Deprez-poulain R*, Hennuyer N, Bosc D, Liang WG, Enee E, Marechal X, Charton J, Totobenazara J, Berte G, Jahklal J, Verdelet T, Dumont J, Dassonneville S, Woitrain E, Gauriot M, Paquet C, Duplan I, Hermant P, Cantrelle F-X, Sevin E, Culot M, Landry V, Herledan A, Piveteau C, Lippens G, Leroux F, Tang W-J*, van Endert P, Staels B, & Deprez B* (2015) Catalytic Site Inhibition of Insulin Degrading Enzyme by a Small Molecule Induces Glucose Intolerance in Mice. Nature Communications 6: 8250 (*co-corresponding authors).

Liang, W.G., Ren, M., Zhao, F., and Tang, W.-J. (2015) Structures of human CCL18, CCL3, and CCL4 reveal molecular determinants for quaternary structures and sensitivity to insulin degrading enzyme. J. Mol. Biol. 417:1345-1358.

Charton, J., Gauriot, M., Totobenazara, J., Hennuyer, N., Dumont, J., Bosc, D., Marechai, X., Elbakali, J., Herledan A., Wen, X., Ronco, C., Gras-Masse, H., Heninot, A., Pottiez, V., Landry, V., Staels, B., Liang W.G., Leroux, F., Tang, W.-J., Deprez, B., and Deprez-Poulain, R. (2015) Structure–activity relationships of imidazole-derived 2-[N-carbamoylmethyl-alkylamino]acetic acids, dual binders of human insulin-degrading enzyme. Eur. J. Med. Chem. 90:547-567.

Tanaka-Matakatsu., M, Miller, J., Borger, D., Tang, W.-J., Du, W. (2014) Daughterless homodimer synergizes with Eyeless to induce Atonal expression and retinal neuron differentiation. Developmental Biology 392:256-265.

King, J.V., Liang, W.G., Scherpelz, K.P., Schilling, A.B., Meredith, S.C., and Tang, W.-J. (2014) Molecular basis of substrate recognition and degradation by human presequence protease. Structure 22:996-1007.

Charton, J., Gauriot, M., Guo, G., Hennuyer, N., Marechal, X., Dumont, J., Hamdane, M., Pottiez, V., Landry, V., Sperandio, O., Flipo, M., Buee, L., Staels, B., Leroux, F., Tang, W.-J., Deprez, B., and Deprez-Poulain, R. (2014) Imidazole-derived 2-[N-carbamoylmethyl-alkylamino]acetic acids, substrate-dependent modulators of insulin-degrading enzyme in amyloid-β hydrolysis. Eur. J. Med. Chem. 79:184-193.

Maianti, J.P., McFedries, A., Foda, Z.H., Kleiner, R.E., Du, X.-Q., Tang, W.-J., Charron, M.J., Seeliger, M.A., Saghatellian, A., and Liu, D.R. (2014) Anti-diabetic activity of insulin degrading enzyme inhibitors mediated by multiple hormones. Nature 511:94-98.

McCord L.A., Liang, W.G., Dowdell, E., Kalas, V., Hoey, R.J., Koide, A., Koide, S., and Tang, W.-J. (2013) Conformational states and recognition of amyloidogenic peptides of human insulin-degrading enzyme Proc. Natl. Acad. Sci. USA 110(34):13827-32.

Tripathi A, Saini V, Marchese A, Volkman BF, Tang WJ, Majetschak M. (2013) Modulation of the CXC Chemokine Receptor 4 Agonist Activity of Ubiquitin through C-Terminal Protein Modification. Biochemistry 52(24):4184-92.

Mones, L., Tang, W.J., and Florian, J. (2013) Empirical valence bond simulations of the chemical mechanism of ATP to cAMP conversion by anthrax edema factor. Biochemistry 52(15):2672-82.

Schuler D., Lübker C., Lushington, GH, Tang, WJ, Shen Y, Richter M, and Seifert R. (2012) Interactions of Bordetella pertussis adenylyl cyclase toxin CyaA with calmodulin mutants and calmodulin antagonists: Comparison with membranous adenylyl cyclase I. Biochem. Pharmacol. 83:839-848.

Cortright, J.J., Lorrain, D.S., Beeler, J.A., Tang, W.J., and Vezina, P. (2012) Previous exposure to delta9-tetrahydrocannibinol enhances locomotor responding to but not self-administration of amphetamine. J. Pharmacol. Exp. Ther. 337:724-733. 

Saini, V., Marchese, A., Tang, W.-J., Majetschak, M. (2011) Structural determinants of ubiquitin-CXC chemokine receptor 4 interaction. J. Biol. Chem. 286(51):44145-52.

Dumetz, F., Jouvion, G., Khun, H., Glomski, I.J., Corre, J.-P., Rougeaux, C., Tang, W.-J., Mock, M., Huerre, M., and Goossens, P. (2011) Noninvasive imaging technologies reveal edema toxin as a key virulence factor in anthrax. Am. J .Pathol. 178:2523-2535.

Ralat, L.A., Kalas, V., Zheng, Z., Goldman, R.D., Sosnick, T.R., Tang, W.-J. (2011) Ubiquitin is a novel substrate for human insulin degrading enzyme. J. Mol. Biol. 406:454-466. 

Ralat, L.A., Guo, Q., Ren, M., Funke, T., Dickey, D.M., Potter, L.R., and Tang, W.-J. (2011) Insulin-degrading enzyme modulates the natriuretic peptide- mediated signaling response. J. Biol. Chem. 286:4670-4679.

Geduhn, J., Dove, S., Shen, Y., Tang, W.J., Konig, B., and Seifert, R. (2011) Bis-halogen-anthraniloyl-substituted nucleoside 5′-triphosphates as potent and selective inhibitors of Bordetella pertussis J. Pharmacol. Exp. Ther. 336:104-115.

Ren, M., Guo, Q., Guo, L., Lenz, M., Qian, F., Koenen, R.R., Xu, H., Schilling, A.B., Weber, C., Ye, R.D., Dinner, A.R., and Tang, W.-J. (2010) Polymerization of MIP-1 chemokine (CCL-3 and CCL-4) and clearance of MIP-1 by insulin degrading enzyme. EMBO J. 29:3952-3966.

Leissring, M.A., Malito, E., Hedouin, S., Reinstatler, L., Sahara, T., Abdul-Hay S.O., Choudhry, S., Maharvi, G.M., Fauq, A.H., Huzarska, M., May, P.S. Choi, S., Logan, T.P., Turk, B.E., Cantley, L.C., Manolopoulou, M., Tang, W.-J., Stein, R.L., Cuny, G.D., and Selkoe, D.J. (2010) Designed inhibitors of insulin-degrading enzyme regulate the catabolism and activity of insulin. PLoS One 5:e10504.

Duverger, A., Carré, J.M., Jee, J., Leppla, S.H., Cormet-Boyaka, E., Tang, W.J., Tomé, D., and Boyaka, P.N. (2010) Contributions of edema factor and protective antigen to the induction of protective immunity by Bacillus anthracis edema toxin as an intranasal adjuvant. J Immunol. 2010 185:5943-52.

Laine, E., Goncalves, C., Karst, J.C., Lesnard, A., Rault, S., Tang, W.J., Malliavin, T.E., Ladant, D., and Blondel, A. (2010) Use of allostery to identify inhibitors of calmodulin-induced activation of Bacillus anthracis edema factor. Proc. Natl. Acad. Sci. USA 107:11277-82

Göttle, M., Dove, S., Kee, F., Schlossmann, J., Geduhn, J., König, B., Shen, Y., Tang, W.-J., Kaever, V., and Seifert R. (2010) Cytidylyl and Uridylyl cyclase activity of Bacillus anthracis edema factor and Bordetella pertussis CyaA. Biochemistry 49:5494-5503.

Bishop, B.L. Lodolce, J.P., Kolodziej, L.E., Boone, D.L., and Tang, W.J. (2010) The role of anthrolysin O in gut epithelial barrier disruption during Bacillus anthracis Biochem. Biophys. Res. Commun. 394:254-259.

Guo Q, Manolopoulou M, Bian Y, Schilling AB, Tang W.J. (2010) Molecular Basis for the Recognition and Cleavages of IGF-II, TGF-alpha, and Amylin by Human Insulin-Degrading Enzyme. J. Mol. Biol. 395:430-443.

Ralat, L.A., Ren, M., Schilling, A.B., and Tang, W.J. (2009) Protective role of CYS-178 against the inactivation and oligomerization of human insulin-degrading enzyme by oxidation and nitrosylation. J. Biol. Chem. 284:34005-18

Hughes, M.A., Burns, D.L., Juris, S.J., Tang, W.J., Clement , K.H., Eaton, L.J., Kelly-Cirino, C.D., McKee, M.L., Powell, B.S., Bishop, B.L., Rudge, T.L., Shine, N., Verma, A, .Willis, M.S., and Morse, S.A. (2009) The Case for Developing Consensus Standards for Research in Microbial Pathogenesis: Bacillus anthracis Toxins as an Example. Infect Immun 77:4182-6.

Chou, Y.H., Kuo, W.L., Rosner, M.R., Tang, W.J., and Goldman, R.D. (2009) Structural changes in intermediate filament networks alter the activity of insulin-degrading enzyme. FASEB J 23:3734-42.

Suryanarayana, S., Wang, J.L., Richter. M., Shen, Y., Tang, W.J., Lushington, G.H., Seifert, R. (2009) Distinct interactions of 2′- and 3′-O-(N-methyl)anthraniloyl-isomers of ATP and GTP with the adenylyl cyclase toxin of Bacillus anthracis, edema factor. Biochem Pharmacol. 78:224-30.

Szarowicz, S.E., During, R.L., Li, W., Quinn, C.P., Tang, W.J., Southwick, F.S. (2009) Bacillus anthracis edema toxin impairs neutrophil actin-based motility. Infect Immun. 77:2455-64.

Bourdeau, R.W., Malito, E., Chenal, A., Bishop, B.L., Musch, M.W., Villereal, M.L., Chang, E.B., Mosser, E.M., Rest, R.F., and Tang, W.J. (2009) Cellular functions and X-ray structure of anthrolysin O, a cholesterol-dependent cytolysin secreted by Bacillus anthracis. J. Biol. Chem. 284:14645-56.

Manolopoulou, M., Guo, Q., Malito, E. Schilling, A, and Tang, W.J. (2009) Molecular basis of catalytic chamber-assisted unfolding and cleavage of human insulin by human insulin degrading enzyme. J Biol Chem 284:14177-88.

Taha HM, Schmidt J, Göttle M, Suryanarayana S, Shen Y, Tang WJ, Gille A, Geduhn J, König B, Dove S, Seifert R. (2009) Molecular analysis of the interaction of anthrax adenylyl cyclase toxin, edema factor, with 2′(3′)-O-(N-(methyl)anthraniloyl)-substituted purine and pyrimidine nucleotides. Mol Pharmacol 75:693-703.

Tang, W.-J. and Guo, Q. (2009) The adenylyl cyclase activity of anthrax edema factor. Molecular Aspects of Medicine 30:423-30.

Hulse, R. E. Ralat, L.A. and Tang, W.-J. (2009) Structure, function, and regulation of insulin-degrading enzyme. Vitamin and Hormones 80:635-48.

Malito, E., Hulse, R.E., and Tang, W.-J. (2008) Amyloid-β degrading cryptidase: insulin degrading enzyme, presequence peptidase, and neprilysin. CMLS 65:2574-85.

Yfanti C, Mengele K, Gkazepis A, Weirich G, Giersig C, Kuo WL, Tang WJ, Rosner M, Schmitt M. (2008) Expression of metalloprotease insulin-degrading enzyme insulysin in normal and malignant human tissues. Int J Mol Med. 2008 22:421-31.

Kastrup, C.J., Boedicker, J.Q., Pomerantsev, A.P., Moayeri, M., Bian, Y., Pompano, R.R., Kline, T.R., Sylvestre, P., Shen, F., Leppla, S.H., Tang, W.-J., and Ismagilov, R.F. (2008) Spatial localization of bacteria controls coagulation of human blood by ‘quorum acting’. Nature Chem Biol 4:742-750.

Weirich, G., Mengele, K., Yfanti, C., Gkazepis, A., Hellmann, D., Welk, A., Giersig, C., Kuo, W.L., Rosner, M.R., Tang, W.-J., and Schmitt, M. (2008) Immunohistochemical evidence for ubiquitous distribution of the metalloendoprotease insulin-degrading enzyme (IDE; insulysin) in human non-malignant tissues and tumor cell lines. Biol Chem 389:1441-1445.

Malito, E., Ralat, L.A. Manolopoulou, M., Tsay, J.L., Wadlington, N.L. and Tang, W.-J. (2008) Molecular Bases for the Recognition of Short Peptide Substrates and Cysteine-Directed Modifications of Human Insulin-Degrading Enzyme. Biochemistry 47:12822-12834.

Spangler, C.M., Spangler, C., Göttle, M. Shen, Y., Tang, W.-J., Seifert, R., and Schäferling, M. (2008) A fluorimetric assay for real-time monitoring of adenylyl cyclase activity based on terbium norfloxacin. Anal Biochem 381:86-93.

Guo, Q., Jureller, J.E., Warren, J., Solomaha, E. Florián, J., and Tang, W.-J. (2008) Protein-protein docking and analysis reveal that two homologous bacterial adenylyl cyclase toxins interact with calmodulin differently. J Biol Chem 283:23836-23845.

Kim, C., Wilcox-Adelman, S., Sano, Y., Tang, W.-J., Collier, R.J., and Park, J.M. (2008) Antiinflammatory cAMP signaling and cell migration genes co-opted by the anthrax bacillus. Proc Natl Acad Sci U S A. 105:6150-5.

Kuo, S.R., Willingham, M.C., Bour, S.H., Andreas, E.A., Park, S.K., Jackson, C., Duesbery, N.S. Leppla, S.H., Tang, W.-J., and Frankel, A.E. (2008) Anthrax toxin-induced shock in rats is associated with pulmonary edema and hemorrhage. Microb Pathog. 44:467-72.

Warren, J., Guo, Q., and Tang, W.-J. (2007) Structure of zinc-bound N-terminal domain of calmodulin reveals the molecular basis for the initial metal-ligated conformation of calmodulin. J. Mol. Biol. 374:517-27.

Li, Q., Krogmann T., Ali M.A., Tang W.-J., and Cohen J.I. (2007) The amino terminus of varicella-zoster virus (VZV) glycoprotein E is required for binding to insulin-degrading enzyme, a VZV receptor. J Virol. 81:8525-8532.

Johnson, E.C.B. Malito, E., Shen, Y., Rich, D., Tang, W.-J. and Kent, S.B.H. (2007) A biomimetic total chemical synthesis of the HIV-1 protease. J. Am. Chem. Soc. 129(37):11480-11490.

Johnson, E.C.B., Malito, E., Shen, Y., Pentelute, B., Rich, R., Florián, J., Tang, W.-J., Kent, S.B.H. (2007) New insights from atomic-resolution structures of chemically synthesized HIV-1 protease in complex with inhibitors. J. Mol. Biol. 373:573-86.

Watson, L.E., Kuo, S.R., Katki, K., Dang, T., Park, S.K., Dostal, D.E. Tang, W.J., Leppla, S.H., and Frankel, A.E. (2007) Anthrax toxins induce shock in rats by depressed cardiac ventricular function. PLoS ONE 2:e466.

Göttle, M., Steindel, P., Shen, Y., Tang, W.-J., Geduhn, J., König, B., and Seifert, R. (2007) Molecular analysis of the interaction of Bordetella pertussis adenylyl cyclase with fluorescent nucleotides. Mol. Pharm. 72:526-35.

Im, H., Manolopoulou, M., Malito, E., Shen, Y., Zhao, J., Neant-Fery, M., Sun, C.-Y., Meredith, S.C., Sisodia, S.S., Leissring, M., and Tang, W.-J. (2007) Structure of substrate-free human insulin degrading enzyme (IDE) and biophysical analysis of ATP-induced conformational switch of IDE. J. Biol. Chem. 282:25453-63.

Hong, J., Doebele, R.C., Lingen, M.W., Quilliam, L.A., Tang, W.-J., and Rosner, M.R. (2007) Anthrax edema toxin inhibits endothelial cell chemotaxis via EPAC and Rap1. J. Biol. Chem. 82:19781-7.

Watson, L.E. Mock, J., Lal, H., Lu, G., Bourdeau, R.W., Tang, W.J., Leppla, S.H., Dostal, D.E., and Frankel, A.E. (2007) Lethal and edema toxins of anthrax induce distinct hemodynamic dysfunction. Front Biosci 12:4670-4675

Firoved, A.M., Moayeri, M., Wiggins, J.F., Shen, Y., Tang, W.-J., and Leppla, S.H. (2007) Anthrax edema toxin sensitizes DBA/2J mice to lethal toxin. Infection and Immunity, 75: 2120-2125.

Shen, Y., Joachimiak, A., Rosner, M.R., and Tang, W.-J. (2006) Structures of human insulin degrading enzyme reveal a new substrate recognition mechanism. Nature 443:870-874. (Highlighted in N&V Nature 443:761, 2006)

Li, P., Kuo, W.-L., Yousef, M., Rosner, M.R., and Tang, W.-J. (2006) The C-terminal domain of human insulin degrading enzyme is required for dimerization and substrate recognition. Biochem. Biophys. Research Comm., 343:1032-1037.

Guo, Q., Shen, Y., Lee, Y.-S., Gibbs, C.S., Mrksich, M., and Tang, W.-J. (2005) Structural basis for the interaction of adenylyl cyclase toxin of Bordetella pertussis with calmodulin. EMBO J. 24:3190-3201.

Hong, J., Beeler, J., Zhukovskaya, N.L., He, W., Tang, W.-J., and Rosner, M.R. (2005) Anthrax edema toxin potency depends on mode of cell entry. Biochem. Biophys. Research Comm., 335:850-857.

Firoved, A.M., Miller, G., Moayeri, M., Kakkar, R., Shen, Y., Wiggins, J., McNally, E.M., Tang, W.-J., and Leppla, S.H. (2005) Bacillus anthracis edema toxin causes extensive tissue lesions and rapid lethality in mice. J. Pathol. 167:1309-1320.

Alappat, E.C. Feig, C., Volkland, J., Boyerinas, B., Samuels, M., Murmann, A.E., Thorburn, A., Kidd, V.J., Slaughter, C., Osborn, S.L., Winoto, A., Tang, W.-J., and Peter, M.E. (2005) Phosphorylation of FADD at serine 194 by CKIα regulates its nonapoptotic activities. Molecular Cell, 19:321-332.

Tournier, J.-N., Quesnel-Hellmann, A., Mathieu, J., Brochier, G., Montecucco, C., Tang, W.-J., Mock, M., Vidal, D.R., and Goossens, P.L. (2005) Anthrax edema and lethal toxins cooperate to impair cytokine secretion during dendritic cell infection. J. Immunol. 174:4934-4941.

Shen, Y., Zhukovskaya, N.L., Guo, Q., Florián, J., and Tang, W.-J. (2005) Calcium-independent calmodulin binding and two-metal-ion catalytic mechanism of anthrax edema factor. EMBO J. 24:929-941.

Paccani,S.R., Tonello, F., Ghittoni, R. Natale, M., Muraro, L., d’elios, M.M., Tang, W.-J., Montecucco, C., and Baldari, C.T. (2005) Anthrax toxins suppress T-lymphocyte activation by disrupting antigen receptor signaling. J. Exp. Med. 201:325-31.

Beeler, J.A., Yan, S.-Z., Bykov, S., Murza, A., Asher, S., Tang, W.-J. (2004) A stable C1b soluble protein and its regulation of soluble type 7 adenylyl cyclase: a prototype for soluble C1b model. Biochemistry 43(49):15463-71.

Lee, Y.-S., Bergson, P., He, W.-S., Mrksich, M., Tang, W.-J. (2004) Discovery of a small molecule that inhibits the interaction of anthrax edema factor with its cellular activator, calmodulin. Chem. & Biol. 11:1139-46

Guo, Q., Shen, Y.-Q., Zhukovskaya, N.L., Florián, J., and Tang, W.-J. (2004) Structural and kinetic analyses of the interaction of anthrax adenylyl cyclase toxin with reaction products, cAMP and pyrophosphate. J. Biol. Chem. 279:29427-29435.

Min, D.-H., Tang, W.-J., and Mrksich, M. (2004) Chemical screening by mass spectrometry to identify inhibitors of anthrax lethal factor. Nature Biotech. 22:717-723.

Shen, Y.-Q., Guo, Q., Zhukovskaya, N.L., Bohm, A., and Tang, W.-J. (2004) Structure of anthrax edema factor-calmodulin-α,β-methyleneadenosine 5’-triphosphate complex reveals an alternative mode of ATP binding to the catalytic site. Biochem. Biophys. Research Comm. 317:309-314.

Simons, P., Biggs, S., Waller, A., Foutz, T., Cimino, D.F., Guo, Q., Lim, W.K., Neubig, R.R., Tang, W.-J., Prossnitz, E., and Sklar, L.A. (2004) Direct evidence for partial agonist activity at the agonist-receptor-G-protein complex step of signal transduction. J. Biol. Chem. 279:13514-21.

Shen, Y.-Q., Zhukovskaya, N.L., Zimmer, M.I., Soelaiman, S., Wang, C.R., Gibbs, C.S., Tang, W.-J. (2004) Selective inhibition of anthrax edema factor by adefovir, a drug for chronic hepatitis B virus infection. Proc. Natl. Acad. Sci. U.S.A. 101:3242-3247.

Papa, S. Zazzeroni, F., Bubici, C., Jayawardena, S., Pham, C., Alvarez, K., Matsuda, S., Nguyen, D.U., Nelsbach, A. H., Melis, T., De Smaele, E., Tang, W.-J., D’Adamio, L., Franzoso, G. (2004) Gadd45β mediates the NF-kB suppression of JNK signaling by targeting MKK7/JNKK2. Cell Biol. 6:146-53.

Beeler, J., and Tang, W.-J. (2003) Expression and purification of soluble adenylyl cyclase system from Escherichia coli. Methods in Molecular Biology, 237:39-53.

Soelaiman, S., Wei, B., Bergson, P., Lee, Y.-S., Shen, Y., Mrksich, M., Shoichet, B., Tang, W.-J. (2003) Structure-based inhibitor discovery against anthrax adenylyl cyclase toxins from pathogenic bacteria that cause anthrax and whooping cough. J. Biol. Chem., 278:25990-25997.

Ulmer, T., Soelaiman, S., Li, S., Klee, C. B., Tang, W.-J., and Bax, A. (2003) Calcium-dependence of the anthrax edema factor calmodulin interaction. J. Biol. Chem. 278:29261-29266.

Shen, Y.-Q., Lee, Y.-S., Soelaiman, S., Bergson, P., Lu, D., Chen, A., Beckingham, K., Grabarek, Z., Mrksich, M., Tang, W.-J. (2002) Physiological calcium concentrations regulate calmodulin binding and catalysis of adenylyl cyclase exotoxins. EMBO J. 21: 6721-6732.

Drum, C.L., Yan, S.-Z., Bard, J., Shen, Y.-Q., Lu, D., Soelaiman, S., Grabarek, Z., Bohm, A.*, and Tang, W.-J.* (2002) Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin. Nature 415:396-402. (Highlighted in N&V Nature 415: 373, 2002; N &V Nature Structure Biology 9:156, 2002; Minireview Cell 108:739, 2002) (*co-corresponding authors).

Yan, S.-Z. and Tang, W.-J. (2001) Improved method to express α subunit of Gs in coli. Methods in Enzymology 344:172-175.

Yan, S.-Z. and Tang, W.-J. (2001) The construction of soluble adenylyl cyclase from human membrane-bound type 7 adenylyl cyclase. Methods in Enzymology 345:231-241.

Drum, C.L., Shen, Y., Rice, P., Bohm, A., and Tang, W.-J. (2001) Crystallization and preliminary X-ray study of the edema factor exotoxin adenylyl cyclase domain from Bacillus anthracis in the presence of its activator, calmodulin. Acta Crystallographica D. Biological crystallography, D57:1881-1884

Yan, S.-Z. Beeler, J. Chen, Y., Shelton, R.K., and Tang, W.-J. (2001) The regulation of human type 7 adenylyl cyclase by C1b and coli peptidyl prolyl isomerase, slyD. J. Biol. Chem. 276: 8500-8506.

Kudlacek, O., Mitterauer, T., Nanoff, C., Hohenegger, M., Tang, W.-J., Freissmuth, M., and Kleuss, C. (2001) Inhibition of adenylyl and guanylyl cyclase isoforms by the antiviral drug foscarnet. J. Biol. Chem. 276(5):3010-3016.

Drum, C.L., Yan, S.-Z., Sarac, R., Mabuchi, Y., Beckingham, K., Bohm, A., Grabarek, Z., and Tang, W.-J. (2000) An extended conformation of calmodulin induces interactions between the structural domains of adenylyl cyclase from Bacillus anthracis to promote catalysis. J. Biol. Chem. 275:36334-36340.

Hou, Ping, Yan, S.-Z., Tang, W.-J., and Nelson, D.J. (1999) The inwardly rectifying K⁺ channel subunit GIRK1 rescues the GIRK2 weaver phenotype. J. Neurosci. 19(19):8327-36.

Chakrabarti S, Wang L, Tang W.-J., Gintzler AR. (1998) Chronic morphine augments adenylyl cyclase phosphorylation: relevance to altered signaling during tolerance/dependence Mol. Pharmacol. 54:949-53.

Mitterauer, T., Hoheregger, M., Tang, W.-J., Nanoff, C., Freissmuth, M. (1998) The C2 catalytic domain of adenylyl cyclase contains the second metal ion (Mn²⁺) binding site. Biochemistry 37:16183-16191.

Chakrabarti, S., Rivera, M., Yan, S.-Z., Tang, W.-J., and Gintzler, A.R. (1998) Chronic morphine augments Gβγ/G_sα stimulation of adenylyl cyclase: relevance to opioid tolerance. Mol. Pharm. 54:655-662.

Yan,S.-Z., Huang, Z.-H., Andrews R.K., and Tang,W.-J. (1998) Conversion of forskolin insensitive to sensitive (mouse type IX) adenylyl cyclase. Mol. Pharm. 53:182-187.

Tang, W.-J., and Hurley,J.H. (1998) Catalytic mechanism and regulation of mammalian adenylyl cyclases. Mol. Pharm. 54:231-240.

Tang, W.-J., Yan, S.-Z., and Drum, C. (1997) Class III adenylyl cyclase – regulation and underlying mechanisms. Advances in Second Messenger and Phosphoprotein Research.  32:137-151.

Yan, S.-Z., Huang, Z.-H., Rao, V.D., Hurley, J.H., and Tang, W.-J. (1997) Three discrete regions of mammalian adenylyl cyclase form a site for G_sα J. Biol. Chem. 272:18849-18854.

Yan, S.-Z., Huang, Z.-H., Shaw, R.S., and Tang, W.-J. (1997) The conserved asparagine and arginine are crucial for catalysis of mammalian adenylyl cyclase. J. Biol. Chem. 272:12342-12349.

Zhang, G., Liu, Y., Qin, J., Vo, B., Tang, W.-J., Ruoho, A.E., and Hurley, J.H. (1997) Characterization and crystallization of a minimal catalytic core domain from mammalian type II adenylyl cyclase. Protein science 6:903-908.

Robbins, J.D., Boring, D.L., Tang, W.-J., Shank, R., Seamon, K.B. (1996) Forskolin carbamate: binding and activation studies with type I adenylyl cyclase. J. Med. Chem. 39:2745-2752.

Sutkowski, E.M., Robbins, J.D., Tang,W.-J., and Seamon, K.B. (1996) Irreversible inhibition of forskolin interation with type I adenylyl cyclase by 6-isothiocyanate derivative of forskolin. Pharmacol. 50:299-305.

Yan, S.-Z., Hahn, D., Huang, Z.-H., and Tang, W.-J. (1996) Two cytoplasmic domains of mammalian adenylyl cyclase form a G_sα and forskolin-activated enzyme in vitro. J. Biol. Chem. 271:10941-10945.