cited by 8
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Telomere shortening and expression of TRF1 and TRF2 in uterine leiomyoma
Oh, B.-K., Choi, Y., & Choi, J. S. (2021) · Molecular Medicine Reports · doi:10.3892/mmr.2021.12243 · Cited by 7
Yin, S., Zhang, F., Song, L., Chen, W., Weng, K., Liu, D., Wang, C., He, Z., Chen, Y., Ma, W., et al. (2022) · Stem Cell Reports · doi:10.1016/j.stemcr.2022.03.005 · Cited by 7
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Bártová, E., Galiová, G., Legartová, S., Stixová, L., Jugová, A., & Kozubek, S. (2010) · Critical Reviews in Eukaryotic Gene Expression · doi:10.1615/critreveukargeneexpr.v20.i3.10 · Cited by 6
Kim, J., Choi, I., & Lee, Y. (2017) · Histochemistry and Cell Biology · doi:10.1007/s00418-017-1591-3 · Cited by 6
Xie, Y., Yang, D. J., He, Q., & Songyang, Z. (2011) · PLoS ONE · doi:10.1371/annotation/21d9bc69-ccac-49b8-82f2-a6303e93618a · Cited by 6
Nera, B., Huang, H.-S., Hendrickson, E. A., & Xu, L. (2019) · Cell Cycle · doi:10.1080/15384101.2019.1598724 · Cited by 4
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Baliou, S., Pelagiadis, I., Apetroaei, M.-M., Vakonaki, E., Arsene, A. L., Hatzidaki, E., Tzatzarakis, M. N., Ιωάννου, Π., Tsatsakis, A. M., & Stiakaki, E. (2025) · Cancers · doi:10.3390/cancers17121936 · Cited by 6
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Scahill, C. M., Digby, Z., Sealy, I. M., White, R. J., Wali, N., Collins, J. E., Stemple, D. L., & Busch‐Nentwich, E. M. (2017) · Wellcome Open Research · doi:10.12688/wellcomeopenres.12530.2 · Cited by 7
Engin, A. B., & Engin, A. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-49844-3_2 · Cited by 4
Wang, Y., Ferrucci, L., Seidman, M. M., & Liu, Y. (2022) · STAR Protocols · doi:10.1016/j.xpro.2022.101610 · Cited by 4
Antiaging Strategies Based on Telomerase Activity
Aydin, Y. (2018) · Springer eBooks · doi:10.1007/978-981-13-1699-9_7 · Cited by 4
Chromosome ends teach unexpected lessons on DNA damage signalling
Chang, S. S. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.199 · Cited by 4
Trapping Rap1 at the telomere to prevent chromosome end fusions
Greenwood, J., & Cooper, J. P. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.299 · Cited by 4
The Role of Microhomology-Mediated End Joining (MMEJ) at Dysfunctional TelomeresPreprint
Billing, D. L., & Sfeir, A. J. (2024) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041687 · Cited by 4
TELS1 stabilizes t-loops independently of TRF2 and controls telomere length in pluripotent cells
Dufourd, J., Huynh, T. H. Y., Sauzet, S., Lai, Q. H., Abagnale, F., Zitouni, S., Giraud-Panis, M.-J. E., Urbach, S., Gilson, É., Tardat, M., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116260 · Cited by 3
Nuclear actin and DNA replication stress regulate telomere maintenance by telomerase
Harman, A., Kartawinata, M., Maroun, N. M., Nguyen, D. R., Rahman, S., Hughes, W. E., Winardi, K., Cohen, S. B., Cesare, A. J., Lamm, N., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-66506-0 · Cited by 9
Quantitative analysis of nuclear deformations and DNA damage foci dynamics by live-cell imaging
Faustini, E., Panza, A., Longaretti, M., & Lottersberger, F. (2023) · Methods in cell biology · doi:10.1016/bs.mcb.2022.12.010 · Cited by 3
Turgut, D., & Soyocak, A. (2012) · InTech eBooks · doi:10.5772/53226 · Cited by 3
Amiard, S., Olivier, M., Allain, E., Choi, K., Smith-Unna, R. D., Henderson, I. R., White, C. I., & Gallego, M. E. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku897 · Cited by 3
Bernal, A., Moltó‐Abad, M., Domínguez, D., & Tusell, L. (2018) · Oncotarget · doi:10.18632/oncotarget.25502 · Cited by 3
wRAPing up the End to Prevent Telomere Fusions
Price, C. M. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.05.005 · Cited by 3
DNA damage response manages cell cycle restriction of senile multipotent mesenchymal stromal cells
Lin, Y., Yu, F., Xu, Y., Wang, Y., Zuo, Y., Wang, C., & Ye, L. (2019) · Molecular Biology Reports · doi:10.1007/s11033-019-05150-6 · Cited by 3
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Zhao, X., Vogirala, V. K., Liu, M., Yu, Z., Rhodes, D., Sandin, S., & Yan, J. (2024) · Communications Biology · doi:10.1038/s42003-024-05838-x · Cited by 2
Zhai, F. (2024) · American Journal of Cancer Research · doi:10.62347/iyvv7581 · Cited by 2
Obesity-Senescence-Breast Cancer: Clinical Presentation of a Common Unfortunate Cycle
Engin, A. B., & Engin, A. (2024) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-63657-8_27 · Cited by 2
Role of Signaling Pathways Regulating Genomic Stability in Cancer
Sheikh, A., Bhat, G. A., Kumar, S., & Mudassar, S. (2025) · Springer eBooks · doi:10.1007/978-981-96-2763-9_13 · Cited by 3
Telomere length dynamics in aging mice
Comartin, P. J. (2012) · Scholarship@Western (Western University) · Cited by 2
Telomere Metabolism and DNA Damage Response
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Metadata
- Authors
- Celli, G. B., & de Lange, T.
- Affiliations
- NYU Langone Health (US)
- Venue
- Nature Cell Biology
- Published
- 2005-06-19
- Volume
- 7
- Issue
- 7
- Pages
- 712-718
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- OpenAlex
- W2035389897
- Semantic Scholar
- f4e3c6cbe3167cb507269beefcc7ad01ad45332d
- Cited by
- 623
- References
- 36
- Citations by year
- 2026: 9 · 2025: 14 · 2024: 28 · 2023: 19 · 2022: 16 · 2021: 27 · 2020: 26 · 2019: 20 · 2018: 22 · 2017: 37 · 2016: 24 · 2015: 37 · 2014: 41 · 2013: 37 · 2012: 41
- FWCI
- 20.17
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM49046-12)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Telomeres, Telomerase, and Senescence
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Keywords
- ATM kinase, TRF2, telomere shortening, non-homologous end joining, DNA ligase IV, DNA damage signaling, 53BP1, γH2AX, telomere dysfunction, p53-deficient cells
- MeSH terms
- Tumor Suppressor p53-Binding Protein 1, DNA Ligase ATP, Animals, Cells, Cultured, Chromosomal Proteins, Non-Histone, Crosses, Genetic, DNA, DNA Damage, DNA-Binding Proteins, Embryo, Mammalian, Fibroblasts, Histones, Mice, Transgenic, Phosphoproteins, Phosphorylation, DNA Ligases, Transfection, Tumor Suppressor Protein p53, Telomere, Protein Serine-Threonine Kinases, Gene Deletion, In Situ Hybridization, Fluorescence, Mice, Knockout, Cell Cycle Proteins, rap1 GTP-Binding Proteins, Tumor Suppressor Proteins, Telomeric Repeat Binding Protein 1, Telomeric Repeat Binding Protein 2, Intracellular Signaling Peptides and Proteins, Mice, Ataxia Telangiectasia Mutated Proteins, Checkpoint Kinase 2
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