Chemical Inhibition of NAT10 Corrects Defects of Laminopathic Cells

Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome

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Lamin a truncation in Hutchinson-Gilford progeria

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Lamin A-dependent nuclear defects in human aging

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Small-molecule–induced DNA damage identifies alternative DNA structures in human genes

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“Laminopathies”: A wide spectrum of human diseases

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Inhibiting farnesylation of progerin prevents the characteristic nuclear blebbing of Hutchinson-Gilford progeria syndrome

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Identifying the proteins to which small-molecule probes and drugs bind in cells

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Blocking protein farnesyltransferase improves nuclear shape in fibroblasts from humans with progeroid syndromes

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Incomplete processing of mutant lamin A in Hutchinson–Gilford progeria leads to nuclear abnormalities, which are reversed by farnesyltransferase inhibition

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Accumulation of the Inner Nuclear Envelope Protein Sun1 Is Pathogenic in Progeric and Dystrophic Laminopathies

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Acetylation of Cytidine in mRNA Promotes Translation Efficiency

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Fighting against Skin Aging: The Way from Bench to Bedside

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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

Salinomycin kills cancer stem cells by sequestering iron in lysosomes

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The RNA modification landscape in human disease

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The Keap1-Nrf2 System: A Mediator between Oxidative Stress and Aging

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Determining consistent prognostic biomarkers of overall survival and vascular invasion in hepatocellular carcinoma

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The Aging Epigenome

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Yeast Kre33 and human NAT10 are conserved 18S rRNA cytosine acetyltransferases that modify tRNAs assisted by the adaptor Tan1/THUMPD1

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 394

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 368

YAP/TAZ activity in stromal cells prevents ageing by controlling cGAS–STING

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Dynamic RNA acetylation revealed by quantitative cross-evolutionary mapping

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Hutchinson-Gilford Progeria Syndrome: A premature aging disease caused by LMNA gene mutations

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Mechanosensing by the Lamina Protects against Nuclear Rupture, DNA Damage, and Cell-Cycle Arrest

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Human NAT10 Is an ATP-dependent RNA Acetyltransferase Responsible for N4-Acetylcytidine Formation in 18 S Ribosomal RNA (rRNA)

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

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

Mutant lamins cause nuclear envelope rupture and DNA damage in skeletal muscle cells

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‘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 255

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

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 214

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 227

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

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 220

Acetylation of MORC2 by NAT10 regulates cell-cycle checkpoint control and resistance to DNA-damaging chemotherapy and radiotherapy in breast cancer

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 210

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 205

N‐acetyltransferase 10 promotes colon cancer progression by inhibiting ferroptosis through N4‐acetylation and stabilization of ferroptosis suppressor protein 1 (FSP1) mRNA

Zheng, 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

Microtubules Deform the Nuclear Membrane and Disrupt Nucleocytoplasmic Transport in Tau-Mediated Frontotemporal Dementia

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

RNA 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 182

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 185

Nuclear 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 184

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

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 171

NAT10‐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

Acetyltransferase NAT10 regulates the Wnt/β-catenin signaling pathway to promote colorectal cancer progression via ac4C acetylation of KIF23 mRNA

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

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

A Single Acetylation of 18 S rRNA Is Essential for Biogenesis of the Small Ribosomal Subunit in Saccharomyces cerevisiae

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Moving Cell Boundaries Drive Nuclear Shaping during Cell Spreading

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A Cell-Intrinsic Interferon-like Response Links Replication Stress to Cellular Aging Caused by Progerin

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 125

ac4C acetylation of RUNX2 catalyzed by NAT10 spurs osteogenesis of BMSCs and prevents ovariectomy-induced bone loss

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

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 119

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

Deacetylation of NAT10 by Sirt1 promotes the transition from rRNA biogenesis to autophagy upon energy stress

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

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

Helicobacter pylori-induced NAT10 stabilizes MDM2 mRNA via RNA acetylation to facilitate gastric cancer progression

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

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

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 115

NAT10 promotes cell proliferation by acetylating CEP170 mRNA to enhance translation efficiency in multiple myeloma

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

Lamin A/C: Function in Normal and Tumor Cells

Dubik, N., & Mai, S. (2020) · Cancers · doi:10.3390/cancers12123688 · Cited by 108

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 114

Inhibition of the acetyltransferase NAT10 normalizes progeric and aging cells by rebalancing the Transportin-1 nuclear import pathway

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 103

The 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 108

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

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

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 102

N4‐Acetylcytidine Drives Glycolysis Addiction in Gastric Cancer via NAT10/SEPT9/HIF‐1α Positive Feedback Loop

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 97

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 100

NAT10 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

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 95

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 92

NAT10-mediated ac4C tRNA modification promotes EGFR mRNA translation and gefitinib resistance in cancer

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

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 88

Imbalanced nucleocytoskeletal connections create common polarity defects in progeria and physiological aging

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 86

NAT10-mediated N 4-acetylcytidine modification is required for meiosis entry and progression in male germ cells

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

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

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

NAT10-dependent N4‐acetylcytidine modification mediates PAN RNA stability, KSHV reactivation, and IFI16-related inflammasome activation

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

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 83

Drugging DNA repair

Jackson, S. P., & Helleday, T. (2016) · Science · doi:10.1126/science.aab0958 · Cited by 81

Maternal 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

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

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

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

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

Loss of nucleolar localization of NAT10 promotes cell migration and invasion in hepatocellular carcinoma

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

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 72

Systematic screening identifies therapeutic antisense oligonucleotides for Hutchinson–Gilford progeria syndrome

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 72

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

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 71

Lamin A and microtubules collaborate to maintain nuclear morphology

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NAT10 regulates the LPS-induced inflammatory response via the NOX2-ROS-NF-κB pathway in macrophages

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N-Acetyltransferase 10 Promotes Micronuclei Formation to Activate the Senescence-Associated Secretory Phenotype Machinery in Colorectal Cancer Cells

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Targeting NAT10 Induces Apoptosis Associated With Enhancing Endoplasmic Reticulum Stress in Acute Myeloid Leukemia Cells

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NAT10 regulates mitotic cell fate by acetylating Eg5 to control bipolar spindle assembly and chromosome segregation

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A high-content imaging-based screening pipeline for the systematic identification of anti-progeroid compounds

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Synthesis of marmycin A and investigation into its cellular activity

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Anchoring a Leviathan: How the Nuclear Membrane Tethers the Genome

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Prelamin A impairs 53BP1 nuclear entry by mislocalizing NUP153 and disrupting the Ran gradient

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Inhibition of NAT10 Suppresses Melanogenesis and Melanoma Growth by Attenuating Microphthalmia-Associated Transcription Factor (MITF) Expression

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Hutchinson-Gilford Progeria Syndrome—Current Status and Prospects for Gene Therapy Treatment

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Nuisance compounds in cellular assays

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Centenarians as a model to discover genetic and epigenetic signatures of healthy ageing

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Regulation of Nuclear Mechanics and the Impact on DNA Damage

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Current Methods and Pipelines for Image-Based Quantitation of Nuclear Shape and Nuclear Envelope Abnormalities

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L’inhibition chimique de NAT10 corrige les défauts des cellules laminopathiques

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Everolimus rescues multiple cellular defects in laminopathy-patient fibroblasts

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Imaging Lamin A/C and laminopathy-Linked Mutations: A Multi-Parameter Analysis of Nuclear Shape, Protein Localization, and Therapeutic Response

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