The DOI matches its Crossref record; 56 of the 57 references it cites were found in a registry or an index.
Damage-induced lncRNAs control the DNA damage response through interaction with DDRNAs at individual double-strand breaks
Open accessAbstract
The DNA damage response (DDR) preserves genomic integrity. Small non-coding RNAs termed DDRNAs are generated at DNA double-strand breaks (DSBs) and are critical for DDR activation. Here we show that active DDRNAs specifically localize to their damaged homologous genomic sites in a transcription-dependent manner. Following DNA damage, RNA polymerase II (RNAPII) binds to the MRE11-RAD50-NBS1 complex, is recruited to DSBs and synthesizes damage-induced long non-coding RNAs (dilncRNAs) from and towards DNA ends. DilncRNAs act both as DDRNA precursors and by recruiting DDRNAs through RNA-RNA pairing. Together, dilncRNAs and DDRNAs fuel DDR focus formation and associate with 53BP1. Accordingly, inhibition of RNAPII prevents DDRNA recruitment, DDR activation and DNA repair. Antisense oligonucleotides matching dilncRNAs and DDRNAs impair site-specific DDR focus formation and DNA repair. We propose that DDR signalling sites, in addition to sharing a common pool of proteins, individually host a unique set of site-specific RNAs necessary for DDR activation.
Overview
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
Verification
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?
The cited source says what the claim attributes to it.
In the citing paper
“Recently, sequence-specific inhibition of DDR activation by antisense oligonucleotides (ASOs)250 and their use in cultured cells and in mouse models to specifically inhibit telomeric DDR38 provided support for this approach.”
From Cellular senescence in ageing: from mechanisms to therapeutic opportunities (2021) · cites this paper as [250]
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.
Citations
Cites
The Sequence Alignment/Map format and SAMtools
Li, H., Handsaker, B., Wysoker, A., Fennell, T., Ruan, J., Homer, N., Marth, G., Abecasis, G., Durbin, R., & 1000 Genome Project Data Processing Subgroup (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp352 · Cited by 62,041
Fast gapped-read alignment with Bowtie 2
Langmead, B., & Salzberg, S. L. (2012) · Nature Methods · doi:10.1038/nmeth.1923 · Cited by 56,400
Dignam, J. D., Lebovitz, R. M., & Roeder, R. G. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.5.1475 · Cited by 11,262
Telomere measurement by quantitative PCR
Cawthon, R. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.10.e47 · Cited by 3,538
Imaging individual mRNA molecules using multiple singly labeled probes
Raj, A., van den Bogaard, P., Rifkin, S. A., van Oudenaarden, A., & Tyagi, S. (2008) · Nature Methods · doi:10.1038/nmeth.1253 · Cited by 2,028
Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications
Polo, S. E., & Jackson, S. P. (2011) · Genes & Development · doi:10.1101/gad.2021311 · Cited by 1,092
RNA-mediated epigenetic regulation of gene expression
Holoch, D., & Moazed, D. (2015) · Nature Reviews Genetics · doi:10.1038/nrg3863 · Cited by 994
53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark
Fradet-Turcotte, A., Canny, M. D., Escribano-Díaz, C., Orthwein, A., Leung, C. C. Y., Huang, H., Landry, M.-C., Kitevski-LeBlanc, J., Noordermeer, S. M., Sicheri, F., et al. (2013) · Nature · doi:10.1038/nature12318 · Cited by 686
Analysis of a piwi-Related Gene Implicates Small RNAs in Genome Rearrangement in Tetrahymena
Mochizuki, K., Fine, N. A., Fujisawa, T., & Gorovsky, M. A. (2002) · Cell · doi:10.1016/s0092-8674(02)00909-1 · Cited by 610
A Role for Small RNAs in DNA Double-Strand Break Repair
Wei, W., Ba, Z., Gao, M., Wu, Y., Ma, Y., Amiard, S., White, C. I., Danielsen, J. M. R., Yang, Y., & Qi, Y. (2012) · Cell · doi:10.1016/j.cell.2012.03.002 · Cited by 575
Flagged first, then by citations
1 of the 57 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 101–200 of 394
Zhang, X., Mao, L., Li, L., He, Z., Wang, N., & Song, Y. (2019) · Journal of Cancer · doi:10.7150/jca.28525 · Cited by 34
Home and Away: The Role of Non-Coding RNA in Intracellular and Intercellular DNA Damage Response
Shaw, A., & Gullerová, M. (2021) · Genes · doi:10.3390/genes12101475 · Cited by 34
Xie, J., Wen, M., Zhang, J., Wang, Z., Wang, M., Qiu, Y., Zhao, W., Zhu, F., Yao, M., Rong, Z., et al. (2022) · Cancer Research · doi:10.1158/0008-5472.can-21-2187 · Cited by 37
Modulating microRNA Processing: Enoxacin, the Progenitor of a New Class of Drugs
Felicetti, T., Cecchetti, V., & Manfroni, G. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00510 · Cited by 33
Ji, J.-H., Min, S., Chae, S., Ha, G., Kim, Y., Park, Y., Lee, C., & Cho, H. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz309 · Cited by 33
Luo, Z., Gao, M., Huang, N., Wang, X., Yang, Z., Yang, H., Huang, Z., & Feng, W. (2019) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-019-1229-5 · Cited by 33
RNA at DNA Double‐Strand Breaks: The Challenge of Dealing with DNA:RNA Hybrids
Domingo‐Prim, J., Bonath, F., & Visa, N. (2020) · BioEssays · doi:10.1002/bies.201900225 · Cited by 32
Post-transcriptional control of cellular differentiation by the RNA exosome complex
de Andrade, I. F., Mehta, C., & Bresnick, E. H. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa883 · Cited by 31
Transcription-coupled DNA double-strand break repair
Guha, S., & Bhaumik, S. R. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103211 · Cited by 34
Fletcher, C. E., Deng, L., Orafidiya, F. A., Yuan, W., Lorentzen, M. P., Cyran, O. W., Varela‐Carver, A., Constantin, T. A., Leach, D. A., Dobbs, F. M., et al. (2022) · Molecular Cancer · doi:10.1186/s12943-022-01540-w · Cited by 32
PARylation During Transcription: Insights into the Fine-Tuning Mechanism and Regulation
Páhi, Z. G., Borsos, B. N., Pantazi, V., Újfaludi, Z., & Pankotai, T. (2020) · Cancers · doi:10.3390/cancers12010183 · Cited by 31
DNA Damage Response and Repair in Boron Neutron Capture Therapy
Mechetin, G. V., & Zharkov, D. O. (2023) · Genes · doi:10.3390/genes14010127 · Cited by 31
Suzuki, M. M., Iijima, K., Ogami, K., Shinjo, K., Murofushi, Y., Xie, J., Wang, X., Kitano, Y., Mamiya, A., Kibe, Y., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40243-8 · Cited by 30
Non-coding RNAs in chromatin folding and nuclear organization
Razin, S. V., & Gavrilov, A. A. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03876-w · Cited by 30
Alternative lengthening of telomeres (ALT) cells viability is dependent on C-rich telomeric RNAs
Rosso, I., Jones-Weinert, C. W., Rossiello, F., Cabrini, M., Brambillasca, S., Muñoz‐Sagredo, L., Lavagnino, Z., Martini, E., Tedone, E., Garrè, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42831-0 · Cited by 28
Self-citationJimeno, S., Prados‐Carvajal, R., & Huertas, P. (2019) · DNA repair · doi:10.1016/j.dnarep.2019.102662 · Cited by 29
Telomere Targeting Approaches in Cancer: Beyond Length Maintenance
Vertecchi, E., Rizzo, A., & Salvati, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073784 · Cited by 29
Chromatin-associated MRN complex protects highly transcribing genes from genomic instability
Salifou, K., Burnard, C., Basavarajaiah, P., Helsmoortel, M., Mac, V., Depierre, D., Grasso, G. I., Franckhauser, C., Beyne, E., Contreras, X., et al. (2021) · Science Advances · doi:10.1126/sciadv.abb2947 · Cited by 27
Integration of DNA damage responses with dynamic spatial genome organization
Stanić, M., & Mekhail, K. (2021) · Trends in Genetics · doi:10.1016/j.tig.2021.08.016 · Cited by 28
Long noncoding RNA and phase separation in cellular stress response
Onoguchi‐Mizutani, R., & Akimitsu, N. (2022) · The Journal of Biochemistry · doi:10.1093/jb/mvab156 · Cited by 27
Refaat, A. M., Nakata, M., Husain, A., Kosako, H., Honjo, T., & Begum, N. A. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112284 · Cited by 31
The dynamic and heterogeneous composition of biomolecular condensates and its functional relevance
Sang, C. C., Upadhyay, S., Nosella, M. L., Forman-Kay, J. D., & Lee, H. O. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-025-00897-2 · Cited by 30
Liao, B., Wang, Z., Zhu, Y., Wang, M., & Liu, Y. (2019) · Artificial Cells Nanomedicine and Biotechnology · doi:10.1080/21691401.2019.1656638 · Cited by 26
RetractedThe Role of Noncoding RNAs in Double-Strand Break Repair
Durut, N., & Scheid, O. M. (2019) · Frontiers in Plant Science · doi:10.3389/fpls.2019.01155 · Cited by 26
Orafidiya, F. A., Deng, L., Bevan, C. L., & Fletcher, C. E. (2022) · Cancers · doi:10.3390/cancers14030755 · Cited by 25
A Role for the Mre11-Rad50-Xrs2 Complex in Gene Expression and Chromosome Organization
Forey, R., Barthe, A., Tittel-Elmer, M., Wéry, M., Barrault, M., Ducrot, C., Seeber, A., Krietenstein, N., Szachnowski, U., Skrzypczak, M., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.11.010 · Cited by 22
Hotspots of single-strand DNA “breakome” are enriched at transcriptional start sites of genes
Cao, H., Zhang, Y., Cai, Y., Tang, L., Gao, F., Xu, D., & Kapranov, P. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.895795 · Cited by 24
A di-acetyl-decorated chromatin signature couples liquid condensation to suppress DNA end synapsis
Bao, K., Ma, Y., Li, Y., Shen, X., Zhao, J., Tian, S., Zhang, C., Liang, C., Zhao, Z., Yang, Y., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.02.002 · Cited by 24
Long noncoding RNA NPCCAT1 promotes nasopharyngeal carcinoma progression via upregulating YY1
Su, H., Liu, L., Zhang, Y., Wang, J., & Zhao, Y. (2018) · Biochimie · doi:10.1016/j.biochi.2018.11.014 · Cited by 23
RNA–DNA hybrids and the convergence with DNA repair
Paull, T. T. (2019) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2019.1670131 · Cited by 22
The Role of Small Noncoding RNA in DNA Double-Strand Break Repair
Rzeszutek, I., & Betlej, G. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218039 · Cited by 21
CtIP-dependent nascent RNA expression flanking DNA breaks guides the choice of DNA repair pathway
Gómez-Cabello, D., Pappas, G., Morante, D. A., Dinant, C., & Bártek, J. (2022) · Nature Communications · doi:10.1038/s41467-022-33027-z · Cited by 25
Phase separation in gene transcription control
Li, C., Li, Z., Wu, Z., & Lu, H. (2023) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2023099 · Cited by 25
Murphy, M. R., Ramadei, A., Doymaz, A., Varriano, S., Natelson, D. M., Yu, A., Aktas, S., Mazzeo, M., Mazzeo, M., Zakusilo, G., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad899 · Cited by 24
SARS-CoV-2 and the DNA damage response
Grand, R. J. A. (2023) · Journal of General Virology · doi:10.1099/jgv.0.001918 · Cited by 25
Long, Q., Šebesta, M., Šedová, K., Haluza, V., Alagia, A., Liu, Z., Štefl, R., & Gullerová, M. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113489 · Cited by 21
ERK2-topoisomerase II regulatory axis is important for gene activation in immediate early genes
Bunch, H., Kim, D., Naganuma, M., Nakagawa, R., Cong, A. T. Q., Jeong, J., Ehara, H., Vu, H., Chang, J. H., Schellenberg, M. J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-44089-y · Cited by 24
Xu, Z., Zhu, M., Geng, L., Zhang, J., Xia, J., Wang, Q., An, H., Xia, A., Yu, Y., Liu, S., et al. (2025) · Drug Resistance Updates · doi:10.1016/j.drup.2025.101241 · Cited by 22
DNA Processing in the Context of Noncoding Transcription
Gowthaman, U., García‐Pichardo, D., Jin, Y., Schwarz, I., & Marquardt, S. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.07.009 · Cited by 21
Eke, I., Bylicky, M. A., Sandfort, V., Chopra, S., Martello, S. E., Graves, E. E., Coleman, C. N., & Aryankalayil, M. J. (2021) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2021.02.024 · Cited by 23
Non-homologous end-joining at challenged replication forks: an RNA connection?
Audoynaud, C., Vagner, S., & Lambert, S. (2021) · Trends in Genetics · doi:10.1016/j.tig.2021.06.010 · Cited by 23
Zhu, J., Huang, Q., Peng, X., Luo, C. H., Liu, S., Liu, Z., Wu, X., & Luo, H. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.799475 · Cited by 22
DNA double-strand break-derived RNA drives TIRR/53BP1 complex dissociation
Ketley, R. F., Battistini, F., Alagia, A., Mondielli, C., Iehl, F., Balikçi, E., Huber, K., Orozco, M., & Gullerová, M. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111526 · Cited by 22
DROSHA is recruited to DNA damage sites by the MRN complex to promote non-homologous end joining
Cabrini, M., Roncador, M., Galbiati, A., Cipolla, L., Maffia, A., Iannelli, F., Sabbioneda, S., di Fagagna, F. D., & Francia, S. (2021) · Journal of Cell Science · doi:10.1242/jcs.249706 · Cited by 22
Self-citationIskandar, M., Barbero, M. X., Jaber, M. T., Chen, R., Gomez-Guevara, R., Cruz, E., & Westerheide, S. D. (2025) · Cancers · doi:10.3390/cancers17020257 · Cited by 30
Seredinski, S., Boos, F., Günther, S., Oo, J. A., Warwick, T., Izquierdo Ponce, J., Lillich, F. F., Proschak, E., Knapp, S., Gilsbach, R., et al. (2022) · Molecular Therapy Nucleic Acids · doi:10.1016/j.omtn.2022.01.016 · Cited by 21
Break‐induced RNA–DNA hybrids (BIRDHs) in homologous recombination: friend or foe?
Gómez‐González, B., & Aguilera, A. (2023) · EMBO Reports · doi:10.15252/embr.202357801 · Cited by 23
Connections between 3′ end processing and DNA damage response: Ten years later
Murphy, M. R., & Kleiman, F. E. (2019) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1571 · Cited by 21
Micellization: A new principle in the formation of biomolecular condensates
Yamazaki, T., Yamamoto, T., & Hirose, T. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.974772 · Cited by 20
Mechanisms of insertions at a DNA double-strand break
Min, J., Zhao, J., Zagelbaum, J., Lee, J., Takahashi, S., Cummings, P., Schooley, A., Dekker, J., Gottesman, M. E., Rabadán, R., et al. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.06.016 · Cited by 21
S-phase Enriched Non-coding RNAs Regulate Gene Expression and Cell Cycle Progression
Yıldırım, Ö., Izgü, E. Ç., Damle, M., Chalei, V., Ji, F., Sadreyev, R. I., Szostak, J. W., & Kingston, R. E. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107629 · Cited by 22
DNA Polymerase θ: A Cancer Drug Target with Reverse Transcriptase Activity
Chen, X. S., & Pomerantz, R. T. (2021) · Genes · doi:10.3390/genes12081146 · Cited by 20
Sweet Melody or Jazz? Transcription Around DNA Double-Strand Breaks
Long, Q., Liu, Z., & Gullerová, M. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.655786 · Cited by 19
Leriche, M., Bonnet, C., Jana, J., Chhetri, G., Mennour, S., Martineau, S., Pennaneach, V., Busso, D., Veaute, X., Bertrand, P., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113412 · Cited by 19
Conservation and Divergence in the Meiocyte sRNAomes of Arabidopsis, Soybean, and Cucumber
Huang, J., Wang, C., Li, X., Fang, X., Huang, N., Wang, Y., Mā, H., Wang, Y., & Copenhaver, G. P. (2019) · PLANT PHYSIOLOGY · doi:10.1104/pp.19.00807 · Cited by 18
Self-citationThe Emerging Role of RNA Modifications in DNA Double-Strand Break Repair
Jimeno, S., Balestra, F. R., & Huertas, P. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.664872 · Cited by 18
NEAT1 modulates the TIRR/53BP1 complex to maintain genome integrity
Kilgas, S., Syed, A., Toolan-Kerr, P., Swift, M. L., Roychoudhury, S., Sarkar, A., Wilkins, S., Quigley, M., Poetsch, A. R., Botuyan, M. V., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-52862-w · Cited by 20
Long noncoding RNAs: p53’s secret weapon in the fight against cancer?
Dangelmaier, E. A., Lazar, S. B., & Lal, A. (2019) · PLoS Biology · doi:10.1371/journal.pbio.3000143 · Cited by 17
Double-Stranded Break Repair in Mammalian Cells and Precise Genome Editing
Ali, A., Xiao, W., Babar, M. E., & Bi, Y. (2022) · Genes · doi:10.3390/genes13050737 · Cited by 19
Yadav, A., Biswas, T., Praveen, A., Ganguly, P., Bhattacharyya, A., Verma, A., Datta, D. B., & Ateeq, B. (2023) · Cancer Research Communications · doi:10.1158/2767-9764.crc-23-0089 · Cited by 17
Yan, J., Chun-hua, X., Li, Y., Tang, B., Xie, S., Hong, T., & Zeng, E. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14435 · Cited by 17
Long noncoding RNA: A resident staff of genomic instability regulation in tumorigenesis
Guo, F., Li, L., Wang, Y., Hu, J., & Cui, J. (2021) · Cancer Letters · doi:10.1016/j.canlet.2021.01.021 · Cited by 16
Self-citationLong noncoding RNA SNHG20 promotes prostate cancer progression via upregulating DDX17
Wu, X., Yan, W., Ji, Z., Zheng, G., & Liu, G. (2019) · Archives of Medical Science · doi:10.5114/aoms.2019.85653 · Cited by 16
Liu, Z., Ajit, K., Wu, Y., Zhu, W., & Gullerová, M. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00111-7 · Cited by 16
RNA takes over control of DNA break repair
Storici, F., & Tichon, A. (2017) · Nature Cell Biology · doi:10.1038/ncb3645 · Cited by 16
MicroRNAs and DNA-Damaging Drugs in Breast Cancer: Strength in Numbers
Plantamura, I., Cosentino, G., & Cataldo, A. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00352 · Cited by 16
Bergstrand, S., O’Brien, E. M., & Farnebo, M. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00051 · Cited by 17
NHP2 downregulation counteracts hTR‐mediated activation of the DNA damage response at ALT telomeres
Raghunandan, M., Geelen, D., Majerová, E., & Decottignies, A. (2021) · The EMBO Journal · doi:10.15252/embj.2020106336 · Cited by 15
Yang, F., Yang, Y. L., Qiu, Y., Tang, L., Xie, L., & Guan, X. (2024) · Cancers · doi:10.3390/cancers16020290 · Cited by 15
Michelini, F., Rossiello, F., di Fagagna, F. D., & Francia, S. (2019) · Nature Protocols · doi:10.1038/s41596-019-0147-5 · Cited by 15
Self-citationncRNAs associated with drug resistance and the therapy of digestive system neoplasms
Feng, W., Su, Z., Yin, Q., Zong, W., Shen, X., & Ju, S. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28551 · Cited by 15
Modafferi, S., Farina, S., Esposito, F., Brandi, O., Salvio, M. D., Valle, I. D., D’Uva, S., Scarian, E., Cicio, G., Riccardi, A., et al. (2025) · Cell Death and Differentiation · doi:10.1038/s41418-025-01530-7 · Cited by 16
Self-citationA Non-Coding RNA Network Involved in KSHV Tumorigenesis
Naipauer, J., Solá, M. E. G., Salyakina, D., Rosario, S., Williams, S. L., Coso, O. A., Abba, M. C., Mesri, E. A., & Lacunza, E. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.687629 · Cited by 14
Zhou, X., Zeng, B., Li, Y., Wang, H., & Zhang, X. (2021) · Molecules · doi:10.3390/molecules26227040 · Cited by 14
LINC00885 promotes cervical cancer progression through sponging miR-3150b-3p and upregulating BAZ2A
Liu, Y., Chen, J., Zhou, L., & Yin, C. (2022) · Biology Direct · doi:10.1186/s13062-021-00314-6 · Cited by 14
CCAR2 functions downstream of the Shieldin complex to promote double-strand break end-joining
Iyer, D., Harada, N., Clairmont, C. S., Jiang, L., Martignetti, D. B., Nguyen, H. Q., He, Y. J., Chowdhury, D., & D’Andrea, A. D. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2214935119 · Cited by 14
Liquid-liquid phase separation of membrane-less condensates: from biogenesis to function
Guan, H., Wang, H., Cai, X. M., Wang, J., Chai, Z., Wang, J., Wang, H., Zhang, M., Wu, Z., Zhu, J., et al. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1600430 · Cited by 13
Schellenbauer, A., Guilly, M., Grall, R., Bars, R. L., Paget, V., Kortulewski, T., Sutcu, H. H., Mathé, C., Hullo, M., Biard, D. S. F., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab980 · Cited by 17
Ranganathan, R., Sapozhnikov, G., Wang, N., Li, S., & Song, Y. (2023) · Translational Medicine of Aging · doi:10.1016/j.tma.2023.06.004 · Cited by 14
Chen, Y., Shen, H., Liu, T., Cao, K., Wan, Z., Du, Z., Wang, H., Yu, Y., Ma, S., Lu, E., et al. (2023) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-023-02829-4 · Cited by 14
Yang, H., & Lan, L. (2024) · FEBS Letters · doi:10.1002/1873-3468.14938 · Cited by 13
Controlling the balance between chromosome break repair pathways
Jimeno, S., Mejías-Navarro, F., Prados‐Carvajal, R., & Huertas, P. (2018) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2018.10.004 · Cited by 17
Vågbø, C. B., & Slupphaug, G. (2020) · DNA repair · doi:10.1016/j.dnarep.2020.102927 · Cited by 16
Current understanding of the role of DDX21 in orchestrating gene expression in health and diseases
Wang, S., Yang, R., Song, M., Li, J., Zhou, Y., Dai, C., & Song, T. (2024) · Life Sciences · doi:10.1016/j.lfs.2024.122716 · Cited by 12
RNA transcripts serve as a template for double-strand break repair in human cells
Jalan, M., Brambati, A., Shah, H., McDermott, N., Patel, J., Zhu, Y., Doymaz, A., Wu, J. F., Anderson, K. S., Gazzo, A. M., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59510-x · Cited by 13
RNAPII-dependent ATM signaling at collisions with replication forks
Einig, E., Jin, C., Andrioletti, V., Maček, B., & Popov, N. (2023) · Nature Communications · doi:10.1038/s41467-023-40924-4 · Cited by 12
Analysis of changes to lncRNAs and their target mRNAs in murine jejunum after radiation treatment
Lu, Q., Gong, W., Wang, J., Ji, K., Sun, X., Xu, C., Du, L., Wang, Y., & Liu, Q. (2018) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13940 · Cited by 13
Self-citationTonnemacher, S., Eltsov, M., & Jakob, B. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21061911 · Cited by 12
Qu, Y., Li, H., Shi, C., Qian, M., Yang, N., Wang, L., Gao, X., & Ni, C. (2020) · BioMed Research International · doi:10.1155/2020/8841511 · Cited by 14
Commuting to Work: Nucleolar Long Non-Coding RNA Control Ribosome Biogenesis from Near and Far
Mamontova, V., Trifault, B., Boten, L., & Burger, K. (2021) · Non-Coding RNA · doi:10.3390/ncrna7030042 · Cited by 14
Wei, C., Li, M., Li, X., Lyu, J., & Zhu, X. M. (2022) · Advanced Biology · doi:10.1002/adbi.202200006 · Cited by 12
Coming Together: RNAs and Proteins Assemble under the Single-Molecule Fluorescence MicroscopePreprint
Jalihal, A. P., Lund, P. E., & Walter, N. G. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a032441 · Cited by 12
Self-citationTetrameric INTS6-SOSS1 complex facilitates DNA:RNA hybrid autoregulation at double-strand breaks
Long, Q., Ajit, K., Šedová, K., Haluza, V., Štefl, R., Dokaneheifard, S., Beckedorff, F., Valencia, M. G., Šebesta, M., Shiekhattar, R., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae937 · Cited by 10
Wu, T., Li, Y., Zhao, Y., Shah, S. B., Shi, L. Z., & Wu, X. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116386 · Cited by 11
Long non-coding RNA SAP30L-AS1 promotes prostate cancer growth through repressing SAP30L
Qin, X., Zhu, W., Lu, A., Wang, G., Ye, X., & Weng, G. (2018) · Gene · doi:10.1016/j.gene.2018.12.047 · Cited by 11
LncRNAs of Saccharomyces cerevisiae bypass the cell cycle arrest imposed by ethanol stress
Lázari, L. C., Wolf, I. R., Schnepper, A. P., & Valente, G. T. (2022) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1010081 · Cited by 11
Long non-coding RNAs in the pathogenesis of heart failure: A literature review
Fan, X., Zhang, Z., Zheng, L., Wei, W., & Chen, Z. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.950284 · Cited by 10
Liu, L., Cui, J., Chen, S., Zhang, X., Wang, S., & Huang, L. (2022) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2022.160819 · Cited by 12
MDC1 maintains active elongation complexes of RNA polymerase II
Pappas, G. D., Munk, S. H. N., Watanabe, K., Thomas, Q. A., Gál, Z., Gram, H. H., Lee, M., Gómez-Cabello, D., Kanellis, D. C., Olivares‐Chauvet, P., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2022.111979 · Cited by 12
Chuang, T.-W., Su, C.-H., Wu, P.-Y., Chang, Y., & Tarn, W. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad143 · Cited by 11
Metadata
- Authors
- Michelini, F., Pitchiaya, S., Vitelli, V., Sharma, S., Gioia, U., Pessina, F., Cabrini, M., Wang, Y., Capozzo, I., Iannelli, F., Matti, V., Francia, S., Shivashankar, G. V., Walter, N. G., & d’Adda di Fagagna, F.
- Affiliations
- IFOM (IT)
- University of Michigan (US)
- Istituto di Genetica Molecolare (IT)
- National University of Singapore (SG)
- ORCID
- Venue
- Nature Cell Biology
- Published
- 2017-11-27
- Volume
- 19
- Issue
- 12
- Pages
- 1400-1411
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC5714282
- OpenAlex
- W2771049305
- Cited by
- 392
- References
- 57
- Citations by year
- 2026: 26 · 2025: 32 · 2024: 40 · 2023: 55 · 2022: 63 · 2021: 62 · 2020: 50 · 2019: 42 · 2018: 19 · 2017: 1
- FWCI
- 12.50
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM098023, R01GM062357)
- National Institute of Allergy and Infectious Diseases (R21AI109791)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer-related molecular mechanisms research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- DNA damage response, long non-coding RNA, DNA double-strand breaks, RNA polymerase II, Mre11-Rad50-Nbs1 complex, 53BP1, DNA repair, antisense oligonucleotides
- MeSH terms
- Tumor Suppressor p53-Binding Protein 1, MRE11 Homologue Protein, Animals, Cell Line, Cell-Free System, DNA Damage, DNA Repair, DNA-Binding Proteins, Models, Biological, Nuclear Proteins, RNA Polymerase II, Transcription, Genetic, Oligonucleotides, Antisense, Acid Anhydride Hydrolases, ATP-Binding Cassette Transporters, Cell Cycle Proteins, Mice, DNA Breaks, Double-Stranded, RNA, Long Noncoding
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