Replication Fork Reversal: Mechanisms and Biological Significance

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

Introduction to Replication Fork Reversal

What is Replication Fork Reversal?

Replication fork reversal is a highly conserved DNA damage response mechanism in which a stalled replication fork undergoes regression—the fork retreats backward, the parental DNA strands re-anneal, and the two nascent (newly synthesized) strands anneal to each other. This process converts the standard three-way junction of a replication fork into a four-way junction that resembles a Holliday junction. The resulting structure is colloquially termed a "chicken-foot" because of its appearance under electron microscopy.

To understand fork reversal, you must first appreciate the architecture of a normal replication fork. At each origin of replication, the replicative helicase (CMG complex in eukaryotes: Cdc45, Mcm2-7, GINS) unwinds the parental duplex, creating two single-stranded templates. DNA polymerases ε and δ synthesize the leading and lagging strands, respectively, in a 5′ to 3′ direction. The fork is a dynamic structure with a defined polarity: the leading strand is synthesized continuously in the direction of fork movement, while the lagging strand is synthesized discontinuously as Okazaki fragments. For a visual reference, see the Replication Fork Diagram and the Replication Fork Labeled resource.

During fork reversal, this architecture is dismantled. The fork moves backward, away from the original direction of replication. The two parental strands re-anneal to reform duplex DNA, and the two nascent strands pair with each other, forming a fourth arm. This fourth arm is a duplex of newly synthesized DNA that extends in the opposite direction from the original fork. The entire structure is a four-way junction with two duplex arms of parental DNA and one duplex arm of nascent DNA, plus a single-stranded region at the junction point.

Why Cells Reverse Their Replication Forks

Cells reverse their replication forks primarily to protect genome integrity. When a replication fork encounters an obstacle—such as a DNA lesion, a protein-DNA crosslink, or a difficult-to-replicate sequence—it stalls. A stalled fork is a dangerous intermediate. If left unprotected, the fork can collapse into a double-strand break (DSB), which is one of the most cytotoxic DNA lesions a cell can experience. A single unrepaired DSB can trigger cell death or promote chromosomal rearrangements that drive cancer.

Fork reversal provides a protective mechanism that achieves several goals simultaneously:

1. Stabilization: The reversed fork is a stable, protected structure that prevents the exposed single-stranded DNA (ssDNA) at the stalled fork from being further processed into a DSB.
2. Time: Reversal gives the cell time to repair the underlying lesion or remove the replication obstacle.
3. Template Switching: The chicken-foot structure allows the nascent leading strand to use the nascent lagging strand as a template for synthesis, bypassing the lesion in a process called template switching.
4. Damage Bypass: The reversed fork provides a substrate for homologous recombination (HR) and other repair pathways to resolve the stalled fork without generating a DSB.

Notably, fork reversal is not a passive consequence of stalling. It is an active, regulated process requiring specific enzymes. Cells that cannot reverse their forks—due to mutations in key regulators—are hypersensitive to replication stress and accumulate DNA damage. This underscores the biological importance of fork reversal as a frontline defense against replication-associated genome instability.

The Molecular Mechanism of Fork Reversal

Key Enzymes and Proteins Involved

Fork reversal is catalyzed by a group of DNA translocases and helicases that recognize stalled forks and remodel them. The major players in eukaryotes include:

• SMARCAL1 (SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin, subfamily A-like 1): A DNA-dependent ATPase that catalyzes fork regression. SMARCAL1 binds to the stalled fork via its HARP (helicase-associated, plant-like) domains and uses ATP hydrolysis to drive re-annealing of the parental strands and annealing of the nascent strands. SMARCAL1 is particularly important for forks stalled at DNA lesions that generate ssDNA gaps.

• ZRANB3 (zinc finger RANBP2-type containing 3): Another annealing helicase that promotes fork reversal. ZRANB3 is recruited to stalled forks through its interaction with polyubiquitinated PCNA (proliferating cell nuclear antigen). It also has endonuclease activity that can cleave the reversed fork, facilitating restart.

• HLTF (helicase-like transcription factor): A RAD5 homolog in humans that possesses both helicase and ubiquitin ligase activities. HLTF promotes fork reversal and also ubiquitinates PCNA to regulate the choice between error-prone and error-free damage bypass pathways.

• RAD51: The central recombinase in homologous recombination. RAD51 forms a nucleoprotein filament on the ssDNA at stalled forks. This filament is essential for fork reversal—RAD51 depletion abolishes fork regression. RAD51's role is to stabilize the reversed fork and promote the strand exchange reactions needed for template switching.

• FBH1 (F-box DNA helicase 1): A helicase that promotes fork reversal, particularly in response to nucleoside depletion.

• BLM and WRN: RecQ helicases that can promote fork regression in vitro. BLM is also involved in resolving the reversed fork after repair is complete.

The process of fork reversal is not a single enzymatic step but a coordinated series of events:

1. Recognition: The stalled fork is recognized by sensor proteins. RPA (replication protein A) coats the exposed ssDNA at the fork. The ATR (ataxia-telangiectasia and Rad3-related) kinase pathway is activated, phosphorylating downstream effectors such as CHK1.

1. RAD51 Loading: RAD51 replaces RPA on the ssDNA, forming a nucleoprotein filament. This step requires mediator proteins such as BRCA2.

1. Regression: A translocase (SMARCAL1, ZRANB3, or HLTF) binds to the fork and uses ATP hydrolysis to drive backward movement. The parental strands re-anneal, and the nascent strands pair.

1. Stabilization: The reversed fork is stabilized by RAD51 and other proteins. The chicken-foot structure can persist for minutes to hours.

1. Processing: Depending on the nature of the lesion, the reversed fork is either resolved by nucleases (leading to fork restart) or used as a substrate for template switching.

The Chicken-Foot Structure

The chicken-foot structure is the hallmark of fork reversal. It is a four-way junction with three duplex arms and one single-stranded region. The name derives from its appearance in electron micrographs: the three duplex arms resemble the toes of a chicken foot.

The structure forms as follows. Consider a fork stalled with the leading strand halted at a lesion. The nascent leading strand is shorter than the nascent lagging strand. During reversal:

• The parental strands re-anneal behind the fork, reforming duplex DNA.
• The nascent leading strand peels away from its template and anneals to the nascent lagging strand.
• The resulting structure has a duplex arm of nascent DNA extending backward from the fork.

The chicken-foot structure is critical for template switching. The 3′ end of the nascent leading strand can prime DNA synthesis using the nascent lagging strand as a template. This allows the replication machinery to bypass the lesion without incorporating an error. After the lesion is bypassed, the fork can be restored to its normal configuration, and replication can resume.

The chicken-foot structure is also a substrate for structure-specific nucleases. For example, MUS81-EME1 can cleave the reversed fork, generating a DSB that is then repaired by homologous recombination. This is a "last resort" pathway that is activated when the fork cannot be restarted by simpler mechanisms.

Triggers and Conditions for Fork Reversal

Replication Stress and DNA Lesions

Fork reversal is triggered by a wide range of conditions that impede replication fork progression. The common denominator is the accumulation of ssDNA at the fork, which recruits RPA and activates the ATR checkpoint. Key triggers include:

• Ultraviolet (UV) damage: UV light creates cyclobutane pyrimidine dimers (CPDs) and 6-4 photoproducts. These lesions block replicative polymerases. Fork reversal is observed within minutes of UV exposure.

• DNA crosslinks: Interstrand crosslinks (ICLs) covalently link the two strands of DNA, preventing their separation. ICLs are potent inducers of fork reversal. Agents such as cisplatin and mitomycin C create ICLs.

• Base damage: Oxidative damage (e.g., 8-oxoguanine) and alkylation damage can stall polymerases. Fork reversal is induced by agents such as hydrogen peroxide and methyl methanesulfonate (MMS).

• Nucleotide depletion: Hydroxyurea (HU) inhibits ribonucleotide reductase, depleting the dNTP pool. Without sufficient dNTPs, polymerases stall. HU is a classic inducer of fork reversal.

• Difficult-to-replicate sequences: Secondary structures such as hairpins, G-quadruplexes, and trinucleotide repeats can impede fork progression and trigger reversal.

• R-loops: RNA-DNA hybrids that form during transcription can collide with replication forks, causing stalling and reversal.

• Topological stress: Positive supercoiling ahead of the fork can impede helicase activity. Topoisomerase inhibitors such as camptothecin induce fork reversal by trapping topoisomerase I cleavage complexes.

Chemical Inhibitors That Induce Reversal

Several chemical agents are commonly used in the laboratory to induce fork reversal experimentally:

The choice of agent depends on the specific question being asked. HU is the most commonly used agent because it induces robust fork reversal in a synchronized manner. However, HU does not create a physical lesion—it simply starves the fork of nucleotides. This distinction is important: fork reversal in response to HU is primarily a protective response to replication stress, whereas fork reversal in response to cisplatin is a response to a physical block.

The Role of Fork Reversal in DNA Repair and Genome Stability

Repair Pathways Linked to Fork Reversal

Fork reversal is intimately connected to several DNA repair pathways. The reversed fork is not an end in itself—it is a substrate for downstream repair processes.

Template Switching: As described above, the chicken-foot structure allows the nascent leading strand to use the nascent lagging strand as a template. This error-free bypass mechanism is a form of recombination-dependent repair. Template switching requires RAD51 and is promoted by the same translocases that drive fork reversal. After the lesion is bypassed, the fork is restored, and replication resumes.

Homologous Recombination: If the reversed fork is cleaved by structure-specific nucleases (e.g., MUS81-EME1), a one-ended DSB is generated. This DSB is repaired by homologous recombination using the sister chromatid as a template. The HR machinery—RAD51, BRCA1, BRCA2, RAD52—is essential for this process. Fork reversal and HR are thus intimately linked: reversal provides the substrate for HR, and HR provides the mechanism for fork restart.

Nucleotide Excision Repair (NER): For bulky lesions such as CPDs, NER can remove the lesion from the DNA. Fork reversal provides time for NER to act. The reversed fork protects the lesion from further processing and keeps the fork in a stable state until NER is complete.

Fanconi Anemia Pathway: The Fanconi anemia (FA) pathway is activated by interstrand crosslinks. FA proteins, including FANCD2 and FANCI, are recruited to stalled forks and promote fork reversal. FANCD2 physically interacts with the fork and stabilizes the reversed structure. Cells with mutations in FA genes are defective in fork reversal and are hypersensitive to crosslinking agents.

Prevention of Double-Strand Breaks

The most important function of fork reversal is the prevention of double-strand breaks. A stalled fork with exposed ssDNA is a fragile structure. The ssDNA can be nicked by endonucleases, or the fork can be cleaved by structure-specific nucleases, generating a DSB. Fork reversal protects against this by:

1. Removing ssDNA from the fork: The re-annealing of parental strands and annealing of nascent strands eliminates the ssDNA that is the substrate for nucleases.

1. Stabilizing the fork: The four-way junction is a more stable structure than a stalled three-way junction. It is resistant to nucleolytic attack.

1. Providing a substrate for error-free repair: The reversed fork can be processed by template switching or HR, both of which are error-free or error-minimizing pathways.

Cells that cannot reverse their forks—for example, cells depleted of SMARCAL1 or RAD51—accumulate DSBs at stalled forks. This is observed as an increase in γ-H2AX foci (a marker of DSBs) and chromosomal aberrations. The link between fork reversal and DSB prevention is so strong that fork reversal is now considered a bona fide genome stability pathway.

Methods to Study Replication Fork Reversal

DNA Fiber Assays

DNA fiber analysis is the most widely used method to study replication fork dynamics, including fork reversal. The technique involves labeling replicating DNA with nucleotide analogs, spreading the DNA on a glass slide, and visualizing the labeled tracts by immunofluorescence.

The standard protocol uses two sequential labels:

1. Labeling: Cells are incubated with 5-iodo-2′-deoxyuridine (IdU) for 20–30 minutes, followed by 5-chloro-2′-deoxyuridine (CldU) for 20–30 minutes. The first label (IdU) is detected with a specific antibody, and the second label (CldU) with a different antibody.

1. Stress Induction: After labeling, cells are treated with a replication stress agent (e.g., HU) for 2–4 hours.

1. Spreading: Cells are lysed on a glass slide, and the DNA is stretched by gravity or by a specialized spreading apparatus.

1. Detection: The labeled tracts are visualized by immunofluorescence microscopy. Fork reversal is detected as a shortening of the labeled tracts (because the fork has moved backward) or as the appearance of "fired" origins (new replication bubbles).

Fork reversal is quantified by measuring the length of the labeled tracts. A reversed fork will have a shorter tract than a non-reversed fork. The percentage of reversed forks can be calculated by comparing tract lengths between treated and untreated cells.

DNA fiber analysis is a powerful technique because it provides single-molecule resolution and can be used to quantify fork reversal in large populations of cells. However, it does not directly visualize the chicken-foot structure—it only infers reversal from tract shortening.

Electron Microscopy

Electron microscopy (EM) is the gold standard for visualizing replication fork reversal. The technique involves:

1. DNA Extraction: Genomic DNA is extracted from cells under conditions that preserve replication intermediates. This typically involves gentle lysis and proteinase K digestion.

1. Enrichment: Replication intermediates are enriched by benzoylated naphthoylated DEAE (BND) cellulose chromatography, which binds to single-stranded DNA.

1. Spreading: The DNA is spread on a carbon-coated grid using the Kleinschmidt technique (cytochrome c spreading) or a variation thereof.

1. Visualization: The DNA is shadowed with platinum and visualized by transmission electron microscopy.

Under EM, a reversed fork appears as a four-way junction with three duplex arms. The chicken-foot structure is clearly visible. EM can also be used to measure the length of the reversed arm, which provides information about the extent of regression.

EM is technically demanding and low-throughput, but it provides definitive evidence for fork reversal. It is often used to validate findings from DNA fiber assays.

Single-Molecule Approaches

Single-molecule techniques provide real-time visualization of fork reversal. These approaches include:

• Magnetic Tweezers: A single DNA molecule is attached to a magnetic bead and a glass surface. The DNA is twisted or stretched to create a replication fork-like structure. Reversal is detected as a change in the DNA's extension.

• Optical Tweezers: Similar to magnetic tweezers but using laser traps to manipulate the DNA.

• Fluorescence Resonance Energy Transfer (FRET): Fork reversal can be monitored in real time by labeling the nascent strands with fluorophores and measuring FRET changes as the strands anneal.

• Nanofabricated Arrays: DNA molecules are stretched in nanochannels, and replication is monitored by fluorescence microscopy.

Single-molecule approaches have revealed that fork reversal is a dynamic process. Forks can reverse and then re-extend (restart) multiple times. The rate of reversal is approximately 1–5 base pairs per second, and the extent of reversal is typically 1–5 kilobases.

Regulation of Fork Reversal

Promoters and Inhibitors of Reversal

Fork reversal is a tightly regulated process. Several proteins promote reversal, while others inhibit it or promote fork restart.

Promoters of Fork Reversal:

• RAD51: Essential for fork reversal. RAD51 nucleoprotein filament formation is required for SMARCAL1-mediated regression.
• SMARCAL1: Catalyzes fork regression.
• ZRANB3: Promotes fork reversal and has endonuclease activity.
• HLTF: Promotes fork reversal and PCNA ubiquitination.
• FBH1: Promotes fork reversal in response to nucleoside depletion.
• FANCD2: Stabilizes reversed forks.
• BLM: Can promote fork regression in vitro.

Inhibitors of Fork Reversal:

• RECQ1: A helicase that promotes fork restart by reversing the reversed fork. RECQ1 counteracts SMARCAL1. The balance between SMARCAL1 and RECQ1 determines whether a fork stays reversed or restarts.
• WRN: Can promote fork regression but also has exonuclease activity that processes reversed forks.
• PARP1: Poly(ADP-ribose) polymerase 1 is recruited to stalled forks and promotes fork reversal. PARP inhibitors (e.g., olaparib) trap PARP1 on DNA and prevent fork reversal.

Regulators of Fork Restart:

• RECQ1: Promotes fork restart by reversing the reversed fork.
• DNA2: A nuclease that processes reversed forks, promoting restart.
• MUS81-EME1: Cleaves reversed forks, generating DSBs that are repaired by HR.

Post-Translational Modifications

Post-translational modifications (PTMs) regulate fork reversal at multiple levels:

Ubiquitination:

• PCNA ubiquitination: In response to replication stress, PCNA is monoubiquitinated at lysine 164 by RAD6-RAD18. This modification recruits ZRANB3 and promotes fork reversal. PCNA can also be polyubiquitinated by HLTF, which promotes error-free template switching.

• SMARCAL1 ubiquitination: SMARCAL1 is ubiquitinated and degraded in response to certain types of stress, limiting the extent of fork reversal.

Phosphorylation:

• ATR/CHK1 pathway: ATR phosphorylates CHK1, which in turn phosphorylates multiple substrates that regulate fork reversal. CHK1 phosphorylates RAD51, promoting its loading at stalled forks. ATR also phosphorylates SMARCAL1, regulating its activity.

• CDK phosphorylation: Cyclin-dependent kinases (CDKs) phosphorylate several fork reversal factors, linking fork reversal to the cell cycle.

SUMOylation:

• RAD51 SUMOylation: SUMOylation of RAD51 promotes its association with stalled forks and facilitates fork reversal.

Acetylation:

• Histone acetylation: Acetylation of histones at stalled forks promotes chromatin remodeling, which facilitates fork reversal.

The regulation of fork reversal is a complex, multi-layered process. The balance between pro-reversal and anti-reversal factors determines the fate of a stalled fork. This balance is critical: too much reversal can lead to excessive fork regression and genome instability, while too little reversal leaves forks unprotected and prone to collapse.

Fork Reversal and Cancer Therapy

Fork Reversal in Chemoresistant Tumors

Fork reversal has emerged as a major determinant of chemoresistance. Many chemotherapeutic agents—including cisplatin, gemcitabine, and hydroxyurea—work by inducing replication stress. Tumors that can effectively reverse their forks are resistant to these agents because they can protect stalled forks and repair the damage.

The connection between fork reversal and chemoresistance is particularly well established for BRCA-deficient tumors. BRCA1 and BRCA2 are essential for homologous recombination and RAD51 loading. BRCA-deficient tumors are hypersensitive to PARP inhibitors and platinum agents. However, some BRCA-deficient tumors develop resistance by restoring fork reversal through alternative mechanisms. For example, loss of RECQ1 or PTIP (PAXIP1) restores fork reversal in BRCA-deficient cells, conferring resistance to PARP inhibitors.

Conversely, tumors with defects in fork reversal are hypersensitive to replication stress. SMARCAL1 mutations are found in some cancers, and these tumors are particularly sensitive to agents that induce replication stress.

Therapeutic Implications

Targeting fork reversal is a promising strategy for cancer therapy. The goal is to identify tumors that depend on fork reversal for survival and to inhibit this process, making the tumors hypersensitive to replication stress.

PARP Inhibitors: PARP inhibitors (e.g., olaparib, niraparib) are already in clinical use for BRCA-deficient tumors. PARP inhibitors trap PARP1 on DNA, preventing fork reversal and promoting fork collapse. This is the mechanism by which PARP inhibitors selectively kill BRCA-deficient cells.

ATR Inhibitors: ATR inhibitors are in clinical development. ATR is essential for the replication stress response, and ATR inhibition prevents fork reversal and promotes fork collapse. ATR inhibitors are being tested in combination with chemotherapeutic agents.

CHK1 Inhibitors: CHK1 inhibitors similarly block the replication stress response and are being tested in clinical trials.

RAD51 Inhibitors: RAD51 is essential for fork reversal. RAD51 inhibitors are in preclinical development and could be used to sensitize tumors to replication stress.

SMARCAL1 Inhibitors: SMARCAL1 is a promising target because it is specifically involved in fork reversal. SMARCAL1 inhibitors could be used to block fork reversal in tumors that depend on this process for survival.

The therapeutic potential of targeting fork reversal is significant. However, the challenge is to develop inhibitors that are specific to cancer cells and do not cause excessive toxicity in normal cells. The replication stress response is essential for all cells, so systemic inhibition of fork reversal could have severe side effects. The hope is that tumors, which experience higher levels of replication stress, will be more sensitive to fork reversal inhibitors than normal cells.

Common Misconceptions and Study Tips

Fork Reversal vs. Fork Collapse

One of the most common misconceptions is confusing fork reversal with fork collapse. These are fundamentally different processes:

Fork reversal is a protective response. Fork collapse is a failure of protection. A collapsed fork is a fork that has been cleaved or has otherwise broken down into a DSB. Fork reversal prevents fork collapse by stabilizing the stalled fork.

Key Points to Remember

1. Fork reversal is active, not passive: It requires specific enzymes (SMARCAL1, ZRANB3, HLTF) and is regulated by post-translational modifications.

1. RAD51 is essential: Without RAD51, fork reversal does not occur. RAD51 is not just for homologous recombination—it is a central player in fork protection.

1. The chicken-foot structure is a four-way junction: It is not a simple "backward movement" of the fork. It involves re-annealing of parental strands and annealing of nascent strands.

1. Fork reversal is reversible: RECQ1 can reverse the reversed fork, restoring the normal three-way junction. The balance between SMARCAL1 and RECQ1 determines fork fate.

1. Fork reversal prevents DSBs: The primary function of fork reversal is to protect stalled forks from nucleolytic attack and collapse.

1. Fork reversal is connected to repair pathways: Template switching, homologous recombination, and the Fanconi anemia pathway all intersect with fork reversal.

1. Fork reversal is a therapeutic target: PARP inhibitors work, in part, by preventing fork reversal. New inhibitors targeting fork reversal factors are in development.

Frequently Asked Questions

What is replication fork reversal?

Replication fork reversal is a protective DNA damage response in which a stalled replication fork regresses backward, forming a four-way junction (the chicken-foot structure). The parental strands re-anneal, and the nascent strands anneal to each other. This process stabilizes the stalled fork and provides a substrate for repair pathways.

Why does replication fork reversal occur?

Fork reversal occurs in response to replication stress—any condition that impedes replication fork progression. This includes DNA lesions (UV damage, crosslinks, base damage), nucleotide depletion, difficult-to-replicate sequences, and R-loops. The purpose of fork reversal is to protect the stalled fork from collapse into a double-strand break and to provide time and substrate for repair.

What is the chicken-foot structure?

The chicken-foot structure is the four-way junction formed during fork reversal. It has three duplex arms: two parental DNA arms and one nascent DNA arm. The structure resembles a chicken foot in electron micrographs. The nascent arm allows template switching, where the leading strand uses the lagging strand as a template to bypass the lesion.

Which proteins are involved in replication fork reversal?

Key proteins include SMARCAL1, ZRANB3, and HLTF (which catalyze fork regression), RAD51 (essential for fork reversal), RECQ1 (which promotes fork restart by reversing the reversed fork), and FANCD2 (which stabilizes reversed forks). The ATR/CHK1 pathway regulates fork reversal through phosphorylation of downstream targets.

How is replication fork reversal studied?

Fork reversal is studied using DNA fiber assays (which measure fork dynamics by labeling replicating DNA), electron microscopy (which directly visualizes the chicken-foot structure), and single-molecule approaches (such as magnetic tweezers and FRET). Each method has advantages and limitations.

What is the difference between fork reversal and fork collapse?

Fork reversal is a protective, reversible process that stabilizes stalled forks. Fork collapse is an irreversible process in which the fork is cleaved or breaks down into a double-strand break. Fork reversal prevents fork collapse.

Does replication fork reversal cause cancer?

No. Fork reversal is a protective mechanism that prevents genome instability. However, defects in fork reversal can contribute to cancer. Cells that cannot reverse their forks accumulate DNA damage and chromosomal aberrations, which can drive tumorigenesis. Conversely, tumors can upregulate fork reversal to resist chemotherapy.

Key Takeaways

• Replication fork reversal is an active, enzyme-catalyzed process that converts a stalled three-way replication fork into a four-way chicken-foot junction.
• The primary function of fork reversal is to protect stalled forks from collapse into double-strand breaks and to provide a substrate for error-free repair.
• SMARCAL1, ZRANB3, and HLTF are the core translocases that drive fork regression; RAD51 is essential for the process.
• Fork reversal is reversible: RECQ1 promotes fork restart by reversing the reversed fork.
• Fork reversal is triggered by diverse forms of replication stress, including UV damage, crosslinks, nucleotide depletion, and R-loops.
• Fork reversal is studied using DNA fiber assays, electron microscopy, and single-molecule techniques.
• Fork reversal is a determinant of chemoresistance and a promising therapeutic target; PARP inhibitors work in part by preventing fork reversal.
• Fork reversal is distinct from fork collapse: reversal is protective and reversible, while collapse is destructive and irreversible.

Further Reading

• Adolph MB, Cortez D. Mechanisms and regulation of replication fork reversal. DNA repair. 2024. PubMed 39089193
• Qiu S et al. Replication Fork Reversal and Protection. Frontiers in cell and developmental biology. 2021. PubMed 34041245
• Quinet A, Lemaçon D, Vindigni A. Replication Fork Reversal: Players and Guardians. Molecular cell. 2017. PubMed 29220651
• Michel B, Sinha AK, Leach DRF. Replication Fork Breakage and Restart in Escherichia coli. Microbiology and molecular biology reviews : MMBR. 2018. PubMed 29898897
• Kondratick CM, Washington MT, Spies M. Making Choices: DNA Replication Fork Recovery Mechanisms. Seminars in cell & developmental biology. 2021. PubMed 33967572
• Thakar T, Moldovan GL. The emerging determinants of replication fork stability. Nucleic acids research. 2021. PubMed 33978751

Related Topics

• Replication Fork Definition
• Replication Fork Bubble
• Replication Fork Stalling
• Replication Fork Helicase

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