Multistep mechanism of G-quadruplex resolution during DNA replication
Open accessAbstract
DNA helicases DHX36 and FANCJ constitute a previously unknown pathway that resolves G-quadruplex structures during DNA replication.
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
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?
Further reports demonstrated that G4s cause replication-dependent DNA-damage or change the overall chromatin structure.
“Further reports demonstrated that G4s cause replication-dependent DNA-damage or change the overall chromatin structure (66,67).”
From G-quadruplex-mediated genomic instability drives SNVs in cancer (2024) · cites this paper as [66]
The Introduction reports that DNA damage induced by G4-stabilizing ligands is replication dependent. The Discussion links G4-related polymerase stalling to possible replication-associated breaks, but also says that G4 structures do not directly cause an accumulation of DNA damage under unperturbed conditions. The claim omits those conditions and presents the damage link more categorically than this paper does. (LLM, conf=0.85)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Cox, J., & Mann, M. (2008) · Nature Biotechnology · doi:10.1038/nbt.1511 · Cited by 14,855 · see citing works
Pérez-Riverol, Y., Csordas, A., Bai, J.-W., Bernal-Llinares, M., Hewapathirana, S., Kundu, D. J., Inuganti, A., Griss, J., Mayer, G., Eisenacher, M., et al. (2018) · Nucleic Acids Res. · doi:10.1093/nar/gky1106 · Cited by 6,216 · see citing works
Quadruplex DNA: sequence, topology and structure
Burge, S., Parkinson, G. N., Hazel, P., Todd, A. K., & Neidle, S. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl655 · Cited by 2,404 · see citing works
Quantitative visualization of DNA G-quadruplex structures in human cells
Biffi, G., Tannahill, D., McCafferty, J., & Balasubramanian, S. (2013) · Nature Chemistry · doi:10.1038/nchem.1548 · Cited by 2,152 · see citing works
Siddiqui-Jain, A., Grand, C., Bearss, D., & Hurley, L. (2002) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.182256799 · Cited by 2,069 · see citing works
Sen, D., & Gilbert, W. (1988) · Nature · doi:10.1038/334364a0 · Cited by 1,668 · see citing works
Prevalence of quadruplexes in the human genome
Huppert, J., & Balasubramanian, S. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki609 · Cited by 1,655 · see citing works
Helix formation by guanylic acid.
Gellert, M., Lipsett, M., & Davies, D. R. (1962) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.48.12.2013 · Cited by 1,430 · see citing works
The regulation and functions of DNA and RNA G-quadruplexes
Varshney, D., Spiegel, J., Zyner, K. G., Tannahill, D., & Balasubramanian, S. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0236-x · Cited by 1,265 · see citing works
Inhibition of telomerase by G-quartet DMA structures
Zahler, A., Williamson, J., Cech, T., & Prescott, D. (1991) · Nature · doi:10.1038/350718a0 · Cited by 1,041 · see citing works
Mammalian Telomeres Resemble Fragile Sites and Require TRF1 for Efficient Replication
Sfeir, A., Kosiyatrakul, S. T., Hockemeyer, D., MacRae, S. L., Karlseder, J., Schildkraut, C. L., & de Lange, T. (2009) · Cell · doi:10.1016/j.cell.2009.06.021 · Cited by 990 · see citing works
Geminin, an inhibitor of DNA replication, is degraded during mitosis.
Mcgarry, T., & Kirschner, M. (1998) · Cell · doi:10.1016/s0092-8674(00)81209-x · Cited by 988 · see citing works
Small-molecule–induced DNA damage identifies alternative DNA structures in human genes
Rodriguez, R., Miller, K. M., Forment, J. V., Bradshaw, C. R., Nikan, M., Britton, S., Oelschlaegel, T., Xhemalce, B., Balasubramanian, S., & Jackson, S. P. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.780 · Cited by 741 · see citing works
Cantor, S. B., Bell, D. W., Ganesan, S., Kass, E. M., Drapkin, R., Grossman, S., Wahrer, D. C. R., Sgroi, D. C., Lane, W. S., Haber, D. A., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00304-x · Cited by 674 · see citing works
CX-5461 is a DNA G-quadruplex stabilizer with selective lethality in BRCA1/2 deficient tumours
Xu, H., Antonio, M. D., McKinney, S. E., Mathew, V., Ho, B., O’Neil, N. J., Santos, N. D., Silvester, J., Wei, V., Garcia, J., et al. (2017) · Nature Communications · doi:10.1038/ncomms14432 · Cited by 574 · see citing works
Walter, J. C., & Newport, J. (2000) · Molecules and Cells · doi:10.1016/s1097-2765(00)80241-5 · Cited by 472 · see citing works
The DNA helicase BRIP1 is defective in Fanconi anemia complementation group J
Levitus, M., Waisfisz, Q., Godthelp, B. C., Vries, Y. D., Hussain, S., Wiegant, W. W., Elghalbzouri-Maghrani, E., Steltenpool, J., Rooimans, M. A., Pals, G., et al. (2005) · Nature Genetics · doi:10.1038/ng1625 · Cited by 432 · see citing works
Human telomeric DNA: G-quadruplex, i-motif and Watson-Crick double helix.
Phan, A., & Mergny, J. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf597 · Cited by 431 · see citing works
Wu, Y., Shin-ya, K., & Brosh, R. M. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02210-07 · Cited by 428 · see citing works
Mutations in BRIP1 confer high risk of ovarian cancer
Rafnar, Þ., Gudbjartsson, D. F., Sulem, P., Jónasdóttir, Á., Sigurðsson, Á., Jónasdóttir, A., Besenbacher, S., Lundin, P., Stacey, S., Guðmundsson, J., et al. (2011) · Nature Genetics · doi:10.1038/ng.955 · Cited by 406 · see citing works
Pacek, M., Tutter, A., Kubota, Y., Takisawa, H., & Walter, J. (2006) · Molecules and Cells · doi:10.1016/j.molcel.2006.01.030 · Cited by 401 · see citing works
Litman, R., Peng, M., Jin, Z., Zhang, F., Zhang, J., Powell, S., Andreassen, P. R., & Cantor, S. B. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.08.004 · Cited by 396 · see citing works
Heterogeneity of eukaryotic replicons, replicon clusters, and replication foci
Berezney, R., Dubey, D., & Huberman, J. (2000) · Chromosoma · doi:10.1007/s004120050399 · Cited by 390 · see citing works
The BRCA1-interacting helicase BRIP1 is deficient in Fanconi anemia
Levran, O., Attwooll, C., Henry, R. T., Milton, K. L., Neveling, K., Rio, P., Batish, S. D., Kalb, R., Velleuer, E., Barral, S., et al. (2005) · Nature Genetics · doi:10.1038/ng1624 · Cited by 370 · see citing works
Multiple pathways cooperate in the suppression of genome instability in Saccharomyces cerevisiae
Myung, K., Chen, C. C., & Kolodner, R. (2001) · Nature · doi:10.1038/35082608 · Cited by 369 · see citing works
Cayrou, C., Coulombe, P., Vigneron, A., Stanojčić, S., Ganier, O., Peiffer, I., Rivals, É., Puy, A., Laurent‐Chabalier, S., Desprat, R., et al. (2011) · Genome Research · doi:10.1101/gr.121830.111 · Cited by 359 · see citing works
Alabert, C., Bukowski-Wills, J.-C., Lee, S.-B., Kustatscher, G., Nakamura, K., Alves, F. D. L., Ménard, P., Mejlvang, J., Rappsilber, J., & Groth, A. (2014) · Nature Cell Biology · doi:10.1038/ncb2918 · Cited by 334 · see citing works
The Mcm2-7 complex has in vitro helicase activity.
Bochman, M. L., & Schwacha, A. (2008) · Molecules and Cells · doi:10.1016/j.molcel.2008.05.020 · Cited by 313 · see citing works
Regulation of Murine Telomere Length by Rtel
Ding, H., Schertzer, M., Wu, X., Gertsenstein, M., Selig, S., Kammori, M., Pourvali, R., Poon, S., Vulto, I., Chavez, E., et al. (2004) · Cell · doi:10.1016/j.cell.2004.05.026 · Cited by 309 · see citing works
Epigenetic Instability due to Defective Replication of Structured DNA
Sarkies, P., Reams, C., Simpson, L. J., & Sale, J. E. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.11.009 · Cited by 302 · see citing works
Structural basis of G-quadruplex unfolding by the DEAH/RHA helicase DHX36
Chen, M. C., Tippana, R., Demeshkina, N., Murat, P., Balasubramanian, S., Myong, S., & Ferré-D'Amaré, A. (2018) · Nature · doi:10.1038/s41586-018-0209-9 · Cited by 291 · see citing works
Disruption of dog-1 in Caenorhabditis elegans triggers deletions upstream of guanine-rich DNA
Cheung, I. K., Schertzer, M. J., Rose, A. M., & Lansdorp, P. M. (2002) · Nature Genetics · doi:10.1038/ng928 · Cited by 270 · see citing works
FANCJ Is a Structure-specific DNA Helicase Associated with the Maintenance of Genomic G/C Tracts
London, T. B. C., Barber, L. J., Mosedale, G., Kelly, G. P., Balasubramanian, S., Hickson, I. D., Boulton, S. J., & Hiom, K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m808152200 · Cited by 252 · see citing works
Mechanism of RAD51-Dependent DNA Interstrand Cross-Link Repair
Long, D. T., Räschle, M., Joukov, V., & Walter, J. C. (2011) · Science · doi:10.1126/science.1204258 · Cited by 238 · see citing works
Repair of a DNA-protein crosslink by replication-coupled proteolysis
Duxin, J. P., Dewar, J. M., Yardimci, H., & Walter, J. (2014) · Cell · doi:10.1016/j.cell.2014.09.024 · Cited by 225 · see citing works
RTEL1 Is a Replisome-Associated Helicase That Promotes Telomere and Genome-Wide Replication
Vannier, J., Sandhu, S., Petalcorin, M. I. R., Wu, X., Nabi, Z., Ding, H., & Boulton, S. J. (2013) · Science · doi:10.1126/science.1241779 · Cited by 220 · see citing works
Direct identification of the active-site nucleophile in a DNA (cytosine-5)-methyltransferase.
Chen, L., Macmillan, A., Chang, W., Ezaz‐Nikpay, K., Lane, W. A. S., & Verdine, G. (1991) · Biochemistry · doi:10.1021/bi00110a002 · Cited by 220 · see citing works
Mutagenic Capacity of Endogenous G4 DNA Underlies Genome Instability in FANCJ-Defective C. elegans
Kruisselbrink, E., Guryev, V., Brouwer, K., Pontier, D. B., Cuppen, E., & Tijsterman, M. (2008) · Current Biology · doi:10.1016/j.cub.2008.05.013 · Cited by 209 · see citing works
Replication-dependent unhooking of DNA interstrand cross-links by the NEIL3 glycosylase
Semlow, D. R., Zhang, J.-Q., Budzowska, M., Drohat, A., & Walter, J. (2016) · Cell · doi:10.1016/j.cell.2016.09.008 · Cited by 201 · see citing works
Facilitation of mRNA deadenylation and decay by the exosome-bound, DExH protein RHAU.
Tran, H., Schilling, M., Wirbelauer, C., Hess, D., & Nagamine, Y. (2004) · Molecules and Cells · doi:10.1016/s1097-2765(03)00481-7 · Cited by 201 · see citing works
Human replication protein A unfolds telomeric G-quadruplexes
Salas, T. R., Petruseva, I. O., Lavrik, O. I., Bourdoncle, A., Mergny, J., Favre, A., & Saintomé, C. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl564 · Cited by 177 · see citing works
Replication-Coupled DNA-Protein Crosslink Repair by SPRTN and the Proteasome in Xenopus Egg Extracts
Larsen, N. B., Gao, A. O., Sparks, J. L., Gallina, I., Wu, R., Mann, M., Räschle, M., Walter, J. C., & Duxin, J. P. (2019) · Molecules and Cells · doi:10.1016/j.molcel.2018.11.024 · Cited by 176 · see citing works
TRAIP is a master regulator of DNA interstrand cross-link repair
Wu, R., Semlow, D. R., Kamimae-Lanning, A. N., Kochenova, O. V., Chistol, G., Hodskinson, M., Amunugama, R., Sparks, J. L., Wang, M., Deng, L., et al. (2019) · Nature · doi:10.1038/s41586-019-1002-0 · Cited by 175 · see citing works
The CMG helicase bypasses DNA-protein cross-links to facilitate their repair
Sparks, J. L., Chistol, G., Gao, A. O., Räschle, M., Larsen, N. B., Mann, M., Duxin, J. P., & Walter, J. (2018) · bioRxiv · doi:10.1101/381582 · Cited by 172
G-Quadruplex DNA as a Molecular Target for Induced Synthetic Lethality in Cancer Cells
McLuckie, K. I. E., Antonio, M. D., Zecchini, H. I., Xian, J., Caldas, C., Krippendorff, B., Tannahill, D., Lowe, C., & Balasubramanian, S. (2013) · Journal of the American Chemical Society · doi:10.1021/ja404868t · Cited by 172 · see citing works
The mechanism of DNA replication termination in vertebrates
Dewar, J. M., Budzowska, M., & Walter, J. (2015) · Nature · doi:10.1038/nature14887 · Cited by 158 · see citing works
Replication of G Quadruplex DNA
Lerner, L. K., & Sale, J. E. (2019) · Genes · doi:10.3390/genes10020095 · Cited by 156 · see citing works
DNA interstrand cross-link repair requires replication fork convergence
Zhang, J.-Q., Dewar, J. M., Budzowska, M., Motnenko, A., Cohn, M., & Walter, J. (2015) · Nature Structural &Molecular Biology · doi:10.1038/nsmb.2956 · Cited by 154 · see citing works
FANCJ promotes DNA synthesis through G‐quadruplex structures
Bosch, P. C., Segura‐Bayona, S., Koole, W., Heteren, J. T. V., Dewar, J. M., Tijsterman, M., & Knipscheer, P. (2014) · The EMBO Journal · doi:10.15252/embj.201488663 · Cited by 154 · see citing works
Self-citationProliferating Cell Nuclear Antigen Uses Two Distinct Modes to Move along DNA*
Kochaniak, A. B., Habuchi, S., Loparo, J., Chang, D. J., Cimprich, K. A., Walter, J., & van Oijen, A. V. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.008706 · Cited by 147 · see citing works
Bharti, S. K., Sommers, J. A., George, F., Kuper, J., Hamon, F., Shin‐ya, K., Teulade‐Fichou, M., Kisker, C., & Brosh, R. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.496463 · Cited by 136 · see citing works
Lemmens, B., van Schendel, R., & Tijsterman, M. (2015) · Nature Communications · doi:10.1038/ncomms9909 · Cited by 133 · see citing works
Regulation of the Rev1–pol ζ complex during bypass of a DNA interstrand cross‐link
Budzowska, M., Graham, T. G. W., Sobeck, A., Shou, W.-G., & Walter, J. C. (2015) · EMBO Journal · doi:10.15252/embj.201490878 · Cited by 132 · see citing works
Mechanism of replication‐coupled DNA interstrand cross‐link repair
Walter, J. (2013) · doi:10.1096/fasebj.27.1_supplement.95.3 · Cited by 132
Liu, H., Zhao, Q., Zhang, T., Wu, Y., Xiong, Y., Wang, S., Ge, Y., He, J., Lv, P., Ou, T., et al. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2016.08.013 · Cited by 128 · see citing works
Do, N. Q., & Phan, A. (2012) · Chemistry · doi:10.1002/chem.201103295 · Cited by 124
Gupta, R., Sharma, S., Sommers, J. A., Kenny, M. K., Cantor, S. B., & Brosh, R. M. (2007) · Blood · doi:10.1182/blood-2006-11-057273 · Cited by 113 · see citing works
G-quadruplex recognition and remodeling by the FANCJ helicase
Wu, C. G., & Spies, M. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw574 · Cited by 105 · see citing works
FANCJ couples replication past natural fork barriers with maintenance of chromatin structure
Schwab, R. A., Nieminuszczy, J., Shin‐ya, K., & Niedźwiedź, W. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201208009 · Cited by 103 · see citing works
G4 Resolvase 1 tightly binds and unwinds unimolecular G4-DNA
Giri, B., Smaldino, P. J., Thys, R. G., Creacy, S., Routh, E. D., Hantgan, R., Lattmann, S., Nagamine, Y., Akman, S., & Vaughn, J. P. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr234 · Cited by 96
Structure of the eukaryotic replicative CMG helicase and pumpjack motion
Yuan, Z.-N., Bai, L., Sun, J.-C., Georgescu, R., Liu, J., O'Donnell, M., & Li, H.-L. (2016) · Nature Structural &Molecular Biology · doi:10.1038/nsmb.3170 · Cited by 90 · see citing works
G-quadruplex-interacting compounds alter latent DNA replication and episomal persistence of KSHV
Madireddy, A., Purushothaman, P., Loosbroock, C., Robertson, E. S., Schildkraut, C. L., & Verma, S. C. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw038 · Cited by 88 · see citing works
Murine Pif1 Interacts with Telomerase and Is Dispensable for Telomere Function In Vivo
Snow, B., Mateyak, M., Paděrová, J., Wakeham, A., Iorio, C., Zakian, V., Squire, J., & Harrington, L. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01866-06 · Cited by 78 · see citing works
Timeless couples G‐quadruplex detection with processing by DDX11 helicase during DNA replication
Lerner, L. K., Holzer, S., Kilkenny, M. L., Šviković, S., Murat, P., Schiavone, D., Eldridge, C. B., Bittleston, A., Maman, J. D., Branzei, D., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019104185 · Cited by 71 · see citing works
Translocation and Stability of Replicative DNA Helicases upon Encountering DNA-Protein Cross-links*
Nakano, T., Miyamoto-Matsubara, M., Shoulkamy, M. I., Salem, A. M. H., Pack, S., Ishimi, Y., & Ide, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.419358 · Cited by 65 · see citing works
p97 Promotes a Conserved Mechanism of Helicase Unloading during DNA Cross-Link Repair
Fullbright, G., Rycenga, H. B., Gruber, J. D., & Long, D. T. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00434-16 · Cited by 64 · see citing works
HSF2BP Interacts with a Conserved Domain of BRCA2 and Is Required for Mouse Spermatogenesis
Brandsma, I., Sato, K., van Rossum-Fikkert, S. E., van Vliet, N., Sleddens–Linkels, E., Reuter, M., Odijk, H., van den Tempel, N., Dekkers, D. H. W., Bezstarosti, K., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.05.096 · Cited by 61 · see citing works
Self-citationMATSUZAKI, K., Borel, V., Adelman, C. A., Schindler, D., & Boulton, S. J. (2015) · Genes & Development · doi:10.1101/gad.272740.115 · Cited by 58 · see citing works
The DEAH-box helicase RHAU is an essential gene and critical for mouse hematopoiesis.
Lai, J., Ponti, S., Pan, D., Kohler, H., Skoda, R., Matthias, P., & Nagamine, Y. (2012) · Blood · doi:10.1182/blood-2011-08-362954 · Cited by 55
Extracts for Analysis of DNA Replication in a Nucleus-Free System.Preprint
Sparks, J. L., & Walter, J. (2019) · Cold Spring Harbor Protocols · doi:10.1101/pdb.prot097154 · Cited by 48 · see citing works
Folding Landscape of a Parallel G-quadruplex
Gray, R., Trent, J., Arumugam, S., & Chaires, J. (2019) · bioRxiv · doi:10.1101/526780 · Cited by 40
Yangyuoru, P. M., Bradburn, D. A., Liu, Z., Xiao, T., & Russell, R. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.815076 · Cited by 34
Enoiu, M., Ho, T. V., Long, D. T., Walter, J., & Schärer, O. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-998-3_15 · Cited by 33
Lac repressor binding to synthetic DNAs of defined nucleotide sequence.
Riggs, A., Lin, S., & Wells, R. (1972) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.69.3.761 · Cited by 32
HSF2BP negatively regulates homologous recombination in DNA interstrand crosslink repair
Sato, K., Brandsma, I., van Rossum-Fikkert, S. E., Verkaik, N. S., Oostra, A. B., Dorsman, J. C., van Gent, D. C., Knipscheer, P., Kanaar, R., & Zelensky, A. N. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz1219 · Cited by 27 · see citing works
Self-citationThe DEAH helicase DHX36 and its role in G-quadruplex-dependent processes
Schult, P., & Paeschke, K. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0292 · Cited by 25 · see citing works
Activation of the FA pathway mediated by phosphorylation and ubiquitination
Ishiai, M., Sato, K., Tomida, J., Kitao, H., Kurumizaka, H., & Takata, M. (2017) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2017.05.003 · Cited by 20 · see citing works
Self-citationHomology-driven assembly of NOn-redundant protEin sequence sets (NOmESS) for mass spectrometry
Temu, T., Mann, M., Räschle, M., & Cox, J. (2015) · Bioinform. · doi:10.1093/bioinformatics/btv756 · Cited by 8 · see citing works
Expression and purification of human FANCI and FANCD2 using Escherichia coli cells
Takahashi, D., Sato, K., Shimomuki, M., Takata, M., & Kurumizaka, H. (2014) · Protein Expression and Purification · doi:10.1016/j.pep.2014.08.012 · Cited by 4 · see citing works
Self-citation
Flagged first, then by citations
3 of the 82 references couldn’t be matched to a known paper.
Research works printed but not linked: 3
- [28]E. Izbicka, R. T. Wheelhouse, E. Raymond, K. K. Davidson, R. A. Lawrence, D. Sun, B. E. Windle, L. H. Hurley, D. D. Von Hoff, Effects of cationic porphyrins as G-quadruplex interactive agents in human tumor cells. Cancer Res. 59, 639– 644 (1999). 9973212
- [31]C. Alabert, J. C. Bukowski-Wills, S. B. Lee, G. Kustatscher, K. Nakamura, F. de Lima Alves, P. Menard, J. Mejlvang, J. Rappsilber, A. Groth, Nascent chromatin capture proteomics determines chromatin dynamics during DNA replication and identifies unknown fork components. Nat. Cell Biol. 16, 281– 291 (2014). 24561620 PMC4283098
- [39]M. Räschle, P. Knipscheer, M. Enoiu, T. Angelov, J. Sun, J. D. Griffith, T. E. Ellenberger, O. D. Scharer, J. C. Walter, Mechanism of replication-coupled DNA interstrand crosslink repair. Cell 134, 969– 980 (2008). 18805090 PMC2748255
Cited by
Sorted by citations
G-Quadruplex-Binding Proteins: Promising Targets for Drug Design
Shu, H.-L., Zhang, R., Xiao, K., Yang, J., & Sun, X. (2022) · Biomolecules · doi:10.3390/biom12050648 · Cited by 78 · see citing works
“FANCJ can unfold and remove G4 structures for efficient DNA replication while its absence will stop replication at G4s and eventually lead to DNA damage [79].”
BackgroundInfluentialUltrafast reversible self-assembly of living tangled matter
Patil, V. P., Tuazon, H., Kaufman, E. M., Chakrabortty, T., Qin, D., Dunkel, J., & Bhamla, M. S. (2022) · Science · doi:10.1126/science.ade7759 · Cited by 68
G-quadruplex resolution: From molecular mechanisms to physiological relevance
Sato, K., & Knipscheer, P. (2023) · DNA repair · doi:10.1016/j.dnarep.2023.103552 · Cited by 64 · see citing works
Self-citationThe FANCJ Helicase Unfolds DNA-Protein Cross-Links to Promote Their Repair
Yaneva, D., Sparks, J. L., Donsbach, M., Zhao, S.-B., Weickert, P., Bezalel-Buch, R., Stingele, J., & Walter, J. (2023) · Molecules and Cells · doi:10.1016/j.molcel.2022.12.005 · Cited by 47 · see citing works
Ligands stimulating antitumour immunity as the next G-quadruplex challenge
Miglietta, G., Marinello, J., Russo, M., & Capranico, G. (2022) · Molecular Cancer · doi:10.1186/s12943-022-01649-y · Cited by 44 · see citing works
“A coordinated action of three helicases, DHX35, FANCJ and the replicative CMG complex, has recently been shown to promote bypass and unfolding of stabilized G4s during replication in an ex-vivo model of Xenopus egg extracts [77].”
BackgroundRNA transcripts regulate G-quadruplex landscapes through G-loop formation
Sato, K., Lyu, J., van den Berg, J., Braat, D., Cruz, V. M., Luzón, C. N., Schimmel, J., Esteban-Jurado, C., Alemany, M., Dreyer, J., et al. (2025) · Science · doi:10.1126/science.adr0493 · Cited by 37 · see citing works
Self-citationG-quadruplex–stalled eukaryotic replisome structure reveals helical inchworm DNA translocation
Batra, S., Allwein, B., Kumar, C., Devbhandari, S., Brüning, J.-G., Bahng, S., Lee, C. M., Marians, K. J., Hite, R. K., & Remus, D. (2025) · Science · doi:10.1126/science.adt1978 · Cited by 42 · see citing works
Rouillon, C., Eckhardt, B. V., Kollenstart, L., Gruss, F., Verkennis, A. E. E., Rondeel, I., Krijger, P. H. L., Ricci, G., Biran, A., van Laar, T., et al. (2022) · bioRxiv · doi:10.1093/nar/gkad171 · Cited by 35 · see citing works
“We used single stranded plasmid DNA as template for DNA synthesis, and it was produced as previously described (64).”
MethodSelf-citationLooping out of control: R-loops in transcription-replication conflict
Kumar, C., & Remus, D. (2023) · Chromosoma · doi:10.1007/s00412-023-00804-8 · Cited by 34 · see citing works
“Consequently, G4s especially on the leading strand template are a source for DNA replication stress associated with genetic or epigenetic instability (Sarkies et al. 2010; Lopes et al. 2011; Sato et al. 2021).”
Creation and resolution of non-B-DNA structural impediments during replication
Mellor, C., Perez, C., & Sale, J. E. (2022) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2022.2121803 · Cited by 37 · see citing works
“Intrastrand DNA structures formed on the lagging strand should pass around the CMG helicase, and this is observed in Xenopus egg extracts (Sato et al. 2021).”
BackgroundInfluentialStructural Unfolding of G-Quadruplexes: From Small Molecules to Antisense Strategies
Fracchioni, G., Vailati, S., Grazioli, M., & Pirota, V. (2024) · Molecules · doi:10.3390/molecules29153488 · Cited by 30
The Cellular Functions and Molecular Mechanisms of G-Quadruplex Unwinding Helicases in Humans
Liu, Y., Zhu, X., Wang, K., Zhang, B., & Qiu, S. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.783889 · Cited by 28 · see citing works
“PIF1 (Dahan et al., 2018), and FANCJ (Sato et al., 2021) were reported to unfold lagging strand G4s.”
BackgroundInfluentialVariation in G-quadruplex sequence and topology differentially impacts human DNA polymerase fidelity
Stein, M., Hile, S. E., Weissensteiner, M. H., Lee, M., Zhang, S., Kejnovský, E., Kejnovská, I., Makova, K. D., & Eckert, K. A. (2022) · DNA Repair · doi:10.1016/j.dnarep.2022.103402 · Cited by 23 · see citing works
Fanconi anemia proteins and genome fragility: unraveling replication defects for cancer therapy
Badra-Fajardo, N., Taraviras, S. L., & Lygerou, Z. (2022) · Trends in cancer · doi:10.1016/j.trecan.2022.01.015 · Cited by 27 · see citing works
G-quadruplex-mediated genomic instability drives SNVs in cancer
Richl, T., Kuper, J., & Kisker, C. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae098 · Cited by 20 · see citing works
“Further reports demonstrated that G4s cause replication-dependent DNA-damage or change the overall chromatin structure ( 66 ,67 ).”
BackgroundMitochondrial RelA empowers mtDNA G-quadruplex formation for hypoxia adaptation in cancer cells
Tang, G.-X., Li, M., Zhou, C., Huang, Z., Chen, S., Chen, X.-C., & Tan, J. (2024) · Cell chemical biology · doi:10.1016/j.chembiol.2024.05.003 · Cited by 17 · see citing works
The Dynamic Regulation of G-Quadruplex DNA Structures by Cytosine Methylation
Stevens, A., de Jong, L., & Kennedy, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052407 · Cited by 17 · see citing works
Conformational Plasticity of Parallel G-Quadruplex─Implications on Duplex-Quadruplex Motifs.
Sannapureddi, R. K. R., Mohanty, M. K., Salmon, L., & Sathyamoorthy, B. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c03218 · Cited by 16 · see citing works
Lansdorp, P. M. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.943622 · Cited by 27 · see citing works
“Such studies should elucidate the balance between proteins that suppress the formation of G4 DNA at telomeres and helicases such as RTEL1, BLM and FANCJ that are capable of unwinding G4 structures (36).”
BackgroundDNA G-quadruplexes: Structural and functional insights
Jonchhe, S., Lahiri, S., & Rothenberg, E. (2025) · DNA repair · doi:10.1016/j.dnarep.2025.103910 · Cited by 12 · see citing works
DHX36 maintains genomic integrity by unwinding G‐quadruplexes
Mizumoto, A., Yokoyama, Y., Miyoshi, T., Takikawa, M., Ishikawa, F., & Sadaie, M. (2023) · Genes to Cells · doi:10.1111/gtc.13061 · Cited by 11 · see citing works
“A recent report suggested the supportive function of DHX36 in DNA replication (Sato et al., 2021).”
BackgroundUltra-Specific G-Quadruplex–Colistin Interaction for Efficient Transcriptome-Wide G4 Mapping
Wei, S., Zhang, X., Feng, Y., Tao, S., Qiu, D., Yan, X., Li, G., Guittat, L., Zhang, W., Monchaud, D., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c01172 · Cited by 11 · see citing works
FANCJ DNA helicase is recruited to the replisome by AND-1 to ensure genome stability
(2024) · doi:10.1038/s44319-023-00044-y · Cited by 11 · see citing works
“…role in resolving G4 structures at DNA replication forks (Cheung et al, 2002; Wu et al, 2008; Schwab et al, 2013; Castillo Bosch et al, 2014; Sato et al, 2021; Van Schendel et al, 2021) and with biochemical studies showing that FANCJ is able to untangle different kinds of G4 DNA…”
BackgroundFANCJ DNA helicase is recruited to the replisome by AND-1 to ensure genome stability
Boavida, A., Napolitano, L. M. R., Santos, D., Cortone, G., Onesti, S., Jegadesan, N. K., Branzei, D., & Pisani, F. M. (2022) · doi:10.1101/2022.10.21.513143 · Cited by 11 · see citing works
“…carried out in different systems (worms (Cheung et al, 2002), chicken DT40 (Sarkies et al, 2012) and human cells (Bharti et al, 2013) and Xenopus laevis cell-free egg extracts (Castillo Bosch et al, 2014; Sato et al, 2021)) pointed towards a prominent role of FANCJ in G4 DNA cellular metabolism.”
BackgroundThompson, M. D., & Byrd, A. K. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf678 · Cited by 11 · see citing works
“Binding of proteins to these DNA secondary structures can modulate processes such as transcription [ 4 , 5 ], and resolution of these secondary structures is crucial to safeguarding genomic stability [ 23 , 24 ] (reviewed in [ 25 ]).”
Karam, J. A. Q., Fréreux, C., Mohanty, B., Dalton, A., Dincman, T., Palanisamy, V., Howley, B. V., & Howe, P. H. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107830 · Cited by 10 · see citing works
“6 C ), has been shown to be required for replication of G4 DNA (69).”
BackgroundYan, J., Bu, L., Wang, Y., Yao, H., Li, G., Zheng, K., & Huang, J. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf543 · Cited by 10 · see citing works
“Given the role of G4s in impeding DNA replication [ 34 ], we further evaluated PyBI’s effects using a DNA polymerase extension assay (Fig.”
Bartosik, A. R., Hou, P., Tang, S., Vaughn, J. P., Smaldino, P. J., Ratan, A., Mayo, M. W., & Wang, Y. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf621 · Cited by 13 · see citing works
How DNA secondary structures drive replication fork instability
Sethi, A., Fernández-Casañas, M., Delpino, B., & Coster, G. (2025) · DNA repair · doi:10.1016/j.dnarep.2025.103913 · Cited by 7 · see citing works
Non-B DNA structures and their contributions to genetic diversity, aging, and disease
Bochalis, E., Dereki, I., Wang, G., Sgourou, A., Vásquez, K. M., & Georgakopoulos‐Soares, I. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag084 · Cited by 7 · see citing works
“The increased stability of G-quadruplexes in the presence of molecules such as PhenDC3 and TMPyP4 counteracts the activity of G-quadruplex-resolving helicases, enhancing previously mentioned events associated with genetic instability [ 283 , 316 ].”
The age‐related decline of helicase function—how G‐quadruplex structures promote genome instability
Frobel, J., & Hänsel‐Hertsch, R. (2024) · FEBS Letters · doi:10.1002/1873-3468.14939 · Cited by 6 · see citing works
G-Quadruplex Unwinding Molecular Mechanisms by Helicases and Their Applications
Sun, J., Wang, Y.-Z., Huang, Y., & Chen, Z. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27041629 · Cited by 6 · see citing works
“Then FANCJ subsequently binds and resolves the G4 itself, enabling DNA polymerase progression [64].”
Pepe, S., Guerra, F., Russo, M., Duardo, R. C., & Capranico, G. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115706 · Cited by 7 · see citing works
Bartosik, A. R., Hou, P.-C., Vaughn, J. P., Smaldino, P. J., Ratan, A., Mayo, M. W., & Yuh-Hwa, W. (2025) · bioRxiv · doi:10.1101/2025.01.03.631217 · Cited by 6
“Under these instances, G4 structures can cause DNA double-strand breaks (DSBs), disrupt histone recycling, or increase mutational rate and genome instability (22, 25–27).”
Control of DNA replication in vitro using a reversible replication barrier
Vontalge, E. J., Kavlashvili, T., Dahmen, S. N., Cranford, M., & Dewar, J. M. (2024) · Nature Protocols · doi:10.1038/s41596-024-00977-1 · Cited by 5
Rare genetic diseases associated with G-quadruplex-induced replication stress
Herr, L. M., Mukhopadhyay, S., Anderson, O. M., Couch, T. H., Jones, C. M., Brosh, R. M., & Rossi, M. S. (2026) · Communications Biology · doi:10.1038/s42003-026-09966-4 · Cited by 3 · see citing works
Hile, S. E., Weissensteiner, M. H., Pytko, K. G., Dahl, J. M., Kejnovský, E., Kejnovská, I., Hedglin, M., Georgakopoulos‐Soares, I., Makova, K. D., & Eckert, K. A. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf352 · Cited by 3 · see citing works
“Using Xenopus egg extracts, G4 structure unwinding by the FANCJ helicase was shown to facilitate replicative DNA synthesis through a G4-forming motif sequence [ 26 ].”
InfluentialLong, S., Zhou, J.-L., Zheng, Y., Xiao, Q., Li, Y., Yin, Z., Tian, W.-X., Xiong, Z., Chen, W., & Liu, M. (2024) · Journal of Photochemistry and Photobiology A: Chemistry · doi:10.1016/j.jphotochem.2024.115783 · Cited by 4 · see citing works
Tateishi-Karimata, H., Kawauchi, K., Takahashi, S., & Sugimoto, N. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c11160 · Cited by 4
Pham, P., Wood, E., Dunbar, E. L., Cox, M., & Goodman, M. F. (2023) · bioRxiv · doi:10.1101/2023.10.01.560376 · Cited by 4
“…to form between the RRS-G4 polymerase blocking site and the 5 -end of the preceding Okazaki’s fragment, whereas the leading strand Pol III probably stalls at the RRS-G4 site and resumes DNA synthesis after G4 structure resolution by SSB or a helicase without generation of ssDNA gaps (32).”
Sommers, J. A., Estep, K. N., Maul, R. W., & Brosh, R. M. (2021) · Methods · doi:10.1016/j.ymeth.2021.12.005 · Cited by 3 · see citing works
Computer‐Aided Design Software and Simulation Tools for DNA Nanoparticles
Trinh, M.-C., & Jun, H. (2025) · Advanced Materials & Technologies · doi:10.1002/admt.202500438 · Cited by 3 · see citing works
Cranford, M., Dahmen, S. N., Cortez, D., & Dewar, J. M. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf975 · Cited by 3 · see citing works
“However, we cannot exclude the possibility that the stalling could also be due to intrinsic properties of the DNA sequence, such as DNA secondary structures [ 85 , 86 ].”
Mechanism of DNA-protein crosslink bypass by CMG helicasePreprint
Kyaw, M., Xie, S., Peitz, E. D. L., & Yardimci, H. (2025) · bioRxiv · doi:10.1101/2025.03.06.641852 · Cited by 3 · see citing works
“Subsequently, the DEAH-box helicase 36 (DHX36) unwinds past the G4 structures to facilitate bypass by CMG [58], a process reminiscent of RTEL1's role in DPC bypass [38].”
Pham, P., Wood, E., Dunbar, E. L., Cox, M., & Goodman, M. F. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae320 · Cited by 3
“- end of the preceding Okazaki’s fragment, whereas the leading strand Pol III probably stalls at the RRS-G4 site and resumes DNA synthesis after G4 structure resolution by SSB or a helicase without generation of ssDNA gaps ( 31 ).”
G quadruplex DNA facilitates a pervasive path to homologous recombinationPreprint
Thakur, B. L., Basak, P., Khurana, S., Sharma, S., Lai, Y.-H., Nguyen, T., Ramanarayanan, V., Zhao, X., Batista, P. J., Stracker, T. H., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.05.730358 · Cited by 1 · see citing works
“…HR. DHX36 primarily targets G4 nucleic acid structures and was recently shown to resolve DNA G4s in a DNA replication-dependent manner ( 22, 23 ), placing DHX36 function in the context of cells that are primed to undergo HR. DHX36 knockdown with two independent siRNAs corroborated…”
Thermally activated history-dependent homogenization of G-quadruplexes in an ALS/FTD-associated gene
Ross, D., Lewis, O., McLean, O., Bhanot, S., Donahue, S., Baker, R., Dias, R., Eagerton, D., Mohanty, V., & Mohanty, B. (2026) · Biophysical Journal · doi:10.1016/j.bpj.2026.01.054 · Cited by 2 · see citing works
“There are many known helicases which interact with and can unwind G4s such as the DEAH-box helicase, Bloom helicase, and Fanconi anemia complementation group J helicase (39).”
mGem: Noncanonical nucleic acid structures—powerful but neglected antiviral targets
Brázda, V., Bowater, R., Pečinka, P., & Bartas, M. (2025) · mBio · doi:10.1128/mbio.02730-25 · Cited by 2
“G4s have been implicated in transcriptional regulation (33), genome replication (34), and recombination (35).”
Mechanistic coupling of enzymatic activities at the replisome
Welikala, M. U., Butterworth, L. J., Beragama-Arachchi, R., & Trakselis, M. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110761 · Cited by 2 · see citing works
“The 3 ′ end of the G4 is sequestered by CMG, and so, it is likely that DHX36 helicase would be unable to melt this type of trapped G4 (206).”
Keahi, D. L., Sanders, M. A., Paul, M. R., Webster, A., Fang, Y., Wiley, T. F., Shalaby, S., Carroll, T. S., Chandrasekharappa, S. C., Sandoval-Garcia, C., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2503872122 · Cited by 2 · see citing works
“FANCJ was shown to directly resolve G4s and prevent replication stalling that was enhanced when G4s were stabilized ( 65 ).”
Germoglio, M., D'Aria, F., Cortone, G., Prodomo, A., Mahtab, M., Morigi, R., Amato, J., Pisani, F., & Giancola, C. (2025) · NAR Cancer · doi:10.1093/narcan/zcaf004 · Cited by 2 · see citing works
“K O cells and, in line with the important role reported for the FANCJ DNA helicase in dismantling G4 DNA structures in metazoans [ 28–32 ], we found that the number of G4 foci was strikingly increased in this line compared with the isogenic control one (Fig.”
Characterization of Unidirectional Replication Forks in the Mouse Genome
Zerbib, A., & Simon, I. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119611 · Cited by 2 · see citing works
RNA transcripts suppress G-quadruplex structures through G-loop formationPreprint
Sato, K., Hendrikx, A., & Knipscheer, P. (2023) · bioRxiv · doi:10.1101/2023.03.09.531892 · Cited by 2 · see citing works
Self-citationThe G-force in the genome: Unknowns on the functional flairs of DNA G-quadruplexes
Gallina, I., & Richter, S. N. (2026) · PLoS Biology · doi:10.1371/journal.pbio.3003874 · Cited by 1 · see citing works
Javadekar, S. M., Das, S., Hanumegowda, S. M., Kumari, S., Choudhary, B., & Raghavan, S. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.111347 · Cited by 1
“Stable G4-DNA can derail the progression of DNA polymerases and stall replication, inadvertently triggering DNA damage and genomic instability (64–67).”
DNA translocation by the CMG helicase: The helical inchworm model
Batra, S., Allwein, B., Wang, Y., Hite, R., & Remus, D. (2026) · Biochemical Society Transactions · doi:10.1042/bst20250145 · Cited by 1 · see citing works
“Recent studies demonstrated that leading-strand G4s impede CMG-mediated fork progression and DNA unwinding [42,43].”
Hilgert, E., Neste, C. V., Bekaert, S.-L., Martens, F., Vanhauwaert, S., Sanders, E., Verstraelen, P., Risseeuw, M., Westerhout, E. M., Grannetia, M. A., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-29898-z · Cited by 1 · see citing works
“Indeed, at least some of the FANCJ functions can also be compensated by other helicases such as DDX11 and DHX36 39,52 .”
Altering translation allows E. coli to overcome G-quadruplex stabilizers
Cueny, R. R., Voter, A. F., McKenzie, A. M., Morgenstern, M., Myers, K. S., Place, M. M., Peters, J. M., Coon, J. J., & Keck, J. L. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf264 · Cited by 1 · see citing works
“For example, G4s can act as barriers to DNA replication in eukaryotes, an effect that is exacerbated upon depletion of accessory DNA helicases [ 7–10 ].”
Enzymatic bypass of G-quadruplex structures containing oxidative lesions
Podbevšek, P., & Plavec, J. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae1157 · Cited by 1 · see citing works
“Other studies also observed polymerase stalling more than one nucleotide up-stream of a stable G4 structure ( 5 ,12 ).”
Altering translation allows E. coli to overcome chemically stabilized G-quadruplexesPreprint
Cueny, R. R., Voter, A. F., McKenzie, A. M., Morgenstern, M., Myers, K. S., Place, M. M., Peters, J. M., Coon, J., & Keck, J. L. (2024) · bioRxiv · doi:10.1101/2024.08.12.607615 · Cited by 1 · see citing works
“For example, G4s can act as barriers to DNA replication in eukaryotes, an effect that is exacerbated upon depletion of accessory DNA helicases (7–10).”
BackgroundKeahi, D. L., Sanders, M. A., Paul, M., Webster, A. L., Fang, Y., Wiley, T., Shalaby, S., Carroll, T. S., Chandrasekharappa, S., Sandoval-Garcia, C., et al. (2024) · bioRxiv · doi:10.1101/2024.07.20.604431 · Cited by 1 · see citing works
“FANCJ was shown to directly resolve G4s and prevent replication stalling that was enhanced when G4s were stabilized (Castillo Bosch et al. 2014; Sato et al. 2021).”
BackgroundHilgert, E., Depestel, L., Roy, N. V., Roberts, S., Durinck, K., & Speleman, F. (2026) · British Journal of Cancer · doi:10.1038/s41416-026-03569-w
Bartosik, A. R., Bujnowska, M., Stovall, D. B., Ratan, A., & Wang, Y. (2026) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2026.2710103
“…on the leading-strand template preferentially destabilizes fork progression and produces distinct polymerase inhibition patterns, whereas G4s at lagging-strand templates do not effectively stall CMG helicase activity (Lopes et al. 2011; Sato et al. 2021; Batra et al. 2025; Hile et al. 2025).”
InfluentialFANCJ and RTEL1 facilitate pre-replication complex disassembly following replisome collision.
Cameron, G., Negi, S., Sato, K., Yardimci, S., Kaya, Ç., McClymont, C., Yadav, A. K., Krejčí, J., Knipscheer, P., Polasek-Sedlackova, H., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.117860
Self-citationImpaired synthesis of both telomere strands and adaptive TERT reduction in RTEL1 ATPase-dead cellsPreprint
Wu, G., Liu, L.-F., Zaug, A., Rinn, J. L., & Cech, T. (2026) · bioRxiv · doi:10.64898/2026.07.23.740398
“These sequences spontaneously form G-quadruplex structures in ssDNA, which act as physical barriers to the replication machinery 7-9 .”
A Cytosine‑Bulged (3+1) Hybrid G‑Quadruplex Formed by the Chicken DNA Replication Origin
You, Y., Suen, M. C., Miao, H., Geng, Y., Din, R. U., Yuan, M., Xue, Q., Li, X., Xu, N., Guo, Z.-H., et al. (2026) · Chemistry · doi:10.1002/chem.71389
“Origin-associated G4s may facilitate replication initiation, whereas stable G4s that persist on the template strand during elongation can impede fork progression and induce replication stress [78, 80, 81].”
You, Q., Kakusho, N., Sasanuma, H., Masai, H., & Li, H.-L. (2026) · Nature Communications · doi:10.1038/s41467-026-75715-0
“However, mounting evidence indicates that FANCJ plays a dominant role in unwinding genomic G4 structures to facilitate unimpeded DNA replication 15,16,33,34 .”
G-quadruplex homeostasis is a determinant of PARP inhibitor toxicity in BRCA2-deficient cells
Sharma, A. B., Krwawicz, J., Tappenden, L., Ramlee, M. K., Abugable, A. A., Zhen, X., Khurana, S., Stracker, T. H., & Lakin, N. (2026) · Nature Communications · doi:10.1038/s41467-026-75083-9
Li, F.-Y., Zhang, S., Chen, Y., Zhu, H., Zhang, Y., Yang, Y.-L., Guo, D., & Zhou, J. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.153557
Human REV1 interacts with DHX36 to promote replication and tolerance of G-quadruplex DNA
Ketkar, A., Paxton, B. C., Zúñiga, O., Sewilam, R. S., Morales, M., Schaller, J., McCollum, R., Jackson, K. E., Lowran, K., Paul, A., et al. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag562
“The general layout of our schematic was informed and inspired by previously reported models [ 46 , 63 ]. pols to (i) maintain close-coupled pol-helicase action and fork progression, (ii) accurate G4 replication, and (iii) suppress formation of persistent ssDNA gaps following G4 stabilization.”
InfluentialMapping Patterns of G-Quadruplex-Forming Sequence Conservation in Primates
Amaral, E. D. O. S., Jara-Espejo, M., & Line, S. R. P. (2026) · Journal of Molecular Evolution · doi:10.1007/s00239-026-10312-9
“Stress from replication fork stalling and inefficient G4 unwinding can lead to the accumulation of DNA double-strand breaks (Sato et al. 2021 ; Varshney et al. 2020 ).”
Thermally activated irreversible homogenization of G-quadruplexes in an ALS/FTD-associated genePreprint
Ross, D., Lewis, O., McLean, O., Bhanot, S., Donahue, S., Baker, R., Dias, R., Eagerton, D., Mohanty, V., & Mohanty, B. (2025) · bioRxiv · doi:10.1101/2025.06.02.657482
“There are many known helicases which interact with and can unwind G4s such as the DEAH-box helicase, Bloom helicase, and Fanconi anemia complementation group J helicase (38).”
Cryo-EM structures of G4-stalled CMG reveal inchworm mechanism of DNA translocationPreprint
Batra, S., Allwein, B., Kumar, C., Devbhandari, S., Brüning, J.-G., Bahng, S., Lee, C., Marians, K. J., Hite, R. K., & Remus, D. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.02.616340
The evolutionary loss of the Eh1 motif in FoxE1 in the lineage of placental mammals
Sharma, M., Larow, V. M., Dobychina, N., Kessler, D., Krasilnikova, M. M., & Yaklichkin, S. (2023) · PLoS ONE · doi:10.1371/journal.pone.0296176
Hutchins, J. R. A., Peiffer, I., Urbach, S., Mergny, J., Marin, P., Maiorano, D., & Méchali, M. (2023) · bioRxiv · doi:10.1101/2023.03.30.534946
“G4s may represent obstacles to the passage of replicative DNA polymerases along the chromatin (Sato et al, 2021), and our findings in S-phase are consistent with a possible role of Dhx36 in the initiation of DNA replication, perhaps by contributing to DNA unwinding, although an additional possible…”
BackgroundInteraction of the platinum complex of tyrosine-β-cyclodextrin with G-quadruplex DNA
Sahayam, A. N. D., Muruganantham, A., Soundarapandian, S., Alexander, A., Pillai, A. S., & Enoch, I. V. (2023) · Nucleosides, Nucleotides & Nucleic Acids · doi:10.1080/15257770.2023.2194338
- Authors
- Sato, K., Martin-Pintado, N., Post, H., Altelaar, M., & Knipscheer, P.
- Affiliations
- University Medical Center Utrecht (NL)
- Oncode Institute, Hubrecht Institute–KNAW and University Medical Center Utrecht, Uppsalalaan 8, Utrecht 3584 CT, Netherlands.
- Utrecht University (NL)
- Corresponding author
- Knipscheer, Puck
- Venue
- Science Advances
- Published
- 2021-09-24
- Volume
- 7
- Issue
- 39
- Pages
- eabf8653-eabf8653
- ISSN
- 2375-2548 (ISSN-L)
- PMC
- PMC8462899
- OpenAlex
- W3199434918
- Cited by
- 80
- References
- 82
- Citations by year
- 2026: 18 · 2025: 21 · 2024: 14 · 2023: 14 · 2022: 8 · 2021: 5
- FWCI
- 3.22
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by-nc
- Locations
- Science Advances (publishedVersion, cc-by-nc)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- KNAW research portal (Royal Academy of Art and Sciences (KNAW)) (publishedVersion, other-oa)
- KNAW Research Portal (The Royal Netherlands Academy of Arts and Sciences) (publishedVersion, other-oa)
- Data Archiving and Networked Services (DANS) (submittedVersion, other-oa)
- Utrecht University Repository (Utrecht University) (submittedVersion, cc-by-nc)
- Utrecht University Repository (Utrecht University) (submittedVersion, other-oa)
- Funders
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek (184.034.019)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Health Sciences › Medicine › Physiology › Telomeres, Telomerase, and Senescence
- Keywords
- DNA replication, genome stability, CMG helicase, Cdc45, MCM2-7 complex, GINS, DHX36, FANCJ, leading strand, lagging strand, genome maintenance, Xenopus egg extracts
- MeSH terms
- DNA Replication, DNA Helicases, Fanconi Anemia, Humans, S Phase, Genomic Instability, G-Quadruplexes
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
