The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
Activation of the Cellular DNA Damage Response in the Absence of DNA Lesions
Open accessAbstract
The cellular DNA damage response (DDR) is initiated by the rapid recruitment of repair factors to the site of DNA damage to form a multiprotein repair complex. How the repair complex senses damaged DNA and then activates the DDR is not well understood. We show that prolonged binding of DNA repair factors to chromatin can elicit the DDR in an ATM (ataxia telangiectasia mutated)– and DNAPK (DNA-dependent protein kinase)–dependent manner in the absence of DNA damage. Targeting of single repair factors to chromatin revealed a hierarchy of protein interactions within the repair complex and suggests amplification of the damage signal. We conclude that activation of the DDR does not require DNA damage and stable association of repair factors with chromatin is likely a critical step in triggering, amplifying, and maintaining the DDR signal.
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In the citing paper
“This conclusion is in line with earlier tethering experiments demonstrating that a DNA lesion is not an obligatory part of the DDR machinery and DDR signaling can occur in its absence, allowing for the possibility of DDR initiation by stimuli other than DNA damage, such as chromatin structure (Bonilla et al., 2008; Soutoglou and Misteli, 2008).”
From Activation of DNA Damage Response Signaling by Condensed Chromatin (2014) · cites this paper as Soutoglou and Misteli, 2008
In the citing paper
“This conclusion is in line with earlier tethering experiments demonstrating that a DNA lesion is not an obligatory part of the DDR machinery and DDR signaling can occur in its absence, allowing for the possibility of DDR initiation by stimuli other than DNA damage, such as chromatin structure (Bonilla et al., 2008; Soutoglou and Misteli, 2008).”
From Activation of DNA Damage Response Signaling by Condensed Chromatin (2014) · cites this paper as Soutoglou and Misteli, 2008
In the citing paper
“No labeling by terminal deoxynucleotidyl transferase dUTP nick end labeling (TUNEL) was detected”
From Activation of DNA Damage Response Signaling by Condensed Chromatin (2014) · cites this paper as Soutoglou and Misteli, 2008
In the citing paper
“The MRN complex, MDC1, and H2AX are essential for the recruitment of ATM to the site of DSBs for efficient ATM-mediated DDR activation.”
From Functional interplay between ATM/ATR-mediated DNA damage response and DNA repair pathways in oxidative stress (2014) · cites this paper as [219]
In the citing paper
“suggesting that DDR activation requires the stable association of DNA repair proteins in HR, but not DNA damage per se [219]”
From Functional interplay between ATM/ATR-mediated DNA damage response and DNA repair pathways in oxidative stress (2014) · cites this paper as [219]
In the citing paper
“the prolonged binding to chromatin by repair proteins, such as Mre11, Nbs1 and MDC1, can elicit an ATM-dependent DDR in the absence of DNA damage”
From Functional interplay between ATM/ATR-mediated DNA damage response and DNA repair pathways in oxidative stress (2014) · cites this paper as [219]
Citations
Cites
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
Chk1 and Chk2 kinases in checkpoint control and cancer
Bartek, J., & Lukas, J. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00110-7 · Cited by 1,513
Hickson, I., Zhao, Y., Richardson, C. J., Green, S. J., Martin, N. M. B., Orr, A. I., Reaper, P. M., Jackson, S. P., Curtin, N. J., & Smith, G. C. M. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-2727 · Cited by 1,220
Stucki, M., Clapperton, J. A., Mohammad, D. H., Yaffe, M. B., Smerdon, S. J., & Jackson, S. P. (2005) · Cell · doi:10.1016/j.cell.2005.09.038 · Cited by 1,164
Sensing and repairing DNA double-strand breaks
Jackson, S. P. (2002) · Carcinogenesis · doi:10.1093/carcin/23.5.687 · Cited by 1,149
Histone H2AX phosphorylation is dispensable for the initial recognition of DNA breaks
Celeste, A., Fernandez-Capetillo, O., Kruhlak, M. J., Pilch, D. R., Staudt, D. W., Lee, A., Bonner, R. F., Bonner, W. M., & Nussenzweig, A. (2003) · Nature Cell Biology · doi:10.1038/ncb1004 · Cited by 989
MDC1 is a mediator of the mammalian DNA damage checkpoint
Stewart, G. S., Wang, B., Bignell, C. R., Taylor, A. M. R., & Elledge, S. J. (2003) · Nature · doi:10.1038/nature01446 · Cited by 874
Lou, Z., Minter‐Dykhouse, K., Franco, S., Gostissa, M., Rivera, M. A., Celeste, A., Manis, J. P., van Deursen, J., Nussenzweig, A., Paull, T. T., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2005.11.025 · Cited by 668
DNA damage-induced G2–M checkpoint activation by histone H2AX and 53BP1
Fernández-Capetillo, Ó., Chen, H. T., Celeste, A., Ward, I. M., Romanienko, P. J., Morales, J. C., Naka, K., Xia, Z., Camerini‐Otero, R. D., Motoyama, N., et al. (2002) · Nature Cell Biology · doi:10.1038/ncb884 · Cited by 657
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Bekker‐Jensen, S., Lukas, C., Kitagawa, R., Melander, F., Kastan, M. B., Bártek, J., & Lukas, J. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200510130 · Cited by 647
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Metadata
- Authors
- Soutoglou, E., & Misteli, T.
- Affiliations
- National Institutes of Health (US)
- Venue
- Science
- Published
- 2008-06-13
- Volume
- 320
- Issue
- 5882
- Pages
- 1507-1510
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC2575099
- OpenAlex
- W2067328670
- Cited by
- 299
- References
- 21
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 9 · 2023: 9 · 2022: 9 · 2021: 7 · 2020: 10 · 2019: 11 · 2018: 14 · 2017: 15 · 2016: 13 · 2015: 15 · 2014: 26 · 2013: 21 · 2012: 19
- FWCI
- 15.89
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Cancer Institute (Z01BC010309)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Effects of Radiation Exposure
- Keywords
- DNA damage response, ATM, DNA repair proteins, chromatin binding, signal amplification, protein-protein interaction
- MeSH terms
- Tumor Suppressor p53-Binding Protein 1, Checkpoint Kinase 1, MRE11 Homologue Protein, Animals, Cell Cycle, Cells, Cultured, Chromatin, Chromosomal Proteins, Non-Histone, DNA Damage, DNA Repair, DNA-Binding Proteins, Histones, Nuclear Proteins, Phosphorylation, Protein Kinases, Recombinant Fusion Proteins, Signal Transduction, Protein Serine-Threonine Kinases, Cell Cycle Proteins, Tumor Suppressor Proteins, NIH 3T3 Cells, DNA Repair Enzymes, Intracellular Signaling Peptides and Proteins, Adaptor Proteins, Signal Transducing, Mice, Ataxia Telangiectasia Mutated Proteins, Checkpoint Kinase 2
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 ›
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