Chemical Inhibition of NAT10 Corrects Defects of Laminopathic Cells

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., Scott, L., Erdos, M. R., Robbins, C. M., Moses, T. Y., Berglund, P., et al. (2003) · Nature · doi:10.1038/nature01629 · Cited by 1,990

Lamin a truncation in Hutchinson-Gilford progeria

De Sandre-Giovannoli, A., Bernard, R., Cau, P., Navarro, C., Amiel, J., Boccaccio, I., Lyonnet, S., Stewart, C. L., Munnich, A., Le Merrer, M., et al. (2003) · Science · doi:10.1126/science.1084125 · Cited by 1,346

Lamin A-dependent nuclear defects in human aging

Scaffidi, P., & Misteli, T. (2006) · Science · doi:10.1126/science.1127168 · Cited by 1,125

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

“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 673

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

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

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 303

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

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

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

Glynn, M. W., & Glover, T. W. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi326 · Cited by 259

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

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

Pharmacotherapy to gene editing: potential therapeutic approaches for Hutchinson–Gilford progeria syndrome

Saxena, S., & Kumar, S. (2020) · GeroScience · doi:10.1007/s11357-020-00167-3 · Cited by 23

Paclitaxel mitigates structural alterations and cardiac conduction system defects in a mouse model of Hutchinson–Gilford progeria syndrome

Macías, Á., Díaz-Larrosa, J. J., Blanco, Y., Fanjul, V., González‐Gómez, C., Gonzalo, P., Andrés‐Manzano, M. J., da Rocha, A. M., Ponce‐Balbuena, D., Allan, A., et al. (2021) · Cardiovascular Research · doi:10.1093/cvr/cvab055 · Cited by 23

NAT10 promotes liver lipogenesis in mouse through N4-acetylcytidine modification of Srebf1 and Scap mRNA

Wang, Z., Wan, X., Khan, M. A., Peng, L., Sun, X., Yi, X., & Chen, K. (2024) · Lipids in Health and Disease · doi:10.1186/s12944-024-02360-1 · Cited by 21

Chromatin phase separation and nuclear shape fluctuations are correlated in a polymer model of the nucleus

Attar, A. G., Paturej, J., Banigan, E. J., & Erbaş, A. (2024) · Nucleus · doi:10.1080/19491034.2024.2351957 · Cited by 21

Arrow pushing in RNA modification sequencing

Bartee, D., Gamage, S. T., Link, C. N., & Meier, J. L. (2021) · Chemical Society Reviews · doi:10.1039/d1cs00214g · Cited by 21

NAT10-mediated mRNA N 4 -acetylation is essential for the translational regulation during oocyte meiotic maturation in mice

Chen, L., Wang, W.-J., Liu, S.-Y., Su, R., Wu, Y.-K., Wu, X., Zhang, S., Qiao, J., Sha, Q., & Fan, H. (2025) · Science Advances · doi:10.1126/sciadv.adp5163 · Cited by 20

The Role of Lamins in the Nucleoplasmic Reticulum, a Pleiomorphic Organelle That Enhances Nucleo-Cytoplasmic Interplay

Stiekema, M., Houben, F., Verheyen, F., Borgers, M. J., Menzel, J., Meschkat, M., van Zandvoort, M. A. M. J., Ramaekers, F. C. S., & Broers, J. L. V. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.914286 · Cited by 20

The E262K mutation in Lamin A links nuclear proteostasis imbalance to laminopathy‐associated premature aging

Ghosh, D. K., Pande, S., Jeevan Kumar, M., Yesodharan, D., Nampoothiri, S., Radhakrishnan, P., Reddy, C. G., Ranjan, A., & Girisha, K. M. (2022) · Aging Cell · doi:10.1111/acel.13688 · Cited by 20

Dock5 is a new regulator of microtubule dynamic instability in osteoclasts

Guimbal, S., Morel, A., Guérit, D., Chardon, M., Blangy, A., & Vives, V. (2019) · Biology of the Cell · doi:10.1111/boc.201900014 · Cited by 19

Filamentous nuclear actin regulation of PML NBs during the DNA damage response is deregulated by prelamin A

Cobb, A. M., Silva, S. A. D., Hayward, R., Sek, K., Ulferts, S., Grosse, R., & Shanahan, C. M. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05491-4 · Cited by 20

Perinuclear damage from nuclear envelope deterioration elicits stress responses that contribute toLMNAcardiomyopathy

Sikder, K., Phillips, E., Zhong, Z., Wang, N., Saunders, J., Mothy, D., Kossenkov, A. V., Schneider, T. G., Nichtová, Z., Csordás, G., et al. (2024) · Science Advances · doi:10.1126/sciadv.adh0798 · Cited by 19

A Link between Replicative Stress, Lamin Proteins, and Inflammation

Willaume, S., Rass, E., Fontanilla-Ramirez, P., Moussa, A., Wanschoor, P., & Bertrand, P. (2021) · Genes · doi:10.3390/genes12040552 · Cited by 28

N4-acetylcytidine modification of ITGB5 mRNA mediated by NAT10 promotes perineural invasion in pancreatic ductal adenocarcinoma

Huang, L., Lu, Y., He, R., Guo, X., Zhou, J., Fu, Z., Li, J., Liu, J., Chen, R., Zhou, Y., et al. (2025) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-025-03362-2 · Cited by 18

Dissecting the oncogenic properties of essential RNA-modifying enzymes: a focus on NAT10

Dalhat, M. H., Narayan, S., Serio, H., & Arango, D. (2024) · Oncogene · doi:10.1038/s41388-024-02975-9 · Cited by 18

The Nuclear Envelope: An Intriguing Focal Point for Neurogenetic Disease

Worman, H. J., & Dauer, W. T. (2014) · Neurotherapeutics · doi:10.1007/s13311-014-0296-8 · Cited by 19

Hutchinson-Gilford Progeria Syndrome: Challenges at Bench and Bedside

Kreienkamp, R., & Gonzalo, S. (2019) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-981-13-3681-2_15 · Cited by 18

N‐acetyltransferase 10 facilitates tumorigenesis of diffuse large B‐cell lymphoma by regulating AMPK/mTOR signalling through N4‐acetylcytidine modification of SLC30A9

Ding, M., Yu, Z., Lu, T., Hu, S., Zhou, X., & Wang, X. (2024) · Clinical and Translational Medicine · doi:10.1002/ctm2.1747 · Cited by 17

Dysregulated ac4C modification of mRNA in a mouse model of early-stage Alzheimer’s disease

Ji, H., Zhou, H.-Q., Qie, J., Lu, W.-M., Gao, H., & Wu, D. (2025) · Cell & Bioscience · doi:10.1186/s13578-025-01389-8 · Cited by 17

Targeting NAT10 Inhibits Hepatocarcinogenesis via ac4C‐Mediated SMAD3 mRNA Stability

Zhang, Y., Dong, Y., Chen, S., Deng, H., Yu, W., Chen, B., Chen, M., Liu, W., Tan, X., Ni, J., et al. (2025) · Exploration · doi:10.1002/exp.20250075 · Cited by 17

N-acetyltransferase 10 regulates alphavirus replication via N4-acetylcytidine (ac4C) modification of the lymphocyte antigen six family member E (LY6E) mRNA

Dang, Y., Li, J., Li, Y., Wang, Y., Zhao, Y., Zhao, N., Li, W., Zhang, H., Ye, C., Ma, H., et al. (2024) · Journal of Virology · doi:10.1128/jvi.01350-23 · Cited by 17

Pluripotent stem cells to model Hutchinson-Gilford progeria syndrome (HGPS): Current trends and future perspectives for drug discovery

Cicero, A. L., & Nissan, X. (2015) · Ageing Research Reviews · doi:10.1016/j.arr.2015.10.002 · Cited by 17

Induced Pluripotent Stem Cells to Study Mechanisms of Laminopathies: Focus on Epigenetics

Crasto, S., & Pasquale, E. D. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00172 · Cited by 20

NAT10 resolves harmful nucleolar R-loops depending on its helicase domain and acetylation of DDX21

Su, K., Zhao, Z., Wang, Y., Sun, S., Liu, X., Zhang, C., Jiang, Y., & Du, X. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01869-3 · Cited by 16

N‐acetyltransferase 10 promotes the progression of oral squamous cell carcinoma through N4‐acetylcytidine RNA acetylation of MMP1 mRNA

Liu, Y., Huang, H., Zhang, C., & Fan, H. (2023) · Cancer Science · doi:10.1111/cas.15946 · Cited by 16

The mechanistic role of NAT10 in cancer: Unraveling the enigmatic web of oncogenic signaling

Rodrigues, P., Bangali, H., Ali, E., Абдрешов, С. Н., Hjazi, A. M., Fenjan, M. N., Alawadi, A. H., Alsaalamy, A. H., Alasheqi, M. Q., & Mustafa, Y. F. (2023) · Pathology - Research and Practice · doi:10.1016/j.prp.2023.154990 · Cited by 16

N-acetyltransferase 10 is implicated in the pathogenesis of cycling T cell-mediated autoimmune and inflammatory disorders in mice

Li, W., Mao, X.-T., Xie, J.-H., Li, J., Liu, B.-Q., Wu, L.-X., Yang, B., Li, Y., & Jin, J. (2024) · Nature Communications · doi:10.1038/s41467-024-53350-x · Cited by 16

NAT10‐mediated RNA ac4C acetylation contributes to the myocardial infarction‐induced cardiac fibrosis

Li, J., Yushanjiang, F., Fang, Z., & Liu, W. (2024) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.70141 · Cited by 16

Alterations in the nuclear proteome of HIV-1 infected T-cells

DeBoer, J., Jagadish, T., Haverland, N. A., Madson, C. J., Ciborowski, P. S., & Belshan, M. (2014) · Virology · doi:10.1016/j.virol.2014.08.029 · Cited by 16

NAT10-mediated N4-acetylcytidine modification in KLF9 mRNA promotes adipogenesis

Wan, X., Wang, L., Khan, M. A., Peng, L., Sun, X., Yi, X., Wang, Z., & Chen, K. (2025) · Cell Death and Differentiation · doi:10.1038/s41418-025-01483-x · Cited by 15

Programmable RNA acetylation with CRISPR–Cas13

Yu, J., Jin, J., Kwon, E., Jang, H., Choi, S.-K., Kim, D., Kim, C., Son, S., Yoon, K., & Heo, W. D. (2025) · Nature Chemical Biology · doi:10.1038/s41589-025-01922-3 · Cited by 15

Loss of NAT10 Reduces the Translation of Kmt5a mRNA Through ac4C Modification in Cardiomyocytes and Induces Heart Failure

Xu, T., Du, T., Zhuang, X., He, X., Yan, Y., Wu, J., Zhou, H., Li, Y., Liao, X., He, J., et al. (2024) · Journal of the American Heart Association · doi:10.1161/jaha.124.035714 · Cited by 15

Bypassing Border Control: Nuclear Envelope Rupture in Disease

Houthaeve, G., Robijns, J., Braeckmans, K., & Vos, W. H. D. (2017) · Physiology · doi:10.1152/physiol.00029.2017 · Cited by 16

Preclinical Advances of Therapies for Laminopathies

Benarroch, L., Cohen, E., Atalaia, A., Yaou, R. B., Bonne, G., & Bertrand, A. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10214834 · Cited by 18

Biological Function and Mechanism of NAT10 in Cancer

Han, Y., Zhang, X., Miao, L., Lin, H., Zhuo, Z., He, J., & Fu, W. (2025) · Cancer Innovation · doi:10.1002/cai2.154 · Cited by 14

NAT10 and N 4 -acetylcytidine restrain R-loop levels and related inflammatory responses

Debnath, T. K., Abell, N. S., Li, Y.-R., Devanathan, S. K., Navedo, E., & Xhemalçe, B. (2025) · Science Advances · doi:10.1126/sciadv.ads6144 · Cited by 14

A Histone Acetyltransferase Inhibitor with Antifungal Activity against CTG clade Candida Species

Tscherner, M., & Kuchler, K. (2019) · Microorganisms · doi:10.3390/microorganisms7070201 · Cited by 16

Consequences of Lmna Exon 4 Mutations in Myoblast Function

Gómez-Domínguez, D., Epifano, C., de Miguel, F., Castaño, A. G., Vilaplana‐Martí, B., Martín, A. L., Amarilla‐Quintana, S., Bertrand, A., Bonne, G., Ramón‐Azcón, J., et al. (2020) · Cells · doi:10.3390/cells9051286 · Cited by 14

DARS-AS1 modulates cell proliferation and migration of gastric cancer cells by regulating miR-330-3p/NAT10 axis

Du, C., Han, X., Zhang, Y., Guo, F., Yuan, H., Wang, F., Li, M., Ning, F., & Wang, W. (2022) · Open Medicine · doi:10.1515/med-2022-0583 · Cited by 14

Doxycycline decelerates aging in progeria mice

Wang, M., Zhang, J., Qiu, J., Ma, X., Xu, C., Wu, Q., Xing, S., Chen, X., & Liu, B. (2024) · Aging Cell · doi:10.1111/acel.14188 · Cited by 14

RNA Modifications in Pathogenic Viruses: Existence, Mechanism, and Impacts

Zou, Y., Guo, Z., Ge, X., & Qiu, Y. (2024) · Microorganisms · doi:10.3390/microorganisms12112373 · Cited by 14

Impact of N-acetyltransferase 10 on macrophage activation and inflammation-induced cardiac dysfunction

Xiao, Z., Wei, X., Li, P., Chen, R., Yu, Z., Liang, Y., Su, Y., & Ge, J. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07796-6 · Cited by 13

Revealing the pharmacological effects of Remodelin against osteosarcoma based on network pharmacology, acRIP-seq and experimental validation

Gao, J., Xu, P., Wang, F., Zhang, W., Min, M., Urba, R., & Fan, L. (2024) · Scientific Reports · doi:10.1038/s41598-024-54197-4 · Cited by 13

Epitranscriptome machinery in Trypanosomatids: New players on the table?

Maran, S. R., Pitta, J. L. D. L. P., Vasconcelos, C. R. D. S., McDermott, S. M., Rezende, A. M., & Moretti, N. S. (2021) · Molecular Microbiology · doi:10.1111/mmi.14688 · Cited by 13

RNA cytidine acetyltransferase NAT10 maintains T cell pathogenicity in inflammatory bowel disease

Li, H., Cai, X., Xu, C., Song, X., Song, X., Kong, Y., Yang, M., Wu, Q., Zheng, S. G., Shao, Y., et al. (2025) · Cell Discovery · doi:10.1038/s41421-025-00781-5 · Cited by 12

NAT10 promotes cancer metastasis by modulating p300/CBP activity through chromatin-associated tRNA

Amin, R., Ha, N., Qiu, T., Holewinski, R. J., Lam, K. C., Lopès, A., Liu, H., Tran, A. D., Lee, M. P., Andrésson, Þ., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.11.010 · Cited by 12

NAT10 mediates TLR2 to promote podocyte senescence in adriamycin-induced nephropathy

Hu, M., Lv, L., Lei, Y., Chen, M., Zhou, S., & Liu, Z. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07515-1 · Cited by 12

Understanding Vascular Diseases: Lessons From Premature Aging Syndromes

Ikeda, Y., Kumagai, H., Motozawa, Y., Suzuki, J.-I., Akazawa, H., & Komuro, I. (2015) · Canadian Journal of Cardiology · doi:10.1016/j.cjca.2015.12.003 · Cited by 12

The multivalent G-quadruplex (G4)-ligands MultiTASQs allow for versatile click chemistry-based investigations

Sperti, F. R., Mitteaux, J., Zell, J., Pipier, A., Valverde, I. E., & Monchaud, D. (2023) · RSC Chemical Biology · doi:10.1039/d3cb00009e · Cited by 12

Hutchinson–Gilford progeria syndrome: unraveling the genetic basis, symptoms, and advancements in therapeutic approaches

Arun, A., Nath, A. R., Thankachan, B., & Unnikrishnan, M. K. (2024) · Therapeutic Advances in Rare Disease · doi:10.1177/26330040241305144 · Cited by 12

NAT10 drives endometriosis progression through acetylation and stabilization of TGFB1 mRNA

Liu, N., YangOu, J., Wei, C., Li, G., Yu, R., Lin, Y., & Hong, X. (2024) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2024.112447 · Cited by 11

Nuclear translocation of the LINE-1 encoded ORF1 protein alters nuclear envelope integrity in human neurons

Znaidi, R., Massiani-Beaudoin, O., Mailly, P., Monnet, H., Bonnifet, T., The Brainbank Neuro-CEB Neuropathology Network, Joshi, R. L., & Fuchs, J. (2025) · Brain Research · doi:10.1016/j.brainres.2025.149579 · Cited by 14

NAT10 exacerbates acute renal inflammation by enhancing N4-acetylcytidine modification of the CCL2/CXCL1 axis

Wang, J.-N., Suo, X.-G., Yu, J.-T., Luo, Q.-C., Ji, M.-L., Zhang, M., Zhu, Q., Cheng, X.-R., Hou, C., Chen, X., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2418409122 · Cited by 11

Competitive binding between DDX21 and SIRT7 enhances NAT10-mediated ac4C modification to promote colorectal cancer metastasis and angiogenesis– DDX21 promotes colorectal cancer metastasis

Song, A., Liu, B., Li, W., Chen, B., Gui, P., Zhang, H., Zhu, C., Xu, Y., Jiang, T., & Song, J. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07656-3 · Cited by 11

Structure of the NAT10 acetyltransferase and mechanism of tRNA acetylation

Zhou, M., Gamage, S. T., Tran, K. A., Bartee, D., Wei, X., Yin, B., Berger, S. L., Meier, J. L., & Marmorstein, R. (2026) · Nature Communications · doi:10.1038/s41467-026-74222-6 · Cited by 11

Evolution and diversification of the nuclear envelope

Padilla-Mejía, N. E., Makarov, A. A., Barlow, L. D., Butterfield, E. R., & Field, M. C. (2021) · Nucleus · doi:10.1080/19491034.2021.1874135 · Cited by 12

An in vivo screen identifies NAT10 as a master regulator of brain metastasis

Chen, J. F.-Y., Xu, P., Cai, W. L., Chen, H., Wingrove, E., Shi, X., Li, W., Biancon, G., Zhang, M., Balabaki, A., et al. (2025) · Science Advances · doi:10.1126/sciadv.ads6021 · Cited by 10

iDHU-Ensem: Identification of dihydrouridine sites through ensemble learning models

Suleman, M. T., Alturise, F., Alkhalifah, T., & Khan, Y. D. (2023) · Digital Health · doi:10.1177/20552076231165963 · Cited by 10

Enhanced cell viscosity: A new phenotype associated with lamin A/C alterations

Jebane, C., Varlet, A., Karnat, M., Cedillo, L. M. H., Lecchi, A., Bedu, F., Desgrouas, C., Vigouroux, C., Vantyghem, M., Viallat, A., et al. (2023) · iScience · doi:10.1016/j.isci.2023.107714 · Cited by 11

Target inhibition of NAT10-mediated ac4C modification prevents seizure behavior in mice

Zhang, A., Yang, J., Wang, M., Li, Y., Hu, T., Xie, J., Xu, Y., & Cao, W. (2025) · Neuropharmacology · doi:10.1016/j.neuropharm.2025.110415 · Cited by 9

N4-acetylcytidine coordinates with NP1 and CPSF5 to facilitate alternative RNA processing during the replication of minute virus of canines

Zhang, X., Qin, S., Huang, F., Liu, H., Wang, J., Chen, Z., Hao, H., Ding, S., Liu, L., Yu, B., et al. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf229 · Cited by 9

Temperature-responsive N-acetylcytidine mRNA modification controls thermosensory flowering in Arabidopsis

Wu, X., Zhang, S., Su, T., Zhang, Y., Wong, C. E., Shen, L., & Yu, H. Q. (2025) · Developmental Cell · doi:10.1016/j.devcel.2025.07.003 · Cited by 9

NAT10 triggers colorectal cancer progression via promoting PPAN-regulated DNA damage repair

Wang, H., Ge, L., Li, J., Zhong, K., Li, S., Ma, N., Tao, L., Zhou, J., Wang, Z., Chang, X., et al. (2025) · Oncogene · doi:10.1038/s41388-025-03661-0 · Cited by 9

SDR enzymes oxidize specific lipidic alkynylcarbinols into cytotoxic protein-reactive species

Demange, P., Joly, E., Marcoux, J., Zanon, P. R. A., Listunov, D., Rullière, P., Barthes, C., Noirot, C., Izquierdo, J.-B., Rozié, A., et al. (2022) · eLife · doi:10.7554/elife.73913 · Cited by 9

Oligonucleotide synthesis under mild deprotection conditions

Chillar, K., Eriyagama, A., Yin, Y., Shahsavari, S., Halami, B., Apostle, A. T., & Fang, S. (2023) · New Journal of Chemistry · doi:10.1039/d2nj03845e · Cited by 9

Recent advances in understanding the role of lamins in health and disease

Reddy, S., & Comai, L. (2016) · F1000Research · doi:10.12688/f1000research.9260.1 · Cited by 9

Nuclear import pathway key to rescuing dominant progerin phenotypes

Wilson, K. L. (2018) · Science Signaling · doi:10.1126/scisignal.aat9448 · Cited by 8

Visualizing RNA Cytidine Acetyltransferase Activity by Northern Blotting

Bryson, K. M., Gamage, S. T., & Meier, J. L. (2020) · Current Protocols in Chemical Biology · doi:10.1002/cpch.89 · Cited by 8

NAT10 and DDX21 Proteins Interact with RNase H1 and Affect the Performance of Phosphorothioate Oligonucleotides

Zhang, L., Bernardo, K. D., Vickers, T. A., Tian, J., Liang, X., & Crooke, S. T. (2022) · Nucleic Acid Therapeutics · doi:10.1089/nat.2021.0107 · Cited by 8

Decreased expression of NAT10 in peripheral blood mononuclear cells from new-onset ankylosing spondylitis and its clinical significance

Luo, Q., Zhu, J., Wang, S., Fu, P., Fu, B., Huang, Z., & Li, J. (2024) · Arthritis Research & Therapy · doi:10.1186/s13075-023-03250-0 · Cited by 8

Mechanical Remodeling of Nuclear Biomolecular Condensates

Soggia, G., ElMaghloob, Y., Boromangnaeva, A.-K., & Jord, A. A. (2024) · Physiology · doi:10.1152/physiol.00027.2024 · Cited by 8

Nucleoskeleton dynamics and functions in health and disease

Schirmer, E. C., Meinke, P., Makarov, A. A., Thanh, P. L., & Sadurska, D. (2015) · Cell Health and Cytoskeleton · doi:10.2147/chc.s53821 · Cited by 8

Iron-dependent lysosomal dysfunction mediated by a natural product hybrid

Mariani, A., Mai, T. T., Zacharioudakis, E., Hienzsch, A., Bartoli, A., Cañeque, T., & Rodriguez, R. (2015) · Chemical Communications · doi:10.1039/c5cc09255h · Cited by 8

Cellular and Animal Models of Striated Muscle Laminopathies

Nicolas, H. A., Akimenko, M., & Tesson, F. (2019) · Cells · doi:10.3390/cells8040291 · Cited by 8

Alkyne‐Tagged Analogue of Jaspine B: New Tool for Identifying Jaspine B Mode of Action

Rozié, A., Santos, C., Fabing, I., Calsou, P., Britton, S., Génisson, Y., & Ballereau, S. (2018) · ChemBioChem · doi:10.1002/cbic.201800496 · Cited by 8

Nucleus–cytoplasm cross‐talk in the aging brain

Benvegnù, S. (2019) · Journal of Neuroscience Research · doi:10.1002/jnr.24446 · Cited by 7

Micropillar-based phenotypic screening platform uncovers involvement of HDAC2 in nuclear deformability

Martewicz, S., Zhu, X., Qu, S., Cui, M., Grespan, E., Luni, C., Jiang, B., Yang, G., & Elvassore, N. (2022) · Biomaterials · doi:10.1016/j.biomaterials.2022.121564 · Cited by 8

Mechanistic study of N-acetyltransferase 10 deficiency enhancing olaparib sensitivity in triple negative breast cancer by inhibiting RAD51 N4-acetylcytidine modification

Li, H., Wu, H., Li, S., Wang, Q., Li, G., Ma, X., Gong, Y., Chu, Y., Jin, S., Chen, X., et al. (2025) · iScience · doi:10.1016/j.isci.2025.112860 · Cited by 6

Nat10 maintains the homeostasis of pluripotent and 2-cell-like states in mouse embryonic stem cells through mRNA cytidine acetylation

Feng, G., Yin, G., Liu, Y., Liu, C., Li, J., Lu, J., Yu, Y., Jin, Z., Wu, Y., Yue, Y., et al. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf504 · Cited by 6

Nanoplastic-induced NAT10/ac4C axis drives both oxidative stress and chemoresistance

Fu, H., Sun, J., Shao, Z., Wang, C.-Y., Bai, L., Zhu, G., Jiang, Z., & Zhang, W. (2025) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2025.140193 · Cited by 6

NAT10 and ac4C modification in cancer immunity and metabolism: emerging mechanisms and therapeutic potential

Yang, Y., Chen, C., Feng, Y., & Lv, Q. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-026-07788-w · Cited by 6

Chemical Probe for Imaging of Polo-like Kinase 4 and Centrioles

Salim, A., Werther, P., Hatzopoulos, G. N., Reymond, L., Wombacher, R., Gönczy, P., & Johnsson, K. (2023) · JACS Au · doi:10.1021/jacsau.3c00271 · Cited by 6

Mitotic deacetylase complex (MiDAC) recognizes the HIV-1 core promoter to control activated viral gene expression

Wilhelm, E., Poirier, M., Rocha, M. D., Bédard, M., McDonald, P. P., Lavigne, P., Hunter, C. L., & Bell, B. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1011821 · Cited by 6

A Flow Cytometry-Based Phenotypic Screen To Identify Novel Endocytic Factors inSaccharomyces cerevisiae

Wrasman, K., Alioto, S. L., Zhang, Y., Hoban, K., Khairy, M., Goode, B. L., & Wendland, B. (2018) · G3 Genes Genomes Genetics · doi:10.1534/g3.118.200102 · Cited by 6

RNA Modification That Breaks the Heart: RNA Acetylase Nat10 Promotes Fibrosis

Kurian, L., & Brandes, R. P. (2023) · Circulation Research · doi:10.1161/circresaha.123.323866 · Cited by 6

The responsive nucleus: morphological signatures of cellular state

Pérez‐Venteo, A., Bosch‐Calvet, M., Garcia‐Cajide, M., & Mauvezin, C. (2026) · Nucleus · doi:10.1080/19491034.2026.2630145 · Cited by 5

The NAT10/ac4C axis: a central nexus linking RNA acetylation to immunometabolic signaling in disease

Shang, C., Wang, X., Huang, Y., Zhu, J., Liu, X. W., Zhang, H., Guan, W., Hao, H., & Zhang, F. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-02768-5 · Cited by 5

NAT10 maintains stem cell homeostasis by mitigating mRNA decay through an ac4C-independent mechanism

Li, W., Huo, Y., Zhang, Z., Liu, Y., Qian, X., Ouyang, J., Gu, R., Han, C., Li, S., Su, R., et al. (2026) · Nature Cell Biology · doi:10.1038/s41556-026-01949-1 · Cited by 5

N-acetyltransferase 10 Promotes Cervical Cancer Progression Via N4-acetylation of SLC7A5 mRNA

Liang, P., Zhou, D., Liao, J., Lai, W., Sheng, X., & Wang, Y. (2025) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl26756 · Cited by 5

Nuclear deformability increases PARPi sensitivity in BRCA1-deficient cells by increasing microtubule-dependent DNA break mobility

Faustini, E., Stritto, A. D., Panza, A., Doksani, Y., & Lottersberger, F. (2025) · Nature Communications · doi:10.1038/s41467-025-60756-8 · Cited by 6

Establishment of a high-content imaging assay for tau aggregation in hiPSC-derived neurons differentiated from two protocols to routinely evaluate compounds and genetic perturbations

Bahnassawy, L., Nicolaisen, N., Untucht, C., Mielich‐Süss, B., Reinhardt, L., Ried, J. S., Morawe, M. P., Geist, D., Finck, A., Käfer, E., et al. (2023) · SLAS DISCOVERY · doi:10.1016/j.slasd.2023.12.009 · Cited by 5

Progeria‐based vascular model identifies networks associated with cardiovascular aging and disease

Ngubo, M., Chen, Z., McDonald, D., Karimpour, R., Shrestha, A., Yockell‐Lelièvre, J., Laurent, A., Besong, O. T. O., Tsai, E. C., Dilworth, F. J., et al. (2024) · Aging Cell · doi:10.1111/acel.14150 · Cited by 6

The N-acetyltransferase 10 inhibitor [11C]remodelin: synthesis and preliminary positron emission tomography study in mice

Luo, R., Zhang, Y., Kumata, K., Xie, L., Kurihara, Y., Ogawa, M., Kokufuta, T., Nengaki, N., Wang, F., & Zhang, M.-R. (2025) · EJNMMI Radiopharmacy and Chemistry · doi:10.1186/s41181-025-00330-1 · Cited by 5

Functional roles and mechanisms of NAT10-mediated RNA ac4C modification in normal development and cancer progression

Xiong, J., Yuan, Y., Li, C., Zhou, Q., Jiang, L., Jiang, X., & Lin, Y. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1795359 · Cited by 4

NAT10 promotes cisplatin resistance and immune escape by increasing the expression of DUSP1 and PD-L1 in gastric cancer

Qian, L., Gao, W., Wang, X., Cui, S., Han, X., Xu, X., Jia, J., & Liu, Z. (2026) · Cell Death Discovery · doi:10.1038/s41420-026-03107-w · Cited by 4

NAT10-mediated N4-acetylcytidine (ac4C) modification of PIK3R2 mRNA promotes malignant progression of glioblastoma

Meng, X., Dong, T., Xu, J., Tian, K., Yang, W., Liu, Z., Qian, Y., Liu, D., Chen, C., Bai, J., et al. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-08328-y · Cited by 4

Targeting the NAT10-HDAC4 positive feedback loop counteracts immunosuppression in breast cancer

Ma, X., Jin, S., Zhang, X., Zhao, L., Wang, H., Liu, S., Li, H., Wang, Q., Gao, S., Wang, J., et al. (2026) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-025-03638-7 · Cited by 4

NAT10-mediated ac4C modifications regulate glioblastoma progression

Lin, L., Yp, X., Guo, Y., Tu, Z., Luo, P., Fang, Z., Zhang, L., Huang, K., & Wu, L. (2026) · Cell Death and Disease · doi:10.1038/s41419-025-08315-3 · Cited by 4

NAT10 promotes the activation of hepatic stellate cells by modulating the TGF-β1-ac4C-COL1A1 axis

Zhang, A., Zhang, Y., Guan, F., Shi, J., Abudula, N., Shao, X., Qi, Q., Liu, W., Xia, T., & Shi, C. (2026) · Hepatology International · doi:10.1007/s12072-025-10998-x · Cited by 4

NAT10-dependent N4-acetylcytidine reprograms R-loops and promotes cancer stem cell growth

Wu, X., Wang, D., Taori, S., Wu, W., Dixit, D., Lv, D., Mullett, S. J., Gelhaus, S. L., Yuan, F., Zhang, P., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.117408 · Cited by 4

NAT10 is critical to block RNA sensing-induced IFN-β transactivation in viral infection

Park, Y., Liu, Y., He, J., Eleya, S., Wu, Z., Fiches, G. N., Zhou, D., Watters, E. G., He, Z., Shanaka, K. A. S. N., et al. (2026) · mBio · doi:10.1128/mbio.01452-26 · Cited by 4

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

Larrieu, D., Rodriguez, R., & Britton, S. (2014) · médecine/sciences · doi:10.1051/medsci/20143008010 · Cited by 2

Everolimus rescues multiple cellular defects in laminopathy-patient fibroblasts

DuBose, A. J., Lichtenstein, S. T., Petrash, N. M., Erdos, M. R., Gordon, L. B., & Collins, F. S. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1802811115 · Cited by 59

Cellular Basis of Laminopathies

Cao, K. (2012) · Wiley eBooks · doi:10.1002/9780470015902.a0022533 · Cited by 1

The curious case of the ageing cells

Gruenbaum, Y. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2666 · Cited by 1

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

Ferreira, C. M. D. A. (2025) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)