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Functional transcription promoters at DNA double-strand breaks mediate RNA-driven phase separation of damage-response factors
Open accessAbstract
Damage-induced long non-coding RNAs (dilncRNA) synthesized at DNA double-strand breaks (DSBs) by RNA polymerase II are necessary for DNA-damage-response (DDR) focus formation. We demonstrate that induction of DSBs results in the assembly of functional promoters that include a complete RNA polymerase II preinitiation complex, MED1 and CDK9. Absence or inactivation of these factors causes a reduction in DDR foci both in vivo and in an in vitro system that reconstitutes DDR events on nucleosomes. We also show that dilncRNAs drive molecular crowding of DDR proteins, such as 53BP1, into foci that exhibit liquid-liquid phase-separation condensate properties. We propose that the assembly of DSB-induced transcriptional promoters drives RNA synthesis, which stimulates phase separation of DDR factors in the shape of foci.
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“One of the most recognizable and common markers of cellular senescence is senescence-associated beta-galactosidase (SA-β-gal)37, which reflects the activity of a lysosomal enzyme that cleaves terminal β-d-galactose residues from β-D-galactosides38.”
From Guidelines for minimal information on cellular senescence experimentation in vivo (2024) · cites this paper as [38]
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Cites
Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
Rust, M., Bates, M., & Zhuang, X. (2006) · Nature Methods · doi:10.1038/nmeth929 · Cited by 7,823
The DNA-damage response in human biology and disease
Jackson, S. P., & Bartek, J. (2009) · Nature · doi:10.1038/nature08467 · Cited by 6,092
Biomolecular condensates: organizers of cellular biochemistry
Banani, S. F., Lee, H. O., Hyman, A. A., & Rosen, M. K. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.7 · Cited by 6,058
CellProfiler: image analysis software for identifying and quantifying cell phenotypes
Carpenter, A. E., Jones, T. R., Lamprecht, M. R., Clarke, C., Kang, I. H., Friman, O., Guertin, D. A., Chang, J. H., Lindquist, R. A., Moffat, J., et al. (2006) · Genome biology · doi:10.1186/gb-2006-7-10-r100 · Cited by 5,212
The DNA Damage Response: Making It Safe to Play with Knives
Ciccia, A., & Elledge, S. J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.019 · Cited by 4,368
Liquid phase condensation in cell physiology and disease
Shin, Y., & Brangwynne, C. P. (2017) · Science · doi:10.1126/science.aaf4382 · Cited by 4,143
Telomere measurement by quantitative PCR
Cawthon, R. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.10.e47 · Cited by 3,550
Germline P Granules Are Liquid Droplets That Localize by Controlled Dissolution/Condensation
Brangwynne, C. P., Eckmann, C. R., Courson, D. S., Rybarska, A., Hoege, C., Gharakhani, J., Jülicher, F., & Hyman, A. A. (2009) · Science · doi:10.1126/science.1172046 · Cited by 3,230
Liquid-Liquid Phase Separation in Biology
Hyman, A. A., Weber, C. A., & Jülicher, F. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100913-013325 · Cited by 3,155
A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation
Patel, A., Lee, H. O., Jawerth, L. M., Maharana, S., Jahnel, M., Hein, M. Y., Stoynov, S., Mahamid, J., Saha, S., Franzmann, T. M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.047 · Cited by 2,927
Coactivator condensation at super-enhancers links phase separation and gene control
Sabari, B. R., Dall’Agnese, A., Boija, A., Klein, I. A., Coffey, E. L., Shrinivas, K., Abraham, B. J., Hannett, N. M., Zamudio, A. V., Manteiga, J. C., et al. (2018) · Science · doi:10.1126/science.aar3958 · Cited by 2,595
Phase transitions in the assembly of multivalent signalling proteins
Li, P., Banjade, S., Cheng, H., Kim, S., Chen, B., Guo, L., Llaguno, M. C., Hollingsworth, J. V., King, D., Banani, S. F., et al. (2012) · Nature · doi:10.1038/nature10879 · Cited by 2,565
Kato, M., Han, T. W., Xie, S., Shi, K., Du, X., Wu, L. C., Mirzaei, H., Goldsmith, E. J., Longgood, J., Pei, J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.017 · Cited by 2,012
Protein Phase Separation: A New Phase in Cell Biology
Boeynaems, S., Alberti, S., Fawzi, N. L., Mittag, T., Polymenidou, M., Rousseau, F., Schymkowitz, J. W. H., Shorter, J., Wolozin, B. L., Bosch, L. V. D., et al. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.004 · Cited by 2,001
Oncogene-induced senescence is a DNA damage response triggered by DNA hyper-replication
Di Micco, R., Fumagalli, M., Cicalese, A., Piccinin, S., Gasparini, P., Luise, C., Schurra, C., Garre’, M., Giovanni Nuciforo, P., Bensimon, A., et al. (2006) · Nature · doi:10.1038/nature05327 · Cited by 1,821
Boija, A., Klein, I. A., Sabari, B. R., Dall’Agnese, A., Coffey, E. L., Zamudio, A. V., Li, C. H., Shrinivas, K., Manteiga, J. C., Hannett, N. M., et al. (2018) · Cell · doi:10.1016/j.cell.2018.10.042 · Cited by 1,815
Phase separation drives heterochromatin domain formation
Strom, A. R., Emelyanov, A. V., Mir, M., Fyodorov, D. V., Darzacq, X., & Karpen, G. H. (2017) · Nature · doi:10.1038/nature22989 · Cited by 1,789
A Phase Separation Model for Transcriptional Control
Hnisz, D., Shrinivas, K., Young, R. A., Chakraborty, A. K., & Sharp, P. A. (2017) · Cell · doi:10.1016/j.cell.2017.02.007 · Cited by 1,753
Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins
Lin, Y., Protter, D. S. W., Rosen, M. K., & Parker, R. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.08.018 · Cited by 1,593
Mediator and RNA polymerase II clusters associate in transcription-dependent condensates
Cho, W.-K., Spille, J.-H., Hecht, M., Lee, C., Li, C., Grube, V., & Cisse, I. I. (2018) · Science · doi:10.1126/science.aar4199 · Cited by 1,403
Elbaum-Garfinkle, S., Kim, Y., Szczepaniak, K., Chen, C. C.-H., Eckmann, C. R., Myong, S., & Brangwynne, C. P. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504822112 · Cited by 1,278
Living on a break: cellular senescence as a DNA-damage response
d'Adda di Fagagna, F. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2440 · Cited by 1,170
Hydrodynamic Radii of Native and Denatured Proteins Measured by Pulse Field Gradient NMR Techniques
Wilkins, D. K., Grimshaw, S. B., Receveur‐Brechot, V., Dobson, C. M., Jones, J. A., & Smith, L. J. (1999) · Biochemistry · doi:10.1021/bi991765q · Cited by 1,013
Ōnuki, A. (2002) · Cambridge University Press eBooks · doi:10.1017/cbo9780511534874 · Cited by 942
RNA phase transitions in repeat expansion disorders
(2017) · doi:10.1038/nature22386 · Cited by 911
TRANSCRIPTION OF EUKARYOTIC PROTEIN-CODING GENES
Lee, T. I., & Young, R. A. (2000) · Annual Review of Genetics · doi:10.1146/annurev.genet.34.1.77 · Cited by 889
Eukaryotic core promoters and the functional basis of transcription initiation
Haberle, V., & Stark, A. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0028-8 · Cited by 774
Liquid Nuclear Condensates Mechanically Sense and Restructure the Genome
Shin, Y., Chang, Y.-C., Lee, D. S. W., Berry, J., Sanders, D. W., Ronceray, P., Wingreen, N. S., Haataja, M., & Brangwynne, C. P. (2018) · Cell · doi:10.1016/j.cell.2018.10.057 · Cited by 676
Exploring RNA transcription and turnover in vivo by using click chemistry
Jao, C. Y., & Salic, A. N. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808480105 · Cited by 674
CDK7 Inhibition Suppresses Super-Enhancer-Linked Oncogenic Transcription in MYCN-Driven Cancer
Chipumuro, E., Marco, E., Christensen, C. L., Kwiatkowski, N. P., Zhang, T., Hatheway, C. M., Abraham, B. J., Sharma, B., Yeung, C. M., Altabef, A. B., et al. (2014) · Cell · doi:10.1016/j.cell.2014.10.024 · Cited by 631
RNA polymerase II clustering through carboxy-terminal domain phase separation
Boehning, M., Dugast‐Darzacq, C., Rankovic, M., Hansen, A. S., Yu, T., Marie-Nelly, H., McSwiggen, D. T., Kokić, G., Dailey, G. M., Cramer, P., et al. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0112-y · Cited by 610
53BP1 promotes non-homologous end joining of telomeres by increasing chromatin mobility
Dimitrova, N., Chen, Y.-C. M., Spector, D. L., & de Lange, T. (2008) · Nature · doi:10.1038/nature07433 · Cited by 604
Ostwald Ripening of Two-Phase Mixtures
Voorhees, P. W. (1992) · Annual Review of Materials Science · doi:10.1146/annurev.ms.22.080192.001213 · Cited by 601
Probing protein heterogeneity in the plasma membrane using PALM and pair correlation analysis
Sengupta, P., Jovanović‐Talisman, T., Skoko, D., Renz, M., Veatch, S. L., & Lippincott‐Schwartz, J. (2011) · Nature Methods · doi:10.1038/nmeth.1704 · Cited by 588
Liquid demixing of intrinsically disordered proteins is seeded by poly(ADP-ribose)
Altmeyer, M., Neelsen, K. J., Teloni, F., Pozdnyakova, I., Pellegrino, S., Grøfte, M., Rask, M., Streicher, W. W., Jungmichel, S., Nielsen, M. L., et al. (2015) · Nature Communications · doi:10.1038/ncomms9088 · Cited by 581
Phase-separation mechanism for C-terminal hyperphosphorylation of RNA polymerase II
Lu, H., Yu, D., Hansen, A. S., Ganguly, S., Liu, R., Heckert, A. B., Darzacq, X., & Zhou, Q. (2018) · Nature · doi:10.1038/s41586-018-0174-3 · Cited by 576
Site-specific DICER and DROSHA RNA products control the DNA-damage response
Francia, S., Michelini, F., Saxena, A., Tang, D. T. P., de Hoon, M., Anelli, V., Mione, M., Carninci, P., & di Fagagna, F. D. (2012) · Nature · doi:10.1038/nature11179 · Cited by 553
Video-rate nanoscopy using sCMOS camera–specific single-molecule localization algorithms
Huang, F., Hartwich, T. M. P., Rivera-Molina, F. E., Lin, Y., Duim, W. C., Long, J. J., Uchil, P. D., Myers, J. R., Baird, M. A., Mothes, W., et al. (2013) · Nature Methods · doi:10.1038/nmeth.2488 · Cited by 531
Polyubiquitin chain-induced p62 phase separation drives autophagic cargo segregation
Sun, D., Wu, R., Zheng, J., Li, P., & Yu, L. (2018) · Cell Research · doi:10.1038/s41422-018-0017-7 · Cited by 521
mRNA structure determines specificity of a polyQ-driven phase separation
Langdon, E. M., Qiu, Y., Niaki, A. G., McLaughlin, G. A., Weidmann, C. A., Gerbich, T. M., Smith, J. A., Crutchley, J., Termini, C. M., Weeks, K. M., et al. (2018) · Science · doi:10.1126/science.aar7432 · Cited by 514
RNA transcription modulates phase transition-driven nuclear body assembly
Berry, J., Weber, S. C., Vaidya, N., Haataja, M., & Brangwynne, C. P. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1509317112 · Cited by 501
Roles of ATM and NBS1 in chromatin structure modulation and DNA double-strand break repair
Berkovich, E., Monnat, R. J., & Kastan, M. B. (2007) · Nature Cell Biology · doi:10.1038/ncb1599 · Cited by 477
CDK7-Dependent Transcriptional Addiction in Triple-Negative Breast Cancer
Wang, Y., Zhang, T., Kwiatkowski, N. P., Abraham, B. J., Lee, T. I., Xie, S., Yuzugullu, H., Von, T., Li, H., Lin, Z., et al. (2015) · Cell · doi:10.1016/j.cell.2015.08.063 · Cited by 464
Phase separation of 53BP1 determines liquid‐like behavior of DNA repair compartments
Kilic, S., Lezaja, A., Gatti, M., Bianco, E., Michelena, J., Imhof, R., & Altmeyer, M. (2019) · The EMBO Journal · doi:10.15252/embj.2018101379 · Cited by 456
Physical principles of intracellular organization via active and passive phase transitions
Berry, J. M., Brangwynne, C. P., & Haataja, M. (2018) · Reports on Progress in Physics · doi:10.1088/1361-6633/aaa61e · Cited by 452
Targeting Transcriptional Addictions in Small Cell Lung Cancer with a Covalent CDK7 Inhibitor
Christensen, C. L., Kwiatkowski, N. P., Abraham, B. J., Carretero, J., Al‐Shahrour, F., Zhang, T., Chipumuro, E., Herter-Sprie, G. S., Akbay, E. A., Altabef, A. B., et al. (2014) · Cancer Cell · doi:10.1016/j.ccell.2014.10.019 · Cited by 446
A forward chemical genetic screen reveals an inhibitor of the Mre11–Rad50–Nbs1 complex
Dupré, A., Boyer-Châtenet, L., Sattler, R. M., Modi, A. P., Lee, J., Nicolette, M. L., Kopelovich, L., Jasin, M., Baer, R. J., Paull, T. T., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.63 · Cited by 426
Michelini, F., Pitchiaya, S., Vitelli, V., Sharma, S., Gioia, U., Pessina, F., Cabrini, M., Wang, Y., Capozzo, I., Iannelli, F., et al. (2017) · Nature Cell Biology · doi:10.1038/ncb3643 · Cited by 392
Self-citationBouchard, J. J., Otero, J. H., Scott, D. C., Szulc, E., Martin, E. W., Sabri, N., Granata, D., Marzahn, M. R., Lindorff‐Larsen, K., Salvatella, X., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.08.027 · Cited by 387
Hexanediol: a chemical probe to investigate the material properties of membrane-less compartments
Kroschwald, S., Maharana, S., & Alberti, S. (2017) · Matters · doi:10.19185/matters.201702000010 · Cited by 369
Phase separation of ligand-activated enhancers licenses cooperative chromosomal enhancer assembly
Nair, S. J., Lu, Y., Meluzzi, D., Oh, S., Yang, F., Friedman, M. J., Wang, S. S., Suter, T., Alshareedah, I., Gamliel, A., et al. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0190-5 · Cited by 365
Gunn, A., & Stark, J. M. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-998-3_27 · Cited by 363
Differential Dynamic Microscopy: Probing Wave Vector Dependent Dynamics with a Microscope
Cerbino, R., & Trappe, V. (2008) · Physical Review Letters · doi:10.1103/physrevlett.100.188102 · Cited by 356
Self-citationPARP-1 Regulates Chromatin Structure and Transcription through a KDM5B-Dependent Pathway
Krishnakumar, R., & Kraus, W. L. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.08.014 · Cited by 345
53BP1 facilitates long-range DNA end-joining during V(D)J recombination
Difilippantonio, S., Gapud, E. J., Wong, N., Huang, C., Mahowald, G. K., Chen, H. T., Kruhlak, M. J., Callén, E., Livák, F., Nussenzweig, M. C., et al. (2008) · Nature · doi:10.1038/nature07476 · Cited by 302
A User’s Guide for Phase Separation Assays with Purified Proteins
Alberti, S., Saha, S., Woodruff, J. B., Franzmann, T. M., Wang, J., & Hyman, A. A. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.06.038 · Cited by 292
Veatch, S. L., Machta, B. B., Shelby, S. A., Chiang, E. N., Holowka, D. A., & Baird, B. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031457 · Cited by 290
Bekker‐Jensen, S., Lukas, C., Melander, F., Bártek, J., & Lukas, J. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200503043 · Cited by 280
Aymard, F., Aguirrebengoa, M., Guillou, E., Javierre, B. M., Bugler, B., Arnould, C., Rocher, V., Iacovoni, J. S., Biernacka, A., Skrzypczak, M., et al. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3387 · Cited by 263
BRCA2 controls DNA:RNA hybrid level at DSBs by mediating RNase H2 recruitment
D’Alessandro, G., Whelan, D. R., Howard, S. M., Vitelli, V., Renaudin, X., Adamowicz, M., Iannelli, F., Jones-Weinert, C. W., Lee, M.-Y., Matti, V., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-07799-2 · Cited by 246
Self-citationDrosha drives the formation of DNA:RNA hybrids around DNA break sites to facilitate DNA repair
Lu, W.-T., Hawley, B. R., Skalka, G., Baldock, R. A., Smith, E. M., Bader, A. S., Malewicz, M., Watts, F. Z., Wilczynska, A., & Bushell, M. (2018) · Nature Communications · doi:10.1038/s41467-018-02893-x · Cited by 229
Centrosomes are autocatalytic droplets of pericentriolar material organized by centrioles
Zwicker, D., Decker, M., Jaensch, S., Hyman, A. A., & Jülicher, F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1404855111 · Cited by 228
A unified architecture of transcriptional regulatory elements
Andersson, R., Sandelin, A., & Danko, C. G. (2015) · Trends in Genetics · doi:10.1016/j.tig.2015.05.007 · Cited by 225
Nuclear position dictates DNA repair pathway choice
Lemaître, C., Grabarz, A., Tsouroula, K., Andronov, L., Furst, A., Pankotai, T., Heyer, V., Rogier, M., Attwood, K. M., Kessler, P., et al. (2014) · Genes & Development · doi:10.1101/gad.248369.114 · Cited by 209
Rulten, S. L., Rotheray, A., Green, R. L., Grundy, G. J., Moore, D. A. Q., Gómez-Herreros, F., Hafezparast, M., & Caldecott, K. W. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt835 · Cited by 190
Transcription-coupled and DNA damage-dependent ubiquitination of RNA polymerase II in vitro
Lee, K., Wang, D., Lippard, S. J., & Sharp, P. A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.072068399 · Cited by 182
Scattering information obtained by optical microscopy: Differential dynamic microscopy and beyond
Giavazzi, F., Brogioli, D., Trappe, V., Bellini, T., & Cerbino, R. (2009) · Physical Review E · doi:10.1103/physreve.80.031403 · Cited by 159
Self-citationThe Hierarchy of Transcriptional Activation: From Enhancer to Promoter
Vernimmen, D., & Bickmore, W. A. (2015) · Trends in Genetics · doi:10.1016/j.tig.2015.10.004 · Cited by 155
Francia, S., Cabrini, M., Matti, V., Oldani, A., & di Fagagna, F. D. (2016) · Journal of Cell Science · doi:10.1242/jcs.182188 · Cited by 145
Self-citationSurface Fluctuations and Coalescence of Nucleolar Droplets in the Human Cell Nucleus
Caragine, C. M., Haley, S. C., & Zidovska, A. (2018) · Physical Review Letters · doi:10.1103/physrevlett.121.148101 · Cited by 138
Pryde, F. E., Khalili, S., Robertson, K., Selfridge, J., Ritchie, A., Melton, D. W., Jullien, D., & Adachi, Y. (2005) · Journal of Cell Science · doi:10.1242/jcs.02336 · Cited by 131
Mammalian NET-seq analysis defines nascent RNA profiles and associated RNA processing genome-wide
Nojima, T., Gomes, T., Carmo‐Fonseca, M., & Proudfoot, N. J. (2016) · Nature Protocols · doi:10.1038/nprot.2016.012 · Cited by 111
Nucleosomal regulation of chromatin composition and nuclear assembly revealed by histone depletion
Zierhut, C., Jenness, C., Kimurâ, H., & Funabiki, H. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2845 · Cited by 106
Rossiello, F., Aguado, J., Sepe, S., Iannelli, F., Nguyen, Q., Pitchiaya, S., Carninci, P., & d’Adda di Fagagna, F. (2017) · Nature Communications · doi:10.1038/ncomms13980 · Cited by 105
Analysis of replication factories in human cells by super-resolution light microscopy
Cseresnyés, Z., Schwarz, U., & Green, C. (2009) · BMC Cell Biology · doi:10.1186/1471-2121-10-88 · Cited by 87
From “Cellular” RNA to “Smart” RNA: Multiple Roles of RNA in Genome Stability and Beyond
Michelini, F., Jalihal, A. P., Francia, S., Meers, C., Neeb, Z. T., Rossiello, F., Gioia, U., Aguado, J., Jones-Weinert, C., Luke, B., et al. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00487 · Cited by 85
Self-citationGalbiati, A., Beauséjour, C., & d'Adda di Fagagna, F. (2017) · Aging Cell · doi:10.1111/acel.12573 · Cited by 79
Self-citationGioia, U., Francia, S., Cabrini, M., Brambillasca, S., Michelini, F., Jones-Weinert, C. W., & di Fagagna, F. D. (2019) · Scientific Reports · doi:10.1038/s41598-019-42892-6 · Cited by 71
Self-citationDignam and Roeder Nuclear Extract PreparationPreprint
Carey, M., Peterson, C. L., & Smale, S. T. (2009) · Cold Spring Harbor Protocols · doi:10.1101/pdb.prot5330 · Cited by 61
Liquid Nuclear Condensates Mechanically Sense and Restructure the Genome
Shin, Y., Chang, Y.-C., Lee, D. S. W., Berry, J. M., Sanders, D. W., Ronceray, P., Wingreen, N. S., Haataja, M., & Brangwynne, C. P. (2019) · Cell · doi:10.1016/j.cell.2019.02.025 · Cited by 61
Viscosity effect on capillary waves at liquid interfaces
Jeng, U., Esibov, L., Crow, L., & Steyerl, A. (1998) · Journal of Physics Condensed Matter · doi:10.1088/0953-8984/10/23/004 · Cited by 60
Radebaugh, C. A., Matthews, J. L., Geiss, G. K., Liu, F., Wong, J., Bateman, E., Camier, S., Sentenac, A., & Paule, M. R. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.1.597 · Cited by 59
Shape Fluctuations of Interacting Fluid Droplets
Hu, G., Krall, A. H., & Weitz, D. A. (1994) · Physical Review Letters · doi:10.1103/physrevlett.73.3435 · Cited by 50
Noninvasive determination of cell nucleoplasmic viscosity by fluorescence correlation spectroscopy
Liang, L., Wang, X., Xing, D., Chen, T., & Chen, W. R. (2009) · Journal of Biomedical Optics · doi:10.1117/1.3088141 · Cited by 49
The molecular basis of eukaryotic transcription (Nobel Lecture).
Kornberg, R. (2007) · Angewandte Chemie · doi:10.1002/anie.200701832 · Cited by 27
Radebaugh, C. A., Matthews, J. L., Geiss, G. K., et al. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.1.597-605.1994 · Cited by 22
DNA Damage In Situ Ligation Followed by Proximity Ligation Assay (DI-PLA)
Galbiati, A., & di Fagagna, F. D. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8931-7_2 · Cited by 17
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Rossiello, F., Jurk, D., Passos, J. F., & d’Adda di Fagagna, F. (2022) · Nature Cell Biology · doi:10.1038/s41556-022-00842-x · Cited by 754
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Mehta, S., & Zhang, J. (2022) · Nature reviews. Cancer · doi:10.1038/s41568-022-00444-7 · Cited by 464
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Metadata
- Authors
- Pessina, F., Giavazzi, F., Yin, Y., Gioia, U., Vitelli, V., Galbiati, A., Barozzi, S., Garre, M., Oldani, A., Flaus, A., Cerbino, R., Parazzoli, D., Rothenberg, E., & d’Adda di Fagagna, F.
- Affiliations
- IFOM (IT)
- University of Milan (IT)
- New York University (US)
- Ollscoil na Gaillimhe – University of Galway (IE)
- ORCID
- Venue
- Nature Cell Biology
- Published
- 2019-09-30
- Volume
- 21
- Issue
- 10
- Pages
- 1286-1299
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC6859070
- OpenAlex
- W2975196800
- Cited by
- 360
- References
- 86
- Citations by year
- 2026: 31 · 2025: 48 · 2024: 53 · 2023: 49 · 2022: 63 · 2021: 71 · 2020: 42 · 2019: 2
- FWCI
- 14.72
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Archivio Istituzionale della Ricerca (Universita Degli Studi Di Milano) (submittedVersion, other-oa)
- Funders
- Marie Curie international mobility fellowship part of Structured International Post Doc Program
- Fondazione Cariplo (2016-0998)
- Regione Lombardia
- Associazione Italiana per la Ricerca sul Cancro (MFAG 2018-22083)
- AriSLA
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- DNA double-strand breaks, MED1, CDK9, 53BP1, liquid-liquid phase separation, condensate, macromolecular crowding, nucleosome reconstitution, transcriptional promoter
- MeSH terms
- Tumor Suppressor p53-Binding Protein 1, DNA, DNA Repair, Gene Expression Regulation, HeLa Cells, Histones, Humans, Osteoblasts, Promoter Regions, Genetic, RNA Polymerase II, Transcription, Genetic, Signal Transduction, Cyclin-Dependent Kinase 9, Cell Line, Tumor, DNA Breaks, Double-Stranded, Mediator Complex Subunit 1, HEK293 Cells, RNA, Long Noncoding, Ataxia Telangiectasia Mutated Proteins
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 ›
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