The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
A SIRT2-Selective Inhibitor Promotes c-Myc Oncoprotein Degradation and Exhibits Broad Anticancer Activity
Open accessAbstract
Summary Targeting sirtuins for cancer treatment has been a topic of debate due to conflicting reports and lack of potent and specific inhibitors. We have developed a thiomyristoyl lysine compound, TM, as a potent SIRT2-specific inhibitor with broad anticancer effect in various human cancer cells and mouse models of breast cancer. Mechanistically, SIRT2 inhibition promotes c-Myc ubiquitination and degradation. The anticancer effect of TM correlates with its ability to decrease c-Myc level. TM had limited effects on non-cancerous cells and tumor-free mice, suggesting that cancer cells have an increased dependency on SIRT2 that can be exploited for therapeutic benefit. Our studies demonstrate that SIRT2-selective inhibitors are promising anticancer agents and may represent a general strategy to target certain c-Myc-driven cancers.
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Cites
The landscape of somatic copy-number alteration across human cancers
Beroukhim, R., Mermel, C. H., Porter, D., Wei, G., Raychaudhuri, S., Donovan, J., Barretina, J., Boehm, J. S., Dobson, J., Urashima, M., et al. (2010) · Nature · doi:10.1038/nature08822 · Cited by 4,017
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
Reflecting on 25 years with MYC
Meyer, N., & Penn, L. Z. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2231 · Cited by 1,575
Sirt5 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-citationThe first identification of lysine malonylation substrates and its regulatory enzyme
Peng, C., Lu, Z., Xie, Z., Cheng, Z., Chen, Y., Tan, M., Luo, H., Zhang, Y., He, W., Yang, K., et al. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.012658 · Cited by 751
SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine
Jiang, H., Khan, S., Wang, Y., Charron, G., He, B., Sebastian, C., Du, J., Kim, R., Ge, E., Mostoslavsky, R., et al. (2013) · Nature · doi:10.1038/nature12038 · Cited by 697
Self-citationFeldman, J. L., Baeza, J., & Denu, J. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.c113.511261 · Cited by 637 · cited 2×
“Recent studies suggested that different sirtuins may have different acyl group specificity (Du et al., 2011; Feldman et al., 2013; Jiang et al., 2013; Zhu et al., 2012), which can be utilized to design inhibitors specific for different sirtuins (He et al.”
RNA G-quadruplexes cause eIF4A-dependent oncogene translation in cancer
Wolfe, A. L., Singh, K., Zhong, Y., Drewe, P., Rajasekhar, V. K., Sanghvi, V. R., Mavrakis, K. J., Jiang, M., Roderick, J. E., Van der Meulen, J., et al. (2014) · Nature · doi:10.1038/nature13485 · Cited by 635
Efficient Demyristoylase Activity of SIRT2 Revealed by Kinetic and Structural Studies
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Cited by
NAD+ metabolism, stemness, the immune response, and cancer
Navas, L. E., & Carnero, A. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00354-w · Cited by 517
He, M., Chiang, H.-H., Luo, H., Zheng, Z., Qiao, Q., Wang, L., Tan, M., Ohkubo, R., Mu, W.-C., Zhao, S., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.01.009 · Cited by 425
SIRT2: Controversy and multiple roles in disease and physiology
Wang, Y., Yang, J., Hong, T., Chen, X., & Cui, L. (2019) · Ageing Research Reviews · doi:10.1016/j.arr.2019.100961 · Cited by 282
Acetylation regulates ribonucleotide reductase activity and cancer cell growth
Chen, G., Luo, Y., Warncke, K., Sun, Y., Yu, D. S., Fu, H., Behera, M., Ramalingam, S. S., Doetsch, P. W., Duong, D. M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11214-9 · Cited by 82
Construction of Thioamide Peptides from Chiral Amino Acids
Liao, Y., Zhang, S., & Jiang, X. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202303625 · Cited by 27
Metadata
- Authors
- Jing, H., Hu, J., He, B., Negrón Abril, Y. L., Stupinski, J., Weiser, K., Carbonaro, M., Chiang, Y.-L., Southard, T., Giannakakou, P., Weiss, R. S., & Lin, H.
- Venue
- Cancer Cell
- Publisher
- Elsevier BV
- Published
- 2016-03
- Volume
- 29
- Issue
- 3
- Pages
- 297-310
- ISSN
- 1535-6108 (ISSN-L)
- OpenAlex
- W4250618045
- Cited by
- 229
- References
- 9
- FWCI
- 9.92
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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