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2. Hosseinzadeh, P., Watson, P. R., Craven, T. W., Li, X., Rettie, S., Pardo-Avila, F., Bera, A. K., Mulligan, V. K., Lu, P., Ford, A. S., Weitzner, B. D., Stewart, L. J., Moyer, A. P., Di Piazza, M., Whalen, J. G., Greisen, P., Christianson, D. W., & Baker, D. (2021). Anchor extension: a structure-guided approach to design cyclic peptides targeting enzyme active sites [Article]. Nature Communications, 12(1), Article 3384. https://doi.org/10.1038/s41467-021-23609-8

3. Faylo, J. L., van Eeuwen, T., Kim, H. J., Gorbea Colón, J. J., Garcia, B. A., Murakami, K., & Christianson, D. W. (2021). Structural insight on assembly-line catalysis in terpene biosynthesis [Article]. Nature Communications, 12(1), Article 3487. https://doi.org/10.1038/s41467-021-23589-9

4. Ronnebaum, T. A., Eaton, S. A., Brackhahn, E. A. E., & Christianson, D. W. (2021). Engineering the Prenyltransferase Domain of a Bifunctional Assembly-Line Terpene Synthase [Article]. Biochemistry, 60(42), 3162-3172. https://doi.org/10.1021/acs.biochem.1c00600

5. Faylo, J. L., Ronnebaum, T. A., & Christianson, D. W. (2021). Assembly-Line Catalysis in Bifunctional Terpene Synthases [Article]. Accounts of Chemical Research, 54(20), 3780-3791. https://doi.org/10.1021/acs.accounts.1c00296

6. Campiani, G., Cavella, C., Osko, J. D., Brindisi, M., Relitti, N., Brogi, S., Saraswati, A. P., Federico, S., Chemi, G., Maramai, S., Carullo, G., Jaeger, B., Carleo, A., Benedetti, R., Sarno, F., Lamponi, S., Rottoli, P., Bargagli, E., Bertucci, C., . . . Prasse, A. (2021). Harnessing the Role of HDAC6 in Idiopathic Pulmonary Fibrosis: Design, Synthesis, Structural Analysis, and Biological Evaluation of Potent Inhibitors [Article]. Journal of Medicinal Chemistry, 64(14), 9960-9988. https://doi.org/10.1021/acs.jmedchem.1c00184

7. Olaoye, O. O., Watson, P. R., Nawar, N., Geletu, M., Sedighi, A., Bukhari, S., Raouf, Y. S., Manaswiyoungkul, P., Erdogan, F., Abdeldayem, A., Cabral, A. D., Hassan, M. M., Toutah, K., Shouksmith, A. E., Gawel, J. M., Israelian, J., Radu, T. B., Kachhiyapatel, N., De Araujo, E. D., . . . Gunning, P. T. (2021). Unique Molecular Interaction with the Histone Deacetylase 6 Catalytic Tunnel: Crystallographic and Biological Characterization of a Model Chemotype [Article]. Journal of Medicinal Chemistry, 64(5), 2691-2704. https://doi.org/10.1021/acs.jmedchem.0c01922

8. Osko, J. D., Porter, N. J., Decroos, C., Lee, M. S., Watson, P. R., Raible, S. E., Krantz, I. D., Deardorff, M. A., & Christianson, D. W. (2021). Structural analysis of histone deacetylase 8 mutants associated with Cornelia de Lange Syndrome spectrum disorders [Article]. Journal of Structural Biology, 213(1), Article 107681. https://doi.org/10.1016/j.jsb.2020.107681

9. Herbst-Gervasoni, C. J., & Christianson, D. W. (2021). X-ray Crystallographic Snapshots of Substrate Binding in the Active Site of Histone Deacetylase 10 [Article]. Biochemistry, 60(4), 303-313. https://doi.org/10.1021/acs.biochem.0c00936

10. Ronnebaum, T. A., Gardner, S. M., & Christianson, D. W. (2020). An Aromatic Cluster in the Active Site of epi-Isozizaene Synthase Is an Electrostatic Toggle for Divergent Terpene Cyclization Pathways [Article]. Biochemistry, 59(50), 4744-4754. https://doi.org/10.1021/acs.biochem.0c00876

11. He, H., Bian, G., Herbst-Gervasoni, C. J., Mori, T., Shinsky, S. A., Hou, A., Mu, X., Huang, M., Cheng, S., Deng, Z., Christianson, D. W., Abe, I., & Liu, T. (2020). Discovery of the cryptic function of terpene cyclases as aromatic prenyltransferases [Article]. Nature Communications, 11(1), Article 3958. https://doi.org/10.1038/s41467-020-17642-2

12. Saraswati, A. P., Relitti, N., Brindisi, M., Osko, J. D., Chemi, G., Federico, S., Grillo, A., Brogi, S., McCabe, N. H., Turkington, R. C., Ibrahim, O., O’Sullivan, J., Lamponi, S., Ghanim, M., Kelly, V. P., Zisterer, D., Amet, R., Hannon Barroeta, P., Vanni, F., . . . Campiani, G. (2020). Spiroindoline-Capped Selective HDAC6 Inhibitors: Design, Synthesis, Structural Analysis, and Biological Evaluation [Article]. ACS Medicinal Chemistry Letters, 11(11), 2268-2276. https://doi.org/10.1021/acsmedchemlett.0c00395

13. Reßing, N., Sönnichsen, M., Osko, J. D., Schöler, A., Schliehe-Diecks, J., Skerhut, A., Borkhardt, A., Hauer, J., Kassack, M. U., Christianson, D. W., Bhatia, S., & Hansen, F. K. (2020). Multicomponent Synthesis, Binding Mode, and Structure-Activity Relationship of Selective Histone Deacetylase 6 (HDAC6) Inhibitors with Bifurcated Capping Groups [Article]. Journal of Medicinal Chemistry, 63(18), 10339-10351. https://doi.org/10.1021/acs.jmedchem.9b01888

14. Osko, J. D., & Christianson, D. W. (2020). Binding of inhibitors to active-site mutants of CD1, the enigmatic catalytic domain of histone deacetylase 6 [Article]. Acta Crystallographica Section F: Structural Biology Communications, 76, 428-437. https://doi.org/10.1107/S2053230X20010250

15. Herbst-Gervasoni, C. J., Steimbach, R. R., Morgen, M., Miller, A. K., & Christianson, D. W. (2020). Structural Basis for the Selective Inhibition of HDAC10, the Cytosolic Polyamine Deacetylase [Article]. ACS Chemical Biology, 15(8), 2154-2163. https://doi.org/10.1021/acschembio.0c00362

16. Morgen, M., Steimbach, R. R., Géraldy, M., Hellweg, L., Sehr, P., Ridinger, J., Witt, O., Oehme, I., Herbst-Gervasoni, C. J., Osko, J. D., Porter, N. J., Christianson, D. W., Gunkel, N., & Miller, A. K. (2020). Design and Synthesis of Dihydroxamic Acids as HDAC6/8/10 Inhibitors [Article]. ChemMedChem, 15(13), 1163-1174. https://doi.org/10.1002/cmdc.202000149

17. Blank, P. N., Barnett, A. A., Ronnebaum, T. A., Alderfer, K. E., Gillott, B. N., Christianson, D. W., & Himmelberger, J. A. (2020). Structural studies of geranylgeranylglyceryl phosphate synthase, a prenyltransferase found in thermophilic Euryarchaeota [Article]. Acta Crystallographica Section D: Structural Biology, 76, 542-557. https://doi.org/10.1107/S2059798320004878

18. Osko, J. D., & Christianson, D. W. (2020). Structural determinants of affinity and selectivity in the binding of inhibitors to histone deacetylase 6 [Review]. Bioorganic and Medicinal Chemistry Letters, 30(8), Article 127023. https://doi.org/10.1016/j.bmcl.2020.127023

19. Ronnebaum, T. A., Gupta, K., & Christianson, D. W. (2020). Higher-order oligomerization of a chimeric αβγ bifunctional diterpene synthase with prenyltransferase and class II cyclase activities is concentration-dependent [Article]. Journal of Structural Biology, 210(1), Article 107463. https://doi.org/10.1016/j.jsb.2020.107463

20. Osko, J. D., Porter, N. J., Narayana Reddy, P. A., Xiao, Y. C., Rokka, J., Jung, M., Hooker, J. M., Salvino, J. M., & Christianson, D. W. (2020). Exploring Structural Determinants of Inhibitor Affinity and Selectivity in Complexes with Histone Deacetylase 6 [Article]. Journal of Medicinal Chemistry, 63(1), 295-308. https://doi.org/10.1021/acs.jmedchem.9b01540

21. Osko, J. D., & Christianson, D. W. (2019). Structural Basis of Catalysis and Inhibition of HDAC6 CD1, the Enigmatic Catalytic Domain of Histone Deacetylase 6 [Article]. Biochemistry, 58(49), 4912-4924. https://doi.org/10.1021/acs.biochem.9b00934

22. Herbst-Gervasoni, C. J., & Christianson, D. W. (2019). Binding of N8-Acetylspermidine Analogues to Histone Deacetylase 10 Reveals Molecular Strategies for Blocking Polyamine Deacetylation [Article]. Biochemistry, 58(49), 4957-4969. https://doi.org/10.1021/acs.biochem.9b00906

23. Porter, N. J., & Christianson, D. W. (2019). Structure, mechanism, and inhibition of the zinc-dependent histone deacetylases [Review]. Current Opinion in Structural Biology, 59, 9-18. https://doi.org/10.1016/j.sbi.2019.01.004

24. Osko, J. D., Roose, B. W., Shinsky, S. A., & Christianson, D. W. (2019). Structure and Function of the Acetylpolyamine Amidohydrolase from the Deep Earth Halophile Marinobacter subterrani [Article]. Biochemistry, 58(36), 3755-3766. https://doi.org/10.1021/acs.biochem.9b00582

25. Blank, P. N., Barrow, G. H., & Christianson, D. W. (2019). Crystal structure of F95Q epi-isozizaene synthase, an engineered sesquiterpene cyclase that generates biofuel precursors β- and γ-curcumene [Article]. Journal of Structural Biology, 207(2), 218-224. https://doi.org/10.1016/j.jsb.2019.05.011

26. Roose, B. W., & Christianson, D. W. (2019). Structural Basis of Tryptophan Reverse N-Prenylation Catalyzed by CymD [Article]. Biochemistry, 58(30), 3232-3242. https://doi.org/10.1021/acs.biochem.9b00399

27. Blank, P. N., Shinsky, S. A., & Christianson, D. W. (2019). Structure of Sesquisabinene Synthase 1, a Terpenoid Cyclase That Generates a Strained [3.1.0] Bridged-Bicyclic Product [Article]. ACS Chemical Biology, 14(5), 1011-1019. https://doi.org/10.1021/acschembio.9b00218

28. Vögerl, K., Ong, N., Senger, J., Herp, D., Schmidtkunz, K., Marek, M., Müller, M., Bartel, K., Shaik, T. B., Porter, N. J., Robaa, D., Christianson, D. W., Romier, C., Sippl, W., Jung, M., & Bracher, F. (2019). Synthesis and Biological Investigation of Phenothiazine-Based Benzhydroxamic Acids as Selective Histone Deacetylase 6 Inhibitors [Article]. Journal of Medicinal Chemistry, 62(3), 1138-1166. https://doi.org/10.1021/acs.jmedchem.8b01090

29. Welker Leng, K. R., Castañeda, C. A., Decroos, C., Islam, B., Haider, S. M., Christianson, D. W., & Fierke, C. A. (2019). Phosphorylation of Histone Deacetylase 8: Structural and Mechanistic Analysis of the Phosphomimetic S39E Mutant [Article]. Biochemistry, 4480-4493. https://doi.org/10.1021/acs.biochem.9b00653

30. Osko, J. D., & Christianson, D. W. (2019). Methods for the expression, purification, and crystallization of histone deacetylase 6–inhibitor complexes. In Methods in Enzymology (Vol. 626, pp. 447-474).

31. Porter, N. J., & Christianson, D. W. (2019). Preparation of a new construct of human histone deacetylase 8 for the crystallization of enzyme-inhibitor complexes. In Methods in Enzymology (Vol. 626, pp. 561-585).

32. Christianson, D. W. (2018). Correction: Structural and chemical biology of terpenoid cyclases (Chemical Reviews (2017) 117 (11570-11648) DOI: 10.1021/acs.chemrev.7b00287) [Erratum]. Chemical Reviews, 118(24), 11795. https://doi.org/10.1021/acs.chemrev.8b00682

33. Porter, N. J., Shen, S., Barinka, C., Kozikowski, A. P., & Christianson, D. W. (2018). Molecular Basis for the Selective Inhibition of Histone Deacetylase 6 by a Mercaptoacetamide Inhibitor [Article]. ACS Medicinal Chemistry Letters, 9(12), 1301-1305. https://doi.org/10.1021/acsmedchemlett.8b00487

34. Bhatia, S., Krieger, V., Groll, M., Osko, J. D., Reßing, N., Ahlert, H., Borkhardt, A., Kurz, T., Christianson, D. W., Hauer, J., & Hansen, F. K. (2018). Discovery of the First-in-Class Dual Histone Deacetylase-Proteasome Inhibitor [Article]. Journal of Medicinal Chemistry, 61(22), 10299-10309. https://doi.org/10.1021/acs.jmedchem.8b01487

35. Blank, P. N., Pemberton, T. A., Chow, J. Y., Poulter, C. D., & Christianson, D. W. (2018). Crystal Structure of Cucumene Synthase, a Terpenoid Cyclase That Generates a Linear Triquinane Sesquiterpene [Article]. Biochemistry, 57(44), 6326-6335. https://doi.org/10.1021/acs.biochem.8b00899

36. Porter, N. J., Osko, J. D., Diedrich, D., Kurz, T., Hooker, J. M., Hansen, F. K., & Christianson, D. W. (2018). Histone Deacetylase 6-Selective Inhibitors and the Influence of Capping Groups on Hydroxamate-Zinc Denticity [Article]. Journal of Medicinal Chemistry, 61(17), 8054-8060. https://doi.org/10.1021/acs.jmedchem.8b01013

37. Porter, N. J., Wagner, F. F., & Christianson, D. W. (2018). Entropy as a Driver of Selectivity for Inhibitor Binding to Histone Deacetylase 6 [Article]. Biochemistry, 57(26), 3916-3924. https://doi.org/10.1021/acs.biochem.8b00367

38. Shinsky, S. A., & Christianson, D. W. (2018). Polyamine Deacetylase Structure and Catalysis: Prokaryotic Acetylpolyamine Amidohydrolase and Eukaryotic HDAC10 [Review]. Biochemistry, 57(22), 3105-3114. https://doi.org/10.1021/acs.biochem.8b00079

39. Mackwitz, M. K. W., Hamacher, A., Osko, J. D., Held, J., Schöler, A., Christianson, D. W., Kassack, M. U., & Hansen, F. K. (2018). Multicomponent Synthesis and Binding Mode of Imidazo[1,2- a]pyridine-Capped Selective HDAC6 Inhibitors [Article]. Organic Letters, 20(11), 3255-3258. https://doi.org/10.1021/acs.orglett.8b01118

40. Porter, N. J., Mahendran, A., Breslow, R., & Christianson, D. W. (2017). Unusual zinc-binding mode of HDAC6-selective hydroxamate inhibitors [Article]. Proceedings of the National Academy of Sciences of the United States of America, 114(51), 13459-13464. https://doi.org/10.1073/pnas.1718823114

41. Blank, P. N., Barrow, G. H., Chou, W. K. W., Duan, L., Cane, D. E., & Christianson, D. W. (2017). Substitution of Aromatic Residues with Polar Residues in the Active Site Pocket of epi-Isozizaene Synthase Leads to the Generation of New Cyclic Sesquiterpenes [Article]. Biochemistry, 56(43), 5798-5811. https://doi.org/10.1021/acs.biochem.7b00895

42. Porter, N. J., & Christianson, D. W. (2017). Binding of the Microbial Cyclic Tetrapeptide Trapoxin A to the Class i Histone Deacetylase HDAC8 [Article]. ACS Chemical Biology, 12(9), 2281-2286. https://doi.org/10.1021/acschembio.7b00330

43. Christianson, D. W. (2017). Structural and Chemical Biology of Terpenoid Cyclases [Review]. Chemical Reviews, 117(17), 11570-11648. https://doi.org/10.1021/acs.chemrev.7b00287

44. Bitler, B. G., Wu, S., Park, P. H., Hai, Y., Aird, K. M., Wang, Y., Zhai, Y., Kossenkov, A. V., Vara-Ailor, A., Rauscher, F. J., Zou, W., Speicher, D. W., Huntsman, D. G., Conejo-Garcia, J. R., Cho, K. R., Christianson, D. W., & Zhang, R. (2017). ARID1A-mutated ovarian cancers depend on HDAC6 activity [Article]. Nature Cell Biology, 19(8), 962-973. https://doi.org/10.1038/ncb3582

45. Hai, Y., Shinsky, S. A., Porter, N. J., & Christianson, D. W. (2017). Histone deacetylase 10 structure and molecular function as a polyamine deacetylase [Article]. Nature Communications, 8, Article 15368. https://doi.org/10.1038/ncomms15368

46. Pemberton, T. A., Chen, M., Harris, G. G., Chou, W. K. W., Duan, L., Köksal, M., Genshaft, A. S., Cane, D. E., & Christianson, D. W. (2017). Exploring the Influence of Domain Architecture on the Catalytic Function of Diterpene Synthases [Article]. Biochemistry, 56(14), 2010-2023. https://doi.org/10.1021/acs.biochem.7b00137

47. Porter, N. J., Christianson, N. H., Decroos, C., & Christianson, D. W. (2016). Structural and Functional Influence of the Glycine-Rich Loop G302GGGY on the Catalytic Tyrosine of Histone Deacetylase 8 [Article]. Biochemistry, 55(48), 6718-6729. https://doi.org/10.1021/acs.biochem.6b01014

48. Christianson, D. W., & Scrutton, N. S. (2016). Editorial overview: Catalysis and regulation: enzyme structure, mechanism, and biosynthetic pathways [Editorial]. Current Opinion in Structural Biology, 41, viii-x. https://doi.org/10.1016/j.sbi.2016.09.005

49. Chen, M., Harris, G. G., Pemberton, T. A., & Christianson, D. W. (2016). Multi-domain terpenoid cyclase architecture and prospects for proximity in bifunctional catalysis [Review]. Current Opinion in Structural Biology, 41, 27-37. https://doi.org/10.1016/j.sbi.2016.05.010

50. Deardorff, M. A., Porter, N. J., & Christianson, D. W. (2016). Structural aspects of HDAC8 mechanism and dysfunction in Cornelia de Lange syndrome spectrum disorders [Review]. Protein Science, 25(11), 1965-1976. https://doi.org/10.1002/pro.3030

51. Hai, Y., & Christianson, D. W. (2016). Histone deacetylase 6 structure and molecular basis of catalysis and inhibition [Article]. Nature Chemical Biology, 12(9), 741-747. https://doi.org/10.1038/nchembio.2134

52. Pemberton, T. A., & Christianson, D. W. (2016). General base-general acid catalysis by terpenoid cyclases [Review]. Journal of Antibiotics, 69(7), 486-493. https://doi.org/10.1038/ja.2016.39

53. Chen, M., Chou, W. K. W., Al-Lami, N., Faraldos, J. A., Allemann, R. K., Cane, D. E., & Christianson, D. W. (2016). Probing the Role of Active Site Water in the Sesquiterpene Cyclization Reaction Catalyzed by Aristolochene Synthase [Article]. Biochemistry, 55(20), 2864-2874. https://doi.org/10.1021/acs.biochem.6b00343

54. Grundy, D. J., Chen, M., González, V., Leoni, S., Miller, D. J., Christianson, D. W., & Allemann, R. K. (2016). Mechanism of Germacradien-4-ol Synthase-Controlled Water Capture [Article]. Biochemistry, 55(14), 2112-2121. https://doi.org/10.1021/acs.biochem.6b00115

55. Chen, M., Chou, W. K. W., Toyomasu, T., Cane, D. E., & Christianson, D. W. (2016). Structure and Function of Fusicoccadiene Synthase, a Hexameric Bifunctional Diterpene Synthase [Article]. ACS Chemical Biology, 11(4), 889-899. https://doi.org/10.1021/acschembio.5b00960

56. Gantt, S. M. L., Decroos, C., Lee, M. S., Gullett, L. E., Bowman, C. M., Christianson, D. W., & Fierke, C. A. (2016). General Base-General Acid Catalysis in Human Histone Deacetylase 8 [Article]. Biochemistry, 55(5), 820-832. https://doi.org/10.1021/acs.biochem.5b01327

57. Hai, Y., & Christianson, D. W. (2016). Crystal structures of Leishmania mexicana arginase complexed with α,α-disubstituted boronic amino-acid inhibitors [Article]. Acta Crystallographica Section:F Structural Biology Communications, 72, 300-306. https://doi.org/10.1107/S2053230X16003630

58. Harris, G. G., Lombardi, P. M., Pemberton, T. A., Matsui, T., Weiss, T. M., Cole, K. E., Köksal, M., Murphy, F. V., Vedula, L. S., Chou, W. K. W., Cane, D. E., & Christianson, D. W. (2015). Structural Studies of Geosmin Synthase, a Bifunctional Sesquiterpene Synthase with αα Domain Architecture That Catalyzes a Unique Cyclization-Fragmentation Reaction Sequence [Article]. Biochemistry, 54(48), 7142-7155. https://doi.org/10.1021/acs.biochem.5b01143

59. Decroos, C., Christianson, N. H., Gullett, L. E., Bowman, C. M., Christianson, K. E., Deardorff, M. A., & Christianson, D. W. (2015). Biochemical and Structural Characterization of HDAC8 Mutants Associated with Cornelia de Lange Syndrome Spectrum Disorders [Article]. Biochemistry, 54(42), 6501-6513. https://doi.org/10.1021/acs.biochem.5b00881

60. Decroos, C., & Christianson, D. W. (2015). Design, Synthesis, and Evaluation of Polyamine Deacetylase Inhibitors, and High-Resolution Crystal Structures of Their Complexes with Acetylpolyamine Amidohydrolase [Article]. Biochemistry, 54(30), 4692-4703. https://doi.org/10.1021/acs.biochem.5b00536

61. Decroos, C., Clausen, D. J., Haines, B. E., Wiest, O., Williams, R. M., & Christianson, D. W. (2015). Variable active site loop conformations accommodate the binding of macrocyclic largazole analogues to HDAC8 [Article]. Biochemistry, 54(12), 2126-2135. https://doi.org/10.1021/acs.biochem.5b00010

62. Hai, Y., Kerkhoven, E. J., Barrett, M. P., & Christianson, D. W. (2015). Crystal structure of an arginase-like protein from Trypanosoma brucei that evolved without a binuclear manganese cluster [Article]. Biochemistry, 54(2), 458-471. https://doi.org/10.1021/bi501366a

63. Decroos, C., Bowman, C. M., Moser, J. A. S., Christianson, K. E., Deardorff, M. A., & Christianson, D. W. (2014). Compromised structure and function of HDAC8 mutants identified in Cornelia de Lange Syndrome spectrum disorders [Article]. ACS Chemical Biology, 9(9), 2157-2164. https://doi.org/10.1021/cb5003762

64. Hai, Y., Edwards, J. E., Van Zandt, M. C., Hoffmann, K. F., & Christianson, D. W. (2014). Crystal structure of Schistosoma mansoni arginase, a potential drug target for the treatment of schistosomiasis [Article]. Biochemistry, 53(28), 4671-4684. https://doi.org/10.1021/bi5004519

65. Li, R., Chou, W. K. W., Himmelberger, J. A., Litwin, K. M., Harris, G. G., Cane, D. E., & Christianson, D. W. (2014). Reprogramming the chemodiversity of terpenoid cyclization by remolding the active site contour of epi-isozizaene synthase [Article]. Biochemistry, 53(7), 1155-1168. https://doi.org/10.1021/bi401643u

66. Kaiser, F. J., Ansari, M., Braunholz, D., Gil-Rodríguez, M. C., Decroos, C., Wilde, J. J., Fincher, C. T., Kaur, M., Bando, M., Amor, D. J., Atwal, P. S., Bahlo, M., Bowman, C. M., Bradley, J. J., Brunner, H. G., Clark, D., Campo, M. D., Di Donato, N., Diakumis, P., . . . Deardorff, M. A. (2014). Loss-of-function HDAC8 mutations cause a phenotypic spectrum of Cornelia de Lange syndrome-like features, ocular hypertelorism, large fontanelle and X-linked inheritance [Article]. Human Molecular Genetics, 23(11), 2888-2900, Article ddu002. https://doi.org/10.1093/hmg/ddu002

67. Köksal, M., Potter, K., Peters, R. J., & Christianson, D. W. (2014). 1.55 Å-resolution structure of ent-copalyl diphosphate synthase and exploration of general acid function by site-directed mutagenesis [Article]. Biochimica et Biophysica Acta – General Subjects, 1840(1), 184-190. https://doi.org/10.1016/j.bbagen.2013.09.004

68. Hai, Y., Dugery, R. J., Healy, D., & Christianson, D. W. (2013). Formiminoglutamase from Trypanosoma cruzi is an arginase-like manganese metalloenzyme [Article]. Biochemistry, 52(51), 9294-9309. https://doi.org/10.1021/bi401352h

69. Chen, M., Al-Lami, N., Janvier, M., D’Antonio, E. L., Faraldos, J. A., Cane, D. E., Allemann, R. K., & Christianson, D. W. (2013). Mechanistic insights from the binding of substrate and carbocation intermediate analogues to aristolochene synthase [Article]. Biochemistry, 52(32), 5441-5453. https://doi.org/10.1021/bi400691v

70. Köksal, M., Chou, W. K. W., Cane, D. E., & Christianson, D. W. (2013). Unexpected reactivity of 2-fluorolinalyl diphosphate in the active site of crystalline 2-methylisoborneol synthase [Article]. Biochemistry, 52(31), 5247-5255. https://doi.org/10.1021/bi400797c

71. Decroos, C., Bowman, C. M., & Christianson, D. W. (2013). Synthesis and evaluation of N8-acetylspermidine analogues as inhibitors of bacterial acetylpolyamine amidohydrolase [Article]. Bioorganic and Medicinal Chemistry, 21(15), 4530-4540. https://doi.org/10.1016/j.bmc.2013.05.045

72. Genshaft, A., Moser, J. A. S., D’Antonio, E. L., Bowman, C. M., & Christianson, D. W. (2013). Energetically unfavorable amide conformations for N6-acetyllysine side chains in refined protein structures [Article]. Proteins: Structure, Function and Bioinformatics, 81(6), 1051-1057. https://doi.org/10.1002/prot.24262

73. D’Antonio, E. L., Ullman, B., Roberts, S. C., Dixit, U. G., Wilson, M. E., Hai, Y., & Christianson, D. W. (2013). Crystal structure of arginase from Leishmania mexicana and implications for the inhibition of polyamine biosynthesis in parasitic infections [Article]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 535(2), 163-176. https://doi.org/10.1016/j.abb.2013.03.015

74. Liedtke, A. J., Adeniji, A. O., Chen, M., Byrns, M. C., Jin, Y., Christianson, D. W., Marnett, L. J., & Penning, T. M. (2013). Development of potent and selective indomethacin analogues for the inhibition of AKR1C3 (type 5 17β-hydroxysteroid dehydrogenase/prostaglandin F synthase) in castrate-resistant prostate cancer [Article]. Journal of Medicinal Chemistry, 56(6), 2429-2446. https://doi.org/10.1021/jm3017656

75. Faraldos, J. A., Gonzalez, V., Li, A., Yu, F., Köksal, M., Christianson, D. W., & Allemann, R. K. (2012). Probing the mechanism of 1,4-conjugate elimination reactions catalyzed by terpene synthases [Article]. Journal of the American Chemical Society, 134(51), 20844-20848. https://doi.org/10.1021/ja311022s

76. D’Antonio, E. L., Hai, Y., & Christianson, D. W. (2012). Structure and function of non-native metal clusters in human arginase i [Article]. Biochemistry, 51(42), 8399-8409. https://doi.org/10.1021/bi301145n

77. Deardorff, M. A., Bando, M., Nakato, R., Watrin, E., Itoh, T., Minamino, M., Saitoh, K., Komata, M., Katou, Y., Clark, D., Cole, K. E., De Baere, E., Decroos, C., Di Donato, N., Ernst, S., Francey, L. J., Gyftodimou, Y., Hirashima, K., Hullings, M., . . . Shirahige, K. (2012). HDAC8 mutations in Cornelia de Lange syndrome affect the cohesin acetylation cycle [Article]. Nature, 489(7415), 313-317. https://doi.org/10.1038/nature11316

78. Dantonio, E. L., & Christianson, D. W. (2012). Binding of the unreactive substrate analog l-2-amino-3-guanidinopropionic acid (dinor-l-arginine) to human arginase I [Article]. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 68(8), 889-893. https://doi.org/10.1107/S1744309112027820

79. Chen, M., Adeniji, A. O., Twenter, B. M., Winkler, J. D., Christianson, D. W., & Penning, T. M. (2012). Crystal structures of AKR1C3 containing an N-(aryl)amino-benzoate inhibitor and a bifunctional AKR1C3 inhibitor and androgen receptor antagonist. Therapeutic leads for castrate resistant prostate cancer [Article]. Bioorganic and Medicinal Chemistry Letters, 22(10), 3492-3497. https://doi.org/10.1016/j.bmcl.2012.03.085

80. Chen, M., Drury, J. E., Christianson, D. W., & Penning, T. M. (2012). Conversion of human steroid 5β-reductase (AKR1D1) into 3β-hydroxysteroid dehydrogenase by single point mutation E120H: Example of perfect enzyme engineering [Article]. Journal of Biological Chemistry, 287(20), 16609-16622. https://doi.org/10.1074/jbc.M111.338780

81. Köksal, M., Chou, W. K. W., Cane, D. E., & Christianson, D. W. (2012). Structure of geranyl diphosphate C -methyltransferase from Streptomyces coelicolor and implications for the mechanism of isoprenoid modification [Article]. Biochemistry, 51(14), 3003-3010. https://doi.org/10.1021/bi300109c

82. Köksal, M., Chou, W. K. W., Cane, D. E., & Christianson, D. W. (2012). Structure of 2-methylisoborneol synthase from Streptomyces coelicolor and implications for the cyclization of a noncanonical C -methylated monoterpenoid substrate [Article]. Biochemistry, 51(14), 3011-3020. https://doi.org/10.1021/bi201827a

83. Lombardi, P. M., Cole, K. E., Dowling, D. P., & Christianson, D. W. (2011). Structure, mechanism, and inhibition of histone deacetylases and related metalloenzymes [Review]. Current Opinion in Structural Biology, 21(6), 735-743. https://doi.org/10.1016/j.sbi.2011.08.004

84. Ilies, M., Dowling, D. P., Lombardi, P. M., & Christianson, D. W. (2011). Synthesis of a new trifluoromethylketone analogue of l-arginine and contrasting inhibitory activity against human arginase i and histone deacetylase 8 [Article]. Bioorganic and Medicinal Chemistry Letters, 21(19), 5854-5858. https://doi.org/10.1016/j.bmcl.2011.07.100

85. D’Antonio, E. L., & Christianson, D. W. (2011). Crystal structures of complexes with cobalt-reconstituted human arginase i [Article]. Biochemistry, 50(37), 8018-8027. https://doi.org/10.1021/bi201101t

86. Cole, K. E., Dowling, D. P., Boone, M. A., Phillips, A. J., & Christianson, D. W. (2011). Structural basis of the antiproliferative activity of largazole, a depsipeptide inhibitor of the histone deacetylases [Article]. Journal of the American Chemical Society, 133(32), 12474-12477. https://doi.org/10.1021/ja205972n

87. Ilies, M., Di Costanzo, L., Dowling, D. P., Thorn, K. J., & Christianson, D. W. (2011). Binding of α,α-disubstituted amino acids to arginase suggests new avenues for inhibitor design [Article]. Journal of Medicinal Chemistry, 54(15), 5432-5443. https://doi.org/10.1021/jm200443b

88. Lombardi, P. M., Angell, H. D., Whittington, D. A., Flynn, E. F., Rajashankar, K. R., & Christianson, D. W. (2011). Structure of prokaryotic polyamine deacetylase reveals evolutionary functional relationships with eukaryotic histone deacetylases [Article]. Biochemistry, 50(11), 1808-1817. https://doi.org/10.1021/bi101859k

89. Cole, K. E., Gattis, S. G., Angell, H. D., Fierke, C. A., & Christianson, D. W. (2011). Structure of the metal-dependent deacetylase LpxC from Yersinia enterocolitica complexed with the potent inhibitor CHIR-090 [Article]. Biochemistry, 50(2), 258-265. https://doi.org/10.1021/bi101622a

90. Köksal, M., Jin, Y., Coates, R. M., Croteau, R., & Christianson, D. W. (2011). Taxadiene synthase structure and evolution of modular architecture in terpene biosynthesis [Article]. Nature, 469(7328), 116-122. https://doi.org/10.1038/nature09628

91. KÖksal, M., Hu, H., Coates, R. M., Peters, R. J., & Christianson, D. W. (2011). Structure and mechanism of the diterpene cyclase ent-copalyl diphosphate synthase [Article]. Nature Chemical Biology, 7(7), 431-433. https://doi.org/10.1038/nchembio.578

92. Aaron, J. A., & Christianson, D. W. (2010). Trinuclear metal clusters in catalysis by terpenoid synthases [Article]. Pure and Applied Chemistry, 82(8), 1585-1597. https://doi.org/10.1351/PAC-CON-09-09-37

93. Zakharian, T. Y., & Christianson, D. W. (2010). Design and synthesis of C60-benzenesulfonamide conjugates [Article]. Tetrahedron Letters, 51(28), 3645-3648. https://doi.org/10.1016/j.tetlet.2010.05.017

94. Dowling, D. P., Ilies, M., Olszewski, K. L., Portugal, S., Mota, M. M., Llinás, M., & Christianson, D. W. (2010). Crystal structure of arginase from plasmodium falciparum and implications for l -arginine depletion in malarial infection [Article]. Biochemistry, 49(26), 5600-5608. https://doi.org/10.1021/bi100390z

95. Smith Iii, A. B., Xiong, H., Charnley, A. K., Brenner, M., Mesaros, E. F., Kenesky, C. S., Di Costanzo, L., Christianson, D. W., & Hirschmann, R. (2010). Design, synthesis, and structural analysis of D, L -mixed polypyrrolinones. 2. Macrocyclic hexapyrrolinones [Article]. Organic Letters, 12(13), 2994-2997. https://doi.org/10.1021/ol101008y

96. Dowling, D. P., Gattis, S. G., Fierke, C. A., & Christianson, D. W. (2010). Structures of metal-substituted human histone deacetylase 8 provide mechanistic inferences on biological function [Article]. Biochemistry, 49(24), 5048-5056. https://doi.org/10.1021/bi1005046

97. Herbert, D. R., Orekov, T., Roloson, A., Ilies, M., Perkins, C., O’Brien, W., Cederbaum, S., Christianson, D. W., Zimmermann, N., Rothenberg, M. E., & Finkelman, F. D. (2010). Arginase I suppresses IL-12/IL-23p40-driven intestinal inflammation during acute schistosomiasis [Article]. Journal of Immunology, 184(11), 6438-6446. https://doi.org/10.4049/jimmunol.0902009

98. Ilies, M., Di Costanzo, L., North, M. L., Scott, J. A., & Christianson, D. W. (2010). 2-Aminoimidazole amino acids as inhibitors of the binuclear manganese metalloenzyme human arginase i [Article]. Journal of Medicinal Chemistry, 53(10), 4266-4276. https://doi.org/10.1021/jm100306a

99. Di Costanzo, L., Ilies, M., Thorn, K. J., & Christianson, D. W. (2010). Inhibition of human arginase I by substrate and product analogues [Article]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 496(2), 101-108. https://doi.org/10.1016/j.abb.2010.02.004

100. Aaron, J. A., Lin, X., Cane, D. E., & Christianson, D. W. (2010). Structure of epi-isozizaene synthase from streptomyces coelicolor A3(2), a platform for new terpenoid cyclization templates [Article]. Biochemistry, 49(8), 1787-1797. https://doi.org/10.1021/bi902088z

101. Köksal, M., Zimmer, I., Schnitzler, J. P., & Christianson, D. W. (2010). Structure of isoprene synthase illuminates the chemical mechanism of teragram atmospheric carbon emission [Article]. Journal of Molecular Biology, 402(2), 363-373. https://doi.org/10.1016/j.jmb.2010.07.009

102. Jae, H. K., Bugaj, L. J., Young, J. O., Bivalacqua, T. J., Ryoo, S., Soucy, K. G., Santhanam, L., Webb, A., Camara, A., Sikka, G., Nyhan, D., Shoukas, A. A., Ilies, M., Christianson, D. W., Champion, H. C., & Berkowitz, D. E. (2009). Arginase inhibition restores NOS coupling and reverses endothelial dysfunction and vascular stiffness in old rats [Article]. Journal of Applied Physiology, 107(4), 1249-1257. https://doi.org/10.1152/japplphysiol.91393.2008

103. Drury, J. E., Di Costanzo, L., Penning, T. M., & Christianson, D. W. (2009). Inhibition of human steroid 5β-reductase (AKR1D1) by finasteride and structure of the enzyme-inhibitor complex [Article]. Journal of Biological Chemistry, 284(30), 19786-19790. https://doi.org/10.1074/jbc.C109.016931

104. Gennadios, H. A., Gonzalez, V., Di Costanzo, L., Li, A., Yu, F., Miller, D. J., Allemann, R. K., & Christianson, D. W. (2009). Crystal structure of (+)-δ-cadinene synthase from Gossypium arboreum and evolutionary divergence of metal binding motifs for catalysis [Article]. Biochemistry, 48(26), 6175-6183. https://doi.org/10.1021/bi900483b

105. Di Costanzo, L., Drury, J. E., Christianson, D. W., & Penning, T. M. (2009). Structure and catalytic mechanism of human steroid 5β-reductase (AKR1D1) [Review]. Molecular and Cellular Endocrinology, 301(1-2), 191-198. https://doi.org/10.1016/j.mce.2008.09.013

106. Di Costanzo, L., Penning, T. M., & Christianson, D. W. (2009). Aldo-keto reductases in which the conserved catalytic histidine is substituted [Article]. Chemico-Biological Interactions, 178(1-3), 127-133. https://doi.org/10.1016/j.cbi.2008.10.046

107. Shishova, E. Y., Di Costanzo, L., Emig, F. A., Ash, D. E., & Christianson, D. W. (2009). Probing the specificity determinants of amino acid recognition by arginase [Article]. Biochemistry, 48(1), 121-131. https://doi.org/10.1021/bi801911v

108. Zakharian, T. Y., Di Costanzo, L., & Christianson, D. W. (2008). (S)-2-amino-6-nitrohexanoic acid binds to human arginase i through multiple nitro-metal coordination interactions in the binuclear manganese cluster [Article]. Journal of the American Chemical Society, 130(51), 17254-17255. https://doi.org/10.1021/ja807702q

109. Dowling, D. P., Gantt, S. L., Gattis, S. G., Fierke, C. A., & Christianson, D. W. (2008). Structural studies of human histone deacetylase 8 and its site-specific variants complexed with substrate and inhibitors [Article]. Biochemistry, 47(51), 13554-13563. https://doi.org/10.1021/bi801610c

110. Santhanam, L., Christianson, D. W., Nyhan, D., & Berkowitz, D. E. (2008). Arginase and vascular aging [Review]. Journal of Applied Physiology, 105(5), 1632-1642. https://doi.org/10.1152/japplphysiol.90627.2008

111. Dowling, D. P., Di Costanzo, L., Gennadios, H. A., & Christianson, D. W. (2008). Evolution of the arginase fold and functional diversity [Review]. Cellular and Molecular Life Sciences, 65(13), 2039-2055. https://doi.org/10.1007/s00018-008-7554-z

112. Di Costanzo, L., Drury, J. E., Penning, T. M., & Christianson, D. W. (2008). Crystal structure of human liver Δ4-3-ketosteroid 5β-reductase (AKR1D1) and implications for substrate binding and catalysis [Article]. Journal of Biological Chemistry, 283(24), 16830-16839. https://doi.org/10.1074/jbc.M801778200

113. Aaron, J. A., Chambers, J. M., Jude, K. M., Di Costanzo, L., Dmochowski, I. J., & Christianson, D. W. (2008). Structure of a 129Xe-cryptophane biosensor complexed with human carbonic anhydrase II [Article]. Journal of the American Chemical Society, 130(22), 6942-6943. https://doi.org/10.1021/ja802214x

114. Shishova, E. Y., Yu, F., Miller, D. J., Faraldos, J. A., Zhao, Y., Coates, R. M., Allemann, R. K., Cane, D. E., & Christianson, D. W. (2008). X-ray crystallographic studies of substrate binding to aristolochene synthase suggest a metal ion binding sequence for catalysis [Article]. Journal of Biological Chemistry, 283(22), 15431-15439. https://doi.org/10.1074/jbc.M800659200

115. Christianson, D. W. (2008). Unearthing the roots of the terpenome [Review]. Current Opinion in Chemical Biology, 12(2), 141-150. https://doi.org/10.1016/j.cbpa.2007.12.008

116. Ryoo, S., Gupta, G., Benjo, A., Lim, H. K., Camara, A., Sikka, G., Lim, H. K., Sohi, J., Santhanam, L., Soucy, K., Tuday, E., Baraban, E., Ilies, M., Gerstenblith, G., Nyhan, D., Shoukas, A., Christianson, D. W., Alp, N. J., Champion, H. C., . . . Berkowitz, D. E. (2008). Endothelial arginase II: A novel target for the treatment of atherosclerosis [Article]. Circulation Research, 102(8), 923-932. https://doi.org/10.1161/CIRCRESAHA.107.169573

117. Vedula, L. S., Jiang, J., Zakharian, T., Cane, D. E., & Christianson, D. W. (2008). Structural and mechanistic analysis of trichodiene synthase using site-directed mutagenesis: Probing the catalytic function of tyrosine-295 and the asparagine-225/serine-229/glutamate-233-Mg2 +B motif [Article]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 469(2), 184-194. https://doi.org/10.1016/j.abb.2007.10.015

118. Zakharian, T. Y., Di Costanzo, L., & Christianson, D. W. (2008). Synthesis of (2S)-2-amino-7,8-epoxyoctanoic acid and structure of its metal-bridging complex with human arginase i [Article]. Organic and Biomolecular Chemistry, 6(18), 3240-3243. https://doi.org/10.1039/b811797g

119. Vedula, L. S., Zhao, Y., Coates, R. M., Koyama, T., Cane, D. E., & Christianson, D. W. (2007). Exploring biosynthetic diversity with trichodiene synthase [Article]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 466(2), 260-266. https://doi.org/10.1016/j.abb.2007.06.016

120. Santhanam, L., Lim, H. K., Lim, H. K., Miriel, V., Brown, T., Patel, M., Balanson, S., Ryoo, S., Anderson, M., Irani, K., Khanday, F., Di Costanzo, L., Nyhan, D., Hare, J. M., Christianson, D. W., Rivers, R., Shoukas, A., & Berkowitz, D. E. (2007). Inducible NO synthase-dependent S-nitrosylation and activation of arginase1 contribute to age-related endothelial dysfunction [Article]. Circulation Research, 101(7), 692-702. https://doi.org/10.1161/CIRCRESAHA.107.157727

121. Di Costanzo, L., Moulin, M., Haertlein, M., Meilleur, F., & Christianson, D. W. (2007). Expression, purification, assay, and crystal structure of perdeuterated human arginase I [Article]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 465(1), 82-89. https://doi.org/10.1016/j.abb.2007.04.036

122. Di Costanzo, L., Pique, M. E., & Christianson, D. W. (2007). Crystal structure of human arginase I complexed with thiosemicarbazide reveals an unusual thiocarbonyl μ-sulfide ligand in the binuclear manganese cluster [Article]. Journal of the American Chemical Society, 129(20), 6388-6389. https://doi.org/10.1021/ja071567j

123. Srivastava, D. K., Jude, K. M., Banerjee, A. L., Haldar, M., Manokaran, S., Kooren, J., Mallik, S., & Christianson, D. W. (2007). Structural analysis of charge discrimination in the binding of inhibitors to human carbonic anhydrases I and II [Article]. Journal of the American Chemical Society, 129(17), 5528-5537. https://doi.org/10.1021/ja068359w

124. Christianson, D. W. (2007). Roots of biosynthetic diversity [Short Survey]. Science, 316(5821), 60-61. https://doi.org/10.1126/science.1141630

125. Shin, H., Gennadios, H. A., Whittington, D. A., & Christianson, D. W. (2007). Amphipathic benzoic acid derivatives: Synthesis and binding in the hydrophobic tunnel of the zinc deacetylase LpxC [Article]. Bioorganic and Medicinal Chemistry, 15(7), 2617-2623. https://doi.org/10.1016/j.bmc.2007.01.044

126. Shishova, E. Y., Di Costanzo, L., Cane, D. E., & Christianson, D. W. (2007). X-ray crystal structure of aristolochene syrithase from Aspergillus terreus and evolution of templates for the cyclization of farnesyl biphosphate [Article]. Biochemistry, 46(7), 1941-1951. https://doi.org/10.1021/bi0622524

127. Di Costanzo, L., Gomez, G. A., & Christianson, D. W. (2007). Crystal Structure of Lactaldehyde Dehydrogenase from Escherichia coli and Inferences Regarding Substrate and Cofactor Specificity [Article]. Journal of Molecular Biology, 366(2), 481-493. https://doi.org/10.1016/j.jmb.2006.11.023

128. Krishnamurthy, V. M., Bohall, B. R., Kim, C. Y., Moustakas, D. T., Christianson, D. W., & Whitesides, G. M. (2007). Thermodynamic parameters for the association of fluorinated benzenesulfonamides with bovine carbonic anhydrase II [Article]. Chemistry – An Asian Journal, 2(1), 94-105. https://doi.org/10.1002/asia.200600360

129. De Vivo, M., Ensing, B., Dal Peraro, M., Gomez, G. A., Christianson, D. W., & Klein, M. L. (2007). Proton shuttles and phosphatase activity in soluble epoxide hydrolase [Article]. Journal of the American Chemical Society, 129(2), 387-394. https://doi.org/10.1021/ja066150c

130. Gennadios, H. A., & Christianson, D. W. (2006). Binding of uridine 5′-diphosphate in the “basic patch” of the zinc deacetylase LpxC and implications for substrate binding [Article]. Biochemistry, 45(51), 15216-15223. https://doi.org/10.1021/bi0619021

131. Di Costanzo, L., Flores Jr, L. V., & Christianson, D. W. (2006). Stereochemistry of guanidine-metal interactions: Implications for L-arginine-metal interactions in protein structure and function [Article]. Proteins: Structure, Function and Genetics, 65(3), 637-642. https://doi.org/10.1002/prot.21127

132. Christianson, D. W. (2006). Structural biology and chemistry of the terpenoid cyclases [Article]. Chemical Reviews, 106(8), 3412-3442. https://doi.org/10.1021/cr050286w

133. Gennadios, H. A., Whittington, D. A., Li, X., Fierke, C. A., & Christianson, D. W. (2006). Mechanistic inferences from the binding of ligands to LpxC, a metal-dependent deacetylase [Article]. Biochemistry, 45(26), 7940-7948. https://doi.org/10.1021/bi060823m

134. Christianson, D. W. (2006). Five golden rings [Review]. Science, 311(5766), 1382-1383. https://doi.org/10.1126/science.1125298

135. Jude, K. M., Banerjee, A. L., Haldar, M. K., Manokaran, S., Roy, B., Mallik, S., Srivastava, D. K., & Christianson, D. W. (2006). Ultrahigh resolution crystal structures of human carbonic anhydrases I and II complexed with “two-prong” inhibitors reveal the molecular basis of high affinity [Article]. Journal of the American Chemical Society, 128(9), 3011-3018. https://doi.org/10.1021/ja057257n

136. Gomez, G. A., Morisseau, C., Hammock, B. D., & Christianson, D. W. (2006). Human soluble epoxide hydrolase: Structural basis of inhibition by 4-(3-cyclohexylureido)-carboxylic acids [Article]. Protein Science, 15(1), 58-64. https://doi.org/10.1110/ps.051720206

137. Colleluori, D. M., Reczkowski, R. S., Emig, F. A., Cama, E., Cox, J. D., Scolnick, L. R., Compher, K., Jude, K., Han, S., Viola, R. E., Christianson, D. W., & Ash, D. E. (2005). Probing the role of the hyper-reactive histidine residue of arginase [Article]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 444(1), 15-26. https://doi.org/10.1016/j.abb.2005.09.009

138. Vedula, L. S., Cane, D. E., & Christianson, D. W. (2005). Role of arginine-304 in the diphosphate-triggered active site closure mechanism of trichodiene synthase [Article]. Biochemistry, 44(38), 12719-12727. https://doi.org/10.1021/bi0510476

139. Di Costanzo, L., Sabio, G., Mora, A., Rodriguez, P. C., Ochoa, A. C., Centeno, F., & Christianson, D. W. (2005). Crystal structure of human arginase I at 1.29-Å resolution and exploration of inhibition in the immune response [Article]. Proceedings of the National Academy of Sciences of the United States of America, 102(37), 13058-13063. https://doi.org/10.1073/pnas.0504027102

140. Hernick, M., Gennadios, H. A., Whittington, D. A., Rusche, K. M., Christianson, D. W., & Fierke, C. A. (2005). UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism [Article]. Journal of Biological Chemistry, 280(17), 16969-16978. https://doi.org/10.1074/jbc.M413560200

141. Vedula, L. S., Rynkiewicz, M. J., Pyun, H. J., Coates, R. M., Cane, D. E., & Christianson, D. W. (2005). Molecular recognition of the substrate diphosphate group governs product diversity in trichodiene synthase mutants [Article]. Biochemistry, 44(16), 6153-6163. https://doi.org/10.1021/bi050059o

142. Christianson, D. W. (2005). Arginase: Structure, mechanism, and physiological role in male and female sexual arousal [Article]. Accounts of Chemical Research, 38(3), 191-201. https://doi.org/10.1021/ar040183k

143. Shin, H., Cama, E., & Christianson, D. W. (2004). Design of amino acid aldehydes as transition-state analogue inhibitors of arginase [Article]. Journal of the American Chemical Society, 126(33), 10278-10284. https://doi.org/10.1021/ja047788w

144. Cama, E., Pethe, S., Boucher, J. L., Han, S., Emig, F. A., Ash, D. E., Viola, R. E., Mansuy, D., & Christianson, D. W. (2004). Inhibitor coordination interactions in the binuclear manganese cluster of arginase [Article]. Biochemistry, 43(28), 8987-8999. https://doi.org/10.1021/bi0491705

145. Gomez, G. A., Morisseau, C., Hammock, B. D., & Christianson, D. W. (2004). Structure of Human Epoxide Hydrolase Reveals Mechanistic Inferences on Bifunctional Catalysis in Epoxide and Phosphate Ester Hydrolysis [Article]. Biochemistry, 43(16), 4716-4723. https://doi.org/10.1021/bi036189j

146. Whittington, D. A., Grubb, J. H., Waheed, A., Shah, G. N., Sly, W. S., & Christianson, D. W. (2004). Expression, assay, and structure of the extracellular domain of murine carbonic anhydrase XIV: Implications for selective inhibition of membrane-associated isozymes [Article]. Journal of Biological Chemistry, 279(8), 7223-7228. https://doi.org/10.1074/jbc.M310809200

147. Kim, N. N., Christianson, D. W., & Traish, A. M. (2004). Role of arginase in the male and female sexual arousal response [Conference Paper]. Journal of Nutrition, 134(10 SUPPL.), 2873S-2879S. https://doi.org/10.1093/jn/134.10.2873s

148. Cama, E., Shin, H., & Christianson, D. W. (2003). Design of Amino Acid Sulfonamides as Transition-State Analogue Inhibitors of Arginase [Article]. Journal of the American Chemical Society, 125(43), 13052-13057. https://doi.org/10.1021/ja036365b

149. Xu, L., Hilliard, B., Carmody, R. J., Tsabary, G., Shin, H., Christianson, D. W., & Chen, Y. H. (2003). Arginase and autoimmune inflammation in the central nervous system [Article]. Immunology, 110(1), 141-148. https://doi.org/10.1046/j.1365-2567.2003.01713.x

150. Cama, E., Colleluori, D. M., Emig, F. A., Shin, H., Kim, S. W., Kim, N. N., Traish, A. M., Ash, D. E., & Christianson, D. W. (2003). Human arginase II: Crystal structure and physiological role in male and female sexual arousal [Article]. Biochemistry, 42(28), 8445-8451. https://doi.org/10.1021/bi034340j

151. Whittington, D. A., Rusche, K. M., Shin, H., Fierke, C. A., & Christianson, D. W. (2003). Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis [Article]. Proceedings of the National Academy of Sciences of the United States of America, 100(14), 8146-8150. https://doi.org/10.1073/pnas.1432990100

152. Cama, E., Emig, F. A., Ash, D. E., & Christianson, D. W. (2003). Structural and functional importance of first-shell metal ligands in the binuclear manganese cluster of arginase I [Article]. Biochemistry, 42(25), 7748-7758. https://doi.org/10.1021/bi030074y

153. Whittington, D. A., Wise, M. L., Urbansky, M., Coates, R. M., Croteau, R. B., & Christianson, D. W. (2002). Bornyl diphosphate synthase: Structure and strategy for carbocation manipulation by a terpenoid cyclase [Article]. Proceedings of the National Academy of Sciences of the United States of America, 99(24), 15375-15380. https://doi.org/10.1073/pnas.232591099

154. Seemann, M., Zhai, G., De Kraker, J. W., Paschall, C. M., Christianson, D. W., & Cane, D. E. (2002). Pentalenene synthase. Analysis of active site residues by site-directed mutagenesis [Article]. Journal of the American Chemical Society, 124(26), 7681-7689. https://doi.org/10.1021/ja026058q

155. Jude, K. M., Wright, S. K., Tu, C., Silverman, D. N., Viola, R. E., & Christianson, D. W. (2002). Crystal structure of F65A/Y131C-methylimidazole carbonic anhydrase V reveals architectural features of an engineered proton shuttle [Article]. Biochemistry, 41(8), 2485-2491. https://doi.org/10.1021/bi015808q

156. Kim, C. Y., Whittington, D. A., Chang, J. S., Liao, J., May, J. A., & Christianson, D. W. (2002). Structural aspects of isozyme selectivity in the binding of inhibitors to carbonic anhydrases II and IV [Article]. Journal of Medicinal Chemistry, 45(4), 888-893. https://doi.org/10.1021/jm010163d

157. Rynkiewicz, M. J., Cane, D. E., & Christianson, D. W. (2002). X-ray crystal structures of D100E trichodiene synthase and its pyrophosphate complex reveal the basis for terpene product diversity [Article]. Biochemistry, 41(6), 1732-1741. https://doi.org/10.1021/bi011960g

158. Grzybowski, B. A., Ishchenko, A. V., Kim, C. Y., Topalov, G., Chapman, R., Christianson, D. W., Whitesides, G. M., & Shakhnovich, E. I. (2002). Combinatorial computational method gives new picomolar ligands for a known enzyme [Article]. Proceedings of the National Academy of Sciences of the United States of America, 99(3), 1270-1273. https://doi.org/10.1073/pnas.032673399

159. Madder, R. D., Kim, C. Y., Chandra, P. P., Doyon, J. B., Baird Jr, T. A., Fierke, C. A., Christianson, D. W., Voet, J. G., & Jain, A. (2002). Twisted amides inferred from QSAR analysis of hydrophobicity and electronic effects on the affinity of fluoroaromatic inhibitors of carbonic anhydrase [Article]. Journal of Organic Chemistry, 67(2), 582-584. https://doi.org/10.1021/jo0159385

160. Rynkiewicz, M. J., Cane, D. E., & Christianson, D. W. (2001). Structure of trichodiene synthase from Fusarium sporotrichioides provides mechanistic inferences on the terpene cyclization cascade [Article]. Proceedings of the National Academy of Sciences of the United States of America, 98(24), 13543-13548. https://doi.org/10.1073/pnas.231313098

161. Kim, C. Y., Chandra, P. P., Jain, A., & Christianson, D. W. (2001). Fluoroaromatic – Fluoroaromatic interactions between inhibitors bound in the crystal lattice of human carbonic anhydrase II [Article]. Journal of the American Chemical Society, 123(39), 9620-9627. https://doi.org/10.1021/ja011034p

162. Whittington, D. A., Waheed, A., Ulmasov, B., Shah, G. N., Grubb, J. H., Sly, W. S., & Christianson, D. W. (2001). Crystal structure of the dimeric extracellular domain of human carbonic anhydrase XII, a bitopic membrane protein overexpressed in certain cancer tumor cells [Article]. Proceedings of the National Academy of Sciences of the United States of America, 98(17), 9545-9550. https://doi.org/10.1073/pnas.161301298

163. Lavulo, L. T., Sossong Jr, T. M., Brigham-Burke, M. R., Doyle, M. L., Cox, J. D., Christianson, D. W., & Ash, D. E. (2001). Subunit-subunit interactions in trimeric arginase. Generation of active monomers by mutation of a single amino acid [Article]. Journal of Biological Chemistry, 276(17), 14242-14248. https://doi.org/10.1074/jbc.M010575200

164. Cox, J. D., Cama, E., Colleluori, D. M., Pethe, S., Boucher, J. L., Mansuy, D., Ash, D. E., & Christianson, D. W. (2001). Mechanistic and metabolic inferences from the binding of substrate analogues and products to arginase [Article]. Biochemistry, 40(9), 2689-2701. https://doi.org/10.1021/bi002318+

165. Kim, N. N., Cox, J. D., Baggio, R. F., Emig, F. A., Mistry, S. K., Harper, S. L., Speicher, D. W., Morris Jr, S. M., Ash, D. E., Traish, A., & Christianson, D. W. (2001). Probing erectile function: S-(2-boronoethyl)-L-cysteine binds to arginase as a transition state analogue and enhances smooth muscle relaxation in human penile corpus cavernosum [Article]. Biochemistry, 40(9), 2678-2688. https://doi.org/10.1021/bi002317h

166. Kim, C. Y., Chang, J. S., Doyon, J. B., Baird Jr, T. T., Fierke, C. A., Jain, A., & Christianson, D. W. (2000). Contribution of fluorine to protein – Ligand affinity in the binding of fluoroaromatic inhibitors to carbonic anhydrase II [Article]. Journal of the American Chemical Society, 122(49), 12125-12134. https://doi.org/10.1021/ja002627n

167. Wendt, K. U., Poralla, K., Shulz, G. E., Starks, C. M., Bock, K., Chappell, J., Noel, J., Zhai, G., Cane, D. E., & Christianson, D. W. (2000). Structures of enzymes involved in terpenoid biosynthesis [Article]. Chemtracts, 13(13), 844-852. https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034493550&partnerID=40&md5=23180356154ee74a15aacd7520d5e267

168. Cox, J. D., Hunt, J. A., Compher, K. M., Fierke, C. A., & Christianson, D. W. (2000). Structural influence of hydrophobic core residues on metal binding and specificity in carbonic anhydrase II [Article]. Biochemistry, 39(45), 13687-13694. https://doi.org/10.1021/bi001649j

169. Caruthers, J. M., Kang, I., Rynkiewicz, M. J., Cane, D. E., & Christianson, D. W. (2000). Crystal structure determination of aristolochene synthase from the blue cheese mold, Penicillium roqueforti [Article]. Journal of Biological Chemistry, 275(33), 25533-25539. https://doi.org/10.1074/jbc.M000433200

170. Yamada, T., Morisseau, C., Maxwell, J. E., Argiriadi, M. A., Christianson, D. W., & Hammock, B. D. (2000). Biochemical evidence for the involvement of tyrosine in epoxide activation during the catalytic cycle of epoxide hydrolase [Article]. Journal of Biological Chemistry, 275(30), 23082-23088. https://doi.org/10.1074/jbc.M001464200

171. Argiriadi, M. A., Morisseau, C., Goodrow, M. H., Dowdy, D. L., Hammock, B. D., & Christianson, D. W. (2000). Binding of alkylurea inhibitors to epoxide hydrolase implicates active site tyrosines in substrate activation [Article]. Journal of Biological Chemistry, 275(20), 15265-15270. https://doi.org/10.1074/jbc.M000278200

172. Doyon, J. B., Hansen, E. A. M., Kim, C. H., Chang, J. S., Christianson, D. W., Madder, R. D., Voet, J. G., Baird Jr, T. A., Fierke, C. A., & Jain, A. (2000). Linear free energy relationships implicate three modes of binding for fluoroaromatic inhibitors to a mutant of carbonic anhydrase II [Article]. Organic Letters, 2(9), 1189-1192. https://doi.org/10.1021/ol005608r

173. Stams, T., & Christianson, D. W. (2000). X-ray crystallographic studies of mammalian carbonic anhydrase isozymes [Review]. EXS(90), 159-174. https://doi.org/10.1007/978-3-0348-8446-4_9

174. Hunt, J. A., Lesburg, C. A., Christianson, D. W., Thompson, R. B., & Fierke, C. A. (2000). Active-site engineering of carbonic anhydrase and its application to biosensors [Review]. EXS(90), 221-240. https://doi.org/10.1007/978-3-0348-8446-4_12

175. Ash, D. E., Cox, J. D., & Christianson, D. W. (2000). Arginase: a binuclear manganese metalloenzyme [Review]. Metal ions in biological systems, 37, 407-428. https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033631648&partnerID=40&md5=97e3503f0af20b84362d3535043f94bd

176. Baggio, R., Cox, J. D., Harper, S. L., Speicher, D. W., & Christianson, D. W. (1999). A new chromophoric assay for arginase activity [Article]. Analytical Biochemistry, 276(2), 251-253. https://doi.org/10.1006/abio.1999.4355

177. Christianson, D. W., & Cox, J. D. (1999). Catalysis by metal-activated hydroxide in zinc and manganese metalloenzymes. In Annual Review of Biochemistry (Vol. 68, pp. 33-57).

178. Argiriadi, M. A., Morisseau, C., Hammock, B. D., & Christianson, D. W. (1999). Detoxification of environmental mutagens and carcinogens: Structure, mechanism, and evolution of liver epoxide hydrolase [Article]. Proceedings of the National Academy of Sciences of the United States of America, 96(19), 10637-10642. https://doi.org/10.1073/pnas.96.19.10637

179. Baggio, R., Emig, F. A., Christianson, D. W., Ash, D. E., Chakder, S., & Rattan, S. (1999). Biochemical and functional profile of a newly developed potent and isozyme-selective arginase inhibitor [Article]. Journal of Pharmacology and Experimental Therapeutics, 290(3), 1409-1416. https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032797908&partnerID=40&md5=176a81fa7304527a589f450e4cbc254d

180. Paschall, C. M., Hasserodt, J., Jones, T., Lerner, R. A., Janda, K. D., & Christianson, D. W. (1999). Convergence of catalytic antibody and terpene cyclase mechanisms: Polyene cyclization directed by carbocation – π interactions [Article]. Angewandte Chemie – International Edition, 38(12), 1743-1747. https://doi.org/10.1002/(SICI)1521-3773(19990614)38:12<1743::AID-ANIE1743>3.0.CO;2-3

181. Cox, J. D., Kim, N. N., Traish, A. M., & Christianson, D. W. (1999). Arginase-boronic acid complex highlights a physiological role in erectile function [Article]. Nature Structural Biology, 6(11), 1043-1047. https://doi.org/10.1038/14929

182. Niranjanakumari, S., Stams, T., Crary, S. M., Christianson, D. W., & Fierke, C. A. (1998). Protein component of the ribozyme ribonuclease P alters substrate recognition by directly contacting precursor tRNA [Article]. Proceedings of the National Academy of Sciences of the United States of America, 95(26), 15212-15217. https://doi.org/10.1073/pnas.95.26.15212

183. Green, N., Houk, K. N., Shulz, G. E., Back, K., Chappell, J., Noel, J., Zhai, G., Cane, D. E., & Christianson, D. W. (1998). Structures of enzymes involved in terpenoid biosynthesis [Note]. Chemtracts, 11(7), 537-545. https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031725718&partnerID=40&md5=319074afe41495d24409d3367b984a91

184. Stams, T., Niranjanakumari, S., Fierke, C. A., & Christianson, D. W. (1998). Ribonuclease P protein structure: Evolutionary origins in the translational apparatus [Article]. Science, 280(5364), 752-755. https://doi.org/10.1126/science.280.5364.752

185. Lukacs, C. M., Rubin, H., & Christianson, D. W. (1998). Engineering an anion-binding cavity in antichymotrypsin modulates the ‘spring-loaded’ serpin-protease interaction [Article]. Biochemistry, 37(10), 3297-3304. https://doi.org/10.1021/bi972359e

186. Lesburg, C. A., Caruthers, J. M., Paschall, C. M., & Christianson, D. W. (1998). Managing and manipulating carbocations in biology: Terpenoid cyclase structure and mechanism [Article]. Current Opinion in Structural Biology, 8(6), 695-703. https://doi.org/10.1016/S0959-440X(98)80088-2

187. Stams, T., Chen, Y., Boriack-Sjodin, P. A., Hurt, J. D., Liao, J., May, J. A., Dean, T., Laipis, P., Silverman, D. N., & Christianson, D. W. (1998). Structures of murine carbonic anhydrase IV and human carbonic anhydrase II complexed with brinzolamide: Molecular basis of isozyme-drug discrimination [Article]. Protein Science, 7(3), 556-563. https://doi.org/10.1002/pro.5560070303

188. Ash, D. E., Scolnick, L. R., Kanyo, Z. F., Vockley, J. G., Cederbaum, S. D., & Christianson, D. W. (1998). Molecular basis of hyperargininemia: Structure-function consequences of mutations in human liver arginase [Article]. Molecular Genetics and Metabolism, 64(4), 243-249. https://doi.org/10.1006/mgme.1998.2677

189. Boriack-Sjodin, P. A., Zeitlin, S., Chen, H. H., Crenshaw, L., Gross, S., Dantanarayana, A., Delgado, P., May, J. A., Dean, T., & Christianson, D. W. (1998). Structural analysis of inhibitor binding to human carbonic anhydrase II [Article]. Protein Science, 7(12), 2483-2489. https://doi.org/10.1002/pro.5560071201

190. Lesburg, C. A., Huang, C. C., Christianson, D. W., & Fierke, C. A. (1997). Histidine → carboxamide ligand substitutions in the zinc binding site of carbonic anhydrase II alter metal coordination geometry but retain catalytic activity [Article]. Biochemistry, 36(50), 15780-15791. https://doi.org/10.1021/bi971296x

191. Lesburg, C. A., Zhai, G., Cane, D. E., & Christianson, D. W. (1997). Crystal structure of pentalenene synthase: Mechanistic insights on terpenoid cyclization reactions in biology [Article]. Science, 277(5333), 1820-1824. https://doi.org/10.1126/science.277.5333.1820

192. Scolnick, L. R., Kanyo, Z. F., Cavalli, R. C., Ash, D. E., & Christianson, D. W. (1997). Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function [Article]. Biochemistry, 36(34), 10558-10565. https://doi.org/10.1021/bi970800v

193. Christianson, D. W. (1997). Structural chemistry and biology of manganese metalloenzymes [Review]. Progress in Biophysics and Molecular Biology, 67(2-3), 217-243. https://doi.org/10.1016/S0079-6107(97)88477-5

194. Scolnick, L. R., Clements, A. M., Liao, J., Crenshaw, L., Hellberg, M., May, J., Dean, T. R., & Christianson, D. W. (1997). Novel binding mode of hydroxamate inhibitors to human carbonic anhydrase II [Article]. Journal of the American Chemical Society, 119(4), 850-851. https://doi.org/10.1021/ja963832z

195. Baggio, R., Elbaum, D., Kanyo, Z. F., Carroll, P. J., Cavalli, R. C., Ash, D. E., & Christianson, D. W. (1997). Inhibition of Mn2+2-arginase by borate leads to the design of a transition state analogue inhibitor, 2(S)-amino-6-boronohexanoic acid [Article]. Journal of the American Chemical Society, 119(34), 8107-8108. https://doi.org/10.1021/ja971312d

196. Scolnick, L. R., & Christianson, D. W. (1996). X-ray crystallographic studies of alanine-65 variants of carbonic anhydrase II reveal the structural basis of compromised proton transfer in catalysis [Article]. Biochemistry, 35(51), 16429-16434. https://doi.org/10.1021/bi9617872

197. Stams, T., Nair, S. K., Okuyama, T., Waheed, A., Sly, W. S., & Christianson, D. W. (1996). Crystal structure of the secretory form of membrane-associated human carbonic anhydrase IV at 2.8-Å resolution [Article]. Proceedings of the National Academy of Sciences of the United States of America, 93(24), 13589-13594. https://doi.org/10.1073/pnas.93.24.13589

198. Kanyo, Z. F., Scolnick, L. R., Ash, D. E., & Christianson, D. W. (1996). Structure of a unique binuclear manganese cluster in arginase [Article]. Nature, 383(6600), 554-557. https://doi.org/10.1038/383554a0

199. Lukacs, C. M., Zhong, J. Q., Plotnick, M. I., Rubin, H., Cooperman, B. S., & Christianson, D. W. (1996). Arginine substitutions in the hinge region of antichymotrypsin affect serpin β-sheet rearrangement [Review]. Nature Structural Biology, 3(10), 888-893. https://doi.org/10.1038/nsb1096-888

200. Heck, R. W., Ann Boriack-Sjodin, P., Qian, M., Tu, C., Christianson, D. W., Laipis, P. J., & Silverman, D. N. (1996). Structure-based design of an intramolecular proton transfer site in murine carbonic anhydrase V [Article]. Biochemistry, 35(36), 11605-11611. https://doi.org/10.1021/bi9608018

201. Elbaum, D., Nair, S. K., Patchan, M. W., Thompson, R. B., & Christianson, D. W. (1996). Structure-based design of a sulfonamide probe for fluorescence anisotropy detection of zinc with a carbonic anhydrase-based biosensor [Article]. Journal of the American Chemical Society, 118(35), 8381-8387. https://doi.org/10.1021/ja954102e

202. Stavridi, E. S., O’Malley, K., Lukacs, C. M., Moore, W. T., Lambris, J. D., Christianson, D. W., Rubin, H., & Cooperman, B. S. (1996). Structural change in α-chymotrypsin induced by complexation with α1- antichymotrypsin as seen by enhanced sensitivity to proteolysis [Article]. Biochemistry, 35(33), 10608-10615. https://doi.org/10.1021/bi9605806

203. Huang, C. C., Lesburg, C. A., Kiefer, L. L., Fierke, C. A., & Christianson, D. W. (1996). Reversal of the hydrogen bond to zinc ligand histidine-119 dramatically diminishes catalysis and enhances metal equilibration kinetics in carbonic anhydrase II [Article]. Biochemistry, 35(11), 3439-3446. https://doi.org/10.1021/bi9526692

204. Nair, S. K., Elbaum, D., & Christianson, D. W. (1996). Unexpected binding mode of the sulfonamide fluorophore 5-Dimethylamino-1-naphthalene sulfonamide to human carbonic anhydrase II Implications for the development of a zinc biosensor [Article]. Journal of Biological Chemistry, 271(2), 1003-1007. https://doi.org/10.1074/jbc.271.2.1003

205. Lukacs, C. M., & Christianson, D. W. (1996). Is the binding of β-amyloid protein to antichymotrypsin in Alzheimer plaques mediated by a β-strand insertion? [Article]. Proteins: Structure, Function and Genetics, 25(4), 420-424. https://doi.org/10.1002/prot.2

206. Thompson, R. B., Ge, Z., Patchan, M. W., Fierke, C. A., McCall, K. A., Elbaum, D., & Christianson, D. W. (1996). Determination of multiple analytes using a fiber optic biosensor based on fluorescence energy transfer. Proceedings of SPIE – The International Society for Optical Engineering,

207. Christianson, D. W., & Fierke, C. A. (1996). Carbonic Anhydrase: Evolution of the Zinc Binding Site by Nature and by Design [Article]. Accounts of Chemical Research, 29(7), 331-339. https://doi.org/10.1021/ar9501232

208. Boriack-Sjodin, P. A., Heck, R. W., Laipis, P. J., Silverman, D. N., & Christianson, D. W. (1995). Structure determination of murine mitochondrial carbonic anhydrase V at 2.45-Å resolution: Implications for catalytic proton transfer and inhibitor design [Article]. Proceedings of the National Academy of Sciences of the United States of America, 92(24), 10949-10953. https://doi.org/10.1073/pnas.92.24.10949

209. Ippolito, J. A., Nair, S. K., Alexander, R. S., Kiefer, L. L., Fierke, C. A., & Christianson, D. W. (1995). Structure of His94→Asp carbonic anhydrase II in a new crystalline form reveals a partially occupied zinc binding site [Article]. Protein Engineering, Design and Selection, 8(10), 975-980. https://doi.org/10.1093/protein/8.10.975

210. Nair, S. K., Christianson, D. W., Krebs, J. F., & Fierke, C. A. (1995). Structural Basis of Inhibitor Affinity to Variants of Human Carbonic Anhydrase II [Article]. Biochemistry, 34(12), 3981-3989. https://doi.org/10.1021/bi00012a016

211. Katz, D. S., & Christianson, D. W. (1995). Structural aspects of the serpin reaction coordinate [Article]. Perspectives in Drug Discovery and Design, 2(3), 459-474. https://doi.org/10.1007/BF02172038

212. Boriack, P. A., Christianson, D. W., Kingery-Wood, J., & Whitesides, G. M. (1995). Secondary Interactions Significantly Removed from the Sulfonamide Binding Pocket of Carbonic Anhydrase II Influence Inhibitor Binding Constants [Article]. Journal of Medicinal Chemistry, 38(13), 2286-2291. https://doi.org/10.1021/jm00013a004

213. Ippolito, J. A., Baird Jr, T. T., McGee, S. A., Christianson, D. W., & Fierke, C. A. (1995). Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity [Article]. Proceedings of the National Academy of Sciences of the United States of America, 92(11), 5017-5021. https://doi.org/10.1073/pnas.92.11.5017

214. Lesburg, C. A., Lloyd, M. D., Cane, D. E., & Christianson, D. W. (1995). Crystallization and preliminary X‐ray diffraction analysis of recombinant pentalenene synthase [Article]. Protein Science, 4(11), 2436-2438. https://doi.org/10.1002/pro.5560041124

215. Lesburg, C. A., & Christianson, D. W. (1995). X-ray Crystallographic Studies of Engineered Hydrogen Bond Networks in a Protein–Zinc Binding Site [Article]. Journal of the American Chemical Society, 117(26), 6838-6844. https://doi.org/10.1021/ja00131a005

216. Katz, D. S., White, S. P., Huang, W., Kumar, R., & Christianson, D. W. (1994). Structure determination of aquomet porcine hemoglobin at 2.8 Å resolution [Article]. Journal of Molecular Biology, 244(5), 541-553. https://doi.org/10.1006/jmbi.1994.1751

217. Ippolito, J. A., & Christianson, D. W. (1994). Structural Consequences of Redesigning a Protein-Zinc Binding Site [Article]. Biochemistry, 33(51), 15241-15249. https://doi.org/10.1021/bi00255a004

218. Buna, A. M. C., Alexander, R. S., & Christianson, D. W. (1994). Mapping Protein-Peptide Affinity: Binding of Peptidylsulfonamide Inhibitors to Human Carbonic Anhydrase II [Article]. Journal of the American Chemical Society, 116(12), 5063-5068. https://doi.org/10.1021/ja00091a006

219. Jain, A., Whitesides, G. M., Alexander, R. S., & Christianson, D. W. (1994). Identification of Two Hydrophobic Patches in the Active-Site Cavity of Human Carbonic Anhydrase II by Solution-Phase and Solid-State Studies and Their Use in the Development of Tight-Binding Inhibitors [Article]. Journal of Medicinal Chemistry, 37(13), 2100-2105. https://doi.org/10.1021/jm00039a023

220. Nair, S. K., Ludwig, P. A., & Christianson, D. W. (1994). Two-Site Binding of Phenol in the Active Site of Human Carbonic Anhydrase II: Structural Implications for Substrate Association [Article]. Journal of the American Chemical Society, 116(8), 3659-3660. https://doi.org/10.1021/ja00087a086

221. Wei, A., Rubin, H., Cooperman, B. S., & Christianson, D. W. (1994). Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop [Article]. Nature Structural Biology, 1(4), 251-258. https://doi.org/10.1038/nsb0494-251

222. Smith, G. M., Alexander, R. S., Christianson, D. W., McKeever, B. M., Ponticello, G. S., Springer, J. P., Randall, W. C., Baldwin, J. J., & Habecker, C. N. (1994). Positions of His‐64 and a bound water in human carbonic anhydrase II upon binding three structurally related inhibitors [Article]. Protein Science, 3(1), 118-125. https://doi.org/10.1002/pro.5560030115

223. Kiefer, L. L., Fierke, C. A., Ippolito, J. A., & Christianson, D. W. (1993). Redesigning the Zinc Binding Site of Human Carbonic Anhydrase II: Structure of a His2Asp-Zn2+ Metal Coordination Polyhedron [Article]. Journal of the American Chemical Society, 115(26), 12581-12582. https://doi.org/10.1021/ja00079a046

224. Krebs, J. F., Ippolito, J. A., Christianson, D. W., & Fierke, C. A. (1993). Structural and functional importance of a conserved hydrogen bond network in human carbonic anhydrase II [Article]. Journal of Biological Chemistry, 268(36), 27458-27466. https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027752970&partnerID=40&md5=cff978bc470a84ed6c63b3b7722c14a8

225. Katz, D. S., Wei, A., Zhong, Q., Rubin, H., Cooperman, B. S., & Christianson, D. W. (1993). Crystallization and atomic resolution X-ray diffraction analysis of antichymotrypsin variants [Article]. Biochemical and Biophysical Research Communications, 196(2), 752-757. https://doi.org/10.1006/bbrc.1993.2313

226. Katz, D. S., & Christianson, D. W. (1993). Modeling the uncleaved serpin antichymotrypsin and its chymotrypsin complex [Article]. Protein Engineering, Design and Selection, 6(7), 701-709. https://doi.org/10.1093/protein/6.7.701

227. Nair, S. K., & Christianson, D. W. (1993). Structural Consequences of Hydrophilic Amino Acid Substitutions in the Hydrophobic Pocket of Human Carbonic Anhydrase II [Article]. Biochemistry, 32(17), 4506-4514. https://doi.org/10.1021/bi00068a005

228. Nair, S. K., & Christianson, D. W. (1993). Crystallographic studies of azide binding to human carbonic anhydrase II [Article]. European Journal of Biochemistry, 213(1), 507-515. https://doi.org/10.1111/j.1432-1033.1993.tb17788.x

229. Alexander, R. S., Christianson, D. W., Kiefer, L. L., & Fierke, C. A. (1993). Engineering the Zinc Binding Site of Human Carbonic Anhydrase II: Structure of the His-94→Cys Apoenzyme in a New Crystalline Form [Article]. Biochemistry, 32(6), 1510-1518. https://doi.org/10.1021/bi00057a015

230. Tweedy, N. B., Paterno, S. A., Fierke, C. A., Nair, S. K., & Christianson, D. W. (1993). Structure and Energetics of a Non-Proline cis-Peptidyl Linkage in a Proline-202 → Alanine Carbonic Anhydrase II Variant [Article]. Biochemistry, 32(41), 10944-10949. https://doi.org/10.1021/bi00092a003

231. Ippolito, J. A., & Christianson, D. W. (1993). Structure of an Engineered His3Cys Zinc Binding Site in Human Carbonic Anhydrase II [Article]. Biochemistry, 32(38), 9901-9905. https://doi.org/10.1021/bi00089a005

232. Lee, M. H., Pankratz, H. S., Wang, S., Scott, R. A., Finnegan, M. G., Johnson, M. K., Ippolito, J. A., Christianson, D. W., & Hausinger, R. P. (1993). Purification and characterization of Klebsiella aerogenes UreE protein: A nickel‐binding protein that functions in urease metallocenter assembly [Article]. Protein Science, 2(6), 1042-1052. https://doi.org/10.1002/pro.5560020617

233. Firby, R. J., Christianson, D., & McDougal, T. (1993). Fast local mapping to support navigation and object localization. Proceedings of SPIE – The International Society for Optical Engineering,

234. Wei, A., Rubin, H., Cooperman, B. S., Schechter, N., & Christianson, D. W. (1992). Crystallization, activity assay and preliminary X-ray diffraction analysis of the uncleaved form of the serpin antichymotrypsin [Article]. Journal of Molecular Biology, 226(1), 273-276. https://doi.org/10.1016/0022-2836(92)90140-F

235. Kanyo, Z. F., Chen, C. Y., Daghigh, F., Ash, D. E., & Christianson, D. W. (1992). Crystallization and oligomeric structure of rat liver arginase [Article]. Journal of Molecular Biology, 224(4), 1175-1177. https://doi.org/10.1016/0022-2836(92)90479-4

236. Cappalonga, A. M., Alexander, R. S., & Christianson, D. W. (1992). Structural comparison of sulfodiimine and sulfonamide inhibitors in their complexes with zinc enzymes [Article]. Journal of Biological Chemistry, 267(27), 19192-19197. https://www.scopus.com/inward/record.uri?eid=2-s2.0-0026673902&partnerID=40&md5=94bc579b125dadf6b4e5456e223af51b

237. Ippolito, J. A., & Christianson, D. W. (1992). The contribution of halogen atoms to protein-ligand interactions [Article]. International Journal of Biological Macromolecules, 14(4), 193-197. https://doi.org/10.1016/S0141-8130(05)80026-1

238. Nair, S. K., & Christianson, D. W. (1991). Structural properties of human carbonic anhydrase II at pH 9.5 [Article]. Biochemical and Biophysical Research Communications, 181(2), 579-584. https://doi.org/10.1016/0006-291X(91)91229-6

239. Nair, S. K., & Christianson, D. W. (1991). Unexpected pH-Dependent Conformation of His-64, the Proton Shuttle of Carbonic Anhydrase II [Article]. Journal of the American Chemical Society, 113(25), 9455-9458. https://doi.org/10.1021/ja00025a005

240. Nair, S. K., Calderone, T. L., Christianson, D. W., & Fierke, C. A. (1991). Altering the mouth of a hydrophobic pocket. Structure and kinetics of human carbonic anhydrase II mutants at residue Val-121 [Article]. Journal of Biological Chemistry, 266(26), 17320-17325. https://www.scopus.com/inward/record.uri?eid=2-s2.0-0026047767&partnerID=40&md5=5e67d7c0d83de6c09302601d8559af72

241. Alexander, R. S., Nair, S. K., & Christianson, D. W. (1991). Engineering the Hydrophobic Pocket of Carbonic Anhydrase II [Article]. Biochemistry, 30(46), 11064-11072. https://doi.org/10.1021/bi00110a008

242. Krebs, J. F., Fierke, C. A., Alexander, R. S., & Christianson, D. W. (1991). Conformational Mobility of His-64 in the Thr-200 → Ser Mutant of Human Carbonic Anhydrase II [Article]. Biochemistry, 30(38), 9153-9160. https://doi.org/10.1021/bi00102a005

243. Kanyo, Z. F., & Christianson, D. W. (1991). Biological recognition of phosphate and sulfate [Article]. Journal of Biological Chemistry, 266(7), 4264-4268. https://www.scopus.com/inward/record.uri?eid=2-s2.0-0025832606&partnerID=40&md5=aad092f183087e1d7d7668cb7e1da0d4

244. Christianson, D. W. (1991). Structural biology of zinc. In Advances in Protein Chemistry (Vol. 42, pp. 281-355).

245. Christianson, D. W., & Alexander, R. S. (1990). Another catalytic triad? [Letter]. Nature, 346(6281), 225. https://doi.org/10.1038/346225b0

246. Alexander, R. S., Kanyo, Z. F., Chirlian, L. E., & Christianson, D. W. (1990). Stereochemistry of Phosphate-Lewis Acid Interactions: Implications for Nucleic Acid Structure and Recognition [Article]. Journal of the American Chemical Society, 112(3), 933-937. https://doi.org/10.1021/ja00159a004

247. Ippolito, J. A., Alexander, R. S., & Christianson, D. W. (1990). Hydrogen bond stereochemistry in protein structure and function [Article]. Journal of Molecular Biology, 215(3), 457-471. https://doi.org/10.1016/S0022-2836(05)80364-X

248. Christianson, D. W., & Lipscomb, W. N. (1989). Carboxypeptidase A [Article]. Accounts of Chemical Research, 22(2), 62-69. https://doi.org/10.1021/ar00158a003

249. Christianson, D. W., & Alexander, R. S. (1989). Carboxylate-Histidine-Zinc Interactions in Protein Structure and Function [Article]. Journal of the American Chemical Society, 111(16), 6412-6419. https://doi.org/10.1021/ja00198a065

250. Christianson, D. W., Mangani, S., Shoham, G., & Lipscomb, W. N. (1989). Binding of D-phenylalanine and D-tyrosine to carboxypeptidase A [Article]. Journal of Biological Chemistry, 264(22), 12849-12853. https://www.scopus.com/inward/record.uri?eid=2-s2.0-0024335390&partnerID=40&md5=270fed74ae87c3328c5ad92e8a239856

251. Shoham, G., Christianson, D. W., & Oren, D. A. (1988). Complex between carboxypeptidase A and a hydrated ketomethylene substrate analogue [Article]. Proceedings of the National Academy of Sciences of the United States of America, 85(3), 684-688. https://doi.org/10.1073/pnas.85.3.684

252. Christianson, D. W., & Lipscomb, W. N. (1988). Comparison of Carboxypeptidase A and Thermolysin: Inhibition by Phosphonamidates [Article]. Journal of the American Chemical Society, 110(16), 5560-5565. https://doi.org/10.1021/ja00224a047

253. Christianson, D. W., & Lipscomb, W. N. (1987). Carboxypeptidase A: Novel Enzyme-Substrate-Product Complex [Article]. Journal of the American Chemical Society, 109(18), 5536-5538. https://doi.org/10.1021/ja00252a046

254. Christianson, D. W., David, P. R., & Lipscomb, W. N. (1987). Mechanism of carboxypeptidase A: Hydration of a ketonic substrate analogue (protein crystallography/zinc protease/enzyme-inhibitor complex) [Article]. Proceedings of the National Academy of Sciences of the United States of America, 84(6), 1512-1515. https://doi.org/10.1073/pnas.84.6.1512

255. Christianson, D. W., & Lipscomb, W. N. (1986). Structure of the Complex between an Unexpectedly Hydrolyzed Phosphonamidate Inhibitor and Carboxypeptidase A [Article]. Journal of the American Chemical Society, 108(3), 545-546. https://doi.org/10.1021/ja00263a052

256. Christianson, D. W., & Lipscomb, W. N. (1986). The Complex between Carboxypeptidase A and a Possible Transition-State Analogue: Mechanistic Inferences from High-Resolution X-ray Structures of Enzyme-Inhibitor Complexes [Article]. Journal of the American Chemical Society, 108(16), 4998-5003. https://doi.org/10.1021/ja00276a048

257. Christianson, D. W., & Lipscomb, W. N. (1986). X-ray crystallographic investigation of substrate binding to carboxypeptidase A at subzero temperature [Article]. Proceedings of the National Academy of Sciences of the United States of America, 83(20), 7568-7572. https://doi.org/10.1073/pnas.83.20.7568

258. Christianson, D. W., & Lipscomb, W. N. (1985). A Molecular Orbital Evaluation of Possible Factors Affecting the Homolytic Activation of Coenzyme B12 [Article]. Journal of the American Chemical Society, 107(9), 2682-2686. https://doi.org/10.1021/ja00295a021

259. Christianson, D. W., & Lipscomb, W. N. (1985). Binding of a possible transition state analogue to the active site of carboxypeptidase A [Article]. Proceedings of the National Academy of Sciences of the United States of America, 82(20), 6840-6844. https://doi.org/10.1073/pnas.82.20.6840

260. Christianson, D. W., Lipscomb, W. N., & Kuo, L. C. (1985). Novel Structure of the Complex between Carboxypeptidase A and a Ketonic Substrate Analogue [Article]. Journal of the American Chemical Society, 107(26), 8281-8283. https://doi.org/10.1021/ja00312a089

261. Shoharr, G., Christianson, D. W., Bartsch, R. A., Heo, G. S., Olsher, U., & Lipscomb, W. N. (1984). Crystal and Molecular Structure of the Complex between sym-Dibenzo-14-crown-4-oxyacetate and Li+, [C20H21O7]∼⦁Li+⦁7.5H2O [Article]. Journal of the American Chemical Society, 106(5), 1280-1285. https://doi.org/10.1021/ja00317a018