Chemical inhibition of NAT10 corrects defects of laminopathic cells
Open accessAbstract
Remodelin Nuclear Defects: Deregulation of A-type lamin proteins leads to disorganization of chromatin structure and misshapen nuclei, which are believed to underlie the pathologies of various human diseases, including the premature aging disorder Hutchinson Gilford progeria syndrome (HGPS) and various cancers. Larrieu et al. (p. 527 ) developed a small molecule, Remodelin, that not only improved nuclear shape defects of human lamin A/C–depleted cells, HGPS cells, and aged normal cells, but also decreased the levels of a DNA damage marker and improved global cellular fitness.
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?
Remodelin is a small molecule that inhibits acetyl-transferase NAT10.
“Remodelin, a small molecule that inhibits the acetyl-transferase protein NAT10 (Larrieu et al., 2014).”
From The Aging Epigenome (2016) · cites this paper as Larrieu et al., 2014
HGPS patient-derived cells treated with Remodelin had improved nuclear architecture and increased chromatin compaction, consistent with heterochromatin gain.
“when cells derived from patients with the progeria disease HGPS were treated with the drug Remodelin, the cells had improved nuclear architecture and increased chromatin compaction, consistent with a gain of heterochromatin (Larrieu et al., 2014).”
From The Aging Epigenome (2016) · cites this paper as Larrieu et al., 2014
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
Recurrent de novo point mutations in lamin A cause Hutchinson–Gilford progeria syndrome
Eriksson, M., Brown, W. T., Gordon, L. B., Glynn, M. W., Singer, J. I., Scott, L. J., Erdos, M. R., Robbins, C. M., Moses, T. Y., Berglund, P., et al. (2003) · Nature · doi:10.1038/nature01629 · Cited by 2,217 · see citing works
Lamin A Truncation in Hutchinson-Gilford Progeria
Sandre‐Giovannoli, A. D., Bernard, R., Cau, P., Navarro, C. L., Amiel, J., Boccaccio, I., Lyonnet, S., Stewart, C. L., Münnich, A., Merrer, M. F. L., et al. (2003) · Science · doi:10.1126/science.1084125 · Cited by 1,472 · see citing works
Lamin A-Dependent Nuclear Defects in Human Aging
Scaffidi, P., & Misteli, T. (2006) · Science · doi:10.1126/science.1127168 · Cited by 1,224 · 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
Self-citation“Laminopathies”: A wide spectrum of human diseases
Worman, H. J., & Bonne, G. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.03.028 · Cited by 657 · see citing works
Capell, B. C., Erdos, M. R., Madigan, J. P., Fiordalisi, J. J., Varga, R., Conneely, K. N., Gordon, L. B., Der, C. J., Cox, A. D., & Collins, F. S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506001102 · Cited by 395 · see citing works
Identifying the proteins to which small-molecule probes and drugs bind in cells
Ong, S., Schenone, M., Margolin, A. A., Li, X., Do, K., Doud, M. K., Mani, D. R., Kuai, L., Wang, X., Wood, J. L., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900191106 · Cited by 304 · see citing works
Toth, J. I., Yang, S. H., Qiao, X., Beigneux, A. P., Gelb, M. H., Moulson, C. L., Miner, J. H., Young, S. G., & Fong, L. G. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505767102 · Cited by 292 · see citing works
Glynn, M. W., & Glover, T. W. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi326 · Cited by 259 · see citing works
Chen, C., Chi, Y., Mutalif, R., Starost, M. F., Myers, T. G., Anderson, S. A., Stewart, C. L., & Jeang, K. (2012) · Cell · doi:10.1016/j.cell.2012.01.059 · Cited by 221 · see citing works
Shen, Q., Zheng, X.-Z., McNutt, M. A., Guang, L., Sun, Y., Wang, J., Gong, Y., Hou, L., & Zhang, B. (2009) · Experimental Cell Research · doi:10.1016/j.yexcr.2009.03.007 · Cited by 178 · see citing works
Decreased and aberrant nuclear lamin expression in gastrointestinal tract neoplasms
Moss, S. F., Krivosheyev, V., Souza, A., Chin, K., Gaetz, H. P., Chaudhary, N., Worman, H. J., & Holt, P. R. (1999) · Gut · doi:10.1136/gut.45.5.723 · Cited by 140 · see citing works
Nuclear A-type lamins are differentially expressed in human lung cancer subtypes.
Broers, J. L. V., Raymond, Y., Rot, M. K., Kuijpers, H. J. H., WAGENAAR, S. S., & Ramaekers, F. C. S. (1993) · PubMed Central · Cited by 135 · see citing works
Chimenti, F., Bizzarri, B., Maccioni, E., Secci, D., Bolasco, A., Chimenti, P., Fioravanti, R., Granese, A., Carradori, S., Tosi, F., et al. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800885d · Cited by 134 · see citing works
Li, X., Foley, E. A., Molloy, K. R., Li, Y., Chait, B. T., & Kapoor, T. M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja210528v · Cited by 128 · see citing works
Targeting Isoprenylcysteine Methylation Ameliorates Disease in a Mouse Model of Progeria
Ibrahim, M. X., Sayin, V. I., Akula, M. K., Liu, M., Fong, L. G., Young, S. G., & Bergö, M. O. (2013) · Science · doi:10.1126/science.1238880 · Cited by 124 · see citing works
Chi, Y., Haller, K., Péloponèse, J., & Jeang, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703098200 · Cited by 122 · see citing works
Expression of individual lamins in basal cell carcinomas of the skin
Venables, R. S., McLean, S., Lunny, D. P., Moteleb, E., Morley, S., Quinlan, R. A., Lane, E. B., & Hutchison, C. (2001) · British Journal of Cancer · doi:10.1054/bjoc.2000.1632 · Cited by 111 · see citing works
Depletion of nucleophosmin leads to distortion of nucleolar and nuclear structures in HeLa cells
Amin, M. A., Matsunaga, S., Uchiyama, S., & Fukui, K. (2008) · Biochemical Journal · doi:10.1042/bj20081411 · Cited by 98 · see citing works
Verstraeten, V. L. R. M., Peckham, L. A., Olive, M., Capell, B. C., Collins, F. S., Nabel, E. G., Young, S. G., Fong, L. G., & Lammerding, J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1019532108 · Cited by 85 · see citing works
Galiová, G., Bártová, E., Raška, I., Krejčí, J., & Kozubek, S. (2008) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2008.01.013 · Cited by 81 · see citing works
RNA helicase module in an acetyltransferase that modifies a specific tRNA anticodon
Chimnaronk, S., Suzuki, T., Manita, T., Ikeuchi, Y., Yao, M., Suzuki, T., & Tanaka, I. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.69 · Cited by 79 · see citing works
Amin, M. A., Matsunaga, S., Ma, N., Takata, H., Yokoyama, M., Uchiyama, S., & Fukui, K. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.06.092 · Cited by 77 · see citing works
Tamiello, C. C., Kamps, M. A. F., van den Wijngaard, A., Verstraeten, V. L. R. M., Baaijens, F. F., Broers, J. L. V., & Bouten, C. V. C. (2013) · Nucleus · doi:10.4161/nucl.23388 · Cited by 63 · see citing works
Suzuki, N., Villar, K. D., & Tamanoi, F. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10499 · Cited by 43 · see citing works
Wang, Y., Östlund, C., Choi, J. C., Swayne, T. C., Gundersen, G. G., & Worman, H. J. (2012) · Nucleus · doi:10.4161/nucl.21675 · Cited by 29 · see citing works
Wang, G., Gao, X., Huang, Y., Yao, Z., Shi, Q., & Wu, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.100396 · Cited by 18 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Acetylation of Cytidine in mRNA Promotes Translation Efficiency
Arango, D., Sturgill, D., Alhusaini, N., Dillman, A. A., Sweet, T. J., Hanson, G., Hosogane, M., Sinclair, W. R., Nanan, K. K., Mandler, M. D., et al. (2018) · Cell · doi:10.1016/j.cell.2018.10.030 · Cited by 862 · see citing works
Fighting against Skin Aging: The Way from Bench to Bedside
Zhang, S., & Duan, E. (2018) · Cell Transplantation · doi:10.1177/0963689717725755 · Cited by 739 · see citing works
The expanding world of tRNA modifications and their disease relevance
Suzuki, T. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00342-0 · Cited by 733 · see citing works
Salinomycin kills cancer stem cells by sequestering iron in lysosomes
Mai, T. T., Hamaï, A., Hienzsch, A., Cañeque, T., Müller, S., Wicinski, J., Cabaud, O., Leroy, C., David, A., Acevedo, V., et al. (2017) · Nature Chemistry · doi:10.1038/nchem.2778 · Cited by 612 · see citing works
Self-citationThe RNA modification landscape in human disease
Jonkhout, N., Tran, J., Smith, M. A., Schönrock, N., Mattick, J. S., & Novoa, E. M. (2017) · RNA · doi:10.1261/rna.063503.117 · Cited by 606 · see citing works
The Keap1-Nrf2 System: A Mediator between Oxidative Stress and Aging
Yu, C., & Xiao, J.-H. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6635460 · Cited by 537 · see citing works
Menyhárt, O., Nagy, Á., & Győrffy, B. (2018) · Royal Society Open Science · doi:10.1098/rsos.181006 · Cited by 507 · see citing works
Booth, L. N., & Brunet, A. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.013 · Cited by 499 · see citing works
Sharma, S., Langhendries, J.-L., Watzinger, P., Kötter, P., Entian, K., & Lafontaine, D. L. J. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv075 · Cited by 387 · see citing works
Chromatin histone modifications and rigidity affect nuclear morphology independent of lamins
Stephens, A. D., Liu, P. Z., Banigan, E. J., Almassalha, L. M., Backman, V., Adam, S. A., Goldman, R. D., & Marko, J. F. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-06-0410 · Cited by 350 · see citing works
YAP/TAZ activity in stromal cells prevents ageing by controlling cGAS–STING
Sladitschek, H. L., Guarnieri, A., Brumana, G., Zanconato, F., Battilana, G., Xiccato, R. L., Panciera, T., Forcato, M., Bicciato, S., Guzzardo, V., et al. (2022) · Nature · doi:10.1038/s41586-022-04924-6 · Cited by 346 · see citing works
Dynamic RNA acetylation revealed by quantitative cross-evolutionary mapping
Sas‐Chen, A., Thomas, J. M., Matzov, D., Taoka, M., Nance, K. D., Nir, R., Bryson, K. M., Shachar, R., Liman, G. L. S., Burkhart, B. W., et al. (2020) · Nature · doi:10.1038/s41586-020-2418-2 · Cited by 328 · see citing works
Hutchinson-Gilford Progeria Syndrome: A premature aging disease caused by LMNA gene mutations
Gonzalo, S., Kreienkamp, R., & Askjaer, P. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2016.06.007 · Cited by 324 · see citing works
Mechanosensing by the Lamina Protects against Nuclear Rupture, DNA Damage, and Cell-Cycle Arrest
Cho, S., Vashisth, M., Abbas, A. K., Majkut, S., Vogel, K., Xia, Y., Ivanovska, I. L., Irianto, J., Tewari, M., Zhu, K., et al. (2019) · Developmental Cell · doi:10.1016/j.devcel.2019.04.020 · Cited by 301 · see citing works
Ito, S., Horikawa, S., Suzuki, T., Kawauchi, H., Tanaka, Y., Suzuki, T., & Suzuki, T. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.c114.602698 · Cited by 297 · see citing works
Epigenetic changes during aging and their reprogramming potential
Kane, A. E., & Sinclair, D. A. (2019) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2019.1570075 · Cited by 283 · see citing works
Mutant lamins cause nuclear envelope rupture and DNA damage in skeletal muscle cells
Earle, A., Kirby, T. J., Fedorchak, G. R., Isermann, P., Patel, J., Iruvanti, S., Moore, S. A., Bonne, G., Wallrath, L. L., & Lammerding, J. (2019) · Nature Materials · doi:10.1038/s41563-019-0563-5 · Cited by 243 · see citing works
‘View From A Bridge’: A New Perspective on Eukaryotic rRNA Base Modification
Sharma, S., & Lafontaine, D. L. J. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.07.008 · Cited by 231 · see citing works
NAT10 Drives Cisplatin Chemoresistance by Enhancing ac4C-Associated DNA Repair in Bladder Cancer
Xie, R., Liang Cheng, C., Huang, M. X., Huang, L., Chen, Z., Zhang, Q., Li, H., Lu, J., Wang, H., Zhou, Q., et al. (2023) · Cancer Research · doi:10.1158/0008-5472.can-22-2233 · Cited by 214 · see citing works
NAT10 regulates p53 activation through acetylating p53 at K120 and ubiquitinating Mdm2
Liu, X., Tan, Y., Zhang, C., Zhang, Y., Zhang, L., Ren, P., Deng, H., Luo, J., Ke, Y., & Du, X. (2016) · EMBO Reports · doi:10.15252/embr.201540505 · Cited by 212 · see citing works
DNA replication stress: Causes, resolution and disease
Mazouzi, A., Velimezi, G., & Loizou, J. I. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.09.030 · Cited by 211 · see citing works
Nesprin-2G, a Component of the Nuclear LINC Complex, Is Subject to Myosin-Dependent Tension
Arsenovic, P. T., Ramachandran, I., Bathula, K., Zhu, R., Narang, J. D., Noll, N. A., Lemmon, C. A., Gundersen, G. G., & Conway, D. E. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2015.11.014 · Cited by 210 · see citing works
Chromatin’s physical properties shape the nucleus and its functions
Stephens, A. D., Banigan, E. J., & Marko, J. F. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.02.006 · Cited by 206 · see citing works
Liu, H., Liu, Y., Yang, F., Zhang, L., Zhang, F., Hu, X., Shao, Z., & Li, D. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa130 · Cited by 205 · see citing works
Targeting of NAT10 enhances healthspan in a mouse model of human accelerated aging syndrome
Balmus, G., Larrieu, D., Barros, A. C., Collins, C., Abrudan, M. I., Demir, M., Geisler, N. J., Lelliott, C. J., White, J. K., Karp, N. A., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03770-3 · Cited by 203 · see citing works
Self-citationZheng, X. W., Wang, Q., Zhou, Y., Zhang, D., Geng, Y., Hu, W., Wu, C., Shi, Y., & Jiang, J. (2022) · 癌症：英文版 · doi:10.1002/cac2.12363 · Cited by 196 · see citing works
Paonessa, F., Evans, L., Solanki, R., Larrieu, D., Wray, S., Hardy, J., Jackson, S. P., & Livesey, F. J. (2019) · Cell Reports · doi:10.1016/j.celrep.2018.12.085 · Cited by 189 · see citing works
Self-citationRNA modification: mechanisms and therapeutic targets
Qiu, L., Qian, J., Li, Y., & Han, J. (2023) · Molecular Biomedicine · doi:10.1186/s43556-023-00139-x · Cited by 180 · see citing works
Visualizing biologically active small molecules in cells using click chemistry
Cañeque, T., Müller, S., & Rodriguez, R. (2018) · Nature Reviews Chemistry · doi:10.1038/s41570-018-0030-x · Cited by 176 · see citing works
Self-citationNuclear rupture at sites of high curvature compromises retention of DNA repair factors
Xia, Y., Ivanovska, I. L., Zhu, K., Smith, L., Irianto, J., Pfeifer, C. R., Alvey, C. M., Ji, J., Liu, D., Cho, S., et al. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201711161 · Cited by 176 · see citing works
Acetylation of Cytidine Residues Boosts HIV-1 Gene Expression by Increasing Viral RNA Stability
Tsai, K., Vasudevan, A. A. J., Campos, C. M., Emery, A., Swanstrom, R. I., & Cullen, B. R. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.05.011 · Cited by 176 · see citing works
CRISPR-Cas9D10A nickase-based genotypic and phenotypic screening to enhance genome editing
Chiang, T.-W. W., le Sage, C., Larrieu, D., Demir, M., & Jackson, S. P. (2016) · Scientific Reports · doi:10.1038/srep24356 · Cited by 165 · see citing works
Self-citationNAT10‐mediated mRNA N4‐acetylcytidine modification promotes bladder cancer progression
Wang, G., Zhang, M., Zhang, Y., Xie, Y., Zou, J., Zhong, J., Zheng, Z., Zhou, X., Zheng, Y., Chen, B., et al. (2022) · Clinical and Translational Medicine · doi:10.1002/ctm2.738 · Cited by 160 · see citing works
Jin, C., Wang, T., Zhang, D., Yang, P., Zhang, C., Peng, W., Jin, K., Wang, L., Zhou, J., Peng, C., et al. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-022-02551-7 · Cited by 154 · see citing works
Hallmarks of progeroid syndromes: lessons from mice and reprogrammed cells
Carrero, D., Soria-Valles, C., & López-Otín, C. (2016) · Disease Models & Mechanisms · doi:10.1242/dmm.024711 · Cited by 153 · see citing works
Ito, S., Akamatsu, Y., Noma, A., 木村聡, Miyauchi, K., Ikeuchi, Y., Suzuki, T., & Suzuki, T. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.593996 · Cited by 150 · see citing works
Moving Cell Boundaries Drive Nuclear Shaping during Cell Spreading
Li, Y., Lovett, D. B., Zhang, Q., Neelam, S., Kuchibhotla, R. A., Zhu, R., Gundersen, G. G., Lele, T. P., & Dickinson, R. B. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.07.006 · Cited by 124 · see citing works
Kreienkamp, R., Graziano, S., Coll-Bonfill, N., Bedia‐Diaz, G., Cybulla, E., Vindigni, A., Dorsett, D., Kubben, N., Batista, L. F. Z., & Gonzalo, S. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.01.090 · Cited by 124 · see citing works
Yang, W., Li, H., Wu, Y., Mi, R., Liu, W. Z., Shen, X., Lu, Y., Jiang, Y., Ma, M. J., & Shen, H. (2021) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2021.06.022 · Cited by 124 · see citing works
MORC2 regulates DNA damage response through a PARP1-dependent pathway
Zhang, L., & Li, D. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz545 · Cited by 117 · see citing works
Nuclear envelopathies: a complex LINC between nuclear envelope and pathology
Janin, A., Bauer, D., Ratti, F., Millat, G., & Méjat, A. (2017) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-017-0698-x · Cited by 114 · see citing works
Liu, X., Cai, S., Zhang, C., Liu, Z., Luo, J., Xing, B., & Du, X. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky777 · Cited by 114 · see citing works
A Chemical Signature for Cytidine Acetylation in RNA
Thomas, J. M., Briney, C. A., Nance, K. D., López, J. E., Thorpe, A. L., Fox, S. D., Bortolin‐Cavaillé, M., Sas‐Chen, A., Arango, D., Oberdoerffer, S., et al. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b06636 · Cited by 114 · see citing works
Deng, M., Zhang, L., Zheng, W., Chen, J., Du, N., Li, M., Chen, W., Huang, Y., Zeng, N., Song, Y., et al. (2023) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-022-02586-w · Cited by 111 · see citing works
The Power of Sophisticated Phenotypic Screening and Modern Mechanism-of-Action Methods
Wagner, B. K., & Schreiber, S. L. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2015.11.008 · Cited by 110 · see citing works
Causes and consequences of nuclear envelope alterations in tumour progression
Bell, E. S., & Lammerding, J. (2016) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2016.06.007 · Cited by 110 · see citing works
Wei, R., Cui, X., Min, J., Lin, Z., Zhou, Y., Guo, M., An, X., Liu, H., Janz, S., Gu, C., et al. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.01.015 · Cited by 110 · see citing works
Lamin A/C: Function in Normal and Tumor Cells
Dubik, N., & Mai, S. (2020) · Cancers · doi:10.3390/cancers12123688 · Cited by 108 · see citing works
Nuclear envelope dysfunction and its contribution to the aging process
Martins, F., Sousa, J., Pereira, C. D., Silva, O. A. B. D. C. E., & Rebelo, S. (2020) · Aging Cell · doi:10.1111/acel.13143 · Cited by 107 · see citing works
Larrieu, D., Viré, E. A., Robson, S. C., Breusegem, S. Y., Kouzarides, T., & Jackson, S. P. (2018) · Science Signaling · doi:10.1126/scisignal.aar5401 · Cited by 101 · see citing works
Self-citationThe nuclear lamina in health and disease
Dobrzynska, A., Gonzalo, S., Shanahan, C. M., & Askjaer, P. (2016) · Nucleus · doi:10.1080/19491034.2016.1183848 · Cited by 101 · see citing works
NAT10 is upregulated in hepatocellular carcinoma and enhances mutant p53 activity
Li, Q., Liu, X., Jin, K., Lu, M., Zhang, C., Du, X., & Xing, B. (2017) · BMC Cancer · doi:10.1186/s12885-017-3570-4 · Cited by 98 · see citing works
Quantitative nucleotide resolution profiling of RNA cytidine acetylation by ac4C-seq
Gamage, S. T., Sas‐Chen, A., Schwartz, S., & Meier, J. L. (2021) · Nature Protocols · doi:10.1038/s41596-021-00501-9 · Cited by 97 · see citing works
An overview of treatment strategies for Hutchinson-Gilford Progeria syndrome
Harhouri, K., Frankel, D., Bartoli, C., Roll, P., Sandre‐Giovannoli, A. D., & Lévy, N. (2018) · Nucleus · doi:10.1080/19491034.2018.1460045 · Cited by 96 · see citing works
Yang, Q., Lei, X., He, J., Peng, Y., Zhang, Y., Ling, R., Wu, C., Zhang, G., Zheng, B., Chen, X., et al. (2023) · Advanced Science · doi:10.1002/advs.202300898 · Cited by 96 · see citing works
Unravelling the genomic targets of small molecules using high-throughput sequencing
Rodriguez, R., & Miller, K. M. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3796 · Cited by 94 · see citing works
Self-citationNAT10 Is Involved in Cardiac Remodeling Through ac4C-Mediated Transcriptomic Regulation
Shi, J., Yang, C., Zhang, J., Zhao, K., Li, P., Kong, C., Wu, X., Sun, H., Zheng, R., Sun, W. Y., et al. (2023) · Circulation Research · doi:10.1161/circresaha.122.322244 · Cited by 93 · see citing works
Nuclear Morphological Abnormalities in Cancer: A Search for Unifying Mechanisms
Singh, I., & Lele, T. P. (2022) · Results and problems in cell differentiation · doi:10.1007/978-3-031-06573-6_16 · Cited by 92 · see citing works
DNA damage induces nuclear envelope rupture through ATR-mediated phosphorylation of lamin A/C
Kovacs, M. T., Vallette, M., Wiertsema, P., Dingli, F., Loew, D., Nader, G. P. F., Piel, M., & Ceccaldi, R. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.09.023 · Cited by 87 · see citing works
Wei, W., Zhang, S., Han, H., Wang, X., Zheng, S., Wang, Z., Yang, C., Wang, L., Ma, J., Guo, S., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112810 · Cited by 86 · see citing works
Nuclear lamins: Structure and function in mechanobiology
Vahabikashi, A., Adam, S. A., Medalia, O., & Goldman, R. D. (2022) · APL Bioengineering · doi:10.1063/5.0082656 · Cited by 85 · see citing works
Chang, W., Wang, Y., Luxton, G. W. G., Östlund, C., Worman, H. J., & Gundersen, G. G. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1809683116 · Cited by 84 · see citing works
Chen, L., Wang, W., Liu, Q., Wu, Y.-K., Wu, Y., Jiang, Y., Liao, X.-Q., Huang, F., Li, Y., Shen, L., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac594 · Cited by 84 · see citing works
Declining lamin B1 expression mediates age-dependent decreases of hippocampal stem cell activity
bin Imtiaz, M. K., Jaeger, B. N., Bottes, S., Machado, R. A. C., Vidmar, M., Moore, D. L., & Jessberger, S. (2021) · Cell Stem Cell · doi:10.1016/j.stem.2021.01.015 · Cited by 83 · see citing works
Profiling Cytidine Acetylation with Specific Affinity and Reactivity
Sinclair, W. R., Arango, D., Shrimp, J. H., Zengeya, T. T., Thomas, J. M., Montgomery, D. C., Fox, S. D., Andrésson, Þ., Oberdoerffer, S., & Meier, J. L. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00734 · Cited by 83 · see citing works
Yan, Q., Zhou, J., Wang, Z., Ding, X., Ma, X., Wan, L., Jia, X., Gao, S., & Lu, C. (2023) · Nature Communications · doi:10.1038/s41467-023-42135-3 · Cited by 81 · see citing works
In silico synchronization reveals regulators of nuclear ruptures in lamin A/C deficient model cells
Robijns, J., Molenberghs, F., Sieprath, T., Corne, T., Verschuuren, M., & Vos, W. H. D. (2016) · Scientific Reports · doi:10.1038/srep30325 · Cited by 80 · see citing works
Jackson, S. P., & Helleday, T. (2016) · Science · doi:10.1126/science.aab0958 · Cited by 80 · see citing works
Self-citationMaternal NAT10 orchestrates oocyte meiotic cell-cycle progression and maturation in mice
Jiang, X., Cheng, Y. D., Zhu, Y., Xu, C., Li, Q., Xing, X., Li, W., Zou, J., Meng, L., Azhar, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39256-0 · Cited by 79 · see citing works
Emerging roles of RNA ac4C modification and NAT10 in mammalian development and human diseases
Zhang, Y., Lei, Y., Dong, Y., Chen, S., Sun, S., Zhou, F., Zhao, Z., Chen, B., Lv, W., Chen, J., et al. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108576 · Cited by 79 · see citing works
Probing small ribosomal subunit RNA helix 45 acetylation across eukaryotic evolution
Bortolin‐Cavaillé, M., Quillien, A., Gamage, S. T., Thomas, J. M., Sas‐Chen, A., Sharma, S., Plisson‐Chastang, C., Vandel, L., Blader, P., Lafontaine, D. L. J., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac404 · Cited by 77 · see citing works
NAT10 as a potential prognostic biomarker and therapeutic target for HNSCC
Tao, W., Tian, G., Xu, S., Li, J., Zhang, Z., & Li, J. (2021) · Cancer Cell International · doi:10.1186/s12935-021-02124-2 · Cited by 76 · see citing works
Autoacetylation of NAT10 is critical for its function in rRNA transcription activation
Cai, S., Liu, X., Zhang, C., Xing, B., & Du, X. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.12.092 · Cited by 72 · see citing works
Tan, Y., Zheng, J., Liu, X., Lu, M., Zhang, C., Xing, B., & Du, X. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.04.047 · Cited by 72 · see citing works
Site-Specific Synthesis of N 4 -Acetylcytidine in RNA Reveals Physiological Duplex Stabilization
Bartee, D., Nance, K. D., & Meier, J. L. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.1c11985 · Cited by 71 · see citing works
Puttaraju, M., Jackson, M., Klein, S., Shilo, A., Bennett, C. F., Gordon, L. B., Rigo, F., & Misteli, T. (2021) · Nature Medicine · doi:10.1038/s41591-021-01262-4 · Cited by 70 · see citing works
N4-acetylcytidine regulates the replication and pathogenicity of enterovirus 71
Hao, H., Liu, W., Miao, Y., Ma, L., Yu, B., Liu, L., Yang, C., Zhang, K., Chen, Z., Yang, J., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac675 · Cited by 69 · see citing works
DNA double-strand break–capturing nuclear envelope tubules drive DNA repair
Shokrollahi, M., Stanić, M., Hundal, A. K., Chan, J. N. Y., Urman, D., Jordan, C. A., Hakem, A., Espín, R., Hao, J., Krishnan, R., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01286-7 · Cited by 68 · see citing works
Lamin A and microtubules collaborate to maintain nuclear morphology
Tariq, Z., Zhang, H., Chia-Liu, A., Shen, Y., Gete, Y. G., Xiong, Z., Tocheny, C. E., Campanello, L., Wu, D., Losert, W., et al. (2017) · Nucleus · doi:10.1080/19491034.2017.1320460 · Cited by 67 · see citing works
NAT10 regulates the LPS-induced inflammatory response via the NOX2-ROS-NF-κB pathway in macrophages
Zhang, Z., Zhang, Y., Cai, Y., Li, D., He, J., Feng, Z., & Xu, Q. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2023.119521 · Cited by 67 · see citing works
Montgomery, D. C., Sorum, A. W., & Meier, J. L. (2014) · Journal of the American Chemical Society · doi:10.1021/ja502372j · Cited by 66 · see citing works
Current insights into LMNA cardiomyopathies: Existing models and missing LINCs
Brayson, D., & Shanahan, C. M. (2017) · Nucleus · doi:10.1080/19491034.2016.1260798 · Cited by 66 · see citing works
Cao, Y., Yao, M., Wu, Y., Ma, N., Liu, H., & Zhang, B. (2020) · Translational Oncology · doi:10.1016/j.tranon.2020.100783 · Cited by 65 · see citing works
Dalhat, M. H., Mohammed, M. R. S., Ahmad, A., Khan, M. I., & Choudhry, H. (2021) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30155 · Cited by 65 · see citing works
Zi, J., Han, Q., Gu, S., McGrath, M., Kane, S., Song, C., & Ge, Z. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.598107 · Cited by 64 · see citing works
Zheng, J., Tan, Y., Liu, X., Zhang, C., Su, K., Jiang, Y. Z., Luo, J., Li, L., & Du, X. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-021-00899-5 · Cited by 64 · see citing works
Graziano, S., Kreienkamp, R., Coll-Bonfill, N., & Gonzalo, S. (2018) · Nucleus · doi:10.1080/19491034.2018.1454168 · Cited by 63 · see citing works
Recent Advances on the Structure and Function of RNA Acetyltransferase Kre33/NAT10
Sleiman, S., & Dragon, F. (2019) · Cells · doi:10.3390/cells8091035 · Cited by 62 · see citing works
Qu, Z., Pang, X., Mei, Z., Li, Y., Zhang, Y., Huang, C., Liu, K., Yu, S., Wang, C., Sun, Z., et al. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103145 · Cited by 62 · see citing works
Kubben, N., Brimacombe, K. R., Donegan, M., Li, Z., & Misteli, T. (2015) · Methods · doi:10.1016/j.ymeth.2015.08.024 · Cited by 61 · see citing works
Synthesis of marmycin A and investigation into its cellular activity
Cañeque, T., Gomes, F., Mai, T. T., Maestri, G., Malacrìa, M., & Rodriguez, R. (2015) · Nature Chemistry · doi:10.1038/nchem.2302 · Cited by 61 · see citing works
Self-citationAnchoring a Leviathan: How the Nuclear Membrane Tethers the Genome
Czapiewski, R., Robson, M. I., & Schirmer, E. C. (2016) · Frontiers in Genetics · doi:10.3389/fgene.2016.00082 · Cited by 61 · see citing works
Dalhat, M. H., Altayb, H. N., Khan, M. I., & Choudhry, H. (2021) · Scientific Reports · doi:10.1038/s41598-021-84908-0 · Cited by 60 · see citing works
Prelamin A impairs 53BP1 nuclear entry by mislocalizing NUP153 and disrupting the Ran gradient
Cobb, A. M., Larrieu, D., Warren, D. T., Liu, Y., Srivastava, S., Smith, A. J. O., Bowater, R. P., Jackson, S. P., & Shanahan, C. M. (2016) · Aging Cell · doi:10.1111/acel.12506 · Cited by 60 · see citing works
Self-citationOh, T.-I., Lee, Y.-M., Lim, B. O., & Lim, J.-H. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18091924 · Cited by 60 · see citing works
Hutchinson-Gilford Progeria Syndrome—Current Status and Prospects for Gene Therapy Treatment
Piekarowicz, K., Machowska, M., Dzianisava, V., & Rzepecki, R. (2019) · Cells · doi:10.3390/cells8020088 · Cited by 60 · see citing works
Nuisance compounds in cellular assays
Dahlin, J. L., Auld, D. S., Rothenaigner, I., Haney, S., Sexton, J. Z., Nissink, J. W. M., Walsh, J. J., Lee, J. A., Strelow, J. M., Willard, F. S., et al. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.01.021 · Cited by 60 · see citing works
Centenarians as a model to discover genetic and epigenetic signatures of healthy ageing
Puca, A. A., Spinelli, C., Accardi, G., Villa, F., & Caruso, C. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2017.10.004 · Cited by 58 · see citing works
Regulation of Nuclear Mechanics and the Impact on DNA Damage
dos Santos, Á., & Toseland, C. P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22063178 · Cited by 56 · see citing works
Janssen, A. F. J., Breusegem, S. Y., & Larrieu, D. (2022) · Cells · doi:10.3390/cells11030347 · Cited by 56 · see citing works
Self-citation
- Authors
- Larrieu, D., Britton, S., Demir, M., Rodriguez, R., & Jackson, S. P.
- Affiliations
- University of Cambridge (GB)
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Britton, Sébastien
- Rodriguez, Raphaël
- Jackson, Stephen P.
- Venue
- Science
- Published
- 2014-05-02
- Volume
- 344
- Issue
- 6183
- Pages
- 527-532
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC4246063
- OpenAlex
- W2008052894
- Cited by
- 431
- References
- 27
- Citations by year
- 2026: 51 · 2025: 64 · 2024: 45 · 2023: 45 · 2022: 39 · 2021: 32 · 2020: 22 · 2019: 31 · 2018: 28 · 2017: 26 · 2016: 24 · 2015: 14 · 2014: 10
- FWCI
- 10.06
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- HAL (submittedVersion)
- Apollo (University of Cambridge) (submittedVersion)
- Apollo
- Funders
- Wellcome Trust (092096/Z/10/Z, WT092096, 092096)
- Cancer Research UK (18796, C6/A11224, C6946 /A14492, 11224, A11224)
- Medical Research Council (MR/L019116/1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Skin and Cellular Biology Research
- Keywords
- NAT10, lamin A/C, laminopathies, Hutchinson-Gilford progeria syndrome, Remodelin, nuclear organization, chromatin organization, microtubule reorganization, DNA damage, premature aging, histone acetylation
- MeSH terms
- Cell Nucleus, Chromatin, Enzyme Inhibitors, Humans, Hydrazones, Microtubules, Progeria, Thiazoles, Nocodazole, Protein Structure, Tertiary, RNA, Small Interfering, Lamin Type A, Cell Line, Tumor, N-Terminal Acetyltransferases, N-Terminal Acetyltransferase E
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
