Cited by 2,079DNA Repair MechanismsTelomeres, Telomerase, and SenescenceBacterial Genetics and Biotechnology

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Causes and consequences of replication stress

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Zeman, Michelle K., Cimprich, Karlene A.·2014·Nature Cell Biology

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Abstract

Replication stress is a complex phenomenon that has serious implications for genome stability, cell survival and human disease. Generation of aberrant replication fork structures containing single-stranded DNA activates the replication stress response, primarily mediated by the kinase ATR (ATM- and Rad3-related). Along with its downstream effectors, ATR stabilizes and helps to restart stalled replication forks, avoiding the generation of DNA damage and genome instability. Understanding this response may be key to diagnosing and treating human diseases caused by defective responses to replication stress.

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The DNA-damage response in human biology and disease
Jackson, S. P., & Bartek, J. (2009) · Nature · doi:10.1038/nature08467 · Cited by 6,092
The DNA Damage Response: Making It Safe to Play with Knives
Ciccia, A., & Elledge, S. J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.019 · Cited by 4,368
Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
Shi, Y., Lan, F., Matson, C., Mulligan, P., Whetstine, J. R., Cole, P. A., Casero, R. A., & Shi, Y. (2004) · Cell · doi:10.1016/j.cell.2004.12.012 · Cited by 4,051
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
Genomic instability — an evolving hallmark of cancer
Negrini, S., Gorgoulis, V. G., & Halazonetis, T. D. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2858 · Cited by 2,397
An Oncogene-Induced DNA Damage Model for Cancer Development
Halazonetis, T. D., Gorgoulis, V. G., & Bartek, J. (2008) · Science · doi:10.1126/science.1140735 · Cited by 1,851
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Marechal, A., & Zou, L. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a012716 · Cited by 1,514
DNA secondary structures: stability and function of G-quadruplex structures
Bochman, M. L., Paeschke, K., & Zakian, V. A. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3296 · Cited by 1,485
Ciliopathies
Hildebrandt, F., Benzing, T., & Katsanis, N. (2011) · New England Journal of Medicine · doi:10.1056/nejmra1010172 · Cited by 1,331
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Schlacher, K., Christ, N., Siaud, N., Egashira, A., Wu, H., & Jasin, M. (2011) · Cell · doi:10.1016/j.cell.2011.03.041 · Cited by 1,292

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Authors: Zeman, M. K., & Cimprich, K. A.
Affiliations: Stanford Medicine (US)
Corresponding author: Cimprich, Karlene A.
ORCID: Cimprich, Karlene A.
Venue: Nature Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2013-12-24
Volume: 16
Issue: 1
Pages: 2-9
ISSN: 1465-7392 (ISSN-L)
1476-4679
DOI: 10.1038/ncb2897
PMC: PMC4354890
OpenAlex: W2040860750
Cited by: 2,079
References: 142
Citations by year: 2026: 158 · 2025: 182 · 2024: 173 · 2023: 197 · 2022: 190 · 2021: 233 · 2020: 209 · 2019: 162 · 2018: 147 · 2017: 150 · 2016: 137 · 2015: 103 · 2014: 37
FWCI: 8.50
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
Locations: Nature Cell Biology (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute of General Medical Sciences (R01GM100489)
National Institute of Environmental Health Sciences (R01ES016486)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Telomeres, Telomerase, and Senescence
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords: replication stress, genomic instability, ATR kinase, replication stress response, replication fork restart, single-stranded DNA, DNA damage response, cell survival, DNA replication defects, human disease
MeSH terms: Disease, DNA Replication, Eukaryotic Cells, Humans, Models, Biological, Stress, Physiological

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