1. Zhang L, Lin H. “Using Clickable NAD+ Analogs to Label Substrate Proteins of PARPs.” Methods Mol Biol. July 11, 2017 Link
  2. Zhang X, Spiegelman NA, Nelson OD, Jing H, Lin H. “SIRT6 regulates Ras-related protein R-Ras2 by lysine defatty-acylation.” eLife. April 13, 2017 Link
  3. Dong M, Horitani M, Dzikovski B, Freed JH, Ealick SE, Hoffman BM, Lin H. “Substrate-Dependent Cleavage Site Selection by Unconventional Radical S-Adenosylmethionine Enzymes in Diphthamide Biosynthesis.” J Am Chem Soc. April 6, 2017 Link
  4. Wang Y, Fung YME, Zhang W, He B, Chung MWH, Jin J, Hu J, Lin H, Hao Q. “Deacylation mechanism by SIRT2 Revealed in the 1′-SH-2′-O-Myristoyl Intermediate Structure”, Cell Chem Biol. March 16, 2017 Link
  5. Aramsangtienchai P, Spiegelman NA, Cao J, Lin H. “S-Palmitoylation of Junctional Adhesion Molecule C Regulates Its Tight Junction Localization and Cell Migration.” J Biol Chem. Feb 14, 2017 Link
  6. Wang ZA, Kurra Y, Wang X, Zeng Y, Lee Y, Sharma V, Lin H, Dai SY, Liu WR. “A Versatile approach for site-specific lysine acetylation in proteins.” Angewandte Chemie. Jan 2, 2017 Link
  7. Tong Z, Wang M, Wang Y, Kim DD, Grenier JK, Cao J, Sadhukhan S, Hao Q, Lin H. “SIRT7 Is an RNA-Activated Protein Lysine Deacylase.” ACS Chem Biol. Nov 22, 2016 Link
  8. Lin Z, Dong M, Zhang Y, Lee EA, Lin H. “Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification”, Nat Chem Biol. Oct 3, 2016 Link
  9. Jin J, He B, Zhang X, Lin H, Wang Y. “SIRT2 Reverses 4-Oxonanoyl Lysine Modification on Histones”, J Am Chem Soc. 138, 12304-12307, 2016 Link
  10. Dong M, Horitani M, Dzikovski B, Pandelia M, Krebs C, Freed JH, Hoffman BM, Lin H. “Organometallic complex formed by an unconventional radical S-Adenosylmethionine Enzyme”, J Am Chem Soc. 138, 9755–9758, 2016 Link
  11. Aramsangtienchai P, Spiegelman NA, He B, Miller SP, Dai L, Zhao Y, Lin H. “HDAC8 catalyzes the hydrolysis of long chain fatty acyl lysine”, ACS Chem Biol. 2016 10.1021/acschembio.6b00396 Link
  12. Zhang X, Khan S, Jiang H, Antonyak MA, Chen X, Spiegelman NA, Shrimp JH, Cerione RA, Lin H. “Identifying the functional contribution of the defatty-acylase activity of SIRT6”, Nature Chemical Biology 12, 614–620,
  13. Tong Z, Wang Y, Zhang X, Kim DD, Sadhukhan S, Hao Q, Lin H. “SIRT7 Is Activated by DNA and Deacetylates Histone H3 in the Chromatin Context”, ACS Chem Biol. 11, 742-7, 2016 Link
  14. Jing H, Hu J, He B, Negrón Abril YL, Stupinski J, Weiser K, Carbonaro M, Chiang YL, Southard T, Giannakakou P, Weiss RS, Lin H. “A SIRT2-Selective Inhibitor Promotes c-Myc Oncoprotein Degradation and Exhibits Broad Anticancer Activity”, Cancer Cell. 29, 297-310, 2016 Link
  15. Chiang YL, Lin H. “An improved fluorogenic assay for SIRT1, SIRT2, and SIRT3”, Org Biomol Chem. 14, 2186-9, 2016 Link
  16. Li Z, Kim DD, Nelson OD, Otwell AE, Richardson RE, Callister SJ, Lin H. “Molecular dissection of a putative iron reductase from Desulfotomaculum reducens MI-1”, Biochem Biophys Res Commun 467, 503-8, 2015 Link
  17. Jing H, and Lin H. “Sirtuins in Epigenetic Regulation”, Chem. Rev., 115, 2350-2375, 2015 Link
  18. Liu X, Sadhukhan S, Sun S, Wagner GR, Hirschey MD, Qi L, Lin H, Locasale JW, “High resolution metabolomics with acyl-CoA profiling reveals widespread remodeling in response to diet.” Mol. Cell. Proteomics 2015, mcp.M114.044859 Link
  19. Teng YB, Jing H, Aramsangtienchai P, He B, Khan S, Hu J, Lin H, Hao Q, “Efficient demyristoylase activity of SIRT2 revealed by kinetic and structural studies.” Sci. Rep. 5, 8529, 2015. Link
  20. Otwell AE, Sherwood RW, Zhang S, Nelson OD, Li Z, Lin H, Callister SJ, Richardson RE, “Identification of proteins capable of metal reduction from the proteome of the Gram-positive bacterium Desulfotomaculum reducens MI-1 using an NADH-based activity assay.” Environ. Microbiol. 2014 Link
  21. He B, Hu J,   Zhang X, and Lin H. “Thiomyristoyl peptides as cell-permeable Sirt6 inhibitors”, Org. Biomol. Chem., 12, 7498-7502, 2014 Link
  22. Lin Z, Su X, Chen W, Ci B, Zhang S, Lin H. Dph7 catalyzes a previously unknown demethylation step in diphthamide biosynthesis. J Am Chem Soc. 2014 Link
  23. Shrimp JH, Hu J, Dong M, Wang BS, Macdonald RJ, Jiang H, Hao Q, Yen A, Lin H. Revealing CD38 Cellular Localization Using a Cell Permeable, Mechanism-Based Fluorescent Small Molecule Probe. J Am Chem Soc. 2014 Link
  24. Dong M, Su X, Dzikovski B, Dando EE, Zhu X, Du J, Freed JH, Lin H. Dph3 is an electron donor for dph1-dph2 in the first step of eukaryotic diphthamide biosynthesis. J Am Chem Soc. 136, 1754-7, 2014 Link
  25. G. Colak, Z. Xie, A. Zhu, L. Dai, Z. Lu, Y. Zhang, X. Wan, Y. Chen, Y.H. Cha, H. Lin, Y. Zhao, and M. Tan, “Identification of Lysine Succinylation Substrates and the Succinylation Regulatory Enzyme CobB in Escherichia coli”. Mol. Cell. Proteomics, 12, 3509-3520, 2013
  26. Yu J, Sadhukhan S, Noriega LG, Moullan N, He B, Weiss RS, Lin H, Schoonjans K, Auwerx J. “Metabolic Characterization of a Sirt5 deficient mouse model”, Sci. Rep. 3, 2806, 2013.
  27. Su X, Lin Z, Lin H. The biosynthesis and biological function of diphthamide. Crit Rev Biochem Mol Biol. 2013 Link
  28. Hu J, He B, Bhargava S, Lin H. A fluorogenic assay for screening Sirt6 modulators. Org Biomol Chem. 11, 5213-6, 2013 Link
  29. Jiang H, Khan S, Wang Y, Charron G, He B, Sebastian C, Du J, Kim R, Ge E, Mostoslavsky R, Hang HC, Hao Q, Lin H. SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine. Nature. 496, 110-3. 2013 Link
  30. Jiang H, Lin H. Labeling Substrate Proteins of Poly(ADP-ribose) Polymerases with Clickable NAD Analog. Curr Protoc Chem Biol. 4, 19-34, 2012 Link
  31. Su X, Lin Z, Chen W, Jiang H, Zhang S, Lin H. Chemogenomic approach identified yeast YLR143W as diphthamide synthetase. Proc Natl Acad Sci U S A. 109, 19983-7, 2012 Link
  32. Jiang H, Sherwood R, Zhang S, Zhu X, Liu Q, Graeff R, Kriksunov IA, Lee HC, Hao Q, Lin H. Identification of ADP-ribosylation sites of CD38 mutants by precursor ion scanning mass spectrometry. Anal Biochem. 433, 218-26. 2012 Link
  33. Zhou Y, Zhang H, He B, Du J, Lin H, Cerione RA, Hao Q. The bicyclic intermediate structure provides insights into the desuccinylation mechanism of human sirtuin 5 (SIRT5). J Biol Chem. 287, 28307-14, 2012 Link
  34. Lin H, Su X, He B. Protein lysine acylation and cysteine succination by intermediates of energy metabolism, ACS Chem Biol. 7, 947-60, 2012 Link
  35. He B, Du J, Lin H. Thiosuccinyl peptides as Sirt5-specific inhibitors, J Am Chem Soc, 134, 1922-5, 2012 Link
  36. Su X, Chen W, Lee W, Jiang H, Zhang S, Lin H. YBR246W is required for the third step of diphthamide biosynthesis, J Am Chem Soc, 134(2), 773-6, 2012 Link
  37. Zhu AY, Zhou Y, Khan S, Deitsch KW, Hao Q, Lin H. Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine, ACS Chem Biol. 7, 155-9, 2012 Link
  38. J. Du, Y. Zhou, X. Su, J. Yu, S. Khan, H. Jiang, J. Kim, J. Woo, J. Kim, B. Choi, B. He, W. Chen, S. Zhang, R. Cerione, J. Auwerx, Q. Hao, and H.Lin. Sirt5 is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase, Science. Vol. 334, No 6507, 806-809, 2011 Link
  39. H. Lin, “S-Adenosylmethionine-dependent alkylation reactions: When are radical reactions used?” Bioorg. Chem. 39, 161-170, 2011
  40. X. Zhu, B. Dzikovski, X. Su, A.T. Torelli, Y. Zhang, S.E. Ealick, J.H. Freed, and H. Lin. Mechanistic understanding of Pyrococcus horikoshii Dph2, a [4Fe-4S] enzyme required for diphthamide biosynthesis, Mol. BioSystems. 7, 74-81, 2011 Link
  41. J. Congleton, H. Jiang, F. Malavasi, H. Lin, A. Yen, “ATRA-induced HL-60 myeloid leukemia cell differentiation depends on the CD38 cytosolic tail needed for membrane localization, but CD38 enzymatic activity is unnecessary” Exp. Cell Res. 317, 910-919 2011
  42. X. Zhu, J. Kim, X. Su, and H. Lin. Reconstitution of diphthine synthase activity in vitro, Biochemistry. 49, 9649-9657, 2010 . Link
  43. Hong Jiang, Jun Hyun Kim, Kristine M. Frizzell, W. Lee Kraus and Hening Lin;Clickable NAD Analogues for Labeling Substrate Proteins of Poly(ADP-ribose) Polymerases, JACS. 2010Link
  44. Yang Zhang, Xuling Zhu, Andrew T. Torelli, Michael Lee, Boris Dzikovski, Rachel M. Koralewski, Eileen Wang, Jack Freed, Carsten Krebs, Steven E. Ealick & Hening Lin;Diphthamide biosynthesis requires an organic radical generated by an iron–sulphur enzyme, Nature. 465,891-896, 2010 Link
  45. Q. Liu, R. Graeff, I. A. Kriksunov, H. Jiang, B. Zhang, B. V. L. Potter, N. Oppenheimer, H. Lin, H. C. Lee, Q. Hao, “Structural Basis for Enzymatic Evolution from a Dedicated ADP-ribosyl Cyclase to a Multi- functional NAD Hydrolase”, J. Biol. Chem., 284, 27637-27645, 2009. Link
  46. H. Jiang, J. Congleton, Q. Liu, P. Merchant, F. Malavasi, H.C. Lee, Q. Hao, A. Yen, H. Lin, “Mechanism-Based Small Molecule Probes for Labeling CD38 on Live Cells”, J. Am. Chem. Soc., 131, 1658-1659 (2009) Link Highlighted in Nat. Chem. Biol. 5, 149, 2009 Link
  47. J. Du, H. Jiang, H. Lin, “Investigating the ADP-ribosyltransferase activity of sirtuins with NAD analogs and 32P-NAD”, Biochemistry 48, 2878–2890, 2009 Link
  48. Q. Liu, I.A. Kriksunov, H. Jiang, R. Graeff, H. Lin, H.C. Lee, Q. Hao,“Covalent and non-covalent intermediates of an NAD utilizing enzyme – human CD38”, Chem. Biol. 15,1068-78, 2008 Link
  49. H. Lin, J. Du, H. Jiang, “Posttranslational modifications to regulate protein function”, Wiley Encyclopedia of Chemical Biology, 2008. John Wiley & Sons, Inc. DOI: 10.1002/9780470048672. wecb467 Link
  50. H. Lin, “Nicotinamide adenine dinucleotide: beyond a redox coenzyme”, Org. Biomol. Chem., 5, 2541-2554 2007 Link