The DOI matches its Crossref record; 37 of the 38 references it cites were found in a registry or an index.
ATR disruption leads to chromosomal fragmentation and early embryonic lethality
Open accessAbstract
Although a small decrease in survival and increase in tumor incidence was observed in ATR +/− mice, ATR −/− embryos die early in development, subsequent to the blastocyst stage and prior to 7.5 days p.c. In culture, ATR −/− blastocysts cells continue to cycle into mitosis for 2 days but subsequently fail to expand and die of caspase-dependent apoptosis. Importantly, caspase-independent chromosome breaks are observed in ATR −/− cells prior to widespread apoptosis, implying that apoptosis is caused by a loss of genomic integrity. These data show that ATR is essential for early embryonic development and must function in processes other than regulation of p53.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
In the citing paper
“ATR is an essential gene for the initiation and regulation of NER and for genome maintenance 17, 36, 37.”
From Xeroderma Pigmentosa Group A (XPA), Nucleotide Excision Repair and Regulation by ATR in Response to Ultraviolet Irradiation (2017) · cites this paper as [36]
In the citing paper
“ATR was originally cloned as a member of the phosphoinositide 3-kinase–related kinase (PIKK) family and is essential for early embryonic development [32, 80, 81].”
From Functional interplay between ATM/ATR-mediated DNA damage response and DNA repair pathways in oxidative stress (2014) · cites this paper as [81]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
A mammalian protein targeted by G1-arresting rapamycin–receptor complex
Brown, E. J., Albers, M. W., Bum Shin, T., ichikawa, K., Keith, C. T., Lane, W. S., & Schreiber, S. L. (1994) · Nature · doi:10.1038/369756a0 · Cited by 2,053
Self-citationTumor 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
Activation of the ATM Kinase by Ionizing Radiation and Phosphorylation of p53
Canman, C. E., Lim, D.-S., Cimprich, K. A., Taya, Y., Tamai, K., Sakaguchi, K., Appella, E., Kastan, M. B., & Siliciano, J. D. (1998) · Science · doi:10.1126/science.281.5383.1677 · Cited by 2,042
Linkage of ATM to Cell Cycle Regulation by the Chk2 Protein Kinase
Matsuoka, S. (1998) · Science · doi:10.1126/science.282.5395.1893 · Cited by 1,322
Embryonic lethality and radiation hypersensitivity mediated by Rad51 in mice lacking Brca2
Sharan, S. K., Morimatsu, M., Albrecht, U., Lim, D., Regel, E., Dinh, C. Q., Sands, A., Gregor Eichele, C., Hasty, P., & Bradley, A. (1997) · Nature · doi:10.1038/386804a0 · Cited by 1,087
A role for ATR in the DNA damage-induced phosphorylation of p53
Tibbetts, R. S., Brumbaugh, K. M., Williams, J. M., Sarkaria, J. N., Cliby, W. A., Shieh, S.-Y., Taya, Y., Prives, C., & Abraham, R. T. (1999) · Genes & Development · doi:10.1101/gad.13.2.152 · Cited by 1,046
(1999) · PubMed · Cited by 1,030
Cortez, D., Wang, Y., Qin, J., & Elledge, S. J. (1999) · Science · doi:10.1126/science.286.5442.1162 · Cited by 1,020
Dynamic changes of BRCA1 subnuclear location and phosphorylation state are initiated by DNA damage
Scully, R., Chen, J., Ochs, R. L., Keegan, K., Hoekstra, M., Feunteun, J., & Livingston, D. M. (1997) · Cell · doi:10.1016/s0092-8674(00)80503-6 · Cited by 900
14-3-3σ is required to prevent mitotic catastrophe after DNA damage
Chan, T. A., Hermeking, H., Lengauer, C., Kinzler, K. W., & Vogelstein, B. (1999) · Nature · doi:10.1038/44188 · Cited by 895
Flagged first, then by citations
1 of the 38 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 501–600 of 945
BK Polyomavirus Activates the DNA Damage Response To Prolong S Phase
Justice, J., Needham, J. M., & Thompson, S. R. (2019) · Journal of Virology · doi:10.1128/jvi.00130-19 · Cited by 37
The Connection Between Cell Fate and Telomere
Engin, A. B., & Engin, A. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-49844-3_3 · Cited by 39
Control of genome stability by Slx protein complexes
Rouse, J. W. (2009) · Biochemical Society Transactions · doi:10.1042/bst0370495 · Cited by 38
C. elegans: A model of Fanconi anemia and ICL repair
Youds, J. L., Barber, L. J., & Boulton, S. J. (2008) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2008.11.007 · Cited by 37
Sakasai, R., Shinohe, K., Ichijima, Y., Okita, N., Shibata, A., Asahina, K., & Teraoka, H. (2006) · Genes to Cells · doi:10.1111/j.1365-2443.2006.00942.x · Cited by 38
Igarashi, T., Mazevet, M., Yasuhara, T., Yano, K., Mochizuki, A., Nishino, M., Yoshida, T., Yoshida, Y., Takamatsu, N., Yoshimi, A., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40578-2 · Cited by 38
Chapter 4 Assessing Metabolic Stress and Autophagy Status in Epithelial Tumors
Mathew, R., Karantza‐Wadsworth, V., & White, E. (2009) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)04004-4 · Cited by 37
RNAi and cancer: Implications and applications.
Abdelrahim, M., Safe, S. H., Baker, C. H., & Abudayyeh, A. (2006) · PubMed Central · Cited by 36
Mak, J. P. Y., Man, W. Y., Chow, J. P. H., Ma, H. T., & Poon, R. Y. C. (2015) · Oncotarget · doi:10.18632/oncotarget.4020 · Cited by 36
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
Zhang, Y., Lai, J., Du, Z., Gao, J., Yang, S., Gorityala, S., Xiong, X., Deng, O., Ma, Z., Yan, C., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.9156 · Cited by 39
Arlander, S. J. H., Greene, B. T., Innes, C. L., & Paules, R. S. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-0675 · Cited by 36
Itakura, E., Sawada, I., & Matsuura, A. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-05-0427 · Cited by 35
Novel Insights into Chk1 Regulation by Phosphorylation
Goto, H., Kasahara, K., & Inagaki, M. (2014) · Cell Structure and Function · doi:10.1247/csf.14017 · Cited by 37
Arend, R. C., Jackson-Fisher, A. J., Jacobs, I. A., Chou, J., & Monk, B. J. (2021) · Cancer Biology & Therapy · doi:10.1080/15384047.2020.1868937 · Cited by 35
Biayna, J., García-Cao, I., Álvarez‐Álvarez, M. M., Salvadores, M., Espinosa‐Carrasco, J., McCullough, M., Supek, F., & Stracker, T. H. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001176 · Cited by 35
Pedroza‐García, J. A., Eekhout, T., Achon, I., Nisa, M., Coussens, G., Vercauteren, I., den Daele, H. V., Pauwels, L., Lijsebettens, M. V., Raynaud, C., et al. (2021) · The Plant Cell · doi:10.1093/plcell/koab158 · Cited by 37
Okita, K., Kiyonari, H., Nobuhisa, I., Kimura, N., Aizawa, S., & Taga, T. (2004) · Genes to Cells · doi:10.1111/j.1365-2443.2004.00791.x · Cited by 35
Clinical Impact of ATR Checkpoint Signalling Failure in Humans
O’Driscoll, M., & Jeggo, P. A. (2003) · Cell Cycle · doi:10.4161/cc.2.3.404 · Cited by 39
Cell resistance to the Cytolethal Distending Toxin involves an association of DNA repair mechanisms
Bezine, E., Malaisé, Y., Loeuillet, A., Chevalier, M., Boutet-Robinet, E. A., Salles, B., Mirey, G., & Vignard, J. (2016) · Scientific Reports · doi:10.1038/srep36022 · Cited by 35
Mutant p53 perturbs DNA replication checkpoint control through TopBP1 and Treslin
Liu, K., Lin, F., Graves, J. D., Lee, Y.-J., & Lin, W.-C. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1619832114 · Cited by 35
Gilmer, T. M., Lai, C.-H., Guo, K., Deland, K., Ashcraft, K. A., Stewart, A. E., Wang, Y., Fu, J., Wood, K. C., Kirsch, D. G., et al. (2024) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-23-0890 · Cited by 35
Zhu, M., & Weiss, R. S. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-10-0957 · Cited by 34
DNA Damage-Sensing Kinases Mediate the Mouse 2-Cell Embryo's Response to Genotoxic Stress
Mu, X., Jin, X., Farnham, M. M. J., Li, Y., & O’Neill, C. (2011) · Biology of Reproduction · doi:10.1095/biolreprod.110.089334 · Cited by 34
Replication Stress Leads to Genome Instabilities inArabidopsisDNA Polymerase Δ Mutants
Schuermann, D., Fritsch, O., Lucht, J. M., & Höhn, B. (2009) · The Plant Cell · doi:10.1105/tpc.109.069682 · Cited by 36
Regulation of replication fork speed: Mechanisms and impact on genomic stability
Merchut‐Maya, J. M., Bártek, J., & Maya‐Mendoza, A. (2019) · DNA repair · doi:10.1016/j.dnarep.2019.102654 · Cited by 36
Dodson, G. E., & Tibbetts, R. S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509577200 · Cited by 34
Molecular mechanisms of trophoblast survival: From implantation to birth
Jurisicova, A., Detmar, J., & Caniggia, I. (2005) · Birth Defects Research Part C Embryo Today Reviews · doi:10.1002/bdrc.20053 · Cited by 34
Kemp, M. G., & Sancar, A. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.719740 · Cited by 35
BRCA1 Activates a G2-M Cell Cycle Checkpoint following 6-Thioguanine–Induced DNA Mismatch Damage
Yamane, K., Schupp, J. E., & Kinsella, T. J. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-2205 · Cited by 33
Lupardus, P. J., & Cimprich, K. A. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-09-0865 · Cited by 34
Removing all obstacles: A critical role for p53 in promoting tissue renewal
Schoppy, D. W., Ruzankina, Y., & Brown, E. J. (2010) · Cell Cycle · doi:10.4161/cc.9.7.11194 · Cited by 32
Self-citationPernaute, B., Pérez-Montero, S., Nieto, J. M. S., Gregorio, A. D., Lima, A., Lawlor, K., Bowling, S., Liccardi, G., Tomás, A., Meier, P., et al. (2022) · Developmental Cell · doi:10.1016/j.devcel.2022.04.020 · Cited by 33
Effect of Immunosuppressants Tacrolimus and Mycophenolate Mofetil on the Keratinocyte UVB Response
Ming, M., Zhao, B., Qiang, L., & He, Y. (2014) · Photochemistry and Photobiology · doi:10.1111/php.12318 · Cited by 32
Molecular genetics of genotoxic stress signalling in plants
Ulm, R. (2003) · Topics in current genetics · doi:10.1007/978-3-540-39402-0_9 · Cited by 32
Lhx8 ablation leads to massive autophagy of mouse oocytes associated with DNA damage†
D’Ignazio, L., Michel, M., Beyer, M., Thompson, K., Forabosco, A., Schlessinger, D., & Pelosi, E. (2018) · Biology of Reproduction · doi:10.1093/biolre/iox184 · Cited by 32
Fikaris, A. J., Lewis, A. E., Abulaiti, A., Tsygankova, O. M., & Meinkoth, J. L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606737200 · Cited by 33
Kim, E.-M. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.3.643 · Cited by 32
SUV4-20 activity in the preimplantation mouse embryo controls timely replicationPreprint
Eid, A., Rodriguez‐Terrones, D., Burton, A., & Torres‐Padilla, M. (2016) · Genes & Development · doi:10.1101/gad.288969.116 · Cited by 32
Stella preserves maternal chromosome integrity by inhibiting 5hmC‐induced γH2AX accumulation
Nakatani, T., Yamagata, K., Kimura, T., Oda, M., Nakashima, H., Hori, M., Sekita, Y., Arakawa, T., Nakamura, T., & Nakano, T. (2015) · EMBO Reports · doi:10.15252/embr.201439427 · Cited by 31
Wang, G., Wang, X., & Xu, X. (2015) · Biomarker Research · doi:10.1186/s40364-015-0043-2 · Cited by 31
Ham, M. F., Takakuwa, T., Luo, W., Liu, A., Horii, A., & Aozasa, K. (2006) · Cancer Science · doi:10.1111/j.1349-7006.2006.00165.x · Cited by 31
de Ru, M. H., Gille, J. J. P., Nieuwint, A. W. M., Bijlsma, J. B., van der Blij, J. F., & van Hagen, J. M. (2005) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.30786 · Cited by 31
Exploiting Replication Stress as a Novel Therapeutic Intervention
Martin, J. C., Hoegel, T. J., Lynch, M. L., Woloszynska‐Read, A., Melendy, T., & Ohm, J. E. (2020) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-20-0651 · Cited by 32
Dormant origin signaling during unperturbed replication
Moiseeva, T. N., & Bakkenist, C. J. (2019) · DNA repair · doi:10.1016/j.dnarep.2019.102655 · Cited by 32
Cui, Y., Palii, S. S., Innes, C. L., & Paules, R. S. (2014) · Cell Cycle · doi:10.4161/15384101.2014.960729 · Cited by 29
Molecular Mechanisms of DNA Replication Checkpoint Activation
Recolin, B., van der Laan, S., Tsanov, N., & Maiorano, D. (2014) · Genes · doi:10.3390/genes5010147 · Cited by 34
Analysis of Poly(ADP-Ribose) Polymerases in Arabidopsis Telomere Biology
Boltz, K. A., Jasti, M., Townley, J. M., & Shippen, D. E. (2014) · PLoS ONE · doi:10.1371/journal.pone.0088872 · Cited by 30
Kemp, M. G., Spandau, D. F., Simman, R., & Travers, J. B. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.765883 · Cited by 30
Loss of XChk1 function triggers apoptosis after the midblastula transition in Xenopus laevis embryos
Carter, A. D., & Sible, J. C. (2003) · Mechanisms of Development · doi:10.1016/s0925-4773(02)00443-4 · Cited by 29
ATR-dependent phosphorylation of ATRIP in response to genotoxic stress
Itakura, E., Umeda, K., Sekoguchi, E., Takata, H., Ohsumi, M., & Matsuura, A. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.08.228 · Cited by 29
PHF11 promotes DSB resection, ATR signaling, and HRPreprint
Gong, Y., Handa, N., Kowalczykowski, S. C., & de Lange, T. (2017) · Genes & Development · doi:10.1101/gad.291807.116 · Cited by 30
Targeting lung cancer through inhibition of checkpoint kinases
Syljuåsen, R. G., Hasvold, G., Hauge, S., & Helland, Å. (2015) · Frontiers in Genetics · doi:10.3389/fgene.2015.00070 · Cited by 29
Emerging targets for radioprotection and radiosensitization in radiotherapy
Kumar, S., Singh, R. K., & Meena, R. (2016) · Tumor Biology · doi:10.1007/s13277-016-5117-8 · Cited by 28
Inhibition of p73 function by Pifithrin-α as revealed by studies in zebrafish embryos
Davidson, W., Ren, Q., Kari, G., Kashi, O., Dicker, A. P., & Rodeck, U. (2008) · Cell Cycle · doi:10.4161/cc.7.9.5786 · Cited by 28
E4F1 Is a Master Regulator of CHK1-Mediated Functions
Grote, D., Moison, C., Duhamel, S., Chagraoui, J., Girard, S., Yang, J., Mayotte, N., Coulombe, Y., Masson, J., Brown, G. W., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.03.019 · Cited by 30
Théard, D., Coisy‐Quivy, M., Ducommun, B., CONCANNON, P. J., & Darbon, J.-M. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.6095 · Cited by 28
Feng, W., Dean, D. C., Hornicek, F. J., Wang, J., Jia, Y., Duan, Z., & Shi, H. (2020) · Therapeutic Advances in Medical Oncology · doi:10.1177/1758835920982853 · Cited by 28
RetractedBertolin, A. P., Canal, B., Yekezare, M., Early, A. E., Zeng, J., Instrell, R., Howell, M., & Diffley, J. F. X. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.06.002 · Cited by 27
The MRE11 complex: An important source of stress relief
Rein, K., & Stracker, T. H. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.10.010 · Cited by 29
Mak, J. P. Y., Man, W. Y., Ma, H. T., & Poon, R. Y. C. (2014) · Oncotarget · doi:10.18632/oncotarget.2508 · Cited by 27
Onksen, J. L., Brown, E. J., & Blendy, J. A. (2011) · Neuropsychopharmacology · doi:10.1038/npp.2010.234 · Cited by 28
Self-citationNuclear lamina dysfunction triggers a germline stem cell checkpoint
Barton, L. J., Duan, T., Ke, W., Luttinger, A., Lovander, K. E., Soshnev, A. A., & Geyer, P. (2018) · Nature Communications · doi:10.1038/s41467-018-06277-z · Cited by 27
Black, J. A., Crouch, K., Lemgruber, L., Lapsley, C. T., Dickens, N. J., Tosi, L. R. O., Mottram, J. C., & McCulloch, R. (2020) · Cell Reports · doi:10.1016/j.celrep.2019.12.049 · Cited by 29
Alterations of DNA damage-response genes ATM and ATR in pyothorax-associated lymphoma
Liu, A., Takakuwa, T., Fujita, S., Ham, M. F., Luo, W.-J., Daibata, M., & Aozasa, K. (2005) · Laboratory Investigation · doi:10.1038/labinvest.3700235 · Cited by 27
Host DNA damage response facilitates African swine fever virus infection
Simões, M., Martins, C. L. V., & Ferreira, F. (2013) · Veterinary Microbiology · doi:10.1016/j.vetmic.2013.01.007 · Cited by 26
The TRESLIN-MTBP complex couples completion of DNA replication with S/G2 transition
Zonderland, G., Vanzo, R., Gadi, S. A., Martín‐Doncel, E., Coscia, F., Mund, A., Lerdrup, M., Benada, J., Boos, D., & Toledo, L. I. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.08.006 · Cited by 26
A distinct response to endogenous DNA damage in the development of Nbs1-deficient cortical neurons
Li, R., Yang, Y., Gao, Y., Wang, Z., & Tong, W. (2012) · Cell Research · doi:10.1038/cr.2012.3 · Cited by 26
D’Souza, F., Uppangala, S., Asampille, G., Salian, S. R., Kalthur, G., Talevi, R., Atreya, H. S., & Adiga, S. K. (2018) · Scientific Reports · doi:10.1038/s41598-018-35342-2 · Cited by 26
Dhoonmoon, A., Schleicher, E. M., Clements, K. E., Nicolae, C. M., & Moldovan, G. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa508 · Cited by 26
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
Friedberg, E. C., & Meira, L. B. (2004) · DNA repair · doi:10.1016/j.dnarep.2004.06.016 · Cited by 27
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
Dubitzky, W., Olaf Wolkenhauer, A., Cho, K., & Yokota, H. (2013) · Springer eBooks · doi:10.1007/978-1-4419-9863-7_100393 · Cited by 26
BMP signaling promotes zebrafish heart regeneration via alleviation of replication stress
Vasudevarao, M. D., Pena, D. P., Ihle, M., Bongiovanni, C., Maity, P., Geissler, D., Mohammadi, H. F., Rall-Scharpf, M., Niemann, J., Mommersteeg, M. T. M., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-56993-6 · Cited by 26
Differential function of NBS1 and ATR in neurogenesis
Zhou, Z., Bruhn, C., & Wang, Z. (2011) · DNA repair · doi:10.1016/j.dnarep.2011.10.021 · 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
Horton, J. K., Stefanick, D. F., Kedar, P. S., & Wilson, S. H. (2007) · DNA repair · doi:10.1016/j.dnarep.2006.12.015 · Cited by 26
ATR cooperates with CTC1 and STN1 to maintain telomeres and genome integrity inArabidopsis
Boltz, K. A., Leehy, K. A., Song, X., Nelson, A. D. L., & Shippen, D. E. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-12-1002 · Cited by 25
ATR signaling in mammalian meiosis: From upstream scaffolds to downstream signaling
Pereira, C., Smolka, M. B., Weiss, R. S., & Brieño‐Enríquez, M. A. (2020) · Environmental and Molecular Mutagenesis · doi:10.1002/em.22401 · Cited by 26
Déry, U., & Masson, J. (2007) · DNA repair · doi:10.1016/j.dnarep.2006.12.009 · Cited by 27
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
The Mitochondria and the Regulation of Cell Fitness During Early Mammalian Development
Lima, A., Burgstaller, J. P., Sanchez-Nieto, J. M., & Rodríguez, T. A. (2017) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2017.10.012 · Cited by 24
ATR regulates neuronal activity by modulating presynaptic firing
Kırtay, M., Sell, J., Marx, C., Haselmann, H., Ceangă, M., Zhou, Z., Rahmati, V., Kirkpatrick, J. M., Buder, K., Grigaravičius, P., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24217-2 · Cited by 24
Regulation of Oocyte Apoptosis: A View from Gene Knockout Mice
Kaur, S., & Kurokawa, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021345 · Cited by 24
Roles of DNA damage in renal tubular epithelial cells injury
Wang, P., Ouyang, J., Jia, Z., Zhang, A., & Yang, Y. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1162546 · Cited by 27
Musich, P. R., Li, Z., & Zou, Y. (2017) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-319-56017-5_4 · Cited by 23
Replication fork integrity and intra-S phase checkpoint suppress gene amplification
Kondratova, A. A., Watanabe, T., Marotta, M. L., Cannon, M. V., Segall, A. M., Serre, D., & Tanaka, H. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv084 · Cited by 23
Chen, C., Chu, P., Lee, L.-Y., Lien, H.-W., Lin, T.-L., Fan, C., Chi, P., Huang, C., & Chang, M.-S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033538 · Cited by 23
Cell Cycle Remodeling and Zygotic Gene Activation at the Midblastula Transition
Zhang, M., Skirkanich, J., Lampson, M. A., & Klein, P. S. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-46095-6_9 · Cited by 23
Drosophila dCBP Is Involved in Establishing the DNA Replication Checkpoint
Smolik, S. M., & Jones, K. L. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01283-06 · Cited by 23
Kerzendorfer, C., Colnaghi, R., Abramowicz, I., Carpenter, G., & O’Driscoll, M. (2013) · DNA repair · doi:10.1016/j.dnarep.2013.04.016 · Cited by 23
Mossafa, H., Tapia, S., Flandrin, G., Troussard, X., & the Groupe Français D'Hématologie, C. (2004) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428194042000191738 · Cited by 23
Goff, P. H., Bhakuni, R., Pulliam, T. H., Lee, J. H., Hall, E. T., & Nghiem, P. (2021) · Cancers · doi:10.3390/cancers13143415 · Cited by 23
Targeting Cell Cycle Checkpoint Kinases to Overcome Intrinsic Radioresistance in Brain Tumor Cells
Vlatkovic, T., Veldwijk, M. R., Giordano, F. A., & Herskind, C. (2022) · Cancers · doi:10.3390/cancers14030701 · Cited by 26
Sugitani, N., Vendetti, F. P., Cipriano, A. J., Pandya, P., Deppas, J. J., Moiseeva, T. N., Schamus-Haynes, S., Wang, Y., Palmer, D., Osmanbeyoglu, H. U., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111371 · Cited by 22
Jamsai, D., O’Connor, A. E., DeBoer, K., Clark, B. J., Smith, S. J., Browne, C. M., Bensley, J. G., Merriman, J. A., Yuen, W. S., Koopman, P. A., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056955 · Cited by 22
Smith‐Roe, S. L., Patel, S. S., Zhou, Y., Simpson, D. A., Rao, S., Ibrahim, J. G., Cordeiro‐Stone, M., & Kaufmann, W. K. (2013) · Cell Cycle · doi:10.4161/cc.23177 · Cited by 25
Rybaczek, D., Musiałek, M. W., & Balcerczyk, A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0142307 · Cited by 22
Yan, J., Yang, X.-P., Kim, Y. S., & Jetten, A. M. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-5950 · Cited by 22
Metadata
- Authors
- Brown, E. J., & Baltimore, D.
- Affiliations
- California Institute of Technology (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2000-02-15
- Volume
- 14
- Issue
- 4
- Pages
- 397-402
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC316378
- OpenAlex
- W2167196101
- Cited by
- 951
- References
- 38
- Citations by year
- 2026: 12 · 2025: 18 · 2024: 24 · 2023: 29 · 2022: 26 · 2021: 26 · 2020: 31 · 2019: 27 · 2018: 30 · 2017: 38 · 2016: 39 · 2015: 46 · 2014: 31 · 2013: 46 · 2012: 34
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion, cc-by)
- Funders
- Cancer Research Institute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Keywords
- ATR kinase, early embryonic lethality, chromosomal fragmentation, caspase-dependent apoptosis, blastocyst, genome stability, p53-independent function, mitotic cycle
- MeSH terms
- Animals, Blastocyst, Cell Transformation, Neoplastic, Chromosome Aberrations, DNA Repair, Fetal Death, Genotype, Mice, Inbred C57BL, Mitosis, Neoplasm Proteins, Neoplasms, Experimental, Transcription Factors, Apoptosis, Protein Serine-Threonine Kinases, Mice, Knockout, Gene Targeting, Gene Expression Regulation, Developmental, Cell Cycle Proteins, BRCA1 Protein, Caspases, BRCA2 Protein, Mice, Ataxia Telangiectasia Mutated Proteins
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