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Gaynes, M. N.; Ronnebaum, T. A.; Schultz, K.; Faylo, J. L.; Marmorstein, R.; Christianson, D. W. Structure of the Prenyltransferase in Bifunctional Copalyl Diphosphate Synthase from Penicillium Fellutanum Reveals an Open Hexamer Conformation. Journal of Structural Biology 2024, 216 (1), 108060. https://doi.org/10.1016/j.jsb.2023.108060.

Wenger, E. S.; Christianson, D. W. Methods for the Preparation and Analysis of the Diterpene Cyclase Fusicoccadiene Synthase. In Methods in Enzymology; Elsevier, 2024; Vol. 699, pp 89–119. https://doi.org/10.1016/bs.mie.2023.11.003.

Gaynes, M. N.; Christianson, D. W. Methods for the Preparation and Analysis of a Bifunctional Class II Diterpene Synthase, Copalyl Diphosphate Synthase from Penicillium Fellutanum. In Methods in Enzymology; Elsevier, 2024; Vol. 699, pp 1–23. https://doi.org/10.1016/bs.mie.2023.11.002.

Sinatra, L.; Vogelmann, A.; Friedrich, F.; Tararina, M. A.; Neuwirt, E.; Colcerasa, A.; König, P.; Toy, L.; Yesiloglu, T. Z.; Hilscher, S.; Gaitzsch, L.; Papenkordt, N.; Zhai, S.; Zhang, L.; Romier, C.; Einsle, O.; Sippl, W.; Schutkowski, M.; Gross, O.; Bendas, G.; Christianson, D. W.; Hansen, F. K.; Jung, M.; Schiedel, M. Development of First-in-Class Dual Sirt2/HDAC6 Inhibitors as Molecular Tools for Dual Inhibition of Tubulin Deacetylation. J. Med. Chem. 2023, 66 (21), 14787–14814. https://doi.org/10.1021/acs.jmedchem.3c01385

König, B.; Watson, P. R.; Reßing, N.; Cragin, A. D.; Schäker-Hübner, L.; Christianson, D. W.; Hansen, F. K. Difluoromethyl-1,3,4-Oxadiazoles Are Selective, Mechanism-Based, and Essentially Irreversible Inhibitors of Histone Deacetylase 6. J. Med. Chem. 2023, 66 (19), 13821–13837. https://doi.org/10.1021/acs.jmedchem.3c01345.

Watson, P. R.; Stollmaier, J. G.; Christianson, D. W. Crystal Structure of Histone Deacetylase 6 Complexed with (R)-Lipoic Acid, an Essential Cofactor in Central Carbon Metabolism. Journal of Biological Chemistry 2023, 299 (10), 105228. https://doi.org/10.1016/j.jbc.2023.105228.

Watson, P. R.; Christianson, D. W. Structure and Function of Kdac1, a Class II Deacetylase from the Multidrug-Resistant Pathogen Acinetobacter Baumannii. Biochemistry 2023, 62 (18), 2689–2699. https://doi.org/10.1021/acs.biochem.3c00288.

Eaton, S. A.; Christianson, D. W. Reprogramming the Cyclization Cascade of Epi -Isozizaene Synthase to Generate Alternative Terpene Products. Biochemistry 2023, 62 (15), 2301–2313. https://doi.org/10.1021/acs.biochem.3c00247.

Watson, P. R.; Gupta, S.; Hosseinzadeh, P.; Brown, B. P.; Baker, D.; Christianson, D. W. Macrocyclic Octapeptide Binding and Inferences on Protein Substrate Binding to Histone Deacetylase 6. ACS Chem. Biol. 2023, 18 (4), 959–968. https://doi.org/10.1021/acschembio.3c00113.

Reßing, N.; Schliehe-Diecks, J.; Watson, P. R.; Sönnichsen, M.; Cragin, A. D.; Schöler, A.; Yang, J.; Schäker-Hübner, L.; Borkhardt, A.; Christianson, D. W.; Bhatia, S.; Hansen, F. K. Development of Fluorinated Peptoid-Based Histone Deacetylase (HDAC) Inhibitors for Therapy-Resistant Acute Leukemia. J. Med. Chem. 2022, 65 (22), 15457–15472. https://doi.org/10.1021/acs.jmedchem.2c01418.

Faylo, J. L.; Van Eeuwen, T.; Gupta, K.; Murakami, K.; Christianson, D. W. Transient Prenyltransferase–Cyclase Association in Fusicoccadiene Synthase, an Assembly-Line Terpene Synthase. Biochemistry 2022, 61 (21), 2417–2430. https://doi.org/10.1021/acs.biochem.2c00509.

Steimbach, R. R.; Herbst-Gervasoni, C. J.; Lechner, S.; Stewart, T. M.; Klinke, G.; Ridinger, J.; Géraldy, M. N. E.; Tihanyi, G.; Foley, J. R.; Uhrig, U.; Kuster, B.; Poschet, G.; Casero, R. A.; Médard, G.; Oehme, I.; Christianson, D. W.; Gunkel, N.; Miller, A. K. Aza-SAHA Derivatives Are Selective Histone Deacetylase 10 Chemical Probes That Inhibit Polyamine Deacetylation and Phenocopy HDAC10 Knockout. J. Am. Chem. Soc. 2022, 144 (41), 18861–18875. https://doi.org/10.1021/jacs.2c05030.

Watson, P. R.; Bai, P.; Wang, C.; Cragin, A. D.; Hooker, J. M.; Christianson, D. W. Aromatic Ring Fluorination Patterns Modulate Inhibitory Potency of Fluorophenylhydroxamates Complexed with Histone Deacetylase 6. Biochemistry 2022, 61 (18), 1945–1954. https://doi.org/10.1021/acs.biochem.2c00332.

Tararina, M. A.; Yee, D. A.; Tang, Y.; Christianson, D. W. Structure of the Repurposed Fungal Terpene Cyclase FlvF Implicated in the C–N Bond-Forming Reaction of Flavunoidine Biosynthesis. Biochemistry 2022, 61 (18), 2014–2024. https://doi.org/10.1021/acs.biochem.2c00335.

Eaton, S. A.; Ronnebaum, T. A.; Roose, B. W.; Christianson, D. W. Structural Basis of Substrate Promiscuity and Catalysis by the Reverse Prenyltransferase N -Dimethylallyl- l -Tryptophan Synthase from Fusarium Fujikuroi. Biochemistry 2022, 61 (18), 2025–2035. https://doi.org/10.1021/acs.biochem.2c00350.

Herp, D.; Ridinger, J.; Robaa, D.; Shinsky, S. A.; Schmidtkunz, K.; Yesiloglu, T. Z.; Bayer, T.; Steimbach, R. R.; Herbst‐Gervasoni, C. J.; Merz, A.; Romier, C.; Sehr, P.; Gunkel, N.; Miller, A. K.; Christianson, D. W.; Oehme, I.; Sippl, W.; Jung, M. First Fluorescent Acetylspermidine Deacetylation Assay for HDAC10 Identifies Selective Inhibitors with Cellular Target Engagement**. ChemBioChem 2022, 23 (14), e202200180. https://doi.org/10.1002/cbic.202200180.

Watson, P. R.; Hooker, J.; Christianson, D. W. Aromatic C‐F Interactions Influence Binding Mode of Inhibitors in HDAC6. The FASEB Journal 2022, 36 (S1), fasebj.2022.36.S1.R2257. https://doi.org/10.1096/fasebj.2022.36.S1.R2257.

Tararina, M. A.; Yee, D. A.; Tang, Y.; Christianson, D. W. Structural Analysis of a Non‐canonical Terpene Synthase. The FASEB Journal 2022, 36 (S1), fasebj.2022.36.S1.R3623. https://doi.org/10.1096/fasebj.2022.36.S1.R3623.

Ronnebaum, T. A.; Eaton, S. A.; Brackhahn, E. A. E.; Faylo, J. L.; Gupta, K.; Christianson, D. W. Assembly‐line Catalysis in Bifunctional Terpene Synthases: (+)‐Copalyl Diphosphate Synthase from Fungal Penicillium Species. The FASEB Journal 2022, 36 (S1), fasebj.2022.36.S1.L7991. https://doi.org/10.1096/fasebj.2022.36.S1.L7991.

Cragin, A.; Watson, P. R.; König, B.; Hansen, F. K.; Christianson, D. W. A Novel Zinc Binding Group for HDAC6 Inhibition. The FASEB Journal 2022, 36 (S1), fasebj.2022.36.S1.R3604. https://doi.org/10.1096/fasebj.2022.36.S1.R3604.

Zeyen, P.; Zeyn, Y.; Herp, D.; Mahmoudi, F.; Yesiloglu, T. Z.; Erdmann, F.; Schmidt, M.; Robaa, D.; Romier, C.; Ridinger, J.; Herbst-Gervasoni, C. J.; Christianson, D. W.; Oehme, I.; Jung, M.; Krämer, O. H.; Sippl, W. Identification of Histone Deacetylase 10 (HDAC10) Inhibitors That Modulate Autophagy in Transformed Cells. European Journal of Medicinal Chemistry 2022, 234, 114272. https://doi.org/10.1016/j.ejmech.2022.114272.

Faylo, J. L.; Christianson, D. W. Visualizing Transiently Associated Catalytic Domains in Assembly-Line Biosynthesis Using Cryo-Electron Microscopy. Journal of Structural Biology 2021, 213 (4), 107802. https://doi.org/10.1016/j.jsb.2021.107802.

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

Faylo, J. L.; Ronnebaum, T. A.; Christianson, D. W. Assembly-Line Catalysis in Bifunctional Terpene Synthases. Acc. Chem. Res. 2021, 54 (20), 3780–3791. https://doi.org/10.1021/acs.accounts.1c00296.

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.; Tedesco, D.; Herp, D.; Senger, J.; Ruberti, G.; Saccoccia, F.; Saponara, S.; Gorelli, B.; Valoti, M.; Kennedy, B.; Sundaramurthi, H.; Butini, S.; Jung, M.; Roach, K. M.; Altucci, L.; Bradding, P.; Christianson, D. W.; Gemma, S.; Prasse, A. Harnessing the Role of HDAC6 in Idiopathic Pulmonary Fibrosis: Design, Synthesis, Structural Analysis, and Biological Evaluation of Potent Inhibitors. J. Med. Chem. 2021, 64 (14), 9960–9988. https://doi.org/10.1021/acs.jmedchem.1c00184.

Faylo, J. L.; Van Eeuwen, T.; Kim, H. J.; Gorbea Colón, J. J.; Garcia, B. A.; Murakami, K.; Christianson, D. W. Structural Insight on Assembly-Line Catalysis in Terpene Biosynthesis. Nat Commun 2021, 12 (1), 3487. https://doi.org/10.1038/s41467-021-23589-9.

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. Anchor Extension: A Structure-Guided Approach to Design Cyclic Peptides Targeting Enzyme Active Sites. Nat Commun 2021, 12 (1), 3384. https://doi.org/10.1038/s41467-021-23609-8.

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.; Christianson, D. W.; Gunning, P. T. Unique Molecular Interaction with the Histone Deacetylase 6 Catalytic Tunnel: Crystallographic and Biological Characterization of a Model Chemotype. J. Med. Chem. 2021, 64 (5), 2691–2704. https://doi.org/10.1021/acs.jmedchem.0c01922.

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. Structural Analysis of Histone Deacetylase 8 Mutants Associated with Cornelia de Lange Syndrome Spectrum Disorders. Journal of Structural Biology 2021, 213 (1), 107681. https://doi.org/10.1016/j.jsb.2020.107681.

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

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

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.; Ulivieri, C.; Herp, D.; Sarno, F.; Di Costanzo, A.; Saccoccia, F.; Ruberti, G.; Jung, M.; Altucci, L.; Gemma, S.; Butini, S.; Christianson, D. W.; Campiani, G. Spiroindoline-Capped Selective HDAC6 Inhibitors: Design, Synthesis, Structural Analysis, and Biological Evaluation. ACS Med. Chem. Lett. 2020, 11 (11), 2268–2276. https://doi.org/10.1021/acsmedchemlett.0c00395.

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

Osko, J. D.; Christianson, D. W. Binding of Inhibitors to Active-Site Mutants of CD1, the Enigmatic Catalytic Domain of Histone Deacetylase 6. Acta Crystallogr F Struct Biol Commun 2020, 76 (9), 428–437. https://doi.org/10.1107/S2053230X20010250.

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

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. Discovery of the Cryptic Function of Terpene Cyclases as Aromatic Prenyltransferases. Nat Commun 2020, 11 (1), 3958. https://doi.org/10.1038/s41467-020-17642-2.

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. Design and Synthesis of Dihydroxamic Acids as HDAC6/8/10 Inhibitors. ChemMedChem 2020, 15 (13), 1163–1174. https://doi.org/10.1002/cmdc.202000149.

Blank, P. N.; Barnett, A. A.; Ronnebaum, T. A.; Alderfer, K. E.; Gillott, B. N.; Christianson, D. W.; Himmelberger, J. A. Structural Studies of Geranylgeranylglyceryl Phosphate Synthase, a Prenyltransferase Found in Thermophilic Euryarchaeota. Acta Crystallogr D Struct Biol 2020, 76 (6), 542–557. https://doi.org/10.1107/S2059798320004878.

Ronnebaum, T. A.; Gupta, K.; Christianson, D. W. Higher-Order Oligomerization of a Chimeric Αβγ Bifunctional Diterpene Synthase with Prenyltransferase and Class II Cyclase Activities Is Concentration-Dependent. Journal of Structural Biology 2020, 210 (1), 107463. https://doi.org/10.1016/j.jsb.2020.107463.

Osko, J. D.; Christianson, D. W. Structural Determinants of Affinity and Selectivity in the Binding of Inhibitors to Histone Deacetylase 6. Bioorganic & Medicinal Chemistry Letters 2020, 30 (8), 127023. https://doi.org/10.1016/j.bmcl.2020.127023.

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. Exploring Structural Determinants of Inhibitor Affinity and Selectivity in Complexes with Histone Deacetylase 6. J. Med. Chem. 2020, 63 (1), 295–308. https://doi.org/10.1021/acs.jmedchem.9b01540.

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

Herbst-Gervasoni, C. J.; Christianson, D. W. Binding of N ⁸-Acetylspermidine Analogues to Histone Deacetylase 10 Reveals Molecular Strategies for Blocking Polyamine Deacetylation. Biochemistry 2019, 58 (49), 4957–4969. https://doi.org/10.1021/acs.biochem.9b00906.

Porter, N. J.; Christianson, D. W. Structure, Mechanism, and Inhibition of the Zinc-Dependent Histone Deacetylases. Current Opinion in Structural Biology 2019, 59, 9–18. https://doi.org/10.1016/j.sbi.2019.01.004.

Welker Leng, K. R.; Castañeda, C. A.; Decroos, C.; Islam, B.; Haider, S. M.; Christianson, D. W.; Fierke, C. A. Phosphorylation of Histone Deacetylase 8: Structural and Mechanistic Analysis of the Phosphomimetic S39E Mutant. Biochemistry 2019, 58 (45), 4480–4493. https://doi.org/10.1021/acs.biochem.9b00653.

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

Blank, P. N.; Barrow, G. H.; Christianson, D. W. Crystal Structure of F95Q Epi-Isozizaene Synthase, an Engineered Sesquiterpene Cyclase That Generates Biofuel Precursors β- and γ-Curcumene. Journal of Structural Biology 2019, 207 (2), 218–224. https://doi.org/10.1016/j.jsb.2019.05.011.

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

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

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. Synthesis and Biological Investigation of Phenothiazine-Based Benzhydroxamic Acids as Selective Histone Deacetylase 6 Inhibitors. J. Med. Chem. 2019, 62 (3), 1138–1166. https://doi.org/10.1021/acs.jmedchem.8b01090.

Porter, N. J.; Christianson, D. W. Preparation of a New Construct of Human Histone Deacetylase 8 for the Crystallization of Enzyme-Inhibitor Complexes. In Methods in Enzymology; Elsevier, 2019; Vol. 626, pp 561–585. https://doi.org/10.1016/bs.mie.2019.06.029.

Osko, J. D.; Christianson, D. W. Methods for the Expression, Purification, and Crystallization of Histone Deacetylase 6–Inhibitor Complexes. In Methods in Enzymology; Elsevier, 2019; Vol. 626, pp 447–474. https://doi.org/10.1016/bs.mie.2019.06.028.

Christianson, D. W. Correction to Structural and Chemical Biology of Terpenoid Cyclases. Chem. Rev. 2018, 118 (24), 11795–11795. https://doi.org/10.1021/acs.chemrev.8b00682.

Porter, N. J.; Shen, S.; Barinka, C.; Kozikowski, A. P.; Christianson, D. W. Molecular Basis for the Selective Inhibition of Histone Deacetylase 6 by a Mercaptoacetamide Inhibitor. ACS Med. Chem. Lett. 2018, 9 (12), 1301–1305. https://doi.org/10.1021/acsmedchemlett.8b00487.

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. Discovery of the First-in-Class Dual Histone Deacetylase–Proteasome Inhibitor. J. Med. Chem. 2018, 61 (22), 10299–10309. https://doi.org/10.1021/acs.jmedchem.8b01487.

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

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

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

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

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

Porter, N. J.; Mahendran, A.; Breslow, R.; Christianson, D. W. Unusual Zinc-Binding Mode of HDAC6-Selective Hydroxamate Inhibitors. Proc. Natl. Acad. Sci. U.S.A. 2017, 114 (51), 13459–13464. https://doi.org/10.1073/pnas.1718823114.

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

Porter, N. J.; Christianson, D. W. Binding of the Microbial Cyclic Tetrapeptide Trapoxin A to the Class I Histone Deacetylase HDAC8. ACS Chem. Biol. 2017, 12 (9), 2281–2286. https://doi.org/10.1021/acschembio.7b00330.

Christianson, D. W. Structural and Chemical Biology of Terpenoid Cyclases. Chem. Rev. 2017, 117 (17), 11570–11648. https://doi.org/10.1021/acs.chemrev.7b00287.

Bitler, B. G.; Wu, S.; Park, P. H.; Hai, Y.; Aird, K. M.; Wang, Y.; Zhai, Y.; Kossenkov, A. V.; Vara-Ailor, A.; Rauscher Iii, F. J.; Zou, W.; Speicher, D. W.; Huntsman, D. G.; Conejo-Garcia, J. R.; Cho, K. R.; Christianson, D. W.; Zhang, R. ARID1A-Mutated Ovarian Cancers Depend on HDAC6 Activity. Nat Cell Biol 2017, 19 (8), 962–973. https://doi.org/10.1038/ncb3582.

Hai, Y.; Shinsky, S. A.; Porter, N. J.; Christianson, D. W. Histone Deacetylase 10 Structure and Molecular Function as a Polyamine Deacetylase. Nat Commun 2017, 8 (1), 15368. https://doi.org/10.1038/ncomms15368.

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. Exploring the Influence of Domain Architecture on the Catalytic Function of Diterpene Synthases. Biochemistry 2017, 56 (14), 2010–2023. https://doi.org/10.1021/acs.biochem.7b00137.

Porter, N. J.; Christianson, N. H.; Decroos, C.; Christianson, D. W. Structural and Functional Influence of the Glycine-Rich Loop G ³⁰² GGGY on the Catalytic Tyrosine of Histone Deacetylase 8. Biochemistry 2016, 55 (48), 6718–6729. https://doi.org/10.1021/acs.biochem.6b01014.

Christianson, D. W.; Scrutton, N. S. Editorial Overview: Catalysis and Regulation: Enzyme Structure, Mechanism, and Biosynthetic Pathways. Current Opinion in Structural Biology 2016, 41, viii–x. https://doi.org/10.1016/j.sbi.2016.09.005.

Chen, M.; Harris, G. G.; Pemberton, T. A.; Christianson, D. W. Multi-Domain Terpenoid Cyclase Architecture and Prospects for Proximity in Bifunctional Catalysis. Current Opinion in Structural Biology 2016, 41, 27–37. https://doi.org/10.1016/j.sbi.2016.05.010.

Deardorff, M. A.; Porter, N. J.; Christianson, D. W. Structural Aspects of HDAC8 Mechanism and Dysfunction in Cornelia de Lange Syndrome Spectrum Disorders. Protein Science 2016, 25 (11), 1965–1976. https://doi.org/10.1002/pro.3030.

Hai, Y.; Christianson, D. W. Histone Deacetylase 6 Structure and Molecular Basis of Catalysis and Inhibition. Nat Chem Biol 2016, 12 (9), 741–747. https://doi.org/10.1038/nchembio.2134.

Pemberton, T. A.; Christianson, D. W. General Base-General Acid Catalysis by Terpenoid Cyclases. J Antibiot 2016, 69 (7), 486–493. https://doi.org/10.1038/ja.2016.39.

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

Chen, M.; Chou, W. K. W.; Toyomasu, T.; Cane, D. E.; Christianson, D. W. Structure and Function of Fusicoccadiene Synthase, a Hexameric Bifunctional Diterpene Synthase. ACS Chem. Biol. 2016, 11 (4), 889–899. https://doi.org/10.1021/acschembio.5b00960.

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

Hai, Y.; Christianson, D. W. Crystal Structures of Leishmania Mexicana Arginase Complexed with α,α-Disubstituted Boronic Amino-Acid Inhibitors. Acta Crystallogr F Struct Biol Commun 2016, 72 (4), 300–306. https://doi.org/10.1107/S2053230X16003630

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

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. Structural Studies of Geosmin Synthase, a Bifunctional Sesquiterpene Synthase with Αα Domain Architecture That Catalyzes a Unique Cyclization–Fragmentation Reaction Sequence. Biochemistry 2015, 54 (48), 7142–7155. https://doi.org/10.1021/acs.biochem.5b01143.

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

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

Decroos, C.; Clausen, D. J.; Haines, B. E.; Wiest, O.; Williams, R. M.; Christianson, D. W. Variable Active Site Loop Conformations Accommodate the Binding of Macrocyclic Largazole Analogues to HDAC8. Biochemistry 2015, 54 (12), 2126–2135. https://doi.org/10.1021/acs.biochem.5b00010.

Hai, Y.; Kerkhoven, E. J.; Barrett, M. P.; Christianson, D. W. Crystal Structure of an Arginase-like Protein from Trypanosoma Brucei That Evolved without a Binuclear Manganese Cluster. Biochemistry 2015, 54 (2), 458–471. https://doi.org/10.1021/bi501366a.

Decroos, C.; Bowman, C. M.; Moser, J.-A. S.; Christianson, K. E.; Deardorff, M. A.; Christianson, D. W. Compromised Structure and Function of HDAC8 Mutants Identified in Cornelia de Lange Syndrome Spectrum Disorders. ACS Chem. Biol. 2014, 9 (9), 2157–2164. https://doi.org/10.1021/cb5003762.

Hai, Y.; Edwards, J. E.; Van Zandt, M. C.; Hoffmann, K. F.; Christianson, D. W. Crystal Structure of Schistosoma Mansoni Arginase, a Potential Drug Target for the Treatment of Schistosomiasis. Biochemistry 2014, 53 (28), 4671–4684. https://doi.org/10.1021/bi5004519.

Kaiser, F. J.; Ansari, M.; Braunholz, D.; Concepción Gil-Rodríguez, M.; 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.; Del Campo, M.; Di Donato, N.; Diakumis, P.; Dubbs, H.; Dyment, D. A.; Eckhold, J.; Ernst, S.; Ferreira, J. C.; Francey, L. J.; Gehlken, U.; Guillén-Navarro, E.; Gyftodimou, Y.; Hall, B. D.; Hennekam, R.; Hudgins, L.; Hullings, M.; Hunter, J. M.; Yntema, H.; Innes, A. M.; Kline, A. D.; Krumina, Z.; Lee, H.; Leppig, K.; Lynch, S. A.; Mallozzi, M. B.; Mannini, L.; Mckee, S.; Mehta, S. G.; Micule, I.; Care4Rare Canada Consortium; Mohammed, S.; Moran, E.; Mortier, G. R.; Moser, J.-A. S.; Noon, S. E.; Nozaki, N.; Nunes, L.; Pappas, J. G.; Penney, L. S.; Pérez-Aytés, A.; Petersen, M. B.; Puisac, B.; Revencu, N.; Roeder, E.; Saitta, S.; Scheuerle, A. E.; Schindeler, K. L.; Siu, V. M.; Stark, Z.; Strom, S. P.; Thiese, H.; Vater, I.; Willems, P.; Williamson, K.; Wilson, L. C.; University of Washington Center for Mendelian Genomics; Hakonarson, H.; Quintero-Rivera, F.; Wierzba, J.; Musio, A.; Gillessen-Kaesbach, G.; Ramos, F. J.; Jackson, L. G.; Shirahige, K.; Pié, J.; Christianson, D. W.; Krantz, I. D.; Fitzpatrick, D. R.; Deardorff, M. A. Loss-of-Function HDAC8 Mutations Cause a Phenotypic Spectrum of Cornelia de Lange Syndrome-like Features, Ocular Hypertelorism, Large Fontanelle and X-Linked Inheritance. Human Molecular Genetics 2014, 23 (11), 2888–2900. https://doi.org/10.1093/hmg/ddu002.

Li, R.; Chou, W. K. W.; Himmelberger, J. A.; Litwin, K. M.; Harris, G. G.; Cane, D. E.; Christianson, D. W. Reprogramming the Chemodiversity of Terpenoid Cyclization by Remolding the Active Site Contour of Epi -Isozizaene Synthase. Biochemistry 2014, 53 (7), 1155–1168. https://doi.org/10.1021/bi401643u.

Köksal, M.; Potter, K.; Peters, R. J.; Christianson, D. W. 1.55Å-Resolution Structure of Ent-Copalyl Diphosphate Synthase and Exploration of General Acid Function by Site-Directed Mutagenesis. Biochimica et Biophysica Acta (BBA) – General Subjects 2014, 1840 (1), 184–190. https://doi.org/10.1016/j.bbagen.2013.09.004.

Hai, Y.; Dugery, R. J.; Healy, D.; Christianson, D. W. Formiminoglutamase from Trypanosoma Cruzi Is An Arginase-Like Manganese Metalloenzyme. Biochemistry 2013, 52 (51), 9294–9309. https://doi.org/10.1021/bi401352h.

Chen, M.; Al-lami, N.; Janvier, M.; D’Antonio, E. L.; Faraldos, J. A.; Cane, D. E.; Allemann, R. K.; Christianson, D. W. Mechanistic Insights from the Binding of Substrate and Carbocation Intermediate Analogues to Aristolochene Synthase. Biochemistry 2013, 52 (32), 5441–5453. https://doi.org/10.1021/bi400691v.

Köksal, M.; Chou, W. K. W.; Cane, D. E.; Christianson, D. W. Unexpected Reactivity of 2-Fluorolinalyl Diphosphate in the Active Site of Crystalline 2-Methylisoborneol Synthase. Biochemistry 2013, 52 (31), 5247–5255. https://doi.org/10.1021/bi400797c.

Decroos, C.; Bowman, C. M.; Christianson, D. W. Synthesis and Evaluation of N8-Acetylspermidine Analogues as Inhibitors of Bacterial Acetylpolyamine Amidohydrolase. Bioorganic & Medicinal Chemistry 2013, 21 (15), 4530–4540. https://doi.org/10.1016/j.bmc.2013.05.045.

D’Antonio, E. L.; Ullman, B.; Roberts, S. C.; Dixit, U. G.; Wilson, M. E.; Hai, Y.; Christianson, D. W. Crystal Structure of Arginase from Leishmania Mexicana and Implications for the Inhibition of Polyamine Biosynthesis in Parasitic Infections. Archives of Biochemistry and Biophysics 2013, 535 (2), 163–176. https://doi.org/10.1016/j.abb.2013.03.015.

Genshaft, A.; Moser, J. S.; D’Antonio, E. L.; Bowman, C. M.; Christianson, D. W. Energetically Unfavorable Amide Conformations for N6‐acetyllysine Side Chains in Refined Protein Structures. Proteins 2013, 81 (6), 1051–1057. https://doi.org/10.1002/prot.24262.

Liedtke, A. J.; Adeniji, A. O.; Chen, M.; Byrns, M. C.; Jin, Y.; Christianson, D. W.; Marnett, L. J.; Penning, T. M. 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. J. Med. Chem. 2013, 56 (6), 2429–2446. https://doi.org/10.1021/jm3017656.

Faraldos, J. A.; Gonzalez, V.; Li, A.; Yu, F.; Köksal, M.; Christianson, D. W.; Allemann, R. K. Probing the Mechanism of 1,4-Conjugate Elimination Reactions Catalyzed by Terpene Synthases. J. Am. Chem. Soc. 2012, 134 (51), 20844–20848. https://doi.org/10.1021/ja311022s.

D’Antonio, E. L.; Hai, Y.; Christianson, D. W. Structure and Function of Non-Native Metal Clusters in Human Arginase I. Biochemistry 2012, 51 (42), 8399–8409. https://doi.org/10.1021/bi301145n.

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.; Ishikawa, Y.; Jaulin, C.; Kaur, M.; Kiyono, T.; Lombardi, P. M.; Magnaghi-Jaulin, L.; Mortier, G. R.; Nozaki, N.; Petersen, M. B.; Seimiya, H.; Siu, V. M.; Suzuki, Y.; Takagaki, K.; Wilde, J. J.; Willems, P. J.; Prigent, C.; Gillessen-Kaesbach, G.; Christianson, D. W.; Kaiser, F. J.; Jackson, L. G.; Hirota, T.; Krantz, I. D.; Shirahige, K. HDAC8 Mutations in Cornelia de Lange Syndrome Affect the Cohesin Acetylation Cycle. Nature 2012, 489 (7415), 313–317. https://doi.org/10.1038/nature11316.

D’Antonio, E. L.; Christianson, D. W. Binding of the Unreactive Substrate Analog L -2-Amino-3-Guanidinopropionic Acid (Dinor- L -Arginine) to Human Arginase I. Acta Crystallogr F Struct Biol Cryst Commun 2012, 68 (8), 889–893. https://doi.org/10.1107/S1744309112027820.

Chen, M.; Drury, J. E.; Christianson, D. W.; Penning, T. M. Conversion of Human Steroid 5β-Reductase (AKR1D1) into 3β-Hydroxysteroid Dehydrogenase by Single Point Mutation E120H. Journal of Biological Chemistry 2012, 287 (20), 16609–16622. https://doi.org/10.1074/jbc.M111.338780.

Chen, M.; Adeniji, A. O.; Twenter, B. M.; Winkler, J. D.; Christianson, D. W.; Penning, T. M. 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. Bioorganic & Medicinal Chemistry Letters 2012, 22 (10), 3492–3497. https://doi.org/10.1016/j.bmcl.2012.03.085.

Köksal, M.; Chou, W. K. W.; Cane, D. E.; Christianson, D. W. Structure of Geranyl Diphosphate C -Methyltransferase from Streptomyces Coelicolor and Implications for the Mechanism of Isoprenoid Modification. Biochemistry 2012, 51 (14), 3003–3010. https://doi.org/10.1021/bi300109c.

Köksal, M.; Chou, W. K. W.; Cane, D. E.; Christianson, D. W. Structure of 2-Methylisoborneol Synthase from Streptomyces Coelicolor and Implications for the Cyclization of a Noncanonical C -Methylated Monoterpenoid Substrate. Biochemistry 2012, 51 (14), 3011–3020. https://doi.org/10.1021/bi201827a.

Lombardi, P. M.; Cole, K. E.; Dowling, D. P.; Christianson, D. W. Structure, Mechanism, and Inhibition of Histone Deacetylases and Related Metalloenzymes. Current Opinion in Structural Biology 2011, 21 (6), 735–743. https://doi.org/10.1016/j.sbi.2011.08.004.

Ilies, M.; Dowling, D. P.; Lombardi, P. M.; Christianson, D. W. Synthesis of a New Trifluoromethylketone Analogue of L-Arginine and Contrasting Inhibitory Activity against Human Arginase I and Histone Deacetylase 8. Bioorganic & Medicinal Chemistry Letters 2011, 21 (19), 5854–5858. https://doi.org/10.1016/j.bmcl.2011.07.100.

D’Antonio, E. L.; Christianson, D. W. Crystal Structures of Complexes with Cobalt-Reconstituted Human Arginase I. Biochemistry 2011, 50 (37), 8018–8027. https://doi.org/10.1021/bi201101t.

Cole, K. E.; Dowling, D. P.; Boone, M. A.; Phillips, A. J.; Christianson, D. W. Structural Basis of the Antiproliferative Activity of Largazole, a Depsipeptide Inhibitor of the Histone Deacetylases. J. Am. Chem. Soc. 2011, 133 (32), 12474–12477. https://doi.org/10.1021/ja205972n.

Ilies, M.; Di Costanzo, L.; Dowling, D. P.; Thorn, K. J.; Christianson, D. W. Binding of α,α-Disubstituted Amino Acids to Arginase Suggests New Avenues for Inhibitor Design. J. Med. Chem. 2011, 54 (15), 5432–5443. https://doi.org/10.1021/jm200443b.

Köksal, M.; Hu, H.; Coates, R. M.; Peters, R. J.; Christianson, D. W. Structure and Mechanism of the Diterpene Cyclase Ent-Copalyl Diphosphate Synthase. Nat Chem Biol 2011, 7 (7), 431–433. https://doi.org/10.1038/nchembio.578.

Lombardi, P. M.; Angell, H. D.; Whittington, D. A.; Flynn, E. F.; Rajashankar, K. R.; Christianson, D. W. Structure of Prokaryotic Polyamine Deacetylase Reveals Evolutionary Functional Relationships with Eukaryotic Histone Deacetylases,. Biochemistry 2011, 50 (11), 1808–1817. https://doi.org/10.1021/bi101859k.

Cole, K. E.; Gattis, S. G.; Angell, H. D.; Fierke, C. A.; Christianson, D. W. Structure of the Metal-Dependent Deacetylase LpxC from Yersinia Enterocolitica Complexed with the Potent Inhibitor CHIR-090,. Biochemistry 2011, 50 (2), 258–265. https://doi.org/10.1021/bi101622a.

Köksal, M.; Jin, Y.; Coates, R. M.; Croteau, R.; Christianson, D. W. Taxadiene Synthase Structure and Evolution of Modular Architecture in Terpene Biosynthesis. Nature 2011, 469 (7328), 116–120. https://doi.org/10.1038/nature09628.

Köksal, M.; Zimmer, I.; Schnitzler, J.-P.; Christianson, D. W. Structure of Isoprene Synthase Illuminates the Chemical Mechanism of Teragram Atmospheric Carbon Emission. Journal of Molecular Biology 2010, 402 (2), 363–373. https://doi.org/10.1016/j.jmb.2010.07.009.

Dowling, D. P.; Ilies, M.; Olszewski, K. L.; Portugal, S.; Mota, M. M.; Llinás, M.; Christianson, D. W. Crystal Structure of Arginase from Plasmodium Falciparum and Implications for l -Arginine Depletion in Malarial Infection,. Biochemistry 2010, 49 (26), 5600–5608. https://doi.org/10.1021/bi100390z.

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. Design, Synthesis, and Structural Analysis of d , l -Mixed Polypyrrolinones. 2. Macrocyclic Hexapyrrolinones. Org. Lett. 2010, 12 (13), 2994–2997. https://doi.org/10.1021/ol101008y.

Zakharian, T. Y.; Christianson, D. W. Design and Synthesis of C60–Benzenesulfonamide Conjugates. Tetrahedron Letters 2010, 51 (28), 3645–3648. https://doi.org/10.1016/j.tetlet.2010.05.017.

Dowling, D. P.; Gattis, S. G.; Fierke, C. A.; Christianson, D. W. Structures of Metal-Substituted Human Histone Deacetylase 8 Provide Mechanistic Inferences on Biological Function,. Biochemistry 2010, 49 (24), 5048–5056. https://doi.org/10.1021/bi1005046.

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. Arginase I Suppresses IL-12/IL-23p40–Driven Intestinal Inflammation during Acute Schistosomiasis. The Journal of Immunology 2010, 184 (11), 6438–6446. https://doi.org/10.4049/jimmunol.0902009.

Ilies, M.; Di Costanzo, L.; North, M. L.; Scott, J. A.; Christianson, D. W. 2-Aminoimidazole Amino Acids as Inhibitors of the Binuclear Manganese Metalloenzyme Human Arginase I. J. Med. Chem. 2010, 53 (10), 4266–4276. https://doi.org/10.1021/jm100306a.

Aaron, J. A.; Christianson, D. W. Trinuclear Metal Clusters in Catalysis by Terpenoid Synthases. Pure and Applied Chemistry 2010, 82 (8), 1585–1597. https://doi.org/10.1351/PAC-CON-09-09-37.

Di Costanzo, L.; Ilies, M.; Thorn, K. J.; Christianson, D. W. Inhibition of Human Arginase I by Substrate and Product Analogues. Archives of Biochemistry and Biophysics 2010, 496 (2), 101–108. https://doi.org/10.1016/j.abb.2010.02.004.

Aaron, J. A.; Lin, X.; Cane, D. E.; Christianson, D. W. Structure of Epi-Isozizaene Synthase from Streptomyces Coelicolor A3(2), a Platform for New Terpenoid Cyclization Templates ^,. Biochemistry 2010, 49 (8), 1787–1797. https://doi.org/10.1021/bi902088z.

Kim, J. H.; Bugaj, L. J.; Oh, Y. J.; 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. Arginase Inhibition Restores NOS Coupling and Reverses Endothelial Dysfunction and Vascular Stiffness in Old Rats. Journal of Applied Physiology 2009, 107 (4), 1249–1257. https://doi.org/10.1152/japplphysiol.91393.2008.

Gennadios, H. A.; Gonzalez, V.; Di Costanzo, L.; Li, A.; Yu, F.; Miller, D. J.; Allemann, R. K.; Christianson, D. W. Crystal Structure of (+)-δ-Cadinene Synthase from Gossypium Arboreum and Evolutionary Divergence of Metal Binding Motifs for Catalysis. Biochemistry 2009, 48 (26), 6175–6183. https://doi.org/10.1021/bi900483b.

Drury, J. E.; Di Costanzo, L.; Penning, T. M.; Christianson, D. W. Inhibition of Human Steroid 5β-Reductase (AKR1D1) by Finasteride and Structure of the Enzyme-Inhibitor Complex. Journal of Biological Chemistry 2009, 284 (30), 19786–19790. https://doi.org/10.1074/jbc.C109.016931.

Di Costanzo, L.; Penning, T. M.; Christianson, D. W. Aldo-Keto Reductases in Which the Conserved Catalytic Histidine Is Substituted. Chemico-Biological Interactions 2009, 178 (1–3), 127–133. https://doi.org/10.1016/j.cbi.2008.10.046.

Di Costanzo, L.; Drury, J. E.; Christianson, D. W.; Penning, T. M. Structure and Catalytic Mechanism of Human Steroid 5β-Reductase (AKR1D1). Molecular and Cellular Endocrinology 2009, 301 (1–2), 191–198. https://doi.org/10.1016/j.mce.2008.09.013.

Shishova, E. Y.; Di Costanzo, L.; Emig, F. A.; Ash, D. E.; Christianson, D. W. Probing the Specificity Determinants of Amino Acid Recognition by Arginase. Biochemistry 2009, 48 (1), 121–131. https://doi.org/10.1021/bi801911v.

Zakharian, T. Y.; Di Costanzo, L.; Christianson, D. W. ( S )-2-Amino-6-Nitrohexanoic Acid Binds to Human Arginase I through Multiple Nitro−Metal Coordination Interactions in the Binuclear Manganese Cluster. J. Am. Chem. Soc. 2008, 130 (51), 17254–17255. https://doi.org/10.1021/ja807702q.

Dowling, D. P.; Gantt, S. L.; Gattis, S. G.; Fierke, C. A.; Christianson, D. W. Structural Studies of Human Histone Deacetylase 8 and Its Site-Specific Variants Complexed with Substrate and Inhibitors ^,. Biochemistry 2008, 47 (51), 13554–13563. https://doi.org/10.1021/bi801610c.

Santhanam, L.; Christianson, D. W.; Nyhan, D.; Berkowitz, D. E. Arginase and Vascular Aging. Journal of Applied Physiology 2008, 105 (5), 1632–1642. https://doi.org/10.1152/japplphysiol.90627.2008.

Dowling, D. P.; Di Costanzo, L.; Gennadios, H. A.; Christianson, D. W. Evolution of the Arginase Fold and Functional Diversity. Cell. Mol. Life Sci. 2008, 65 (13), 2039–2055. https://doi.org/10.1007/s00018-008-7554-z.

Aaron, J. A.; Chambers, J. M.; Jude, K. M.; Di Costanzo, L.; Dmochowski, I. J.; Christianson, D. W. Structure of a ¹²⁹ Xe-Cryptophane Biosensor Complexed with Human Carbonic Anhydrase II. J. Am. Chem. Soc. 2008, 130 (22), 6942–6943. https://doi.org/10.1021/ja802214x.

Di Costanzo, L.; Drury, J. E.; Penning, T. M.; Christianson, D. W. Crystal Structure of Human Liver Δ4-3-Ketosteroid 5β-Reductase (AKR1D1) and Implications for Substrate Binding and Catalysis. Journal of Biological Chemistry 2008, 283 (24), 16830–16839. https://doi.org/10.1074/jbc.M801778200.

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. X-Ray Crystallographic Studies of Substrate Binding to Aristolochene Synthase Suggest a Metal Ion Binding Sequence for Catalysis. Journal of Biological Chemistry 2008, 283 (22), 15431–15439. https://doi.org/10.1074/jbc.M800659200.

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.; Huso, D.; Berkowitz, D. E. Endothelial Arginase II: A Novel Target for the Treatment of Atherosclerosis. Circulation Research 2008, 102 (8), 923–932. https://doi.org/10.1161/CIRCRESAHA.107.169573.

Christianson, D. W. Unearthing the Roots of the Terpenome. Current Opinion in Chemical Biology 2008, 12 (2), 141–150. https://doi.org/10.1016/j.cbpa.2007.12.008.

Vedula, L. S.; Jiang, J.; Zakharian, T.; Cane, D. E.; Christianson, D. W. 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– Mg 2 + B Motif. Archives of Biochemistry and Biophysics 2008, 469 (2), 184–194. https://doi.org/10.1016/j.abb.2007.10.015.

Zakharian, T. Y.; Di Costanzo, L.; Christianson, D. W. Synthesis of (2S)-2-Amino-7,8-Epoxyoctanoic Acid and Structure of Its Metal-Bridging Complex with Human Arginase I. Org. Biomol. Chem. 2008, 6 (18), 3240. https://doi.org/10.1039/b811797g.

Vedula, L. S.; Zhao, Y.; Coates, R. M.; Koyama, T.; Cane, D. E.; Christianson, D. W. Exploring Biosynthetic Diversity with Trichodiene Synthase. Archives of Biochemistry and Biophysics 2007, 466 (2), 260–266. https://doi.org/10.1016/j.abb.2007.06.016.

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. Inducible NO Synthase–Dependent S -Nitrosylation and Activation of Arginase1 Contribute to Age-Related Endothelial Dysfunction. Circulation Research 2007, 101 (7), 692–702. https://doi.org/10.1161/CIRCRESAHA.107.157727.

Di Costanzo, L.; Moulin, M.; Haertlein, M.; Meilleur, F.; Christianson, D. W. Expression, Purification, Assay, and Crystal Structure of Perdeuterated Human Arginase I. Archives of Biochemistry and Biophysics 2007, 465 (1), 82–89. https://doi.org/10.1016/j.abb.2007.04.036.

Srivastava, D. K.; Jude, K. M.; Banerjee, A. L.; Haldar, M.; Manokaran, S.; Kooren, J.; Mallik, S.; Christianson, D. W. Structural Analysis of Charge Discrimination in the Binding of Inhibitors to Human Carbonic Anhydrases I and II. J. Am. Chem. Soc. 2007, 129 (17), 5528–5537. https://doi.org/10.1021/ja068359w.

Di Costanzo, L.; Pique, M. E.; Christianson, D. W. Crystal Structure of Human Arginase I Complexed with Thiosemicarbazide Reveals an Unusual Thiocarbonyl μ-Sulfide Ligand in the Binuclear Manganese Cluster. J. Am. Chem. Soc. 2007, 129 (20), 6388–6389. https://doi.org/10.1021/ja071567j.

Christianson, D. W. Roots of Biosynthetic Diversity. Science 2007, 316 (5821), 60–61. https://doi.org/10.1126/science.1141630.

Shin, H.; Gennadios, H. A.; Whittington, D. A.; Christianson, D. W. Amphipathic Benzoic Acid Derivatives: Synthesis and Binding in the Hydrophobic Tunnel of the Zinc Deacetylase LpxC. Bioorganic & Medicinal Chemistry 2007, 15 (7), 2617–2623. https://doi.org/10.1016/j.bmc.2007.01.044.

Shishova, E. Y.; Di Costanzo, L.; Cane, D. E.; Christianson, D. W. X-Ray Crystal Structure of Aristolochene Synthase from Aspergillus Terreus and Evolution of Templates for the Cyclization of Farnesyl Diphosphate ^,. Biochemistry 2007, 46 (7), 1941–1951. https://doi.org/10.1021/bi0622524.

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

Krishnamurthy, V. M.; Bohall, B. R.; Kim, C.; Moustakas, D. T.; Christianson, D. W.; Whitesides, G. M. Thermodynamic Parameters for the Association of Fluorinated Benzenesulfonamides with Bovine Carbonic Anhydrase II. Chemistry  An Asian Journal 2007, 2 (1), 94–105. https://doi.org/10.1002/asia.200600360.

De Vivo, M.; Ensing, B.; Dal Peraro, M.; Gomez, G. A.; Christianson, D. W.; Klein, M. L. Proton Shuttles and Phosphatase Activity in Soluble Epoxide Hydrolase. J. Am. Chem. Soc. 2007, 129 (2), 387–394. https://doi.org/10.1021/ja066150c.

Gennadios, H. A.; Christianson, D. W. Binding of Uridine 5‘-Diphosphate in the “Basic Patch” of the Zinc Deacetylase LpxC and Implications for Substrate Binding ^,. Biochemistry 2006, 45 (51), 15216–15223. https://doi.org/10.1021/bi0619021.

Di Costanzo, L.; Flores, L. V.; Christianson, D. W. Stereochemistry of Guanidine–Metal Interactions: Implications for L ‐arginine–Metal Interactions in Protein Structure and Function. Proteins 2006, 65 (3), 637–642. https://doi.org/10.1002/prot.21127.

Christianson, D. W. Structural Biology and Chemistry of the Terpenoid Cyclases. Chem. Rev. 2006, 106 (8), 3412–3442. https://doi.org/10.1021/cr050286w.

Gennadios, H. A.; Whittington, D. A.; Li, X.; Fierke, C. A.; Christianson, D. W. Mechanistic Inferences from the Binding of Ligands to LpxC, a Metal-Dependent Deacetylase ^,. Biochemistry 2006, 45 (26), 7940–7948. https://doi.org/10.1021/bi060823m.

Christianson, D. W. Five Golden Rings. Science 2006, 311 (5766), 1382–1383. https://doi.org/10.1126/science.1125298.

Jude, K. M.; Banerjee, A. L.; Haldar, M. K.; Manokaran, S.; Roy, B.; Mallik, S.; Srivastava, D. K.; Christianson, D. W. Ultrahigh Resolution Crystal Structures of Human Carbonic Anhydrases I and II Complexed with “Two-Prong” Inhibitors Reveal the Molecular Basis of High Affinity. J. Am. Chem. Soc. 2006, 128 (9), 3011–3018. https://doi.org/10.1021/ja057257n.

Gomez, G. A.; Morisseau, C.; Hammock, B. D.; Christianson, D. W. Human Soluble Epoxide Hydrolase: Structural Basis of Inhibition by 4‐(3‐cyclohexylureido)‐carboxylic Acids. Protein Science 2006, 15 (1), 58–64. https://doi.org/10.1110/ps.051720206.

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. Probing the Role of the Hyper-Reactive Histidine Residue of Arginase. Archives of Biochemistry and Biophysics 2005, 444 (1), 15–26. https://doi.org/10.1016/j.abb.2005.09.009.

Di Costanzo, L.; Sabio, G.; Mora, A.; Rodriguez, P. C.; Ochoa, A. C.; Centeno, F.; Christianson, D. W. Crystal Structure of Human Arginase I at 1.29-Å Resolution and Exploration of Inhibition in the Immune Response. Proc. Natl. Acad. Sci. U.S.A. 2005, 102 (37), 13058–13063. https://doi.org/10.1073/pnas.0504027102.

Vedula, L. S.; Cane, D. E.; Christianson, D. W. Role of Arginine-304 in the Diphosphate-Triggered Active Site Closure Mechanism of Trichodiene Synthase ^,. Biochemistry 2005, 44 (38), 12719–12727. https://doi.org/10.1021/bi0510476.

Vedula, L. S.; Rynkiewicz, M. J.; Pyun, H.-J.; Coates, R. M.; Cane, D. E.; Christianson, D. W. Molecular Recognition of the Substrate Diphosphate Group Governs Product Diversity in Trichodiene Synthase Mutants ^,. Biochemistry 2005, 44 (16), 6153–6163. https://doi.org/10.1021/bi050059o.

Hernick, M.; Gennadios, H. A.; Whittington, D. A.; Rusche, K. M.; Christianson, D. W.; Fierke, C. A. UDP-3-O-((R)-3-Hydroxymyristoyl)-N-Acetylglucosamine Deacetylase Functions through a General Acid-Base Catalyst Pair Mechanism. Journal of Biological Chemistry 2005, 280 (17), 16969–16978. https://doi.org/10.1074/jbc.M413560200.

Christianson, D. W. Arginase: Structure, Mechanism, and Physiological Role in Male and Female Sexual Arousal. Acc. Chem. Res. 2005, 38 (3), 191–201. https://doi.org/10.1021/ar040183k.

Kim, N. N.; Christianson, D. W.; Traish, A. M. Role of Arginase in the Male and Female Sexual Arousal Response. The Journal of Nutrition 2004, 134 (10), 2873S-2879S. https://doi.org/10.1093/jn/134.10.2873S.

Shin, H.; Cama, E.; Christianson, D. W. Design of Amino Acid Aldehydes as Transition-State Analogue Inhibitors of Arginase. J. Am. Chem. Soc. 2004, 126 (33), 10278–10284. https://doi.org/10.1021/ja047788w.

Cama, E.; Pethe, S.; Boucher, J.-L.; Han, S.; Emig, F. A.; Ash, D. E.; Viola, R. E.; Mansuy, D.; Christianson, D. W. Inhibitor Coordination Interactions in the Binuclear Manganese Cluster of Arginase ^,. Biochemistry 2004, 43 (28), 8987–8999. https://doi.org/10.1021/bi0491705.

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

Whittingtons, D. A.; Grubb, J. H.; Waheed, A.; Shah, G. N.; Sly, W. S.; Christianson, D. W. Expression, Assay, and Structure of the Extracellular Domain of Murine Carbonic Anhydrase XIV. Journal of Biological Chemistry 2004, 279 (8), 7223–7228. https://doi.org/10.1074/jbc.M310809200.

Cama, E.; Shin, H.; Christianson, D. W. Design of Amino Acid Sulfonamides as Transition-State Analogue Inhibitors of Arginase. J. Am. Chem. Soc. 2003, 125 (43), 13052–13057. https://doi.org/10.1021/ja036365b.

Xu, L.; Hilliard, B.; Carmody, R. J.; Tsabary, G.; Shin, H.; Christianson, D. W.; Chen, Y. H. Arginase and Autoimmune Inflammation in the Central Nervous System. Immunology 2003, 110 (1), 141–148. https://doi.org/10.1046/j.1365-2567.2003.01713.x.

Whittington, D. A.; Rusche, K. M.; Shin, H.; Fierke, C. A.; Christianson, D. W. Crystal Structure of LpxC, a Zinc-Dependent Deacetylase Essential for Endotoxin Biosynthesis. Proc. Natl. Acad. Sci. U.S.A. 2003, 100 (14), 8146–8150. https://doi.org/10.1073/pnas.1432990100.

Cama, E.; Emig, F. A.; Ash, D. E.; Christianson, D. W. Structural and Functional Importance of First-Shell Metal Ligands in the Binuclear Manganese Cluster of Arginase I ^,. Biochemistry 2003, 42 (25), 7748–7758. https://doi.org/10.1021/bi030074y.

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. Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal ^,. Biochemistry 2003, 42 (28), 8445–8451. https://doi.org/10.1021/bi034340j.

Whittington, D. A.; Wise, M. L.; Urbansky, M.; Coates, R. M.; Croteau, R. B.; Christianson, D. W. Bornyl Diphosphate Synthase: Structure and Strategy for Carbocation Manipulation by a Terpenoid Cyclase. Proc. Natl. Acad. Sci. U.S.A. 2002, 99 (24), 15375–15380. https://doi.org/10.1073/pnas.232591099.

Seemann, M.; Zhai, G.; De Kraker, J.-W.; Paschall, C. M.; Christianson, D. W.; Cane, D. E. Pentalenene Synthase. Analysis of Active Site Residues by Site-Directed Mutagenesis. J. Am. Chem. Soc. 2002, 124 (26), 7681–7689. https://doi.org/10.1021/ja026058q.

Grzybowski, B. A.; Ishchenko, A. V.; Kim, C.-Y.; Topalov, G.; Chapman, R.; Christianson, D. W.; Whitesides, G. M.; Shakhnovich, E. I. Combinatorial Computational Method Gives New Picomolar Ligands for a Known Enzyme. Proc. Natl. Acad. Sci. U.S.A. 2002, 99 (3), 1270–1273. https://doi.org/10.1073/pnas.032673399.

Rynkiewicz, M. J.; Cane, D. E.; Christianson, D. W. X-Ray Crystal Structures of D100E Trichodiene Synthase and Its Pyrophosphate Complex Reveal the Basis for Terpene Product Diversity ^,. Biochemistry 2002, 41 (6), 1732–1741. https://doi.org/10.1021/bi011960g.

Kim, C.-Y.; Whittington, D. A.; Chang, J. S.; Liao, J.; May, J. A.; Christianson, D. W. Structural Aspects of Isozyme Selectivity in the Binding of Inhibitors to Carbonic Anhydrases II and IV. J. Med. Chem. 2002, 45 (4), 888–893. https://doi.org/10.1021/jm010163d.

Jude, K. M.; Wright, S. K.; Tu, C.; Silverman, D. N.; Viola, R. E.; Christianson, D. W. Crystal Structure of F65A/Y131C-Methylimidazole Carbonic Anhydrase V Reveals Architectural Features of an Engineered Proton Shuttle. Biochemistry 2002, 41 (8), 2485–2491. https://doi.org/10.1021/bi015808q.

Madder, R. D.; Kim, C.-Y.; Chandra, P. P.; Doyon, J. B.; Baird, T. A.; Fierke, C. A.; Christianson, D. W.; Voet, J. G.; Jain, A. Twisted Amides Inferred from QSAR Analysis of Hydrophobicity and Electronic Effects on the Affinity of Fluoroaromatic Inhibitors of Carbonic Anhydrase. J. Org. Chem. 2002, 67 (2), 582–584. https://doi.org/10.1021/jo0159385.

Rynkiewicz, M. J.; Cane, D. E.; Christianson, D. W. Structure of Trichodiene Synthase from Fusarium Sporotrichioides Provides Mechanistic Inferences on the Terpene Cyclization Cascade. Proc. Natl. Acad. Sci. U.S.A. 2001, 98 (24), 13543–13548. https://doi.org/10.1073/pnas.231313098.

Kim, C.-Y.; Chandra, P. P.; Jain, A.; Christianson, D. W. Fluoroaromatic−Fluoroaromatic Interactions between Inhibitors Bound in the Crystal Lattice of Human Carbonic Anhydrase II. J. Am. Chem. Soc. 2001, 123 (39), 9620–9627. https://doi.org/10.1021/ja011034p.

Whittington, D. A.; Waheed, A.; Ulmasov, B.; Shah, G. N.; Grubb, J. H.; Sly, W. S.; Christianson, D. W. Crystal Structure of the Dimeric Extracellular Domain of Human Carbonic Anhydrase XII, a Bitopic Membrane Protein Overexpressed in Certain Cancer Tumor Cells. Proc. Natl. Acad. Sci. U.S.A. 2001, 98 (17), 9545–9550. https://doi.org/10.1073/pnas.161301298.

Lavulo, L. T.; Sossong, T. M.; Brigham-Burke, M. R.; Doyle, M. L.; Cox, J. D.; Christianson, D. W.; Ash, D. E. Subunit-Subunit Interactions in Trimeric Arginase. Journal of Biological Chemistry 2001, 276 (17), 14242–14248. https://doi.org/10.1074/jbc.M010575200.

Kim, N. N.; Cox, J. D.; Baggio, R. F.; Emig, F. A.; Mistry, S. K.; Harper, S. L.; Speicher, D. W.; Morris, S. M.; Ash, D. E.; Traish, A.; Christianson, D. W. 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 ^,. Biochemistry 2001, 40 (9), 2678–2688. https://doi.org/10.1021/bi002317h.

Cox, J. D.; Cama, E.; Colleluori, D. M.; Pethe, S.; Boucher, J.-L.; Mansuy, D.; Ash, D. E.; Christianson, D. W. Mechanistic and Metabolic Inferences from the Binding of Substrate Analogues and Products to Arginase ^,. Biochemistry 2001, 40 (9), 2689–2701. https://doi.org/10.1021/bi002318+.

Kim, C.-Y.; Chang, J. S.; Doyon, J. B.; Baird, T. T.; Fierke, C. A.; Jain, A.; Christianson, D. W. Contribution of Fluorine to Protein−Ligand Affinity in the Binding of Fluoroaromatic Inhibitors to Carbonic Anhydrase II. J. Am. Chem. Soc. 2000, 122 (49), 12125–12134. https://doi.org/10.1021/ja002627n.

Cox, J. D.; Hunt, J. A.; Compher, K. M.; Fierke, C. A.; Christianson, D. W. Structural Influence of Hydrophobic Core Residues on Metal Binding and Specificity in Carbonic Anhydrase II ^,. Biochemistry 2000, 39 (45), 13687–13694. https://doi.org/10.1021/bi001649j.

Caruthers, J. M.; Kang, I.; Rynkiewicz, M. J.; Cane, D. E.; Christianson, D. W. Crystal Structure Determination of Aristolochene Synthase from the Blue Cheese Mold, Penicillium Roqueforti*. Journal of Biological Chemistry 2000, 275 (33), 25533–25539. https://doi.org/10.1074/jbc.M000433200.

Yamada, T.; Morisseau, C.; Maxwell, J. E.; Argiriadi, M. A.; Christianson, D. W.; Hammock, B. D. Biochemical Evidence for the Involvement of Tyrosine in Epoxide Activation during the Catalytic Cycle of Epoxide Hydrolase. Journal of Biological Chemistry 2000, 275 (30), 23082–23088. https://doi.org/10.1074/jbc.M001464200.

Doyon, J. B.; Hansen, E. A. M.; Kim, C.-Y.; Chang, J. S.; Christianson, D. W.; Madder, R. D.; Voet, J. G.; Baird, T. A.; Fierke, C. A.; Jain, A. Linear Free Energy Relationships Implicate Three Modes of Binding for Fluoroaromatic Inhibitors to a Mutant of Carbonic Anhydrase II. Org. Lett. 2000, 2 (9), 1189–1192. https://doi.org/10.1021/ol005608r.

Argiriadi, M. A.; Morisseau, C.; Goodrow, M. H.; Dowdy, D. L.; Hammock, B. D.; Christianson, D. W. Binding of Alkylurea Inhibitors to Epoxide Hydrolase Implicates Active Site Tyrosines in Substrate Activation. Journal of Biological Chemistry 2000, 275 (20), 15265–15270. https://doi.org/10.1074/jbc.M000278200.

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. Structures of Enzymes Involved in Terpenoid Biosynthesis. Chemtracts, 2000, 13, 844–852.

Stams, T.; Christianson, D. W. X-Ray Crystallographic Studies of Mammalian Carbonic Anhydrase Isozymes. In The Carbonic Anhydrases; Chegwidden, W. R., Carter, N. D., Edwards, Y. H., Eds.; Birkhäuser Basel: Basel, 2000; pp 159–174. https://doi.org/10.1007/978-3-0348-8446-4_9.

Hunt, J. A.; Lesburg, C. A.; Christianson, D. W.; Thompson, R. B.; Fierke, C. A. Active-Site Engineering of Carbonic Anhydrase and Its Application to Biosensors. In The Carbonic Anhydrases; Chegwidden, W. R., Carter, N. D., Edwards, Y. H., Eds.; Birkhäuser Basel: Basel, 2000; pp 221–240. https://doi.org/10.1007/978-3-0348-8446-4_12.

Ash, D. E.; Cox, J. D.; Christianson, D. W. Arginase: A Binuclear Manganese Metalloenzyme. Metal ions in biological systems 2000, 455–476.

Baggio, R.; Cox, J. D.; Harper, S. L.; Speicher, D. W.; Christianson, D. W. A New Chromophoric Assay for Arginase Activity. Analytical Biochemistry 1999, 276 (2), 251–253. https://doi.org/10.1006/abio.1999.4355.

Christianson, D. W.; Cox, J. D.; Kim, N. N.; Traish, A. M. [No Title Found]. Nat. Struct Biol. 1999, 6 (11), 1043–1047. https://doi.org/10.1038/14929.

Argiriadi, M. A.; Morisseau, C.; Hammock, B. D.; Christianson, D. W. Detoxification of Environmental Mutagens and Carcinogens: Structure, Mechanism, and Evolution of Liver Epoxide Hydrolase. Proc. Natl. Acad. Sci. U.S.A. 1999, 96 (19), 10637–10642. https://doi.org/10.1073/pnas.96.19.10637.

Paschall, C. M.; Hasserodt, J.; Jones, T.; Lerner, R. A.; Janda, K. D.; Christianson, D. W. Convergence of Catalytic Antibody and Terpene Cyclase Mechanisms: Polyene Cyclization Directed by Carbocation-π Interactions. Angew. Chem. Int. Ed. 1999, 38 (12), 1743–1747. https://doi.org/10.1002/(SICI)1521-3773(19990614)38:12<1743::AID-ANIE1743>3.0.CO;2-3.

Christianson, D. W.; Cox, J. D. Catalysis By Metal-Activated Hydroxide in Zinc and Manganese Metalloenzymes. Annu. Rev. Biochem. 1999, 68 (1), 33–57. https://doi.org/10.1146/annurev.biochem.68.1.33.

Baggio, R.; Emig, F. A.; Christianson, D. W.; Ash, D. E.; Chakder, S.; Rattan, S. Biochemical and Functional Profile of a Newly Developed Potent and Isozyme-Selective Arginase Inhibitor. Journal of Pharmacology and Experimental Therapeutics 1999, 290 (3), 1409–1416.

Niranjanakumari, S.; Stams, T.; Crary, S. M.; Christianson, D. W.; Fierke, C. A. Protein Component of the Ribozyme Ribonuclease P Alters Substrate Recognition by Directly Contacting Precursor tRNA. Proc. Natl. Acad. Sci. U.S.A. 1998, 95 (26), 15212–15217. https://doi.org/10.1073/pnas.95.26.15212.

Lesburg, C. A.; Caruthers, J. M.; Paschall, C. M.; Christianson, D. W. Managing and Manipulating Carbocations in Biology: Terpenoid Cyclase Structure and Mechanism. Current Opinion in Structural Biology 1998, 8 (6), 695–703. https://doi.org/10.1016/S0959-440X(98)80088-2.

Boriack‐Sjodin, P. A.; Zeitlin, S.; Christianson, D. W.; Chen, H.; Crenshaw, L.; Gross, S.; Dantanarayana, A.; Delgado, P.; May, J. A.; Dean, T. Structural Analysis of Inhibitor Binding to Human Carbonic Anhydrase II. Protein Science 1998, 7 (12), 2483–2489. https://doi.org/10.1002/pro.5560071201.

Ash, D. E.; Scolnick, L. R.; Kanyo, Z. F.; Vockley, J. G.; Cederbaum, S. D.; Christianson, D. W. Molecular Basis of Hyperargininemia: Structure-Function Consequences of Mutations in Human Liver Arginase. Molecular Genetics and Metabolism 1998, 64 (4), 243–249. https://doi.org/10.1006/mgme.1998.2677.

Stams, T.; Niranjanakumari, S.; Fierke, C. A.; Christianson, D. W. Ribonuclease P Protein Structure: Evolutionary Origins in the Translational Apparatus. Science 1998, 280 (5364), 752–755. https://doi.org/10.1126/science.280.5364.752.

Lukacs, C. M.; Rubin, H.; Christianson, D. W. Engineering an Anion-Binding Cavity in Antichymotrypsin Modulates the “Spring-Loaded” Serpin−Protease Interaction. Biochemistry 1998, 37 (10), 3297–3304. https://doi.org/10.1021/bi972359e.

Stams, T.; Chen, Y.; Christianson, D. W.; Boriack‐Sjodin, P. A.; Hurt, J. D.; Laipis, P.; Silverman, D. N.; Liao, J.; May, J. A.; Dean, T. Structures of Murine Carbonic Anhydrase IV and Human Carbonic Anhydrase II Complexed with Brinzolamide: Molecular Basis of Isozyme‐drug Discrimination. Protein Science 1998, 7 (3), 556–563. https://doi.org/10.1002/pro.5560070303.

Green, N.; Houk, K. N.; Shulz, G. E.; Back, K.; Chappell, J.; Noel, J.; Zhai, G.; Cane, D. E.; Christianson, D. W. Structures of Enzymes Involved in Terpenoid Biosynthesis. Chemtracts, 1998, 11, 537–545.

Lesburg, C. A.; Huang, C.; Christianson, D. W.; Fierke, C. A. Histidine → Carboxamide Ligand Substitutions in the Zinc Binding Site of Carbonic Anhydrase II Alter Metal Coordination Geometry but Retain Catalytic Activity. Biochemistry 1997, 36 (50), 15780–15791. https://doi.org/10.1021/bi971296x.

Lesburg, C. A.; Zhai, G.; Cane, D. E.; Christianson, D. W. Crystal Structure of Pentalenene Synthase: Mechanistic Insights on Terpenoid Cyclization Reactions in Biology. Science 1997, 277 (5333), 1820–1824. https://doi.org/10.1126/science.277.5333.1820.

Scolnick, L. R.; Kanyo, Z. F.; Cavalli, R. C.; Ash, D. E.; Christianson, D. W. Altering the Binuclear Manganese Cluster of Arginase Diminishes Thermostability and Catalytic Function. Biochemistry 1997, 36 (34), 10558–10565. https://doi.org/10.1021/bi970800v.

Baggio, R.; Elbaum, D.; Kanyo, Z. F.; Carroll, P. J.; Cavalli, R. C.; Ash, D. E.; Christianson, D. W. Inhibition of Mn ²⁺ ₂ -Arginase by Borate Leads to the Design of a Transition State Analogue Inhibitor, 2( S )-Amino-6-Boronohexanoic Acid. J. Am. Chem. Soc. 1997, 119 (34), 8107–8108. https://doi.org/10.1021/ja971312d.

Scolnick, L. R.; Clements, A. M.; Liao, J.; Crenshaw, L.; Hellberg, M.; May, J.; Dean, T. R.; Christianson, D. W. Novel Binding Mode of Hydroxamate Inhibitors to Human Carbonic Anhydrase II. J. Am. Chem. Soc. 1997, 119 (4), 850–851. https://doi.org/10.1021/ja963832z.

Christianson, D. W. Structural Chemistry and Biology of Manganese Metalloenzymes. Progress in Biophysics and Molecular Biology 1997, 67 (2–3), 217–252. https://doi.org/10.1016/S0079-6107(97)88477-5.

Stams, T.; Nair, S. K.; Okuyama, T.; Waheed, A.; Sly, W. S.; Christianson, D. W. Crystal Structure of the Secretory Form of Membrane-Associated Human Carbonic Anhydrase IV at 2.8-Å Resolution. Proc. Natl. Acad. Sci. U.S.A. 1996, 93 (24), 13589–13594. https://doi.org/10.1073/pnas.93.24.13589.

Lukacs, C. M.; Zhong, J. Q.; Plotnick, M. I.; Rubin, H.; Cooperman, B. S.; Christianson, D. W. Arginine Substitutions in the Hinge Region of Antichymotrypsin Affect Serpin β-Sheet Rearrangement. Nat Struct Mol Biol 1996, 3 (10), 888–893. https://doi.org/10.1038/nsb1096-888.

Kanyo, Z. F.; Scolnick, L. R.; Ash, D. E.; Christianson, D. W. Structure of a Unique Binuclear Manganese Cluster in Arginase. Nature 1996, 383 (6600), 554–557. https://doi.org/10.1038/383554a0.

Lukacs, C. M.; Christianson, D. W. Is the Binding of β-Amyloid Protein to Antichymotrypsin in Alzheimer Plaques Mediated by a β-Strand Insertion? Proteins 1996, 25 (4), 420–424. https://doi.org/10.1002/prot.2.

Christianson, D. W.; Fierke, C. A. Carbonic Anhydrase: Evolution of the Zinc Binding Site by Nature and by Design. Acc. Chem. Res. 1996, 29 (7), 331–339. https://doi.org/10.1021/ar9501232.

Thompson, R. B.; Ge, Z.; Patchan, M. W.; Fierke, C. A.; McCall, K. A.; Elbaum, D.; Christianson, D. W. Determination of Multiple Analytes Using a Fiber Optic Biosensor Based on Fluorescence Energy Transfer; Cohn, G. E., Soper, S. A., Chen, C. H. W., Eds.; San Jose, CA, 1996; pp 47–56. https://doi.org/10.1117/12.237624.

Stavridi, E. S.; O’Malley, K.; Lukacs, C. M.; Moore, W. T.; Lambris, J. D.; Christianson, D. W.; Rubin, H.; Cooperman, B. S. Structural Change in α-Chymotrypsin Induced by Complexation with α ₁ -Antichymotrypsin As Seen by Enhanced Sensitivity to Proteolysis. Biochemistry 1996, 35 (33), 10608–10615. https://doi.org/10.1021/bi9605806.

Scolnick, L. R.; Christianson, D. W. X-Ray Crystallographic Studies of Alanine-65 Variants of Carbonic Anhydrase II Reveal the Structural Basis of Compromised Proton Transfer in Catalysis. Biochemistry 1996, 35 (51), 16429–16434. https://doi.org/10.1021/bi9617872.

Huang, C.; Lesburg, C. A.; Kiefer, L. L.; Fierke, C. A.; Christianson, D. W. Reversal of the Hydrogen Bond to Zinc Ligand Histidine-119 Dramatically Diminishes Catalysis and Enhances Metal Equilibration Kinetics in Carbonic Anhydrase II. Biochemistry 1996, 35 (11), 3439–3446. https://doi.org/10.1021/bi9526692.

Heck, R. W.; Boriack-Sjodin, P. A.; Qian, M.; Tu, C.; Christianson, D. W.; Laipis, P. J.; Silverman, D. N. Structure-Based Design of an Intramolecular Proton Transfer Site in Murine Carbonic Anhydrase V. Biochemistry 1996, 35 (36), 11605–11611. https://doi.org/10.1021/bi9608018.

Elbaum, D.; Nair, S. K.; Patchan, M. W.; Thompson, R. B.; Christianson, D. W. Structure-Based Design of a Sulfonamide Probe for Fluorescence Anisotropy Detection of Zinc with a Carbonic Anhydrase-Based Biosensor. J. Am. Chem. Soc. 1996, 118 (35), 8381–8387. https://doi.org/10.1021/ja954102e.

Nair, S. K.; Elbaum, D.; Christianson, D. W. Unexpected Binding Mode of the Sulfonamide Fluorophore 5-Dimethylamino-1-Naphthalene Sulfonamide to Human Carbonic Anhydrase II. Journal of Biological Chemistry 1996, 271 (2), 1003–1007. https://doi.org/10.1074/jbc.271.2.1003.

Boriack-Sjodin, P. A.; Heck, R. W.; Laipis, P. J.; Silverman, D. N.; Christianson, D. W. Structure Determination of Murine Mitochondrial Carbonic Anhydrase V at 2.45-A Resolution: Implications for Catalytic Proton Transfer and Inhibitor Design. Proc. Natl. Acad. Sci. U.S.A. 1995, 92 (24), 10949–10953. https://doi.org/10.1073/pnas.92.24.10949.

Lesburg, C. A.; Lloyd, M. D.; Cane, D. E.; Christianson, D. W. Crystallization and Preliminary X‐ray Diffraction Analysis of Recombinant Pentalenene Synthase. Protein Science 1995, 4 (11), 2436–2438. https://doi.org/10.1002/pro.5560041124.

Lesburg, C. A.; Christianson, D. W. X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in a Protein-Zinc Binding Site. J. Am. Chem. Soc. 1995, 117 (26), 6838–6844. https://doi.org/10.1021/ja00131a005.

Katz, D. S.; Christianson, D. W. Structural Aspects of the Serpin Reaction Coordinate. Perspectives in Drug Discovery and Design 1995, 2 (3), 459–474. https://doi.org/10.1007/BF02172038.

Boriack, P. A.; Christianson, D. W.; Kingery-Wood, J.; Whitesides, G. M. Secondary Interactions Significantly Removed from the Sulfonamide Binding Pocket of Carbonic Anhydrase II Influence Inhibitor Binding Constants. J. Med. Chem. 1995, 38 (13), 2286–2291. https://doi.org/10.1021/jm00013a004.

Ippolito, J. A.; Baird, T. T.; McGee, S. A.; Christianson, D. W.; Fierke, C. A. Structure-Assisted Redesign of a Protein-Zinc-Binding Site with Femtomolar Affinity. Proc. Natl. Acad. Sci. U.S.A. 1995, 92 (11), 5017–5021. https://doi.org/10.1073/pnas.92.11.5017.

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

Ippolito, J. A.; Nair, S. K.; Alexander, R. S.; Kiefer, L. L.; Fierke, C. A.; Christianson, D. W. Structure of His94→Asp Carbonic Anhydrase II in a New Crystalline Form Reveals a Partially Occupied Zinc Binding Site. Protein Eng Des Sel 1995, 8 (10), 975–980. https://doi.org/10.1093/protein/8.10.975.

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

Katz, D. S.; White, S. P.; Huang, W.; Kumar, R.; Christianson, D. W. Structure Determination of Aquomet Porcine Hemoglobin at 2.8 Å Resolution. Journal of Molecular Biology 1994, 244 (5), 541–553. https://doi.org/10.1006/jmbi.1994.1751.

Jain, A.; Whitesides, G. M.; Alexander, R. S.; Christianson, D. W. 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. J. Med. Chem. 1994, 37 (13), 2100–2105. https://doi.org/10.1021/jm00039a023.

Cappalonga Bunn, A. M.; Alexander, R. S.; Christianson, D. W. Mapping Protein-Peptide Affinity: Binding of Peptidylsulfonamide Inhibitors to Human Carbonic Anhydrase II. J. Am. Chem. Soc. 1994, 116 (12), 5063–5068. https://doi.org/10.1021/ja00091a006.

Wei, A.; Rubin, H.; Cooperman, B. S.; Christianson, D. W. Crystal Structure of an Uncleaved Serpin Reveals the Conformation of an Inhibitory Reactive Loop. Nat Struct Mol Biol 1994, 1 (4), 251–258. https://doi.org/10.1038/nsb0494-251.

Nair, S. K.; Ludwig, P. A.; Christianson, D. W. Two-Site Binding of Phenol in the Active Site of Human Carbonic Anhydrase II: Structural Implications for Substrate Association. J. Am. Chem. Soc. 1994, 116 (8), 3659–3660. https://doi.org/10.1021/ja00087a086.

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. Positions of His‐64 and a Bound Water in Human Carbonic Anhydrase II upon Binding Three Structurally Related Inhibitors. Protein Science 1994, 3 (1), 118–125. https://doi.org/10.1002/pro.5560030115.

Krebs, J. F.; Ippolito, J. A.; Christianson, D. W.; Fierke, C. A. Structural and Functional Importance of a Conserved Hydrogen Bond Network in Human Carbonic Anhydrase II. Journal of Biological Chemistry 1993, 268 (36), 27458–27466. https://doi.org/10.1016/S0021-9258(19)74269-0.

Kiefer, L. L.; Ippolito, J. A.; Fierke, C. A.; Christianson, D. W. Redesigning the Zinc Binding Site of Human Carbonic Anhydrase II: Structure of a His2Asp-Zn2+ Metal Coordination Polyhedron. J. Am. Chem. Soc. 1993, 115 (26), 12581–12582. https://doi.org/10.1021/ja00079a046.

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

Katz, D. S.; Wei, A. Z.; Zhong, Q. H.; Rubin, H.; Cooperman, B. S.; Christianson, D. W. Crystallization and Atomic Resolution X-Ray Diffraction Analysis of Antichymotrypsin Variants. Biochemical and Biophysical Research Communications 1993, 196 (2), 752–757. https://doi.org/10.1006/bbrc.1993.2313.

Ippolito, J. A.; Christianson, D. W. Structure of an Engineered His3 Cys Zinc Binding Site in Human Carbonic Anhydrase II. Biochemistry 1993, 32 (38), 9901–9905. https://doi.org/10.1021/bi00089a005.

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. Purification and Characterization of Klebsiella Aerogenes UreE Protein: A Nickel‐binding Protein That Functions in Urease Metallocenter Assembly. Protein Science 1993, 2 (6), 1042–1052. https://doi.org/10.1002/pro.5560020617.

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

Nair, S. K.; Christianson, D. W. Crystallographic Studies of Azide Binding to Human Carbonic Anhydrase II. European Journal of Biochemistry 1993, 213 (1), 507–515. https://doi.org/10.1111/j.1432-1033.1993.tb17788.x.

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

Katz, D. S.; Christianson, D. W. Modeling the Uncleaved Serpin Antichymotrypsin and Its Chymotrypsin Complex. Protein Eng Des Sel 1993, 6 (7), 701–709. https://doi.org/10.1093/protein/6.7.701.

Firby, R. J.; Christianson, D.; McDougal, T. Fast Local Mapping to Support Navigation and Object Localization; Schenker, P. S., Ed.; Boston, MA, 1992; pp 344–352. https://doi.org/10.1117/12.131664.

Cappalonga, A. M.; Alexander, R. S.; Christianson, D. W. Structural Comparison of Sulfodiimine and Sulfonamide Inhibitors in Their Complexes with Zinc Enzymes. Journal of Biological Chemistry 1992, 267 (27), 19192–19197. https://doi.org/10.1016/S0021-9258(18)41760-7.

Ippolito, J. A.; Christianson, D. W. The Contribution of Halogen Atoms to Protein-Ligand Interactions. International Journal of Biological Macromolecules 1992, 14 (4), 193–197. https://doi.org/10.1016/S0141-8130(05)80026-1.

Wei, A.; Rubin, H.; Cooperman, B. S.; Schechter, N.; Christianson, D. W. Crystallization, Activity Assay and Preliminary X-Ray Diffraction Analysis of the Uncleaved Form of the Serpin Antichymotrypsin. Journal of Molecular Biology 1992, 226 (1), 273–276. https://doi.org/10.1016/0022-2836(92)90140-F.

Kanyo, Z. F.; Chen, C.-Y.; Daghigh, F.; Ash, D. E.; Christianson, D. W. Crystallization and Oligomeric Structure of Rat Liver Arginase. Journal of Molecular Biology 1992, 224 (4), 1175–1177. https://doi.org/10.1016/0022-2836(92)90479-4.

Nair, S. K.; Christianson, D. W. Unexpected pH-Dependent Conformation of His-64, the Proton Shuttle of Carbonic Anhydrase II. J. Am. Chem. Soc. 1991, 113 (25), 9455–9458. https://doi.org/10.1021/ja00025a005.

Nair, S. K.; Christianson, D. W. Structural Properties of Human Carbonic Anhydrase II at pH 9.5. Biochemical and Biophysical Research Communications 1991, 181 (2), 579–584. https://doi.org/10.1016/0006-291X(91)91229-6.

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

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

Nair, S. K.; Calderone, T. L.; Christianson, D. W.; Fierke, C. A. Altering the Mouth of a Hydrophobic Pocket. Structure and Kinetics of Human Carbonic Anhydrase II Mutants at Residue Val-121. Journal of Biological Chemistry 1991, 266 (26), 17320–17325. https://doi.org/10.1016/S0021-9258(19)47376-6.

Kanyo, Z. F.; Christianson, D. W. Biological Recognition of Phosphate and Sulfate. Journal of Biological Chemistry 1991, 266 (7), 4264–4268. https://doi.org/10.1016/S0021-9258(20)64316-2.

Christianson, D. W. Structural Biology of Zinc. In Advances in Protein Chemistry; Elsevier, 1991; Vol. 42, pp 281–355. https://doi.org/10.1016/S0065-3233(08)60538-0.

Ippolito, J. A.; Alexander, R. S.; Christianson, D. W. Hydrogen Bond Stereochemistry in Protein Structure and Function. Journal of Molecular Biology 1990, 215 (3), 457–471. https://doi.org/10.1016/S0022-2836(05)80364-X.

Christianson, D. W.; Alexander, R. S. Another Catalytic Triad? Nature 1990, 346 (6281), 225–225. https://doi.org/10.1038/346225b0.

Alexander, R. S.; Kanyo, Z. F.; Chirlian, L. E.; Christianson, D. W. Stereochemistry of Phosphate-Lewis Acid Interactions: Implications for Nucleic Acid Structure and Recognition. J. Am. Chem. Soc. 1990, 112 (3), 933–937. https://doi.org/10.1021/ja00159a004.

Christianson, D. W.; Alexander, R. S. Carboxylate-Histidine-Zinc Interactions in Protein Structure and Function. J. Am. Chem. Soc. 1989, 111 (16), 6412–6419. https://doi.org/10.1021/ja00198a065.

Christianson, D. W.; Mangani, S.; Shoham, G.; Lipscomb, W. N. Binding of D-Phenylalanine and D-Tyrosine to Carboxypeptidase A. Journal of Biological Chemistry 1989, 264 (22), 12849–12853. https://doi.org/10.1016/S0021-9258(18)51564-7.

Christianson, D. W.; Lipscomb, W. N. Carboxypeptidase A. Acc. Chem. Res. 1989, 22 (2), 62–69. https://doi.org/10.1021/ar00158a003.

Christianson, D. W.; Lipscomb, W. N. Comparison of Carboxypeptidase A and Thermolysin: Inhibition by Phosphonamidates. J. Am. Chem. Soc. 1988, 110 (16), 5560–5565. https://doi.org/10.1021/ja00224a047.

Shoham, G.; Christianson, D. W.; Oren, D. A. Complex between Carboxypeptidase A and a Hydrated Ketomethylene Substrate Analogue. Proc. Natl. Acad. Sci. U.S.A. 1988, 85 (3), 684–688. https://doi.org/10.1073/pnas.85.3.684.

Christianson, D. W.; Lipscomb, W. N. Carboxypeptidase A: Novel Enzyme-Substrate-Product Complex. J. Am. Chem. Soc. 1987, 109 (18), 5536–5538. https://doi.org/10.1021/ja00252a046.

Christianson, D. W.; David, P. R.; Lipscomb, W. N. Mechanism of Carboxypeptidase A: Hydration of a Ketonic Substrate Analogue. Proc. Natl. Acad. Sci. U.S.A. 1987, 84 (6), 1512–1515. https://doi.org/10.1073/pnas.84.6.1512.

Christianson, D. W.; Lipscomb, W. N. X-Ray Crystallographic Investigation of Substrate Binding to Carboxypeptidase A at Subzero Temperature. Proc. Natl. Acad. Sci. U.S.A. 1986, 83 (20), 7568–7572. https://doi.org/10.1073/pnas.83.20.7568.

Christianson, D. W.; Lipscomb, W. N. Complex between Carboxypeptidase A and a Possible Transition-State Analog: Mechanistic Inferences from High-Resolution x-Ray Structures of Enzyme-Inhibitor Complexes. J. Am. Chem. Soc. 1986, 108 (16), 4998–5003. https://doi.org/10.1021/ja00276a048.

Christianson, D. W.; Lipscomb, W. N. Structure of the Complex between an Unexpectedly Hydrolyzed Phosphonamidate Inhibitor and Carboxypeptidase A. J. Am. Chem. Soc. 1986, 108 (3), 545–546. https://doi.org/10.1021/ja00263a052.

Christianson, D. W.; Kuo, L. C.; Lipscomb, W. N. Novel Structure of the Complex between Carboxypeptidase A and a Ketonic Substrate Analog. J. Am. Chem. Soc. 1985, 107 (26), 8281–8283. https://doi.org/10.1021/ja00312a089.

Christianson, D. W.; Lipscomb, W. N. Binding of a Possible Transition State Analogue to the Active Site of Carboxypeptidase A. Proc. Natl. Acad. Sci. U.S.A. 1985, 82 (20), 6840–6844. https://doi.org/10.1073/pnas.82.20.6840.

Christianson, D. W.; Lipscomb, W. N. A Molecular Orbital Evaluation of Possible Factors Affecting the Homolytic Activation of Coenzyme B12. J. Am. Chem. Soc. 1985, 107 (9), 2682–2686. https://doi.org/10.1021/ja00295a021.

Shoham, G.; Christianson, D. W.; Bartsch, R. A.; Heo, G. S.; Olsher, U.; Lipscomb, W. N. Crystal and Molecular Structure of the Complex between Sym-Dibenzo-14-Crown-4-Oxyacetate and Lithium(1+) Ion, [C20H21O7]-.Cntdot.Li+.Cntdot.7.5H2O. J. Am. Chem. Soc. 1984, 106 (5), 1280–1285. https://doi.org/10.1021/ja00317a018.