Scholars@Duke

• Background
• 

  Education, Training, & Certifications

  • Ph.D., University of North Carolina at Chapel Hill 1994
• Research
• 

  Selected Grants

  • Studies on the Mechanisms by which SIRT5 Regulates Aging and Disease awarded by National Institutes of Health 2014 - 2024
  • Post-Translational and Epigenetic Control of Branched-Chain Amino Acid Metabolism awarded by National Institutes of Health 2018 - 2022
  • Novel SIRT5 Enzymatic Activity Regulates Cellular Mechanisms of Aging and Disease awarded by National Institutes of Health 2014 - 2019
  • SIRT5 Regulates Mitochondrial Metabolism in Aging and Disease awarded by Ellison Medical Foundation 2013 - 2018
  • Novel SIRT4 Enzymatic Activity Influence Cellular Mechanisms of Aging awarded by National Institutes of Health 2016 - 2017
  • Hormonal regulation of a Ca2+/AMPK signaling pathway awarded by National Institutes of Health 1984 - 2011
  • CaM Kinase Cascades in Endocrine Cells awarded by National Institutes of Health 1997 - 2011
  • Activation & Function Of Human Cam Kinase Iv In T-Cell awarded by National Institutes of Health 1995 - 1998
  • Activation And Function Of Human Cam Kinase Iv In T Cells awarded by National Institutes of Health 1995 - 1998
  • Activation And Function Of Human Cam Kinase Iv In T-Cells awarded by National Institutes of Health 1994 - 1998
• Publications & Artistic Works
• 

  Selected Publications

  • Academic Articles

    • Anderson, Kristin A., Andreas S. Madsen, Christian A. Olsen, and Matthew D. Hirschey. “Metabolic control by sirtuins and other enzymes that sense NAD+, NADH, or their ratio..” Biochim Biophys Acta Bioenerg 1858, no. 12 (December 2017): 991–98. https://doi.org/10.1016/j.bbabio.2017.09.005.
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    • Anderson, Kristin A., Frank K. Huynh, Kelsey Fisher-Wellman, J Darren Stuart, Brett S. Peterson, Jonathan D. Douros, Gregory R. Wagner, et al. “SIRT4 Is a Lysine Deacylase that Controls Leucine Metabolism and Insulin Secretion..” Cell Metab 25, no. 4 (April 4, 2017): 838-855.e15. https://doi.org/10.1016/j.cmet.2017.03.003.
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    • Madsen, Andreas S., Christian Andersen, Mohammad Daoud, Kristin A. Anderson, Jonas S. Laursen, Saswati Chakladar, Frank K. Huynh, et al. “Investigating the Sensitivity of NAD+-dependent Sirtuin Deacylation Activities to NADH..” J Biol Chem 291, no. 13 (March 25, 2016): 7128–41. https://doi.org/10.1074/jbc.M115.668699.
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    • Anderson, Kristin A., Michelle F. Green, Frank K. Huynh, Gregory R. Wagner, and Matthew D. Hirschey. “SnapShot: Mammalian Sirtuins..” Cell 159, no. 4 (November 2014): 956-956.e1. https://doi.org/10.1016/j.cell.2014.10.045.
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    • Tan, Minjia, Chao Peng, Kristin A. Anderson, Peter Chhoy, Zhongyu Xie, Lunzhi Dai, Jeongsoon Park, et al. “Lysine glutarylation is a protein posttranslational modification regulated by SIRT5..” Cell Metab 19, no. 4 (April 1, 2014): 605–17. https://doi.org/10.1016/j.cmet.2014.03.014.
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    • Anderson, Kristin A., Dongning Wang, and Matthew D. Hirschey. “HINT2 and fatty liver disease: mitochondrial protein hyperacetylation gives a hint?.” Hepatology 57, no. 5 (May 2013): 1681–83. https://doi.org/10.1002/hep.26085.
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    • Hershberger, Kathleen A., Jonathan Motley, Matthew D. Hirschey, and Kristin A. Anderson. “Generating mammalian sirtuin tools for protein-interaction analysis..” Methods Mol Biol 1077 (2013): 69–78. https://doi.org/10.1007/978-1-62703-637-5_5.
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    • Anderson, Kristin A., Fumin Lin, Thomas J. Ribar, Robert D. Stevens, Michael J. Muehlbauer, Christopher B. Newgard, and Anthony R. Means. “Deletion of CaMKK2 from the liver lowers blood glucose and improves whole-body glucose tolerance in the mouse..” Mol Endocrinol 26, no. 2 (February 2012): 281–91. https://doi.org/10.1210/me.2011-1299.
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    • Anderson, Kristin A., and Matthew D. Hirschey. “Mitochondrial protein acetylation regulates metabolism..” Essays Biochem 52 (2012): 23–35. https://doi.org/10.1042/bse0520023.
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    • Green, Michelle F., Kristin A. Anderson, and Anthony R. Means. “Characterization of the CaMKKβ-AMPK signaling complex..” Cell Signal 23, no. 12 (December 2011): 2005–12. https://doi.org/10.1016/j.cellsig.2011.07.014.
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    • Kokubo, Manabu, Masahiro Nishio, Thomas J. Ribar, Kristin A. Anderson, Anne E. West, and Anthony R. Means. “BDNF-mediated cerebellar granule cell development is impaired in mice null for CaMKK2 or CaMKIV..” J Neurosci 29, no. 28 (July 15, 2009): 8901–13. https://doi.org/10.1523/JNEUROSCI.0040-09.2009.
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    • Anderson, Kristin A., and Anthony R. Means. “Central control of feeding..” F1000 Biol Rep 1 (January 21, 2009). https://doi.org/10.3410/B1-10.
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    • Anderson, Kristin A., Thomas J. Ribar, Fumin Lin, Pamela K. Noeldner, Michelle F. Green, Michael J. Muehlbauer, Lee A. Witters, Bruce E. Kemp, and Anthony R. Means. “Hypothalamic CaMKK2 contributes to the regulation of energy balance..” Cell Metab 7, no. 5 (May 2008): 377–88. https://doi.org/10.1016/j.cmet.2008.02.011.
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    • Hurley, Rebecca L., Laura K. Barré, Sumintra D. Wood, Kristin A. Anderson, Bruce E. Kemp, Anthony R. Means, and Lee A. Witters. “Regulation of AMP-activated protein kinase by multisite phosphorylation in response to agents that elevate cellular cAMP..” J Biol Chem 281, no. 48 (December 1, 2006): 36662–72. https://doi.org/10.1074/jbc.M606676200.
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    • Hurley, Rebecca L., Kristin A. Anderson, Jeanne M. Franzone, Bruce E. Kemp, Anthony R. Means, and Lee A. Witters. “The Ca2+/calmodulin-dependent protein kinase kinases are AMP-activated protein kinase kinases..” J Biol Chem 280, no. 32 (August 12, 2005): 29060–66. https://doi.org/10.1074/jbc.M503824200.
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    • Chow, Felice A., Kristin A. Anderson, Pamela K. Noeldner, and Anthony R. Means. “The autonomous activity of calcium/calmodulin-dependent protein kinase IV is required for its role in transcription..” J Biol Chem 280, no. 21 (May 27, 2005): 20530–38. https://doi.org/10.1074/jbc.M500067200.
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    • Anderson, Kristin A., Pamela K. Noeldner, Kelie Reece, Brian E. Wadzinski, and Anthony R. Means. “Regulation and function of the calcium/calmodulin-dependent protein kinase IV/protein serine/threonine phosphatase 2A signaling complex..” J Biol Chem 279, no. 30 (July 23, 2004): 31708–16. https://doi.org/10.1074/jbc.M404523200.
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    • Lemrow, Shannon M., Kristin A. Anderson, James D. Joseph, Thomas J. Ribar, Pamela K. Noeldner, and Anthony R. Means. “Catalytic activity is required for calcium/calmodulin-dependent protein kinase IV to enter the nucleus..” J Biol Chem 279, no. 12 (March 19, 2004): 11664–71. https://doi.org/10.1074/jbc.M312613200.
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    • Anderson, Kristin A., and Anthony R. Means. “Defective signaling in a subpopulation of CD4(+) T cells in the absence of Ca(2+)/calmodulin-dependent protein kinase IV..” Mol Cell Biol 22, no. 1 (January 2002): 23–29. https://doi.org/10.1128/mcb.22.1.23-29.2002.
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    • Anderson, K. A., and C. D. Kane. “Ca2+/calmodulin-dependent protein kinase IV and calcium signaling..” Biometals : An International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine 11, no. 4 (December 1998): 331–43. https://doi.org/10.1023/a:1009276932076.
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    • Anderson, K. A., R. L. Means, Q. H. Huang, B. E. Kemp, E. G. Goldstein, M. A. Selbert, A. M. Edelman, R. T. Fremeau, and A. R. Means. “Components of a calmodulin-dependent protein kinase cascade. Molecular cloning, functional characterization and cellular localization of Ca2+/calmodulin-dependent protein kinase kinase beta..” J Biol Chem 273, no. 48 (November 27, 1998): 31880–89. https://doi.org/10.1074/jbc.273.48.31880.
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    • Westphal, R. S., K. A. Anderson, A. R. Means, and B. E. Wadzinski. “A signaling complex of Ca2+-calmodulin-dependent protein kinase IV and protein phosphatase 2A..” Science 280, no. 5367 (May 22, 1998): 1258–61. https://doi.org/10.1126/science.280.5367.1258.
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    • Bae, H., K. Anderson, L. A. Flood, N. P. Skiba, H. E. Hamm, and S. G. Graber. “Molecular determinants of selectivity in 5-hydroxytryptamine1B receptor-G protein interactions..” J Biol Chem 272, no. 51 (December 19, 1997): 32071–77. https://doi.org/10.1074/jbc.272.51.32071.
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    • Anderson, K. A., T. J. Ribar, M. Illario, and A. R. Means. “Defective survival and activation of thymocytes in transgenic mice expressing a catalytically inactive form of Ca2+/calmodulin-dependent protein kinase IV..” Mol Endocrinol 11, no. 6 (June 1997): 725–37. https://doi.org/10.1210/mend.11.6.0011.
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    • Means, A. R., T. J. Ribar, C. D. Kane, S. S. Hook, and K. A. Anderson. “Regulation and properties of the rat Ca2+/calmodulin-dependent protein kinase IV gene and its protein products..” Recent Prog Horm Res 52 (1997): 389–406.
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    • Chatila, T., K. A. Anderson, N. Ho, and A. R. Means. “A unique phosphorylation-dependent mechanism for the activation of Ca2+/calmodulin-dependent protein kinase type IV/GR..” J Biol Chem 271, no. 35 (August 30, 1996): 21542–48. https://doi.org/10.1074/jbc.271.35.21542.
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    • Edelman, A. M., K. I. Mitchelhill, M. A. Selbert, K. A. Anderson, S. S. Hook, D. Stapleton, E. G. Goldstein, A. R. Means, and B. E. Kemp. “Multiple Ca(2+)-calmodulin-dependent protein kinase kinases from rat brain. Purification, regulation by Ca(2+)-calmodulin, and partial amino acid sequence..” J Biol Chem 271, no. 18 (May 3, 1996): 10806–10. https://doi.org/10.1074/jbc.271.18.10806.
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    • Selbert, M. A., K. A. Anderson, Q. H. Huang, E. G. Goldstein, A. R. Means, and A. M. Edelman. “Phosphorylation and activation of Ca(2+)-calmodulin-dependent protein kinase IV by Ca(2+)-calmodulin-dependent protein kinase Ia kinase. Phosphorylation of threonine 196 is essential for activation..” J Biol Chem 270, no. 29 (July 21, 1995): 17616–21. https://doi.org/10.1074/jbc.270.29.17616.
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    • Anderson, K., and G. Meissner. “T-tubule depolarization-induced SR Ca2+ release is controlled by dihydropyridine receptor- and Ca(2+)-dependent mechanisms in cell homogenates from rabbit skeletal muscle..” J Gen Physiol 105, no. 3 (March 1995): 363–83. https://doi.org/10.1085/jgp.105.3.363.
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    • Anderson, K., A. H. Cohn, and G. Meissner. “High-affinity [3H]PN200-110 and [3H]ryanodine binding to rabbit and frog skeletal muscle..” Am J Physiol 266, no. 2 Pt 1 (February 1994): C462–66. https://doi.org/10.1152/ajpcell.1994.266.2.C462.
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    • Ma, J., K. Anderson, R. Shirokov, R. Levis, A. González, M. Karhanek, M. M. Hosey, G. Meissner, and E. Ríos. “Effects of perchlorate on the molecules of excitation-contraction coupling of skeletal and cardiac muscle..” J Gen Physiol 102, no. 3 (September 1993): 423–48. https://doi.org/10.1085/jgp.102.3.423.
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    • Meissner, G., F. A. Lai, K. Anderson, L. Xu, Q. Y. Liu, A. Herrmann-Frank, E. Rousseau, R. V. Jones, and H. B. Lee. “Purification and reconstitution of the ryanodine- and caffeine-sensitive Ca2+ release channel complex from muscle sarcoplasmic reticulum..” Adv Exp Med Biol 304 (1991): 241–56. https://doi.org/10.1007/978-1-4684-6003-2_20.
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    • Anderson, K., F. A. Lai, Q. Y. Liu, E. Rousseau, H. P. Erickson, and G. Meissner. “Structural and functional characterization of the purified cardiac ryanodine receptor-Ca2+ release channel complex..” J Biol Chem 264, no. 2 (January 15, 1989): 1329–35.
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    • Meissner, G., E. Rousseau, F. A. Lai, Q. Y. Liu, and K. A. Anderson. “Biochemical characterization of the Ca2+ release channel of skeletal and cardiac sarcoplasmic reticulum..” Mol Cell Biochem 82, no. 1–2 (July 1988): 59–65. https://doi.org/10.1007/bf00242517.
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    • Lai, F. A., K. Anderson, E. Rousseau, Q. Y. Liu, and G. Meissner. “Evidence for a Ca2+ channel within the ryanodine receptor complex from cardiac sarcoplasmic reticulum..” Biochem Biophys Res Commun 151, no. 1 (February 29, 1988): 441–49. https://doi.org/10.1016/0006-291x(88)90613-4.
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  • Book Sections

    • Huynh, F. K., E. Mcdonnell, K. A. Anderson, and M. D. Hirschey. “Sirtuins.” In Signaling Pathways in Liver Diseases: Third Edition, 374–84, 2015. https://doi.org/10.1002/9781118663387.ch27.
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  • Conference Papers

    • Bae, H., K. Anderson, L. A. Flood, N. P. Skiba, H. E. Hamm, and S. G. Gräber. “Molecular Determinants of Selectivity in Receptor-G protein Interaction.” In Faseb Journal, Vol. 11, 1997.

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