The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine
Open accessAbstract
The Sir2 family of enzymes or sirtuins are known as nicotinamide adenine dinucleotide (NAD)-dependent deacetylases and have been implicated in the regulation of transcription, genome stability, metabolism and lifespan. However, four of the seven mammalian sirtuins have very weak deacetylase activity in vitro. Here we show that human SIRT6 efficiently removes long-chain fatty acyl groups, such as myristoyl, from lysine residues. The crystal structure of SIRT6 reveals a large hydrophobic pocket that can accommodate long-chain fatty acyl groups. We demonstrate further that SIRT6 promotes the secretion of tumour necrosis factor-α (TNF-α) by removing the fatty acyl modification on K19 and K20 of TNF-α. Protein lysine fatty acylation has been known to occur in mammalian cells, but the function and regulatory mechanisms of this modification were unknown. Our data indicate that protein lysine fatty acylation is a novel mechanism that regulates protein secretion. The discovery of SIRT6 as an enzyme that controls protein lysine fatty acylation provides new opportunities to investigate the physiological function of a protein post-translational modification that has been little studied until now.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Additionally, some members of the sirtuin family mediate non-acetyl lysine acylations (for example, succinylation, malonylation and fatty acid acylation)13–15, the cellular functions of which are so far poorly understood16.”
From NAD+ metabolism and its roles in cellular processes during ageing (2021) · cites this paper as [14]
In the citing paper
“Several NAD+-dependent deacetylase, SIRT1, SIRT2, SIRT3 and SIRT6, have been previously reported to possess lysine defatty-acylation activities.15-17”
From HDAC8 catalyzes the hydrolysis of long chain fatty acyl lysine (2016) · cites this paper as [15]
In the citing paper
“The majority of these fatty-acylated proteins have been reported to have N-glycine myristoylation or S-palmitoylation, while only a few proteins are reported to have lysine fatty acylation.15,34”
From HDAC8 catalyzes the hydrolysis of long chain fatty acyl lysine (2016) · cites this paper as [15]
In the citing paper
“and SIRT1, 2, 3 and SIRT6 are capable of hydrolyzing long chain fatty acyl groups from lysine residues.15-17”
From HDAC8 catalyzes the hydrolysis of long chain fatty acyl lysine (2016) · cites this paper as [15]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
The CCP4 suite: programs for protein crystallography
Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317
The TNF and TNF Receptor Superfamilies
Locksley, R. M., Killeen, N., & Lenardo, M. J. (2001) · Cell · doi:10.1016/s0092-8674(01)00237-9 · Cited by 3,650
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510
Sirtuins in mammals: insights into their biological function
Michán, S., & Sinclair, D. A. (2007) · Biochemical Journal · doi:10.1042/bj20070140 · Cited by 1,750
Genomic Instability and Aging-like Phenotype in the Absence of Mammalian SIRT6
Mostoslavsky, R., Chua, K. F., Lombard, D. B., Pang, W. W., Fischer, M. R., Gellon, L., Liu, P., Mostoslavsky, G., Franco, S., Murphy, M. M., et al. (2006) · Cell · doi:10.1016/j.cell.2005.11.044 · Cited by 1,637
Self-citationSirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase
Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., Kim, J., Woo, J., Kim, J. H., Choi, B. H., et al. (2011) · Science · doi:10.1126/science.1207861 · Cited by 1,429
Self-citationPhylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
Frye, R. A. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3000 · Cited by 1,409
SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin
Michishita, E., McCord, R. A., Berber, E., Kioi, M., Padilla-Nash, H., Damian, M., Cheung, P., Kusumoto, R., Kawahara, T. L. A., Barrett, J. C., et al. (2008) · Nature · doi:10.1038/nature06736 · Cited by 1,111
The sirtuin SIRT6 regulates lifespan in male mice
Kanfi, Y., Naiman, S., Amir, G., Peshti, V., Zinman, G., Nahum, L., Bar-Joseph, Z., & Cohen, H. Y. (2012) · Nature · doi:10.1038/nature10815 · Cited by 1,059
Cited by
Sorted by citations
Items 501–600 of 717
The effects of STAT3 acetylation on the transcriptional activity and tumorigenesis
Yan, H., Tang, L., Zhu, Y., & Zhang, Y. (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.117076 · Cited by 9
Activation of SIRT6 Deacetylation by DNA Strand Breaks
Kang, W., Hamza, A., Curry, A. M., Korade, E., Donu, D., & Cen, Y. (2023) · ACS Omega · doi:10.1021/acsomega.3c04859 · Cited by 9
Xu, Y., Ding, K., & Peng, T. (2024) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2024.100730 · Cited by 9
β-Cell-specific ablation of sirtuin 4 does not affect nutrient-stimulated insulin secretion in mice
Huynh, F. K., Peterson, B. S., Anderson, K. A., Lin, Z., Coakley, A. J., Llaguno, F. M. S., Nguyen, T.-T. N., Campbell, J. E., Stephens, S. B., Newgard, C. B., et al. (2020) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00170.2020 · Cited by 9
Hendler‐Neumark, A., Akiva, E., Sandhu, M., Goldberg, D. T., Arbely, E., Jackson, C. J., & Aharoni, A. (2020) · Molecular Biology and Evolution · doi:10.1093/molbev/msaa244 · Cited by 10
Mammalian Sirtuins and Their Relevance in Vascular Calcification
Pan, X., Pi, C., Ruan, X., Zheng, H., Zhang, D., & Liu, X. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.907835 · Cited by 9
Sociali, G., Liessi, N., Grozio, A., Caffa, I., Parenti, M. D., Ravera, S., Tasso, B., Benzi, A., Nencioni, A., Río, A. D., et al. (2019) · Molecular Diversity · doi:10.1007/s11030-019-09971-2 · Cited by 9
Reply to: Binding site for MDL-801 on SIRT6
Huang, Z., Zhao, J., Deng, W., Chen, Y., Shang, J., Song, K., Zhang, L., Wang, C., Lu, S., Yang, X., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00750-5 · Cited by 9
Self-citationDNA stimulates the deacetylase SIRT6 to mono-ADP-ribosylate proteins with histidine repeats
Pederson, N. J., & Diehl, K. L. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108532 · Cited by 8
Zhao, H., & Wu, W. (2025) · Antioxidants · doi:10.3390/antiox14101228 · Cited by 8
Yuan, T., Keijer, J., Guo, A. H., Lombard, D. B., & de Boer, V. C. J. (2020) · Scientific Reports · doi:10.1038/s41598-020-72833-7 · Cited by 9
Sirtuins—Novel Regulators of Epigenetic Alterations in Airway Inflammation
Wu, S., & Liu, H. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.862577 · Cited by 8
Small‐Molecule Modulation of Protein Lipidation: From Chemical Probes to Therapeutics
Wang, Z., Ying, J., Zhang, X., Chen, M., Xiao, Y., Zou, J., & Chen, B. (2023) · ChemBioChem · doi:10.1002/cbic.202300071 · Cited by 8
Hong, J., Raza, S. H. A., Ma, H., Cao, W., Chong, Y., Wu, J., Xi, D., & Deng, W. (2023) · Genomics · doi:10.1016/j.ygeno.2023.110773 · Cited by 8
SIRT6 promotes angiogenesis by enhancing VEGFA secretion via demyristoylation in endothelial cell
Feng, R., Chen, S., Duan, S., Guo, Z., Wu, N., Hong, H., Fang, Z., Wang, L., Du, Y., Wu, L., et al. (2025) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2024.12.006 · Cited by 8
Fu, W., Xiao, Z., Chen, Y., Pei, J., Sun, Y., Zhang, Z., Wu, H., Pei, Y., Wei, S., Wang, Y., et al. (2023) · Biochimie · doi:10.1016/j.biochi.2023.03.002 · Cited by 8
Self-citationSirtuins Function as the Modulators in Aging-related Diseases in Common or Respectively
Wang, Q., & Guo, S. (2015) · Chinese Medical Journal · doi:10.4103/0366-6999.158375 · Cited by 10
Ibrahim, M. A. A., Abdeljawaad, K. A. A., Abdelrahman, A. H. M., Arzumanyan, G., Mekhemer, G. A. H., Abdelbacki, A. M. M., Sidhom, P. A., Sayed, S. R. M., & Hegazy, M. F. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.151701 · Cited by 7
AtSRT1 regulates flowering by regulating flowering integrators and energy signals in Arabidopsis
Wang, P., Su, L., Cao, L., Hu, H., Wan, H., Wu, C., Zheng, Y., Bao, C., & Liu, X. (2024) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2024.108841 · Cited by 7
Bheda, P., & Wolberger, C. (2013) · Nature · doi:10.1038/496041a · Cited by 7
SIRT6 mediates multidimensional modulation to maintain organism homeostasis
Yang, Y., Zhu, M. L., Liang, J., Wang, H., Sun, D., Li, H., & Chen, L. (2022) · Journal of Cellular Physiology · doi:10.1002/jcp.30791 · Cited by 7
Kalbas, D., Meleshin, M., Liebscher, S., Zessin, M., Melesina, J., Schiene‐Fischer, C., Bülbül, E. F., Bordusa, F., Sippl, W., & Schutkowski, M. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00211 · Cited by 7
Sirtuin 6 Is a Critical Epigenetic Regulator of Cancer
Raghu, S., Prabhashankar, A. B., Shivanaiah, B., Tripathi, E., & Sundaresan, N. R. (2022) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-07634-3_10 · Cited by 7
C. eleganssirtuin SIR-2.4 and its mammalian homolog SIRT6 in stress response
Jedrusik, M. A. (2014) · Worm · doi:10.4161/worm.29102 · Cited by 7
Structure-Based Design and Computational Studies of Sirtuin Inhibitors
Karaman, B., Jung, M., & Sippl, W. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802808-7.00011-3 · Cited by 7
Browning of Adipose Tissue and Sirtuin Involvement
Favero, G., Krajčíková, K., Bonomini, F., Rodella, L. F., Tomečková, V., & Rezzani, R. (2018) · InTech eBooks · doi:10.5772/intechopen.74760 · Cited by 7
A one-step specific assay for continuous detection of sirtuin 2 activity
Dai, Q., Zheng, Z., Xia, F., Liu, P., & Li, M. (2019) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2019.05.007 · Cited by 7
Sukuroglu, M. K., Gozelle, M., Özkan, Y., & Eren, G. (2021) · Medicinal Chemistry Research · doi:10.1007/s00044-021-02782-x · Cited by 7
Role of sirtuins in cardiovascular diseases
Ravi, V., Mishra, S., & Sundaresan, N. R. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-814118-2.00021-5 · Cited by 7
Wang, W., Liang, J., Zhang, Y., Wang, J., Miao, X., Chang, Y., & Chen, Y. (2025) · Science Signaling · doi:10.1126/scisignal.adl6441 · Cited by 6
Kim, Y. S., Lim, H., Cho, Y. E., & Hwang, S. (2025) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2024.251 · Cited by 6
Translocation of SIRT6 promotes glycolysis reprogramming to exacerbate diabetic angiopathy
Pang, K., Huang, J., Zhang, S., Guan, Y., Zou, N., Kang, J., Du, H., Zhao, D., Валерьевич, А. Д., Chen, H., et al. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103736 · Cited by 7
Jos, S., Aouti, S., Unni, S., Haridass, V., Gogoi, H., Deshmukh, P. H., Padmanabhan, B., & Padavattan, S. (2021) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2021.1938229 · Cited by 6
Deciphering the Allosteric Activation Mechanism of SIRT6 Using Molecular Dynamics Simulations
Zhao, Z., Du, J., Du, Y., Gao, Y., Yu, M., Zhang, Y., Fang, H., & Hou, X. (2023) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.3c00227 · Cited by 6
Self-citationEffect of quercetin on the protein-substrate interactions in SIRT6: Insight from MD simulations
Zhang, H., Zhang, J., & Zhang, H. (2024) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2024.108778 · Cited by 6
Fröhlich, J., Liorni, N., Mangoni, M., Lochmanová, G., Pírek, P., Kaštánková, N., Pata, P., Kucera, J., Chaldakov, G. N., Tonchev, A. B., et al. (2024) · Clinical Epigenetics · doi:10.1186/s13148-024-01710-1 · Cited by 6
Liang, C., Wang, S., Feng, D., Wang, S., Zheng, C., Qu, Y., Wang, W., Ma, Y., Li, H., Yang, H., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01921 · Cited by 6
Pukhalskaia, A. E., Diatlova, A., Linkova, N. S., & Kvetnoy, I. M. (2022) · Neuroscience and Behavioral Physiology · doi:10.1007/s11055-022-01217-3 · Cited by 6
Chemical Biology Tools for Protein Lysine Acylation
Xie, Y., Du, S., Liu, Z., Liu, M., Xu, Z., Wang, X., Kee, J. X., Yi, F., Sun, H., & Yao, S. Q. (2022) · Angewandte Chemie · doi:10.1002/ange.202200303 · Cited by 6
Creatine kinase brain-type regulates BCAR1 phosphorylation to facilitate DNA damage repair
Yang, B. H., Zhang, W., Sun, L., Lu, B., Yin, C., Zhang, Y., & Jiang, H. (2023) · iScience · doi:10.1016/j.isci.2023.106684 · Cited by 6
Self-citationThe mimics of Nε-acyl-lysine derived from cysteine as sirtuin inhibitors
Wang, C., Wang, F., Chen, X., Zou, Y., Zhu, H., Zhao, Q., Shen, J., Li, Y., Li, Y., & He, B. (2018) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2018.06.030 · Cited by 6
Self-citationNeerukonda, S. N., Katneni, U., Bhandari, N., & Parcells, M. S. (2019) · Avian Diseases · doi:10.1637/aviandiseases-d-19-00117 · Cited by 6
The Enzymatic Activities of Sirtuins
Lin, H. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813499-3.00004-6 · Cited by 6
Self-citationAnalysis of molecular networks and targets mining of Chinese herbal medicines on anti-aging
Jiang, Q.-Y., Zheng, M.-S., Yang, X., & Sun, X.-S. (2016) · BMC Complementary and Alternative Medicine · doi:10.1186/s12906-016-1513-2 · Cited by 6
Histone Acyl Code in Precision Oncology: Mechanistic Insights from Dietary and Metabolic Factors
Neja, S. A., Dashwood, W. M., Dashwood, R. H., & Rajendran, P. (2024) · Nutrients · doi:10.3390/nu16030396 · Cited by 7
Posttranslational Modifications and Death Receptor Signalling
Micheau, O. (2017) · Resistance to targeted anti-cancer therapeutics · doi:10.1007/978-3-319-56805-8_11 · Cited by 6
Binding to medium and long chain fatty acyls is a common property of HEAT and ARM repeat modules
Li, T., Coan, J. P., Krajewski, K., Zhang, L., Elias, J. E., Strahl, B. D., Gozani, O., & Chua, K. F. (2019) · Scientific Reports · doi:10.1038/s41598-019-50817-6 · Cited by 5
Rajabi, N., Hansen, T. N., Nielsen, A. L., Nguyen, H. T., Bæk, M., Bolding, J. E., Bahlke, O. Ø., Petersen, S. E. G., Bartling, C. R. O., Strømgaard, K., et al. (2022) · Angewandte Chemie · doi:10.1002/ange.202115805 · Cited by 5
Catching Sirtuin-2 Intermediates One Structure at the Time
Lee, S., Chen, Z., & Zhang, G. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.03.004 · Cited by 5
Papel pleiotrópico y homeostático de las Sirtuinas en la función biológica humana.
Hernández-Bedolla, M. A., Barajas‐Espinosa, A. R., Ochoa‐Cortés, F., Alonso, D. E. A., Hernández, A. H., Ostoa, Z. B., & Salguero, I. G. D. (2020) · Ciencias Huasteca Boletín Científico de la Escuela Superior de Huejutla · doi:10.29057/esh.v8i16.5721 · Cited by 5
Suppressing SENP1 inhibits esophageal squamous carcinoma cell growth via SIRT6 SUMOylation
Gu, J., Zhang, S., Lin, D., Wang, W., Cheng, J., Zheng, Q., Wang, H., & Tan, L. (2024) · Cellular Oncology · doi:10.1007/s13402-024-00956-4 · Cited by 4
Structural basis of SIRT2 pre-catalysis NAD + binding dynamics and mechanism
Zhang, N., Pow, K. C., Chen, L., & Hao, Q. (2025) · RSC Chemical Biology · doi:10.1039/d5cb00169b · Cited by 4
Self-citationYin, H., Zhang, H., Zheng, S., Guo, R., Wen, J., Liu, M., Li, A., Zhao, M., Yuan, Y., & Gong, Y. (2026) · npj Precision Oncology · doi:10.1038/s41698-026-01355-8 · Cited by 4
Profiling sirtuin activity using Copper-free click chemistry
Curry, A. M., Cohen, I., Zheng, S. G., Wohlfahrt, J., White, D. S., Donu, D., & Cen, Y. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.105413 · Cited by 4
You, W., Montoya, A. L., Dana, S., Franzini, R. M., & Steegborn, C. (2024) · ChemMedChem · doi:10.1002/cmdc.202400273 · Cited by 4
Wang, P., Chen, D., An, J.-X., Lin, S., Liu, T., Li, Y., Chen, L., & He, B. (2022) · Organic & Biomolecular Chemistry · doi:10.1039/d1ob02347k · Cited by 4
Self-citationTargeting cancers and metabolic disorders: The prospects of combining HDAC8 inhibitor and activator
Yusif, M. M. (2022) · European Journal of Medicinal Chemistry Reports · doi:10.1016/j.ejmcr.2022.100097 · Cited by 4
Sirtuin Activation by Small Molecules
Massudi, H., Wu, L. E., & Sinclair, D. A. (2016) · Springer eBooks · doi:10.1007/978-94-024-0962-8_12 · Cited by 4
Zhang, S., Spiegelman, N. A., & Lin, H. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9532-5_11 · Cited by 4
Self-citationRoles for Sirtuins in Cardiovascular Biology
Stein, A., Giblin, W., Guo, A. H., & Lombard, D. B. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813499-3.00012-5 · Cited by 4
Binding to nucleosome poises SIRT6 for histone H3 de-acetylationPreprint
Smirnova, E., Bignon, E., Schultz, P., Pápai, G., & Shem, A. B. (2023) · eLife · doi:10.7554/elife.87989.1 · Cited by 4
Murakami, M., Onizawa, M., Abe, N., Mochimaru, T., Saito, C., Hikichi, R., Uemura, T., Sekimata, M., & Ohira, H. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.150897 · Cited by 3
Sirtuins as mediators and targets of arsenic toxicity: unraveling signaling pathway crosstalk
El-Mahrouk, S. R., & El‐Kadi, A. O. S. (2025) · Archives of Toxicology · doi:10.1007/s00204-025-04158-1 · Cited by 3
Filament formation and NAD processing by noncanonical human FAM118 sirtuins
Baretić, D., Missoury, S., Patel, K., Martinez, M., Coste, F., Zhu, K., Smith, R., Kopasz, A. G., Lu, Y., Bigot, N., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01715-1 · Cited by 3
Matias, É. G. C., Bezerra, K. S., Clemente, W. S., Oliveira, J. I. N., Galvao, D. S., & Fulco, U. L. (2025) · Journal of Molecular Recognition · doi:10.1002/jmr.70016 · Cited by 3
Li, C. S., Jin, H., Meng, R., Baek, S.-W., Kim, S., Chai, O. H., Park, B. H., Lee, N. R., Kim, S. M., & Kim, S. M. (2026) · Cancer Gene Therapy · doi:10.1038/s41417-026-01023-w · Cited by 3
Zhang, W., Wang, J., Yang, L., Shao, Y., Peng, H., Jiang, L., & Sheng, L. (2024) · Journal of Biomedical Research · doi:10.7555/jbr.38.20240172 · Cited by 3
Methods for studying human sirtuins with activity-based chemical probes
Zheng, S. G., Wohlfahrt, J., Cohen, I., & Cen, Y. (2019) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2019.11.004 · Cited by 3
Sirtuins in hematopoiesis and blood malignancies
Vázquez, B. N., Fernández-Duran, I., & Vaquero, A. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-814118-2.00020-3 · Cited by 3
A dual-function chemical probe for detecting erasers of lysine lipoylation
Xie, Y., Zhang, J., Yang, L., Chen, Q., Hao, Q., Zhang, L. N., & Sun, H. (2021) · Frontiers of Chemical Science and Engineering · doi:10.1007/s11705-021-2051-0 · Cited by 3
Self-citationYang, Y., Zou, S., Cai, K., Li, N., Li, Z., Tan, W. L., Wei, L., Zhao, G., & Zhao, W. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105339 · Cited by 3
Chemical Proteomic Profiling of Protein Fatty-Acylation in Microbial Pathogens
Peng, T., & Hang, H. C. (2018) · Current topics in microbiology and immunology · doi:10.1007/82_2018_126 · Cited by 3
Self-citationSirtuins in the biology of aging
Wątroba, M., & Szukiewicz, D. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-814118-2.00002-1 · Cited by 3
Role of SIRT7 in hepatic lipid metabolism
Yamagata, K., Karim, M. F., Sato, Y., & Yoshizawa, T. (2015) · Diabetology International · doi:10.1007/s13340-015-0226-y · Cited by 3
Proteomic Analysis of Protein–Lipid Modifications: Significance and Application
Suazo, K. F., Schey, G. L., Schaber, C., John, A. R. O., & Distefano, M. D. (2019) · Wiley eBooks · doi:10.1002/9781118970195.ch13 · Cited by 3
Role of SIRT7 in Prostate Cancer Progression: New Insight Into Potential Therapeutic Target
Zhang, J., Liu, C., Luo, W., & Sun, B. (2025) · Cancer Medicine · doi:10.1002/cam4.70786 · Cited by 2
Zhu, Z., Mao, P.-Z., Tarn, C., & Cao, Y. (2025) · Communications Chemistry · doi:10.1038/s42004-025-01826-2 · Cited by 2
SIRT Family: Biological Functions and Therapeutic Targets
Wang, J., Jiang, F., ZHANG, F.-Y., Huang, D., Li, X. G., Gao, S., You, H., Wu, Q., Chen, H., & Gong, T. Q. (2026) · MedComm · doi:10.1002/mco2.70866 · Cited by 2
Use of alkyne-tagged myristic acid to detect N-terminal myristoylation
Xu, Y., & Lin, H. (2023) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2023.02.019 · Cited by 3
Self-citationAcylated peptide enrichment utilizing lysine deacylases for lysine acylomics
Tsumagari, K., & Ishihama, Y. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.05.077 · Cited by 2
Li, S., & Yuan, Z. (2023) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2023030 · Cited by 2
Structural Insights Into centSIRT6: Bioinformatic Analysis of N308K and A313S Substitution Effects
Lagunas‐Rangel, F. A. (2025) · Bioinformatics and Biology Insights · doi:10.1177/11779322251339698 · Cited by 2
Qiu, Y., Pápai, G., Shem, A. B., & Bignon, E. (2025) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5c02221 · Cited by 2
As“SIRT”ing the role of an epigenetic modifier in hematopoietic stem cell homeostasis
Magimaidas, A., Badolia, R., Madireddi, P., & Bhavanasi, D. (2016) · Stem Cell Investigation · doi:10.21037/sci.2016.09.09 · Cited by 2
Protein Lysine Acylation: Abundance, Dynamics and Function
Pougovkina, O., & de Boer, V. C. J. (2016) · Springer eBooks · doi:10.1007/978-94-024-0962-8_3 · Cited by 2
Sirtuin functions in the brain: From physiological to pathological aspects
Shao, J., Zhang, T., Liu, T., Quan, Y., Fan, L., Liu, J., Yang, X. Y., Xie, Q. R., & Xia, W. (2014) · Journal of Shanghai Jiaotong University (Science) · doi:10.1007/s12204-014-1562-y · Cited by 2
The Controversy Around Sirtuins and Their Functions in Aging
Sun, Y., & Dang, W. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-801816-3.00017-0 · Cited by 2
What Stressors Cause Cancer and When?
Hughes, C. L., & Waters, M. D. (2017) · John Wiley & Sons, Inc. eBooks · doi:10.1002/9781119023647.ch1 · Cited by 2
Multitasking Roles of the Mammalian Deacetylase SIRT6
Hassanieh, S., & Mostoslavsky, R. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813499-3.00009-5 · Cited by 2
Self-citationFinding the gas pedal on a slow sirtuin
Nielsen, A. L., & Olsen, C. A. (2020) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)49897-8 · Cited by 2
Sirtuin Inhibitors and Activators
Rahnasto‐Rilla, M., Tyni, J., & Lahtela-Kakkonen, M. K. (2019) · Topics in medicinal chemistry · doi:10.1007/7355_2019_70 · Cited by 2
Dual role of sirtuins in cancer
Torrens‐Mas, M., & Roca, P. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822467-0.00011-5 · Cited by 2
Sirtuins, healthspan, and longevity in mammals
Kumar, S., Giblin, W., & Lombard, D. B. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-815962-0.00005-6 · Cited by 2
Nielsen, A. L., Rajabi, N., Kudo, N., Larsen, K. L., Fontenas, M., Lucidi, A., Madsen, A. S., Yoshida, M., & Olsen, C. A. (2020) · Research at the University of Copenhagen (University of Copenhagen) · doi:10.1101/2020.03.20.000380 · Cited by 2
Binding to nucleosome poises human SIRT6 for histone H3 deacetylationPreprint
Smirnova, E., Bignon, E., Schultz, P., Pápai, G., & Shem, A. B. (2023) · eLife · doi:10.7554/elife.87989.3 · Cited by 2
Gu, J., Lao, L., Chen, Y., & Lin, S. (2024) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2024.118013 · Cited by 1
Sirt6 prevents the age-related decline of H 2 S through the control of one-carbon metabolism
Touitou, N., Nahum, L., Feldman-Trabelsi, S., Avivi, M. Y., Aon, M. A., Naiman, S., Rathaus, M., Gertler, A. A., Roichman, A., Dvir, L. B., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2514084122 · Cited by 1
Liu, J., Wang, Y., Su, S., Liu, R., Wang, J., Xie, S., Yin, C., & Zhang, E. (2026) · Toxicology · doi:10.1016/j.tox.2026.154404 · Cited by 1
Self-citationContext-informed subgraph foundation models enable interpretable protein-function prediction
Zhou, Z., Rao, J., Zhang, Z., Ma, R., Yang, J., & Zheng, S. (2026) · Cell Systems · doi:10.1016/j.cels.2026.101535 · Cited by 1
Liu, W., Chen, Z., Huang, Z., & Chen, L. (2026) · Journal of Advanced Research · doi:10.1016/j.jare.2026.06.010 · Cited by 1
Metadata
- Authors
- Jiang, H., Khan, S., Wang, Y., Charron, G., He, B., Sebastian, C., Du, J., Kim, R., Ge, E., Mostoslavsky, R., Hang, H. C., Hao, Q., & Lin, H.
- Affiliations
- Cornell University (US)
- University of Hong Kong (HK)
- Rockefeller University (US)
- Corresponding author
- Hao, Quan
- Lin, Hening
- ORCID
- Venue
- Nature
- Published
- 2013-04
- Volume
- 496
- Issue
- 7443
- Pages
- 110-113
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3635073
- OpenAlex
- W1972924731
- Cited by
- 697
- References
- 29
- Citations by year
- 2026: 29 · 2025: 36 · 2024: 43 · 2023: 44 · 2022: 60 · 2021: 54 · 2020: 58 · 2019: 49 · 2018: 56 · 2017: 61 · 2016: 72 · 2015: 63 · 2014: 47 · 2013: 24
- FWCI
- 32.88
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- The HKU Scholars Hub (University of Hong Kong) (submittedVersion)
- Funders
- National Cancer Institute (R01CA175727)
- National Institute of General Medical Sciences (R01GM093072, R01GM086703, R01GM087544)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK088190)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Keywords
- SIRT6, sirtuins, TNF-alpha secretion, myristoylation, protein secretion regulation, post-translational modification, NAD+-dependent deacetylase, crystal structure
- MeSH terms
- Acylation, Binding Sites, Fatty Acids, Humans, Hydrolysis, Lysine, Protein Processing, Post-Translational, Tumor Necrosis Factor-alpha, Crystallography, X-Ray, Sirtuins, Hydrophobic and Hydrophilic Interactions
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
