Publications | David Frick Lab

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Frick Lab Research (UWM)

COVID-19 (SARS-CoV-2)

Virdi, R. S., R. V. Bavisotto, N. C. Hopper, N. Vuksanovic, T. R. Melkonian, N. R. Silvaggi, and D. N. Frick. 2020. Discovery of Drug-Like Ligands for the Mac1 Domain of SARS-CoV-2 Nsp3. SLAS Discov 25: 1162-1170.
Frick, D. N., Virdi, R. S., Vuksanovic, N., Dahal, N., Silvaggi, N. R. (2020). Molecular Basis for ADP-Ribose Binding to the Mac1 Domain of SARS-CoV-2 nsp3. Biochemistry, 59(28), 2608-2615. PDF
Frick, D. N., Bavisotto, R. V., Hopper, N. C. and Tysoe, W. T. (2025) Analogs of NIH Molecular Probe ML283 Are Potent SARS-CoV-2 Helicase Inhibitors. ACS Chem Biol.

NUDIX

Ray, A., Frick, D. N. (2020). Fluorescent probe displacement assays reveal unique nucleic acid binding properties of human nudix enzymes. Analytical Biochemistry, 595, 113622. PDF
Frick, D. N., Shittu, M., Bock, C. R., Wardle, Z. P., Rauf, A. A., Ramos, J. N., Thomson, J. G., Sheibley, D. J. and O’Handley, S. F. (2025) Optimization of a high throughput screening platform to identify inhibitors of asymmetric diadenosine polyphosphatases. Anal Biochem 697, 115713. PDF

Hepatitis C Virus (HCV)

Corby, M. J., Raicu, V., Frick, D. N. (2019). New Techniques to Study Intracellular Receptors in Living Cells: Insights Into RIG-I-Like Receptor Signaling. Advances in Experimental Medicine and Biology, 1111, 219-240. PDF
Yerukhimovich, M. M., Marohnic, C. C., Frick, D. N. (2018). Role of the Conserved DECH-Box Cysteine in Coupling Hepatitis C Virus Helicase-Catalyzed ATP Hydrolysis to RNA Unwinding. Biochemistry, 57(43), 6247-6255. PDF
Corby, M. J., Stoneman, M. R., Biener, G., Paprocki, J. D., Kolli, R., Raicu, V., and Frick, D. N. (2017). Quantitative microspectroscopic imaging reveals viral and cellular RNA helicase interactions in live cells. J Biol Chem 292, 11165-11177. PDF
Ndjomou, J., Corby, M. J., Sweeney, N. L., Hanson, A. M., Aydin, C., Ali, A., Schiffer, C. A., Li, K., Frankowski, K. J., Schoenen, F. J. & Frick, D. N. (2015) Simultaneously Targeting the NS3 Protease and Helicase Activities for More Effective Hepatitis C Virus Therapy. ACS Chem Biol 10, 1887-1896. PDF
Sweeney, N. L., Hanson, A. M., Mukherjee, S., Ndjomou, J., Geiss, B. J., Steel, J. J., Frankowski, K. J., Li, K., Schoenen, F. J., and Frick, D. N. (2015). Benzothiazole and pyrrolone flavivirus inhibitors targeting the viral helicase. ACS Infect. Dis. 1, 140-148. PDF
Mukherjee, S., Weiner, W. S., Schroeder, C. E., Simpson, D. S., Hanson, A. M., Sweeney, N. L., Marvin, R. K., Ndjomou, J., Kolli, R., Isailovic, D., Schoenen, F. J., and Frick, D. N. (2014). Ebselen Inhibits Hepatitis C Virus NS3 Helicase Binding to Nucleic Acid and Prevents Viral Replication. ACS Chem Biol 9, 2393-2403. PDF
Shadrick, W. R., Mukherjee, S., Hanson, A. M., Sweeney, N. L., and Frick, D. N. (2013) Aurintricarboxylic Acid Modulates the Affinity of Hepatitis C Virus NS3 Helicase for Both Nucleic Acid and ATP. Biochemistry, 52, 6151-6159. PDF
Li, K., Frankowski, K. J., Hanson, A. M., Ndjomou, J., Shanahan, M. A., Mukherjee, S., Kolli, R., Shadrick, W. R., Sweeney, N. L., Belon, C. A., Neuenswander, B., Ferguson, J., Aube, J., Schoenen, F. J., Blagg, B. S. J., and Frick, D. N. (2013) Hepatitis C Virus NS3 Helicase Inhibitor Discovery. Probe Reports from the NIH Molecular Libraries Program. PDF
Shadrick, W. R., Ndjomou, J., Kolli, R., Mukherjee, S., Hanson, A. M., and Frick, D. N. (2013) Discovering New Medicines Targeting Helicases: Challenges and Recent Progress. J. Biomol. Screen 18, 761-781. PDF
Hanson, Alicia M., and Frick, David N. Molecular Beacon based helicase assays on the FLUOstar Omega. BMG Application Notes (2013). PDF
Sweeney, N. L., Shadrick, W. R., Mukherjee, S., Li, K., Frankowski, K. J., Schoenen, F. J. & Frick, D. N. (2013) Primuline Derivatives That Mimic RNA To Stimulate Hepatitis C Virus NS3 Helicase-Catalyzed ATP Hydrolysis. J. Biol. Chem., 288, 19949-19957. PDF
Ndjomou, J., Kolli, R., Mukherjee, S., Shadrick, W. R., Hanson, A. M., Sweeney, N. L., Bartczak, D., Li, K., Frankowski, K. J., Schoenen, F. J. & Frick, D. N. (2012) Fluorescent primuline derivatives inhibit hepatitis C virus NS3-catalyzed RNA unwinding, peptide hydrolysis and viral replicase formation. Antiviral Res. 96, 245-255. PDF
Mukherjee,S., Hanson,A.M., Shadrick,W.R., Ndjomou,J., Sweeney,N.L., Hernandez,J.J., Bartczak,D., Li,K., Frankowski,K.J., Heck,J.A., Arnold,L.A., Schoenen,F.J. and Frick,D.N. (2012) Identification and analysis of hepatitis C virus NS3 helicase inhibitors using nucleic acid binding assays. Nucleic Acids Res. 40, 8607-8621. PDF
Li,K., Frankowski,K.J., Belon,C.A., Neunswander,B., Ndjomou,J., Hanson,A.M., Shanahan,M.A., Schoenen,F.J., Blagg,B.S., Aube,J. and Frick,D.N. (2012) Optimization of Potent Hepatitis C Virus NS3 Helicase Inhibitors Isolated from the Yellow Dyes Thioflavine S and Primuline. J. Med. Chem. 55, 3319-3330. PDF
Hanson,A.M., Hernandez,J.J., Shadrick,W.R. and Frick,D.N. (2012) Identification and analysis of inhibitors targeting the hepatitis C virus NS3 helicase. Methods Enzymol. 511, 463-483. PDF
Belon, C. A., & Frick, D. N. (2010) NS3 Helicase inhibitors. Chapter 12 in Hepatitis C: Antiviral Drug Discovery and Development (He, Y & Tan, S-L, eds.), Horizon press., pp 237-256. PDF

Papers with the Hosssain Lab (UWM)

Rahman, A. F. M. T., Bulbule, S., Belayet, J. B., Benko, A., Gottschalk, C. G., Frick, D. N., Arnold, L. A., Hossain, M. M. and Roy, A. (2024) JRM-28, a Novel HDAC2 Inhibitor, Upregulates Plasticity-Associated Proteins in Hippocampal Neurons and Enhances Morphological Plasticity via Activation of CREB: Implications for Alzheimer’s Disease. Cells 13, 1964.
Belayet, J. B., Beamish, S., Rahaman, M., Alanani, S., Virdi, R. S., Frick, D. N., Rahman, A. F. M. T., Ulicki, J. S., Biswas, S., Arnold, L. A., Roni, M. S. R., Cheng, E. Y., Steeber, D. A., Frick, K. M. and Hossain, M. M. (2022) Development of a Novel, Small-Molecule Brain-Penetrant Histone Deacetylase Inhibitor That Enhances Spatial Memory Formation in Mice. J Med Chem 65, 3388-3403.

Paper with the Peng Lab (UWM)

Zhang, Q., Ali, T., Ponnamperumage, T. N. F., Lin, Z., Setu, N. I., Awoyera, W. O., Oddiri, R. T., Rasmussen, A. D., Felli, M. C., Frick, D. N. and Peng, X. (2025) A Photoinducible DNA Cross-Linking Agent with Potent Cytotoxicity and Selectivity Toward Triple-Negative Breast Cancer Cell Line. Chem Res Toxicol 38, 216-228.

Papers with the Brancale Lab (Cardiff, UK)

Bassetto, M., Leyssen, P., Neyts, J., Yerukhimovich, M. M., Frick, D. N., and Brancale, A. (2017). Shape-based virtual screening, synthesis and evaluation of novel pyrrolone derivatives as antiviral agents against HCV. Bioorg Med Chem Lett 27, 936-940. PDF
Bassetto, M., Ferla, S., Leyssen, P., Neyts, J., Yerukhimovich, M. M., Frick, D. N., O’Donnell, R., and Brancale, A. (2016). Novel symmetrical phenylenediamines as potential anti-hepatitis C virus agents. Antivir. Chem. Chemother. PDF
Bassetto, M., Leyssen, P., Neyts, J., Yerukhimovich, M. M., Frick, D. N., Courtney-Smith, M., and Brancale, A. (2016). In silico identification, design and synthesis of novel piperazine-based antiviral agents targeting the hepatitis C virus helicase. Eur J Med Chem 125, 1115-1131. PDF
Bassetto, M., Leyssen, P., Neyts, J., Yerukhimovich, M. M., Frick, D. N., and Brancale, A. (2016). Computer-aided identification, synthesis and evaluation of substituted thienopyrimidines as novel inhibitors of HCV replication. Eur J Med Chem 123, 31-47. PDF

Paper with Paola Provazzi (São Paulo, Brazil)

Provazzi, P. J., S. Mukherjee, A. M. Hanson, M. L. Nogueira, B. M. Carneiro, D. N. Frick, and P. Rahal. (2015) Analysis of the Enzymatic Activity of an NS3 Helicase Genotype 3a Variant Sequence Obtained from a Relapse Patient. PLoS One 10: e0144638. PDF

Papers with the Barreca and Kaushik-Basu labs

Andreev, I. A., Manvar, D., Barreca, M. L., Belov, D. S., Basu, A., Sweeney, N. L., Ratmanova, N. K., Lukyanenko, E. R., Manfroni, G., Cecchetti, V., Frick, D. N., Altieri, A., Kaushik-Basu, N. & Kurkin, A. V. (2015) Discovery of the 2-phenyl-4,5,6,7-Tetrahydro-1H-indole as a novel anti-hepatitis C virus targeting scaffold. Eur. J. Med. Chem. 96, 250-258. PDF
Kaushik-Basu, N., Ratmanova, N. K., Manvar, D., Belov, D. S., Cevik, O., Basu, A., Yerukhimovich, M. M., Lukyanenko, E. R., Andreev, I. A., Belov, G. M., Manfroni, G., Cecchetti, V., Frick, D. N., Kurkin, A. V., Altieri, A., and Barreca, M. L. (2016). Bicyclic octahydrocyclohepta[b]pyrrol-4(1H)one derivatives as novel selective anti-hepatitis C virus agents. Eur J Med Chem 122: 319-325. PDF

Paper with the Dey lab (UWM)

Mannan, M. A., Shadrick, W. R., Biener, G., Shin, B. S., Anshu, A., Raicu, V., Frick, D. N., and Dey, M. (2013) An Ire1-Phk1 Chimera Reveals a Dispensable Role of Autokinase Activity in Endoplasmic Reticulum Stress Response. J. Mol. Biol. 425, 2083-2099. PDF

Paper with the Bolognesi Lab (Milano, Italy)

Mastrangelo, E., Pezzullo, M., De Burghgraeve, T., Kaptein, S., Pastorino, B., Dallmeier, K., de Lamballerie, X., Neyts, J., Hanson, A. M., Frick, D. N., Bolognesi, M. & Milani, M. (2012) Ivermectin is a potent inhibitor of flavivirus replication specifically targeting NS3 helicase activity: new prospects for an old drug. J. Antimicrob. Chemother. 67, 1884-1894. PDF

Paper with the Schiffer Lab (UMASS Medical School)

Aydin, C., Mukherjee, S., Hanson, A. M., Frick, D. N. & Schiffer, C. A. (2013) The Interdomain Interface in Hepatitis C Virus (HCV) Bifunctional Enzyme Non-Structural Protein 3/4A (NS3/4A) Regulates Protease and Helicase Activities. Protein Science, 22, 1786-1798. PDF

Frick Lab Research (NYMC)

Belon, C. A., High, Y. D., Lin, T. I., Pauwels, F. & Frick, D. N. (2010) Mechanism and specificity of a symmetrical benzimidazole-phenyl-carboxamide helicase inhibitor. Biochemistry, 49(9):1822-32. PDF
Frick, D. N., Ginzburg, O., & Lam, A. M. (2010) A method to monitor NS3 helicase and protease activities together in real time. Methods in Molecular Biology, 587, 223-234. PDF
Belon, C. A. & Frick, D. N. (2009) Helicase Inhibitors as Specifically Targeted Antiviral Therapy For Hepatitis C. Future Virology, 4(3), 277-293. PDF
Rypma, R. S., Lam, A. M. I., & Frick, D. N. (2009) Effect of substrate traps on hepatitis C virus NS3 helicase catalyzed DNA unwinding: Evidence for enzyme catalyzed strand exchange. Chapter 11 in Bacterial DNA, DNA polymerase and DNA helicases (Knudsen, W. D & Bruns. S. S, eds.), Nova Science Publishers, pp. 389-407. PDF
Belon, C. A., & Frick, D. N. (2009) Fuel specificity of the hepatitis C virus NS3 helicase. J Mol Biol, 388,851-864. PDF
Heck, J. A., Meng, X, & Frick, D. N. (2009) Cyclophilin B stimulates RNA synthesis by the hepatitis C virus RNA dependent RNA polymerase.Biochem. Pharm., 77(7):1173-80. PDF
Belon, C. A. & Frick D. N (2008) Monitoring Helicase Activity with Molecular Beacons. Biotechniques, 45(4): 433-42. PDF
Heck, J. A., A. M. Lam, N. Narayanan, and D. N. Frick. (2008) Effects of mutagenic and chain terminating nucleotide analogs on enzymes isolated from various hepatitis C virus genotypes. Antimicrob. Agents Chemother. 52(6) 1901- 1911. PDF
Frick, D. N. (2007) The hepatitis C Virus NS3 protein: A model RNA helicase and potential drug target. Curr. Issues Mol. Biol., 9, 1-20. PDF
Frick, D. N., Banik, S, & Rypma, R. S. (2007) Role of divalent metal cations in ATP hydrolysis catalyzed by the hepatitis C virus NS3 helicase: Magnesium provides a bridge for ATP to fuel unwinding. J. Mol. Biol., 365, 1017-32. PDF
Frick, D. N. (2006) HCV Helicase: Structure, Function, and Inhibition. Chapter 7 in Hepatitis C Viruses: Genomes and Molecular Biology, Horizon press, pp. 207-244. PDF
Frick, D. N. (2006) Step-by-step progress towards understanding the hepatitis C virus RNA helicase. Hepatology, 43, 1392-5. PDF
Frick, D. N. & Lam, A. M. I. (2006) Understanding helicases as a means of virus control. Curr. Pharm. Des., 12, 1315-1338. PDF
Lam, A. M. I. & Frick, D. N. (2006) Hepatitis C Virus Subgenomic Replicon Requires an Active NS3 RNA Helicase, J. Virol., 80, 404-11. PDF
Frick, D. N., Rypma, R. S., Lam, A. M. I., & Frenz, C. (2004) Electrostatic analysis of the hepatitis C virus NS3 helicase reveals both active and allosteric site locations. Nucleic Acids Res., 32, 5519-5528. PDF
Lam, A. M. I., Rypma, R. S., & Frick D. N. (2004) Enhanced nucleic acid binding to ATP-bound Hepatitis C virus NS3 helicase at low pH activates RNA unwinding. Nucleic Acids Res., 32, 4060-4070. PDF
Frick, D. N. (2004) The Hepatitis C virus replicase: Insights into RNA-dependent RNA replication and prospects for rational drug design.Current Org. Chem. 8, 223-241. PDF
Frick, D. N. (2003) Helicases as antiviral drug targets. Drug News Perspect. 16, 355-362. PDF
Frick, D. N., Rypma, R. S., Lam, A. M. I., & Gu, B. (2004) The nonstructural protein 3 Protease/Helicase Requires an Intact Protease Domain to Efficiently Unwind Duplex RNA. J. Biol. Chem. 279, 1269-1280. PDF
Lam, A. M. I., Keeney, D., & Frick, D. N. (2003) Two novel conserved motifs in the hepatitis C virus NS3 protein critical for helicase action. J. Biol. Chem. 278, 44514-24. PDF
Lam., A.M.I. , Keeney, D., Eckert, P. Q. & Frick, D. N. (2003) Hepatitis C virus NS3 ATPase/Helicases from different genotypes exhibit variations in enzymatic properties. J. Virol. 77, 3950-3961. PDF

Paper with the Timm Lab (Germany)

Neumann-Haefelin, C., Frick, D. N. , Wang, J. J. , Pybus, O. G., Salloum, S., Narula, G. S., Eckart, A., Biezynski, A., Eiermann, T., Klenerman, P., Viazov, S., Roggendorf, M., Thimme, R., Reiser, M., & Timm. J. (2008) Analysis of the evolutionary forces in an immunodominant CD8 epitope in the hepatitis C virus at a population level. J. Virol. 82: 3438-3451. PDF

Papers with Pharmasett Inc.

Lemon, S. M., McKeating, J. A., Pietschmann, T., Frick, D. N., Glenn, J. S., Tellinghuisen, T. L., Symons, J., and Furman, P. A. (2010) Development of novel therapies for hepatitis C, Antiviral Res 86, 79-92. PDF

Lam, A. M., Murakami, E., Espiritu, C., Steuer, H. M., Niu, C., Keilman, M., Bao, H., Zennou, V., Bourne, N., Julander, J. G., Morrey, J. D., Smee, D. F., Frick, D. N., Heck, J. A., Wang, P., Nagarathnam, D., Ross, B. S., Sofia, M. J., Otto, M. J., and Furman, P. A. (2010) PSI-7851, a pronucleotide of beta-D-2’-deoxy-2’-fluoro-2’-C-methyluridine monophosphate, is a potent and pan-genotype inhibitor of hepatitis C virus replication, Antimicrob Agents Chemother 54, 3187-3196. PDF

Paper with the Strossberg Lab (Scripps Florida)

Mousseau, G., Kota, S., Takahashi, V., Frick, D. N., and Strosberg, A. D. (2011) Dimerization-driven interaction of hepatitis c virus core protein with NS3 helicase, J Gen Virol 92, 101-111. PDF

Paper with the Chung Lab (Mass General Hospital )

Peng,L.F., Schaefer,E.A., Maloof,N., Skaff,A., Berical,A., Belon,C.A., Heck,J.A., Lin,W., Frick,D.N., Allen,T.M., Miziorko,H.M., Schreiber,S.L. and Chung,R.T. (2011) Ceestatin, a novel small molecule inhibitor of hepatitis C virus replication, inhibits 3-hydroxy-3-methylglutaryl-coenzyme a synthase. J Infect Dis 204, 609-616. PDF

Papers with the Lee Lab (New York Medical College)

Meng, X., Zhou, Y., Lee, E. Y., Lee, M. Y. & Frick, D. N. (2010). The p12 subunit of human polymerase delta modulates the rate and fidelity of DNA synthesis. Biochemistry, 49(17):3545-54. PDF
Meng, X., Zhou, Y., Zhang, S., Lee, E. Y. C, Frick, D. N., & Lee, M. Y. W. T. (2008) DNA damage alters DNA Polymerase delta; to a form that exhibits increased discrimination against modified template bases and mismatched primers. Nucleic Acids Res., 37, 647-657. PDF

Papers with the Richardson Lab (Harvard Medical School)

Frick, D. N., Baradaran, K., & Richardson, C. C. (1998) An N-terminal fragment of the gene 4 helicase/primase of bacteriophage T7 retains primase activity in the absence of helicase activity. Proc. Natl. Acad. Sci. USA 95, 7957-7962. PDF
Frick, D. N., & Richardson, C. C. (1999) Interaction of Bacteriophage T7 gene 4 primase with its template recognition site. J. Biol. Chem. 274, 35889-35898. PDF
Frick, D. N., Kumar, S., & Richardson, C. C. (1999) Interaction of ribonucleoside triphosphates with the Gene 4 Primase of bacteriophage T7. J. Biol. Chem. 274, 35899-35907. PDF
Tseng, T. Y., Frick, D. N., & Richardson, C. C. (2000) Characterization of a novel DNA primase from the Salmonella typhimurium bacteriophage SP6. Biochemistry 39, 1643-1654. PDF
Frick, D. N. & Richardson C. C. (2001) DNA primases. Annu. Rev. Biochem. 70, 39-80. PDF

Papers with the Ellenberger Lab (Harvard Medical School)

Kato, M., Frick, D. N., Lee, J, Tabor, S, Richardson, C. C., & Ellenberger T. (2001) A complex of the bacteriophage T7 primase-helicase and DNA polymerase directs primer utilization. J. Biol. Chem. 276, 21809-21820. PDF

Papers with the Mildvan Lab (Johns Hopkins)

Abeygunawardana, C., Weber, D. J., Frick, D. N., Bessman, M. J., and Mildvan, A. S. (1993) Sequence-specific assignments of the backbone 1H, 13C, and 15N resonances of the MutT Enzyme by heteronuclear multidimensional NMR. Biochemistry 32, 13071-13080. PDF
Frick, D. N., Weber, D. J., Gillespie, J. R., Bessman, M. J., and Mildvan, A. S. (1994) Dual divalent cation requirement of the MutT dGTPase: kinetic and magnetic resonance studies of the metal and substrate complexes. J. Biol. Chem. 269, 1794-1803. PDF
Frick, D. N., Weber, D. J., Abeygunawardana, C., Gittis, A. G., Bessman, M. J., and Mildvan, A. S. (1995) NMR Studies of the conformations and location of nucleotides bound to the E. coli MutT enzyme. Biochemistry 34, 5577-5586. PDF
Abeygunawardana, C., Weber, D. J., Gittis, A. G., Frick, D. N., Miller, A. F., Bessman, M. J., Lin, J., and Mildvan, A. S. (1995) The solution structure of the Escherichia coli MutT Protein: A nucleoside triphosphate pyrophosphohydrolase. Biochemistry 34, 14997-15005. PDF
Lin, J., Abeygunawardana, C., Frick, D. N., Bessman, M. J., & Mildvan, A. S. (1996) Studies of the role of Glu 57 in the mechanism of the E. coli MutT enzyme by mutagenesis and heteronuclear NMR. Biochemistry 35, 6716-6726. PDF
Lin, J., Abeygunawardana, C., Frick, D. N., Bessman, M. J., & Mildvan, A. S. (1997) Solution structure of the quaternary MutT-M2+-AMPCPP-M2+ complex and mechanism of its pyrophosphohydrolase action. Biochemistry 36, 1199-1211. PDF

Papers with the Bessman Lab (Johns Hopkins)

Frick, D. N. and Bessman, M. J. (1995) Cloning, purification, and properties of a Novel NADH pyrophosphatase: Evidence for a Nucleotide pyrophosphatase catalytic domain in MutT-like enzymes. J. Biol. Chem. 270, 1529-1534. PDF
Frick, D. N., Townsend, B. D., & Bessman, M. J. (1995) An E. coli GDP-mannose mannosyl hydrolase shares Homology with the MutT-family of Enzymes. J. Biol. Chem. 270, 24086-24091. PDF
O’Handley, S. F., Frick, D. N., Bullions, L. C., Mildvan, A. S., & Bessman, M. J. (1996) Escherichia coli orf17 Codes for a nucleoside triphosphate pyrophosphohydrolase member of the MutT Family of proteins: Cloning, purification, and characterization of the enzyme. J. Biol. Chem. 271, 24649-24654. PDF
Bessman, M. J., Frick, D. N., & O’Handley, S. F. (1996) The MutT proteins or “nudix” hydrolases, a family of versatile, widely-distributed, enzymes. J. Biol. Chem. 271, 25059-25062. PDF
O’Handley, S. F., Frick, D. N., Dunn, C. A., & Bessman, M. J. (1997) Orf186 Represents a new member of the nudix hydrolases, active on Adenosine(5′)triphospho(5′) adenosine, ADP-ribose, and NADH. J. Biol. Chem. 273, 3192-3197. PDF
Dunn, C. A., O’Handley, S. F., Frick, D. N., & Bessman, M. J. (1999) Studies on the ADP-ribose pyrophosphatase subfamily of the nudix hydrolases and tentative identification of trgB, a gene associated with tellurite resistance. J. Biol. Chem. 274, 32318-32324. PDF