Metabolic Regulation by Lysine Malonylation, Succinylation, and Glutarylation von Hirschey, Matthew D., Zhao, Yingming

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Nonenzymatic Protein Acylation as a Carbon Stress Regulated by Sirtuin Deacylases von Wagner, Gregory R., Hirschey, Matthew D.

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SIRT3 Deficiency and Mitochondrial Protein Hyperacetylation Accelerate the Development of the Metabolic Syndrome von Hirschey, Matthew D., Shimazu, Tadahiro, Jing, Enxuan, Grueter, Carrie A., Collins, Amy M., Aouizerat, Bradley, Stančáková, Alena, Goetzman, Eric, Lam, Maggie M., Schwer, Bjoern, Stevens, Robert D., Muehlbauer, Michael J., Kakar, Sanjay, Bass, Nathan M., Kuusisto, Johanna, Laakso, Markku, Alt, Frederick W., Newgard, Christopher B., Farese, Robert V., Kahn, C. Ronald, Verdin, Eric

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Lipids Reprogram Metabolism to Become a Major Carbon Source for Histone Acetylation von McDonnell, Eoin, Crown, Scott B., Fox, Douglas B., Kitir, Betül, Ilkayeva, Olga R., Olsen, Christian A., Grimsrud, Paul A., Hirschey, Matthew D.

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Role of NAD+ and mitochondrial sirtuins in cardiac and renal diseases von Hershberger, Kathleen A., Martin, Angelical S., Hirschey, Matthew D.

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Lysine Glutarylation Is a Protein Posttranslational Modification Regulated by SIRT5 von Tan, Minjia, Peng, Chao, Anderson, Kristin A., Chhoy, Peter, Xie, Zhongyu, Dai, Lunzhi, Park, Jeongsoon, Chen, Yue, Huang, He, Zhang, Yi, Ro, Jennifer, Wagner, Gregory R., Green, Michelle F., Madsen, Andreas S., Schmiesing, Jessica, Peterson, Brett S., Xu, Guofeng, Ilkayeva, Olga R., Muehlbauer, Michael J., Braulke, Thomas, Mühlhausen, Chris, Backos, Donald S., Olsen, Christian A., McGuire, Peter J., Pletcher, Scott D., Lombard, David B., Hirschey, Matthew D., Zhao, Yingming

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Dietary Restriction and AMPK Increase Lifespan via Mitochondrial Network and Peroxisome Remodeling von Weir, Heather J., Yao, Pallas, Huynh, Frank K., Escoubas, Caroline C., Goncalves, Renata L., Burkewitz, Kristopher, Laboy, Raymond, Hirschey, Matthew D., Mair, William B.

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Old Enzymes, New Tricks: Sirtuins Are NAD+-Dependent De-acylases von Hirschey, Matthew D.

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Loss of BCAA Catabolism during Carcinogenesis Enhances mTORC1 Activity and Promotes Tumor Development and Progression von Ericksen, Russell E., Lim, Siew Lan, McDonnell, Eoin, Shuen, Wai Ho, Vadiveloo, Maya, White, Phillip J., Ding, Zhaobing, Kwok, Royston, Lee, Philip, Radda, George K., Toh, Han Chong, Hirschey, Matthew D., Han, Weiping

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Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling von Verdin, Eric, Hirschey, Matthew D., Finley, Lydia W.S., Haigis, Marcia C.

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Neuronal CRTC-1 Governs Systemic Mitochondrial Metabolism and Lifespan via a Catecholamine Signal von Burkewitz, Kristopher, Morantte, Ianessa, Weir, Heather J.M., Yeo, Robin, Zhang, Yue, Huynh, Frank K., Ilkayeva, Olga R., Hirschey, Matthew D., Grant, Ana R., Mair, William B.

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A Class of Reactive Acyl-CoA Species Reveals the Non-enzymatic Origins of Protein Acylation von Wagner, Gregory R, Bhatt, Dhaval P, O'Connell, Thomas M, Thompson, J Will, Dubois, Laura G, Backos, Donald S, Yang, Hao, Mitchell, Grant A, Ilkayeva, Olga R, Stevens, Robert D, Grimsrud, Paul A, Hirschey, Matthew D

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Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production von Jing, Enxuan, Emanuelli, Brice, Hirschey, Matthew D., Boucher, Jeremie, Lee, Kevin Y., Lombard, David, Verdin, Eric M., Kahn, C. Ronald

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Whole-organism screening for gluconeogenesis identifies activators of fasting metabolism von Gut, Philipp, Baeza-Raja, Bernat, Andersson, Olov, Hasenkamp, Laura, Hsiao, Joseph, Hesselson, Daniel, Akassoglou, Katerina, Verdin, Eric, Hirschey, Matthew D, Stainier, Didier Y R

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SIRT6 Promotes Hepatic Beta-Oxidation via Activation of PPARα von Naiman, Shoshana, Huynh, Frank K., Gil, Reuven, Glick, Yair, Shahar, Yael, Touitou, Noga, Nahum, Liat, Avivi, Matan Y., Roichman, Asael, Kanfi, Yariv, Gertler, Asaf A., Doniger, Tirza, Ilkayeva, Olga R., Abramovich, Ifat, Yaron, Orly, Lerrer, Batia, Gottlieb, Eyal, Harris, Robert A., Gerber, Doron, Hirschey, Matthew D., Cohen, Haim Y.

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Mechanism‐Based Inhibitors of the Human Sirtuin 5 Deacylase: Structure–Activity Relationship, Biostructural, and Kinetic Insight von Rajabi, Nima, Auth, Marina, Troelsen, Kathrin R., Pannek, Martin, Bhatt, Dhaval P., Fontenas, Martin, Hirschey, Matthew D., Steegborn, Clemens, Madsen, Andreas S., Olsen, Christian A.

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Mammalian Sir2 Homolog SIRT3 Regulates Global Mitochondrial Lysine Acetylation von Lombard, David B., Alt, Frederick W., Cheng, Hwei-Ling, Bunkenborg, Jakob, Streeper, Ryan S., Mostoslavsky, Raul, Kim, Jennifer, Yancopoulos, George, Valenzuela, David, Murphy, Andrew, Yang, Yinhua, Chen, Yaohui, Hirschey, Matthew D., Bronson, Roderick T., Haigis, Marcia, Guarente, Leonard P., Farese, Robert V., Weissman, Sherman, Verdin, Eric, Schwer, Bjoern

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Investigating the Sensitivity of NAD+-dependent Sirtuin Deacylation Activities to NADH von Madsen, Andreas S., Andersen, Christian, Daoud, Mohammad, Anderson, Kristin A., Laursen, Jonas S., Chakladar, Saswati, Huynh, Frank K., Colaço, Ana R., Backos, Donald S., Fristrup, Peter, Hirschey, Matthew D., Olsen, Christian A.

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Mitochondrial Acetylome Analysis in a Mouse Model of Alcohol-Induced Liver Injury Utilizing SIRT3 Knockout Mice von Fritz, Kristofer S, Galligan, James J, Hirschey, Matthew D, Verdin, Eric, Petersen, Dennis R

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Ablation of Sirtuin5 in the postnatal mouse heart results in protein succinylation and normal survival in response to chronic pressure overload von Hershberger, Kathleen A., Abraham, Dennis M., Liu, Juan, Locasale, Jason W., Grimsrud, Paul A., Hirschey, Matthew D.

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