DNA Damage Response: How Cells Detect and Repair Damage

By Dr. Zubair Khalid, DVM, MS, PhD · 2026-08-11

Every cell in your body is under constant attack. Your DNA—the blueprint for every protein, every structural component, and every regulatory molecule you possess—is being damaged thousands of times per day. Ultraviolet light from the sun, reactive chemicals produced by your own metabolism, and errors made during DNA replication all threaten the integrity of your genome. If left unrepaired, this damage would lead to mutations, cell death, or cancer.

Yet most of the time, you are completely unaware of this ongoing assault. That is because cells have evolved an elaborate, multi-layered defense system: the DNA damage response (DDR). This network of proteins detects lesions in DNA, signals their presence, halts cell division to buy time, and recruits the appropriate repair machinery. When the DDR works correctly, your genome remains stable across trillions of cell divisions. When it fails, the consequences can be catastrophic.

What Is the DNA Damage Response?

The DNA damage response is the coordinated set of cellular pathways that detect DNA lesions, transmit signals about their presence, and execute repair. It is not a single pathway but a network of overlapping and interacting mechanisms that together maintain genome integrity. The DDR encompasses damage sensors, signal transducers, effectors that enforce cell cycle arrest, and the repair enzymes themselves.

Why DNA damage is a threat

DNA carries information in its sequence of bases—adenine (A), thymine (T), guanine (G), and cytosine (C). Any chemical alteration to these bases, or to the sugar-phosphate backbone that links them, can corrupt that information. Some lesions cause mispairing during replication, leading to permanent mutations. Others physically block the replication machinery, causing replication forks to stall and collapse. The most dangerous lesion, the double-strand break (DSB), severs both strands of the DNA duplex, which can lead to large-scale chromosomal rearrangements or loss of genetic material.

The threat is not hypothetical. Inherited mutations in DDR genes cause severe human diseases characterized by cancer predisposition, neurodegeneration, and premature aging. Ataxia-telangiectasia, caused by mutations in the ATM gene, leads to progressive neurological decline and a high incidence of lymphoid cancers. Mutations in BRCA1 or BRCA2, which function in double-strand break repair, dramatically increase the risk of breast and ovarian cancer. Understanding the DDR is therefore not just an academic exercise—it is central to understanding how cancer arises and how it can be treated.

Overview of the DDR network

The DDR operates through a general scheme. Sensor proteins continuously scan the genome for abnormalities. When they find damage, they recruit and activate transducer kinases—primarily ATM (ataxia-telangiectasia mutated) and ATR (ATM- and Rad3-related)—which phosphorylate downstream targets. These targets include effector kinases such as Chk1 and Chk2, which amplify the signal, and the tumor suppressor p53, which coordinates cellular outcomes. The ultimate effects are cell cycle arrest, activation of DNA repair pathways, or, if the damage is irreparable, programmed cell death (apoptosis) or permanent withdrawal from the cell cycle (senescence).

The DDR is also intimately connected to DNA replication. During S phase, when the genome is being duplicated, the replication machinery encounters obstacles that must be resolved. The Replication Origin fires thousands of times per cell cycle, and each origin creates a replication fork that can stall at damaged bases. The DDR monitors these forks and stabilizes them when they encounter problems.

Types of DNA Damage and Their Causes

DNA damage comes in many forms, each with distinct chemical structures and distinct repair requirements. The sources of damage fall into two broad categories: endogenous (arising from normal cellular processes) and exogenous (arising from environmental exposures).

Endogenous damage

Endogenous damage is caused by molecules and processes inside the cell. The most significant source is reactive oxygen species (ROS)—highly reactive molecules such as superoxide (O₂⁻), hydrogen peroxide (H₂O₂), and hydroxyl radical (•OH) that are produced as byproducts of mitochondrial respiration. ROS can oxidize DNA bases, creating lesions such as 8-oxoguanine (8-oxoG), which mispairs with adenine during replication, causing G:C to T:A transversion mutations. The hydroxyl radical can also abstract hydrogen atoms from the deoxyribose sugar, leading to single-strand breaks (SSBs) in the backbone.

Hydrolysis is another constant threat. The N-glycosidic bond linking a base to its sugar can spontaneously break, creating an abasic (AP) site. It is estimated that each cell loses thousands of bases per day through depurination alone. Cytosine can also undergo spontaneous deamination to form uracil, which is not a normal DNA base and must be removed.

DNA replication itself introduces errors. DNA polymerases have error rates of roughly 10⁻⁵ to 10⁻⁶ per base incorporated, meaning that even with proofreading, mistakes occur. These replication errors—mismatches, insertions, and deletions—are technically a form of DNA damage that must be corrected by the Mismatch Repair pathway.

Exogenous damage

Exogenous damage comes from the environment. Ultraviolet (UV) radiation from sunlight is a major culprit. UV light, particularly in the UVB range (280–315 nm), causes adjacent pyrimidine bases (cytosine and thymine) to form covalent bonds, creating cyclobutane pyrimidine dimers (CPDs) and 6-4 photoproducts. These lesions distort the DNA helix and block replication and transcription.

Ionizing radiation (IR)—X-rays, gamma rays, and particle radiation—deposits energy that can directly break the DNA backbone or generate ROS that attack DNA indirectly. IR is particularly dangerous because it can cause double-strand breaks, the most lethal form of DNA damage. A single unrepaired DSB can be sufficient to kill a cell.

Chemical agents also damage DNA. Alkylating agents such as methyl methanesulfonate (MMS) add methyl groups to bases, which can cause mispairing or block replication. Crosslinking agents such as cisplatin form covalent links between adjacent bases on the same strand (intrastrand crosslinks) or between the two strands (interstrand crosslinks), preventing strand separation during replication and transcription. Polycyclic aromatic hydrocarbons, found in tobacco smoke and charred food, form bulky adducts that distort the DNA helix.

The Effects of DNA Damage are diverse, ranging from silent mutations that have no consequence to catastrophic chromosomal rearrangements that drive cancer. The type of damage dictates which repair pathway is deployed.

Key Players in the DNA Damage Response

The DDR involves dozens of proteins, but a core set of players orchestrates the response. These can be grouped into sensors, transducers, and effectors.

Sensors: MRN complex, RPA

Sensors are proteins that detect DNA damage and initiate the signaling cascade. For double-strand breaks, the primary sensor is the MRN complex, composed of MRE11, RAD50, and NBS1. MRE11 has endonuclease and exonuclease activities that process DNA ends; RAD50 is an ATPase that holds the broken ends together; and NBS1 recruits downstream factors. The MRN complex binds to DSB ends within seconds of their formation and recruits ATM to the site.

For single-stranded DNA (ssDNA), which arises when replication forks stall or when DSBs are resected, the sensor is replication protein A (RPA). RPA is a heterotrimeric protein that coats ssDNA with high affinity, protecting it from nucleases and preventing secondary structure formation. RPA-coated ssDNA is the critical trigger for ATR activation.

Transducers: ATM and ATR

ATM and ATR are phosphoinositide 3-kinase-related kinases (PIKKs) that serve as the central signal transducers of the DDR. They phosphorylate serine or threonine residues followed by glutamine (the SQ/TQ motif) on hundreds of downstream targets.

ATM is activated primarily by double-strand breaks. The MRN complex recruits ATM to the break site, where it undergoes autophosphorylation at serine 1981, converting from an inactive dimer to an active monomer. ATM then phosphorylates a wide range of substrates, including the histone variant H2AX at serine 139 (creating γ-H2AX), the effector kinase Chk2, and p53.

ATR responds to single-stranded DNA, which is present at stalled replication forks and at resected DSBs. ATR is recruited to RPA-coated ssDNA by its binding partner ATRIP (ATR-interacting protein). Full activation requires additional factors, including the 9-1-1 complex (RAD9-HUS1-RAD1) and topoisomerase-binding protein-1 (TOPBP1). ATR phosphorylates Chk1 and p53, among many other targets.

Effectors: Chk1, Chk2, p53

The effector kinases Chk1 and Chk2 amplify the DDR signal and enforce cell cycle arrest. Chk2 is phosphorylated and activated by ATM at threonine 68. Chk1 is phosphorylated by ATR at serine 317 and serine 345. Both kinases phosphorylate the CDC25 phosphatases, which are critical regulators of the cell cycle. Phosphorylation of CDC25A by Chk1 or Chk2 targets it for degradation, while phosphorylation of CDC25C by Chk1 or Chk2 creates a binding site for 14-3-3 proteins, sequestering it in the cytoplasm. Because CDC25 phosphatases activate the cyclin-dependent kinases (CDKs) that drive cell cycle progression, their inactivation halts the cell cycle.

p53 is the master coordinator of the cellular response to damage. It is a transcription factor that is normally kept at low levels by MDM2, an E3 ubiquitin ligase that targets p53 for proteasomal degradation. ATM and ATR phosphorylate both p53 (at serine 15) and MDM2, disrupting their interaction and stabilizing p53. The accumulated p53 then transactivates genes involved in cell cycle arrest (p21), DNA repair (GADD45), and apoptosis (BAX, PUMA). The outcome—repair or death—depends on the extent of damage and the cellular context.

The DNA Damage Response Pathway: Step by Step

The canonical DDR can be broken down into four stages: recognition, transduction, checkpoint activation, and repair.

Damage recognition

The first step is the physical detection of the lesion. For DSBs, the MRN complex binds to the broken ends within seconds. For ssDNA, RPA coats the exposed single strand. For base damage, repair proteins such as the base excision repair enzyme OGG1 (8-oxoguanine DNA glycosylase) scan the DNA for specific lesions. This recognition step is rapid and highly sensitive—a single DSB can trigger a detectable DDR signal.

Signal transduction

Once sensors are bound, they recruit and activate the transducer kinases. MRN recruits ATM to DSBs, leading to ATM autophosphorylation and activation. RPA-coated ssDNA recruits ATR-ATRIP, which is activated by TOPBP1. The activated kinases then phosphorylate their substrates, including H2AX. γ-H2AX spreads over megabase regions flanking the break, creating a platform for the recruitment of additional repair and signaling proteins. This amplification step ensures that even a single lesion generates a robust cellular response.

Checkpoint activation

The transducer kinases activate the effector kinases Chk1 and Chk2, which in turn inhibit the CDC25 phosphatases. This inhibition prevents activation of CDKs, halting the cell cycle at specific checkpoints. The G1/S checkpoint prevents entry into S phase, the intra-S checkpoint slows ongoing replication, and the G2/M checkpoint prevents entry into mitosis. This arrest provides time for repair to occur before the damage is propagated to daughter cells.

Repair and recovery

The final stage is repair itself. The DDR recruits the appropriate repair pathway based on the lesion type and cell cycle phase. Once repair is complete, the signaling cascade is turned off. The kinases are inactivated by phosphatases, γ-H2AX is removed, and the cell cycle resumes. If repair fails, the DDR can trigger apoptosis or senescence to eliminate the damaged cell.

Cell Cycle Checkpoints and DNA Repair

The cell cycle is divided into four phases: G1 (gap 1), S (DNA synthesis), G2 (gap 2), and M (mitosis). The DDR can arrest the cell cycle at three major checkpoints, each with distinct functions.

G1/S checkpoint

The G1/S checkpoint prevents cells with damaged DNA from entering S phase. This checkpoint is primarily controlled by p53. When DNA damage is detected in G1, ATM/ATR activate Chk2/Chk1, which stabilize p53. p53 then induces p21, a CDK inhibitor that binds to and inactivates cyclin E-CDK2 and cyclin D-CDK4/6 complexes. Without CDK activity, the retinoblastoma protein (Rb) remains hypophosphorylated and continues to repress E2F target genes required for S phase entry. The G1/S arrest is sustained, lasting hours to days, allowing time for repair.

Intra-S checkpoint

The intra-S checkpoint responds to damage encountered during replication. When a replication fork stalls at a lesion, RPA-coated ssDNA accumulates, activating ATR. ATR phosphorylates Chk1, which inhibits CDC25A, preventing activation of cyclin A-CDK2. This slows replication origin firing and stabilizes stalled forks. The intra-S checkpoint is particularly important for preventing replication fork collapse, which would convert a single-strand lesion into a double-strand break.

G2/M checkpoint

The G2/M checkpoint prevents cells with damaged or incompletely replicated DNA from entering mitosis. This checkpoint is controlled by both ATM and ATR. Chk1 and Chk2 phosphorylate CDC25C, sequestering it in the cytoplasm and preventing activation of cyclin B-CDK1, the mitotic kinase. The G2/M checkpoint is often the last line of defense before cell division.

Repair pathways overview

The DDR activates specific repair pathways depending on the lesion type. The major pathways are summarized in the table below.

Base Excision Repair handles small, non-helix-distorting lesions. It begins with a glycosylase that removes the damaged base, creating an abasic site. APE1 then nicks the backbone, and DNA polymerase β fills the gap while XRCC1-ligase III seals it.

Nucleotide excision repair handles bulky, helix-distorting lesions. In global genome NER, XPC recognizes the distortion; in transcription-coupled NER, RNA polymerase stalling recruits CSA and CSB. In both cases, a dual incision by XPG and ERCC1-XPF excises a ~24–32 nucleotide oligonucleotide containing the lesion, and the gap is filled by DNA polymerase δ/ε with PCNA.

Double-strand breaks are repaired by two competing pathways. Non-homologous end joining (NHEJ) directly ligates the broken ends. The Ku70/Ku80 heterodimer binds the DSB, recruits DNA-PKcs, and the ends are processed by Artemis and polymerases before ligation by XRCC4-ligase IV. NHEJ is fast but can introduce small insertions or deletions at the junction. Homologous recombination (HR) uses the undamaged sister chromatid as a template for accurate repair. The MRN complex resects the DSB ends to create 3' ssDNA overhangs, which are coated by RPA and then replaced by RAD51 with the help of BRCA2. The RAD51 filament invades the homologous duplex, and DNA synthesis restores the lost information. HR is error-free but only works in S/G2 when a sister chromatid is available. The choice between NHEJ and HR is regulated by cell cycle phase and by proteins such as BRCA1 and 53BP1. For a detailed look at the HR mechanism, see Homologous Recombination.

DNA Damage Response in Prokaryotes

Prokaryotes, such as Escherichia coli, have a simpler but highly effective DDR. The bacterial response is dominated by the SOS response, a global regulatory network that coordinates DNA repair and mutagenesis.

The SOS response

The SOS response is induced when cells experience significant DNA damage, particularly ssDNA accumulation. It involves the coordinated expression of more than 40 genes, including those encoding nucleotide excision repair proteins (UvrA, UvrB, UvrC), translesion synthesis polymerases (Pol II, Pol IV, Pol V), and recombination proteins (RecA, RuvABC). The response is named "SOS" because it represents an emergency reaction to severe genotoxic stress.

RecA and LexA roles

The SOS response is controlled by two key proteins: RecA and LexA. LexA is a transcriptional repressor that binds to SOS boxes in the promoters of SOS genes, keeping them off under normal conditions. RecA is a recombinase that also functions as the sensor of DNA damage.

When DNA damage occurs, ssDNA is generated at stalled replication forks or during repair. RecA binds to this ssDNA, forming a nucleoprotein filament. This activated RecA (RecA*) stimulates the autoproteolytic cleavage of LexA, inactivating the repressor. As LexA is cleaved, SOS genes are derepressed in a hierarchical manner. Genes with high-affinity LexA binding sites (such as uvrA and uvrB, involved in NER) are induced early, while genes with lower affinity sites (such as umuD and umuC, encoding Pol V) are induced later. This temporal ordering ensures that high-fidelity repair is attempted before error-prone translesion synthesis is activated.

When the damage is repaired, ssDNA disappears, RecA is no longer activated, LexA accumulates again, and the SOS response is shut off. The SOS response is thus a tightly regulated, reversible system that allows bacteria to survive genotoxic stress.

How Scientists Study the DNA Damage Response

Studying the DDR requires methods to induce damage, detect it, and manipulate the genes involved.

Inducing damage in the lab

Researchers use a variety of agents to create specific types of DNA damage. UV radiation (typically 254 nm from a germicidal lamp) induces pyrimidine dimers and is used to study NER. Ionizing radiation from a ¹³⁷Cs or ⁶⁰Co source induces DSBs and is used to study ATM signaling and DSB repair. Chemical agents provide more specific lesions: hydrogen peroxide (H₂O₂) at concentrations of 50–500 µM generates oxidative damage; MMS (0.01–0.1%) alkylates bases; cisplatin (1–10 µM) creates crosslinks; and etoposide or camptothecin poison topoisomerases, generating DSBs or replication-associated damage.

Detecting damage and repair

Several assays measure DNA damage and repair. The comet assay (single-cell gel electrophoresis) measures DNA breaks in individual cells. Cells are embedded in agarose, lysed, and subjected to electrophoresis; damaged DNA migrates further, creating a "comet" tail whose length correlates with break frequency. The γ-H2AX assay uses antibodies against phosphorylated H2AX to detect DSBs by immunofluorescence or flow cytometry. Each γ-H2AX focus corresponds to approximately one DSB. The neutral comet assay specifically detects DSBs, while the alkaline version detects both SSBs and DSBs.

Repair can be measured by monitoring the disappearance of damage over time. For example, after UV irradiation, the removal of CPDs can be quantified by ELISA using antibodies specific for the lesion. Host cell reactivation assays measure the ability of cells to repair a damaged reporter plasmid.

Using mutants and RNAi

Genetic approaches are essential for dissecting DDR pathways. Cell lines with mutations in DDR genes—such as ATM-deficient cells from ataxia-telangiectasia patients—allow researchers to determine the role of specific proteins. RNA interference (siRNA or shRNA) can knock down gene expression transiently or stably. CRISPR-Cas9 genome editing enables precise knockout or knock-in of DDR genes. Chemical inhibitors, such as the ATM inhibitor KU-55933 or the ATR inhibitor VE-821, provide rapid and reversible inhibition. These tools, combined with assays for cell survival, checkpoint function, and repair efficiency, allow detailed dissection of DDR mechanisms.

When the DNA Damage Response Fails: Disease and Cancer

Defects in the DDR have profound consequences for human health, most notably in cancer.

Genomic instability

A hallmark of defective DDR is genomic instability—an increased rate of mutations, chromosomal aberrations, and aneuploidy. When checkpoints fail, cells with damaged DNA continue to divide, propagating mutations. When repair pathways are defective, lesions persist and are converted into mutations during replication. Over time, this accumulation of genetic alterations can drive malignant transformation. The link between DNA damage and cancer is so strong that genomic instability is now recognized as an enabling characteristic of cancer. For more on this connection, see DNA Damage Cause Cancer.

Cancer link

Inherited mutations in DDR genes predispose individuals to specific cancers. Mutations in BRCA1 or BRCA2, which are essential for homologous recombination, confer a 40–80% lifetime risk of breast cancer and a 20–40% risk of ovarian cancer. Mutations in the mismatch repair genes MLH1, MSH2, MSH6, or PMS2 cause Lynch syndrome, characterized by colorectal and endometrial cancers. Mutations in ATM cause ataxia-telangiectasia, associated with lymphoid malignancies. Mutations in TP53 (encoding p53) cause Li-Fraumeni syndrome, with a very high lifetime risk of multiple cancer types. These syndromes illustrate the critical role of the DDR in tumor suppression.

Therapeutic targeting of DDR

The DDR is also a target for cancer therapy. Many chemotherapeutic agents, such as cisplatin and etoposide, work by causing DNA damage that kills rapidly dividing cancer cells. More recently, targeted therapies exploit DDR defects in tumors. PARP inhibitors (e.g., olaparib) are effective against BRCA1/BRCA2-deficient tumors. PARP (poly(ADP-ribose) polymerase) is involved in single-strand break repair; when inhibited, SSBs persist and are converted to DSBs during replication. BRCA-deficient cells cannot repair these DSBs by HR, leading to cell death. This concept, known as synthetic lethality, has revolutionized the treatment of BRCA-mutant ovarian and breast cancers.

Common Pitfalls and Misconceptions in Understanding the DDR

Several misconceptions commonly arise when learning about the DDR.

DDR is a network, not a linear pathway

The DDR is often presented as a linear cascade: sensor → transducer → effector → repair. In reality, it is a highly interconnected network with extensive crosstalk, feedback loops, and redundancy. ATM and ATR share many substrates and can partially compensate for each other. Chk1 and Chk2 have overlapping functions. Many proteins have multiple roles; for example, p53 is both an effector of checkpoints and a regulator of repair gene expression. Understanding the DDR requires appreciating this complexity rather than memorizing a simple linear pathway.

Checkpoints vs. repair

Cell cycle checkpoints and DNA repair are distinct processes, though they are coordinated. Checkpoints are signaling mechanisms that arrest the cell cycle; repair pathways are enzymatic processes that remove lesions. A checkpoint arrest does not itself repair anything—it merely provides time for repair to occur. Conversely, repair can occur without checkpoint activation for low levels of damage. Confusing these two concepts leads to a misunderstanding of how the DDR protects the genome.

Prokaryotic vs. eukaryotic DDR

The bacterial SOS response is often used as a model for the eukaryotic DDR, but the two systems differ fundamentally. The SOS response is a transcriptional program controlled by a single repressor (LexA) and a single activator (RecA). The eukaryotic DDR is dominated by post-translational modifications—primarily phosphorylation—and involves dozens of proteins with specialized functions. Eukaryotes have multiple repair pathways for DSBs (NHEJ and HR) with complex regulation, whereas bacteria rely primarily on RecA-mediated homologous recombination. Extrapolating from bacteria to humans without recognizing these differences leads to oversimplification.

Frequently Asked Questions

What is the DNA damage response?

The DNA damage response (DDR) is the network of cellular pathways that detect DNA lesions, signal their presence, arrest the cell cycle, and activate DNA repair mechanisms. It maintains genome integrity by preventing the propagation of damaged DNA to daughter cells.

What are the steps of the DNA damage response?

The DDR proceeds through four stages: (1) damage recognition by sensor proteins such as the MRN complex or RPA; (2) signal transduction by the kinases ATM and ATR; (3) checkpoint activation through effector kinases Chk1 and Chk2, leading to cell cycle arrest; and (4) recruitment of repair machinery to remove the lesion and restore the DNA sequence.

What are the main types of DNA damage?

The main types include base oxidation (e.g., 8-oxoguanine), base deamination (e.g., cytosine to uracil), abasic sites, single-strand breaks, UV-induced pyrimidine dimers, bulky adducts from chemicals, mismatches from replication errors, and double-strand breaks. Each type is repaired by a specific pathway.

How does the DNA damage response work in prokaryotes?

Prokaryotes use the SOS response. RecA binds to single-stranded DNA generated at sites of damage, becoming activated. Activated RecA stimulates the self-cleavage of the LexA repressor, derepressing over 40 genes involved in repair and translesion synthesis. When damage is repaired, the response is shut off.

What is the difference between DNA damage and mutation?

DNA damage is a chemical alteration to the DNA molecule—a lesion such as an oxidized base or a break. A mutation is a change in the DNA sequence that is inherited by daughter cells. Damage can be repaired, restoring the original sequence. If damage is not repaired before replication, it can cause mispairing that becomes a permanent mutation.

Why is the DNA damage response important?

The DDR is essential for survival. It prevents the accumulation of mutations that can cause cancer, maintains the integrity of genes required for normal cellular function, and allows cells to survive environmental genotoxic stress. Defects in the DDR cause human diseases characterized by cancer predisposition and premature aging.

What happens if the DNA damage response fails?

If the DDR fails, DNA damage persists and is converted into mutations during replication. This leads to genomic instability, increased mutation rates, and ultimately cancer. In some cases, unrepaired damage triggers cell death, which can cause tissue degeneration and premature aging.

Key Takeaways

• The DNA damage response is a coordinated network of sensors, transducers, and effectors that detects lesions, halts the cell cycle, and activates repair.
• DNA damage arises from both endogenous sources (reactive oxygen species, hydrolysis, replication errors) and exogenous sources (UV radiation, ionizing radiation, chemicals).
• ATM and ATR are the central signaling kinases, responding to double-strand breaks and single-stranded DNA, respectively; they activate Chk1, Chk2, and p53 to enforce checkpoints.
• The DDR arrests the cell cycle at G1/S, intra-S, and G2/M checkpoints to provide time for repair.
• Major repair pathways include base excision repair, nucleotide excision repair, mismatch repair, homologous recombination, and non-homologous end joining.
• Prokaryotes use the simpler SOS response controlled by RecA and LexA, which differs fundamentally from the eukaryotic DDR.
• Defects in the DDR cause genomic instability and cancer predisposition; DDR proteins such as PARP are now therapeutic targets in cancer treatment.

Further Reading

• Ciccia A, Elledge SJ. The DNA damage response: making it safe to play with knives. Molecular cell. 2010. PubMed 20965415
• Srinivas US et al. ROS and the DNA damage response in cancer. Redox biology. 2019. PubMed 30612957
• Blackford AN, Jackson SP. ATM, ATR, and DNA-PK: The Trinity at the Heart of the DNA Damage Response. Molecular cell. 2017. PubMed 28622525
• Giglia-Mari G, Zotter A, Vermeulen W. DNA damage response. Cold Spring Harbor perspectives in biology. 2011. PubMed 20980439
• Vanderwaeren L et al. Saccharomyces cerevisiae as a Model System for Eukaryotic Cell Biology, from Cell Cycle Control to DNA Damage Response. International journal of molecular sciences. 2022. PubMed 36232965
• Takagi M. DNA damage response and hematological malignancy. International journal of hematology. 2017. PubMed 28374143

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