{"id":7,"date":"2018-10-19T13:58:06","date_gmt":"2018-10-19T13:58:06","guid":{"rendered":"https:\/\/cafnrfaculty.missouri.edu\/tannerlab\/?page_id=7"},"modified":"2026-04-14T18:09:22","modified_gmt":"2026-04-14T18:09:22","slug":"publications","status":"publish","type":"page","link":"https:\/\/cafnrfaculty.missouri.edu\/tannerlab\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"
\n

Tanner Lab publication list in PubMed<\/a><\/p>\n

\n

2026<\/b><\/p>\n

185. Targeting a unique cysteine residue to achieve isoform-selective inhibition of the proline biosynthetic enzyme pyrroline-5-carboxylate reductase 2.<\/strong>
\nT.C. Rossman, K.R. Meeks, G. Purohit, M.J. Naldret, J.J. Tanner,\u00a0 & D. F. Becker
\nACS Chemical Biology, Accepted 04\/14\/2026<\/p>\n

184. Structural Principles of Covalent Flavin Modification in Oxidoreductases<\/strong>
\nJohn J. Tanner
\nBiochemistry, Accepted 04\/14\/2026<\/p>\n

183. Serendipitous Discovery of an Allosteric Inhibitor Binding Groove in the Proline Biosynthetic Enzyme Pyrroline-5-Carboxylate Reductase 1 (PYCR1).<\/a><\/strong>
\nK.R. Meeks, C.J. Mattingly, J.C. Nix, O. Chuk, M.V. Protopopov, O.O. Tarkhanova, & J.J. Tanner.
\nBiochemical Journal, 2026<\/p>\n

2025<\/b><\/p>\n

182. Visualization of Covalent Intermediates and Conformational States of Proline Utilization A by X-ray Crystallography and Molecular Dynamics Simulations<\/strong><\/a>
\nD.P. Buckley, D.F. Becker, & J.J. Tanner
\nJ. Biol. Chem. 2025
\nFull text at JBC website<\/a>
\n<\/p>\n

181. Biochemical, structural, and cellular characterization of S-but-3-yn-2-ylglycine as a mechanism-based covalent inactivator of the flavoenzyme proline dehydrogenase<\/strong><\/a>
\nK.R. Meeks, J. Ji, G.K. Scott, A.C. Campbell, J.C. Nix, A. Tadeo, L.M. Ellerby, C.C. Benz, J.J. Tanner
\nArchives of Biochemistry and Biophysics, 2025.<\/p>\n

<\/p>\n

\n

2024<\/strong><\/p>\n

180. Crystallographic fragment screening of a bifunctional proline catabolic enzyme reveals new inhibitor templates for proline dehydrogenase and L-glutamate-\u03b3-semialdehyde dehydrogenase<\/strong><\/a>
\nK.R. Meeks, A.N. Bogner, J.C. Nix, and J.J. Tanner
\nMolecules, 2024.
\nOpen Access full text<\/a>
\n<\/p>\n

179. Noncovalent Inhibition and Covalent Inactivation of Proline Dehydrogenase by Analogs of N-propargylglycine<\/strong><\/a>
\nJ.J. Tanner, J. Ji, A.N. Bogner, G.K. Scott, S.M. Patel, J. Seravalli, K.S. Gates, C.C. Benz, D.F. Becker
\nBiochemistry, 2024.
\n<\/p>\n

178. Screening a Knowledge-based Library of Low Molecular Weight Compounds Against the Proline Biosynthetic Enzyme PYCR1<\/strong><\/a>
\nK.R. Meeks, A.N. Bogner, & J.J. Tanner
\nProtein Science, 2024.<\/p>\n

177. Biochemical, Structural, and Computational Analyses of Two New Clinically Identified Missense Mutations of ALDH7A1<\/strong><\/a>
\nD.A. Korasick, D.P. Buckley, A. Palpacelli, I. Cursio, E. Cesaroni, J. Cheng, and J.J. Tanner
\nChemico-Biological Interactions, Accepted on 4 Apr 2024.<\/p>\n

176. AI is a viable alternative to high throughput screening: a 318-target study<\/strong><\/a>
\nWallach et al., Scientific Reports, 2024.
\nOpen Access full text<\/a><\/p>\n<\/div>\n

\n

175. Novel Fragment Inhibitors of PYCR1 from Docking-Guided X-Ray Crystallography<\/strong><\/a>
\nKaylen Meeks, Juan Ji, Mykola Protopopov, Olga Tarkhanova, YuriiMoroz, John Tanner
\nJournal of Chemical Information and Modeling, Accepted 07-Feb-2024
\nArticle at ACS website<\/a>
\n<\/p>\n<\/div>\n

\n
\n

2023<\/b><\/b><\/p>\n

174. Structural and functional analysis of two SHMT8 variants associated with soybean cyst nematode resistance<\/a><\/strong>
\nD. A. Korasick, L. F. Owuocha, P. K. Kandoth, J. J. Tanner, M. G. Mitchum and L. J. Beamer
\nFEBS Journal, 2023.<\/p>\n

173. Crystal structure of domain of unknown function 507 (DUF507) reveals a new protein fold<\/strong><\/a>
\nC.E. McKay, J. Cheng, J.J. Tanner
\nScientific Reports, 2023
\nOpen Acess full text<\/a>
\n<\/p>\n

172. Therapeutic targeting of HYPDH\/PRODH2 with N-propargylglycine offers a hyperoxaluria treatment opportunity<\/strong><\/a>
\nJ. Bons, A. Tadeo, G.K. Scott, F. Termayi, J.J. Tanner, B. Schilling, C.B. Benz, L.M. Ellerby
\nBBA – Molecular Basis of Disease, 2023.<\/p>\n

\n

2022<\/b><\/b><\/p>\n

\n

171. Functional impact of a cancer-related variant in human \u03941-pyrroline-5-carboxylate reductase 1<\/strong><\/a>
\nO. Daudu, K.R. Meeks, L. Zhang, J. Seravalli, J.J. Tanner, & D.F. Becker
\nACS Omega, Accepted 12\/26\/2022 (Published 01\/10\/2023).
\nOpen Access full text<\/a><\/p>\n

170. Structure-Based Engineering of Minimal Proline Dehydrogenase Domains for Inhibitor Discovery<\/strong><\/a>
\nA.N. Bogner, J. Ji, & J.J. Tanner
\nProtein Engineering, Design, and Selection, 2022 (Published 11\/30\/2022).
\nPDF<\/a><\/p>\n

169. Expression and Kinetic Characterization of PYCR3<\/strong><\/a>
\nK.R. Meeks and J.J. Tanner
\nArchives of Biochemistry and Biophysics, 2023 (Epub 11\/19\/2022)
\nPDF<\/a>
\n<\/p>\n

168. Kinetic and Structural Characterization of a Flavin-Dependent Putrescine N-Hydroxylase from Acinetobacter baumannii<\/a><\/strong>
\nN.S. Lyons, A.N. Bogner, J.J. Tanner, & P. Sobrado
\nBiochemistry, 2022.<\/p>\n

167. Conformational Preferences of Pyridone Adenine Dinucleotides from Molecular Dynamics Simulations<\/strong><\/a>
\nD.P. Buckley, M.E. Migaud, & J.J. Tanner
\nInt. J. Mol. Sci., 2022.
\nArticle at publisher’s website<\/a><\/p>\n

166. Structure-Affinity Relationships of Reversible Proline Analog Inhibitors Targeting Proline Dehydrogenase<\/a><\/strong>
\nA.N. Bogner and J.J. Tanner
\nRSC Organic & Biomolecular Chemistry, 2022.
\nPDF<\/a>
\n<\/p>\n

165. Artificial Intelligence in the Prediction of Protein-Ligand Interactions: Recent Advances and Future Directions<\/b><\/a><\/p>\n<\/div>\n

\n

A. Dhakal, C. McKay, J.J. Tanner, & J. Cheng
\nBriefings in Bioinformatics, 2022.<\/p>\n<\/div>\n

\n

2021<\/b><\/b><\/p>\n<\/div>\n

\n

164. Evidence for Proline Catabolic Enzymes in the Metabolism of Thiazolidine Carboxylates<\/strong><\/a>
\nY. Mao, J. Seravalli, T.G. Smith, M. Morton, J.J. Tanner, and D.F. Becker
\nBiochemistry, 2021<\/p>\n

163. Kinetics of Human Pyrroline-5-Carboxylate Reductase in L-Thioproline Metabolism<\/strong><\/a>
\nS.M. Patel, J. Seravalli, K.M. Stiers, J.J. Tanner, and D.F. Becker
\nAmino Acids, 2021
\nPart of Amino Acids topical collection on Proline Metabolism in Cancer<\/a><\/p>\n

162. Optimisation of Neuraminidase Expression by HEK-293E Cells for use in Drug Discovery<\/strong><\/a>
\nA.C. Campbell, J.J. Tanner, and K.L. Krause
\nViruses, 2021
\nPart of a special issue on “State-of-the-Art Molecular Virology Research in New Zealand”<\/a><\/p>\n

161. Photoinduced Covalent Irreversible Inactivation of Proline Dehydrogenase by S-Heterocycles<\/strong><\/a>
\nA.C. Campbell, A.R. Prater, A.N. Bogner, T.P. Quinn, K.S. Gates, D.F. Becker and J.J. Tanner
\nACS Chemical Biology, 2021.
\nPDF<\/a>
\n<\/p>\n

160. Probing the Function of a Ligand-Modulated Dynamic Tunnel in Bifunctional Proline Utilization A (PutA)<\/strong><\/a>
\nD.A. Korasick, S.L. Christgen, I.A. Qureshi, D.F. Becker, and J.J. Tanner
\nArchives of Biochemistry and Biophysics, 2021.
\n<\/p>\n

159.Structural and Biochemical Characterization of the Flavin-Dependent Siderophore-Interacting Protein from Acinetobacter baumannii<\/a><\/strong>
\nH. Valentino, D.A. Korasick, David, T.J. Bohac, J.A. Shapiro, T.A. Wencewicz, J.J.\u00a0 Tanner, P. Sobrado
\nACS Omega, 2021.<\/p>\n

158. N-Propargylglycine: a unique suicide inhibitor of proline dehydrogenase with anticancer activity and brain-enhancing mitohormesis properties<\/strong><\/a>
\nG.K. Scott, S. Mahoney, M. Scott, A. Loureiro, A. Lopez-Ramirez, J.J. Tanner, L.M. Ellerby, and C.C. Benz
\nAmino Acids, 2021
\nPart of Amino Acids topical collection on Proline Metabolism in Cancer<\/a><\/p>\n

157. Structural Basis for the Stereospecific Inhibition of the Dual Proline\/Hydroxyproline Catabolic Enzyme ALDH4A1 by Trans-4-Hydroxy-L-Proline<\/strong><\/a>
\nA.N. Bogner, K.M. Stiers, C.M. McKay, D.F. Becker, and J.J. Tanner
\nProtein Science, 2021
\nPDF<\/a><\/p>\n

156. St<\/strong>ructure, Biochemistry, and Gene Expression Patterns of the Proline Biosynthetic Enzyme Pyrroline-5-Carboxylate Reductase (PYCR), An Emerging Cancer Therapy Target<\/strong><\/a>
\nA.N. Bogner, K.M. Stiers, and J.J. Tanner
\nAmino Acids, 2021
\nFull text<\/a>
\nPDF<\/a>
\nPart of Amino Acids topical collection on Proline Metabolism in Cancer<\/a><\/p>\n

155. Disease variants of human delta-1-pyrroline-5-carboxylate reductase 2 (PYCR2)<\/strong><\/a>
\nS.M. Patel, S. Seravalli, X. Liang, J.J. Tanner, D.F. Becker
\nArchives of Biochemistry and Biophysics, 2021<\/p>\n<\/div>\n

\n
\n

2020
\n<\/b><\/p>\n

154. Biochemical Characterization of the Two-Component Flavin-Dependent Monooxygenase Involved in Valanimycin Biosynthesis<\/strong><\/a>
\nH. Li, B. Forson; M. Eckshtain-Levi, H. Valentino, J. Martin Del Campo, J. Tanner, P. Sobrado
\nBiochemistry, 2021<\/p>\n

153. Structural Analysis of Prolines and Hydroxyprolines Binding to the L-glutamate-gamma-semialdehyde Dehydrogenase Active Site of Bifunctional Proline Utillization A<\/strong><\/a>
\nA.C. Campbell, A.N. Bogner, Y. Mao, D.F. Becker, and J.J. Tanner
\nArchives of Biochemistry and Biophysics, 2021<\/p>\n

152. Structural Determinants of Flavin Dynamics in a Class B Monooxygenase<\/strong><\/a>
\nA.C. Campbell, R. Robinson, D. Mena-Aguilar, P. Sobrado, J.J. Tanner
\nBiochemistry, 2020<\/span><\/p>\n

151. DeepCryoPicker: fully automated deep neural network for single protein particle picking in cryo-EM<\/strong><\/a>
\nA. Al-Azzawi, A. Ouadou, M. Highsmith, Y. Duan, J.J. Tanner, J. Cheng
\nBMC Bioinformatics, 2020<\/p>\n

150. In Crystallo<\/em> Screening for Proline Analog Inhibitors of the Proline Cycle Enzyme PYCR1<\/strong><\/a>
\nE.M. Christensen, A.N. Bogner, A. Vandekeere, G.S. Tam, S.M. Patel, D. F. Becker, S.-M. Fendt, and J.J. Tanner
\nJournal of Biological Chemistry, 2020
\nMU press release<\/a>
\nKOMU TV News story<\/a><\/p>\n

149. Impact of missense mutations in the ALDH7A1 gene on enzyme structure and catalytic function<\/strong><\/a>
\nD.A. Korasick and J.J. Tanner
\nBiochimie, 2020
\n
\n<\/b>148. Cautionary tale of using tris(alkyl)phosphine reducing agents with NAD +-dependent enzymes<\/strong><\/a>
\nS.M. Patel, T.G. Smith, M.D. Morton, K.M. Stiers, J. Seravalli, S.J. Mayclin, T.E. Edwards, J.J Tanner, D.F. Becker
\nBiochemistry, 2020
\n
\n<\/b>147. Trapping conformational states of a flavin-dependent N-monooxygenase in crystallo reveals protein and flavin dynamics<\/strong><\/a>
\nA.C. Campbell, K.M. Stiers, J.S. Martin Del Campo, R. Mehra-Chaudhary,\u00a0 P. Sobrado and J.J. Tanner
\nJournal of Biological Chemistry, 2020<\/p>\n

146. Inhibition, crystal structures, and in-solution oligomeric structure of aldehyde dehydrogenase 9A1<\/strong><\/a>
\nJ.W. Wyatt, D.A. Korasick, I.A. Qureshi, A.C. Campbell, K.S. Gates, and J.J. Tanner
\nArchives of Biochemistry and Biophysics, 2020<\/p>\n

145. Structure and function of a flavin-dependent S-monooxygenase from garlic (Allium sativum)<\/strong><\/a>
\nH. Valentino, A.C. Campbell, J.P. Schuermann, N. Sultana, H.G. Nam, S. LeBlanc, J.J. Tanner, and P. Sobrado
\nJournal of Biological Chemistry, 2020<\/p>\n

144. Bioinformatics Methods for Mass Spectrometry-Based Proteomics Data Analysis<\/strong><\/a>
\nChen C, Hou J, Tanner JJ, & Cheng J.
\nInternational Journal of Molecular Sciences, 2020
\n
\n<\/b>143. Covalent Modification of the Flavin in Proline Dehydrogenase by Thiazolidine-2-Carboxylate<\/strong><\/a>
\nCampbell AC, Becker DF, Gates KS, & Tanner JJ.
\nACS Chemical Biology, 2020<\/p>\n

<\/b>142. Impaired folate binding of serine hydroxymethyltransferase 8 from soybean underlies resistance to the soybean cyst nematode<\/strong><\/a>
\nKorasick, D.A, Kandoth, P.K., Tanner, J.J., Mitchum, M.G., and Beamer, L.J.
\nJournal of Biological Chemistry, 2020
\n
\n<\/b><\/b><\/p>\n

\n

2019<\/b><\/p>\n

141. SAXSDom: Modeling Multi-domain Protein Structures Using Small-angle X-ray Scattering Data<\/a>
\nHou, J, Adhikari, B, Tanner, JJ, and Cheng, J
\nPROTEINS: Structure, Function, and Bioinformatics, 2020.
\n<\/b><\/p>\n

140. Structural Analysis of Pathogenic Mutations Targeting Glu427 of ALDH7A1, the Hot Spot Residue of Pyridoxine-Dependent Epilepsy<\/a>
\n<\/b>Laciak, AR, Korasick, DA, Gates, KS, and Tanner, JJ
\nJ. Inherit. Metab. Dis. 2020.
\n
\n<\/b>139. A Super-Clustering Approach for Fully Automated Single Particle Picking in Cryo-EM<\/a>
\nA Al-Azzawi, A. Ouadou, JJ Tanner, and J Cheng
\nGenes, 2019.<\/p>\n

138. Structural and Biochemical Consequences of Pyridoxine-Dependent Epilepsy Mutations That Target the Aldehyde Binding Site of Aldehyde Dehydrogenase ALDH7A1<\/a>
\n<\/b>Laciak AR, Korasick DA, Wyatt JW, Gates KS, and Tanner JJ
\nFEBS Journal. 2020.<\/p>\n

137. AutoCryoPicker: An Unsupervised Learning Approach for Fully Automated Single Particle Picking in Cryo-EM Images<\/a>
\nA Al-Azzawi, A. Ouadou, JJ Tanner, and J Cheng
\nBMC Bioinformatics, 2019.<\/p>\n

136. Structural and biochemical characterization of aldehyde dehydrogenase 12, the last enzyme of proline catabolism in plants<\/a>
\nDA Korasick, R Koncitikova, M Kopecna, E Hajkova, A Vigouroux, S Morera, DF Becker, M Sebela, JJ Tanner, and D Kopecny
\nJ. Mol. Biol. 2019.<\/p>\n

135. Crystal Structure of Aldehyde Dehydrogenase 16 Reveals Trans-Hierical Structural Similarity and a New Dimer<\/a>
\nLiu, L.-K. and Tanner, JJ
\n<\/b>J. Mol. Biol. 2019.
\n
\n<\/b><\/p>\n

\n

2018<\/strong><\/p>\n

134. NAD+ Promotes Assembly of the Active Tetramer of Aldehyde Dehydrogenase 7A1<\/a>
\nKorasick DA, White TA, Chakravarthy S, Tanner JJ.
\nFEBS Lett. 2018.<\/p>\n

133. Redox Modulation of Oligomeric State in Proline Utilization A
\nD. A. Korasick, A. C. Campbell, S. L. Christgen, S. Chakravarthy, T. A. White, D. F. Becker, and J. J. Tanner
\nBiophysical J. 2018.
\nPubMed Abstract<\/a><\/p>\n

132. Steric control of the rate-limiting step of UDP-galactopyranose mutase
\nG. Pierdominici-Sottile, R. Cossio-Perez, I. Da Fonseca, K. Kizjakin, J.J. Tanner, and P. Sobrado
\nBiochemistry, 2018.
\nPubMed Abstract<\/a><\/p>\n

131. The proline cycle as a potential cancer therapy target<\/a>
\nTanner, J.J, Fendt, S.-M. and Becker, D.F.
\nBiochemistry, 2018.<\/p>\n

130. Structural Evidence for Rifampicin Monooxygenase Inactivating Rifampicin by Cleaving Its Ansa-Bridge
\nLiu LK, Dai Y, Abdelwahab H, Sobrado P, Tanner JJ.
\nBiochemistry, 2018.
\nPubMed Abstract<\/a><\/p>\n

129. Determination of Protein Oligomeric Structure from Small-Angle X-ray Scattering
\nDA Korasick and JJ Tanner
\nProtein Sci. 2018.
\nPubMed Abstract<\/a><\/p>\n

128.\u00a0 Flavin-N5 Covalent Intermediate in the Non-redox Dehalogenation Reaction Catalyzed by an Atypical Flavoenzyme
\nY Dai, K Kizjakina, AC Campbell, DA Korasick,\u00a0 JJ Tanner and P Sobrado
\nChemBioChem. 2018.
\nPubMed Abstract<\/a><\/p>\n

\n

2017<\/strong><\/p>\n

127. Structural Basis for the Substrate Inhibition of Proline Utilization A by Proline
\nDA Korasick, TA Pemberton, BW Arentson, DF Becker, and JJ Tanner
\nMolecules, 2017.
\nPubMed Abstract<\/a><\/p>\n

126. Discovery of the Membrane Binding Domain in Trifunctional Proline Utilization A
\nS.L. Christgen, W. Zhu, N. Sanyal, B. Bibi, J.J. Tanner, D.F. Becker
\nBiochemistry, 2017.
\nPubMed Abstract<\/a><\/p>\n

125. Importance of the C-terminus of ALDH7A1 for Oligomerization and Catalytic Activity.
\nKorasick D, Wyatt J, Luo M, Laciak AR, Ruddraraju K, Gates KS, Henzl MT, Tanner JJ.
\nBiochemistry, 2017.
\nPubMed Abstract<\/a><\/p>\n

124. Structural Biology of Proline Catabolic Enzymes
\nTanner JJ.
\nAntioxid Redox Signal. 2017.
\nPubMed Abstract<\/a><\/p>\n

123. Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure
\nDA Korasick, Singh H, Pemberton TA, Luo M, Dhatwalia R, Tanner JJ.
\nFEBS J. 2017.
\nPubMed Abstract<\/a><\/p>\n

122. Structure, function, and mechanism of proline utilization A (PutA)
\nLiu LK, Becker DF, Tanner JJ.
\nArch Biochem Biophys. 2017 Oct 15;632:142-157. doi: 10.1016\/j.abb.2017.07.005. Epub 2017 Jul 14.
\nPubMed Abstract<\/a><\/p>\n

121. Multiple functionalities of reduced flavin in the non-redox reaction catalyzed by UDP-galactopyranose mutase
\nSobrado P, Tanner JJ
\nArch Biochem Biophys. 2017 Oct 15;632:59-65. doi: 10.1016\/j.abb.2017.06.015. Epub 2017 Jun 24.
\nPubMed Abstract<\/a><\/p>\n

120. Identification of a Conserved Histidine as Critical for the Catalytic Mechanism and Functional Switching of the Multifunctional Proline Utilization A Protein
\nMoxley MA, Zhang L, Christgen S, Tanner JJ, Becker DF.
\nBiochemistry, 2017.
\nPubMed Abstract<\/a><\/p>\n

119. DA Korasick, TT Gamage, S Christgen, KM Stiers, LJ Beamer, MT Henzl, DF Becker and JJ Tanner
\nStructure and characterization of a class 3B proline utilization A: ligand-induced dimerization and importance of the C-terminal domain for catalysis
\nJ. Biol. Chem. 2017 Jun 9;292(23):9652-9665. doi: 10.1074\/jbc.M117.786855. Epub 2017 Apr 18.
\nPubMed Abstract<\/a><\/p>\n

118. Punthasee P, Laciak AR, Cummings AH, Ruddraraju KV, Lewis SM, Hillebrand R, Singh H, Tanner JJ, Gates KS.
\nCovalent Allosteric Inactivation of Protein Tyrosine Phosphatase 1B (PTP1B) by an Inhibitor-Electrophile Conjugate
\nBiochemistry. 2017 Apr 11;56(14):2051-2060.
\nPubMed Abstract<\/a><\/p>\n

117. Christensen EM, Patel SM, Korasick DA, Campbell AC, Krause KL, Becker DF, Tanner JJ
\nResolving the Cofactor Binding Site in the Proline Biosynthetic Enzyme Human Pyrroline-5-Carboxylate Reductase 1.
\nJ. Biol. Chem. (2017) 292(17) 7233-7243.
\nPubMed Abstract<\/a><\/p>\n

116. Korasick DA, Tanner JJ, Henzl MT.
\nImpact of disease-Linked mutations targeting the oligomerization interfaces of aldehyde dehydrogenase 7A1.
\nChem Biol Interact (2017) Oct 1;276:31-39. doi: 10.1016\/j.cbi.2017.01.002. Epub 2017 Jan 10.
\nPubMed Abstract<\/a><\/p>\n

\n

2016<\/strong><\/p>\n

115. K. Stiers, C. Lee, J. Nix, J.J. Tanner, and L.J. Beamer
\nSynchrotron-based macromolecular crystallography module for an undergraduate biochemistry laboratory course
\nJ. Appl. Cryst. (2016). 49, 2235-2243.
\nPubMed Abstract<\/a><\/p>\n

114. B.W. Arentson, E.L. Hayes, W. Zhu, H. Singh, J.J. Tanner, and D.F. Becker
\nEngineering a Trifunctional Proline Utilization A Chimera By Fusing a DNA-Binding Domain to a Bifunctional PutA
\nBiosci Rep. 2016 Nov 22;36(6).
\nPubMed Abstract<\/a><\/p>\n

113. M. Luo, T.T. Gamage, B.W. Arentson, K.N. Schlasner, D.F. Becker and J.J. Tanner
\nStructures of Proline Utilization A Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown Function
\nJ Biol Chem. (2016) 291(46):24065-24075.
\nPubMed Abstract<\/a><\/p>\n

112. John J. Tanner
\nEmpirical Power Laws for the Radii of Gyration of Protein Oligomers
\nActa Crystallogr D Biol Crystallogr.\u00a0 (2016) 72, 1119-1129.
\nPubMed Abstract<\/a><\/p>\n

111. Liu LK, Abdelwahab H, Martin Del Campo JS, Mehra-Chaudhary R, Sobrado P, Tanner JJ.
\nThe Structure of the Antibiotic Deactivating, N-hydroxylating Rifampicin Monooxygenase.
\nJ Biol Chem. (2016) 291 (41), 21553-21562.
\nPubMed Abstract<\/a><\/p>\n

110. Tanner JJ, Frey BB, Pemberton TA, Henzl MT.
\nEF-5 is the high-affinity Mg2+ site in ALG-2.
\nBiochemistry 2016, 55, 5128\u22125141.
\nPubMed Abstract<\/a><\/p>\n

109. Mehra-Chaudhary R, Dai Y, Sobrado P, Tanner JJ
\nIn Crystallo<\/i> Capture of a Covalent Intermediate in the UDP-Galactopyranose Mutase Reaction.
\nBiochemistry (2016) 55(6):833-6.
\nPubMed Abstract<\/a><\/p>\n

\n

2015<\/strong><\/p>\n

108. J.J. Tanner
\nSAXS fingerprints of aldehyde dehydrogenase oligomers
\nData in Brief (2015) 5, 745-751.
\nPubMed Abstract<\/a><\/p>\n

107. R. Dhatwalia, H. Singh, T.J. Reilly, and J.J. Tanner
\nCrystal Structure and Tartrate Inhibition of Legionella pneumophila Histidine Acid Phosphatase
\nArch. Biochem. Biophys. (2015) 585, 1 November 2015, Pages 32-38.
\nPubMed Abstract<\/a><\/p>\n

106. R. Robinson, I.A. Qureshi, C.A. Klancher, P.J. Rodriguez, J.J. Tanner, P. Sobrado
\nContribution to catalysis of ornithine binding residues in ornithine N5-monooxygenase
\nArch. Biochem. Biophys. (2015) 585, 1 November 2015, Pages 25-31.
\nPubMed Abstract<\/a><\/p>\n

105. Lewis SM, Li Y, Catalano MJ, Laciak AR, Singh H, Seiner DR, Reilly TJ, Tanner JJ, Gates KS.
\nInactivation of protein tyrosine phosphatases by dietary isothiocyanates
\nBioorg. Med. Chem. Lett. (2015) 25(20):4549-52.
\nPubMed Abstract<\/a><\/p>\n

104. M. Luo and J.J. Tanner
\nStructural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1.
\nBiochemistry (2015). 8;54(35):5513-22.
\nPubMed Abstract<\/a><\/p>\n

103. Gres AT, Kirby KA, KewalRamani VN, Tanner JJ, Pornillos O, and Sarafianos SG.
\nX-ray crystal structures of native HIV-1 capsid protein reveal conformational variability.
\nScience (2015) 349(6243):99-103.
\nPubMed Abstract<\/a><\/p>\n

102.\u00a0 M Luo, KS Gates, MT Henzl, and JJ Tanner
\nDiethylaminobenzaldehyde is a Covalent, Irreversible Inactivator of ALDH7A1
\nACS Chem. Biol. (2015) 10(3):693-697
\nPubMed Abstract<\/a><\/p>\n

101.\u00a0 N Sanyal, BW Arentson, M Luo, JJ Tanner, and\u00a0 Donald F. Becker
\nFirst Evidence for Substrate Channeling Between Proline Catabolic Enzymes: A Validation of the Rosetta Stone Hypothesis of Protein-Protein Interactions
\nJ. Biol. Chem. (2015) 290(4):2225-2234.
\nPubMed Abstract<\/a><\/p>\n

\n

2014<\/strong><\/p>\n

100.\u00a0 Da Fonseca I , Qureshi IA, Ritcha Mehra-Chaudhary R, Kizjakina K, Tanner JJ, Sobrado, P.
\nContributions of Unique Active Site Residues of Eukaryotic UDP-Galactopyranose Mutases to Substrate Recognition and Active Site Dynamics
\nBiochemistry (2014) 53(49):7794-804.
\nPubMed Abstract<\/a><\/p>\n

99.\u00a0 Luo M, Christgen, S., Sanyal, N, Arentson BW, Becker DF, Tanner JJ,
\nEvidence that the C-terminal Domain of a Type B PutA Protein Contributes to Aldehyde Dehydrogenase Activity and Substrate Channeling
\nBiochemistry (2014) 53(35):5661-73.
\nPubMed Abstract<\/a><\/p>\n

98.\u00a0 Arentson BW, Luo M, Pemberton TA, Tanner JJ, Becker DF.
\nKinetic and Structural Characterization of Tunnel-Perturbing Mutants in Bradyrhizobium japonicum Proline Utilization A (PutA).
\nBiochemistry (2014) 12;53(31):5150-61.
\nPubMed Abstract<\/a><\/p>\n

97. H. Singh, B.W. Arentson, D.F. Becker, and J.J. Tanner
\nStructures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone binding site
\nProc. Natl. Acad. Sci. USA (2014) 111(9):3389-94
\nPubMed Abstract<\/a><\/p>\n

96. Pemberton TA, Srivastava D, Sanyal N, Henzl MT, Becker DF, Tanner JJ.
\nStructural Studies of Yeast \u03941-pyrroline-5-carboxylate Dehydrogenase (aka ALDH4A1): Active Site Flexibility and Oligomeric State.
\nBiochemistry. (2014) 53(8):1350-9
\nPubMed Abstract<\/a><\/p>\n

95. Moxley MA, Sanyal N, Krishnan N, Tanner JJ, Becker DF.
\nEvidence for Hysteretic Substrate Channeling in the Proline Dehydrogenase and \u03941-pyrroline-5-carboxylate Dehydrogenase Coupled Reaction of Proline Utilization A (PUTA).
\nJ. Biol. Chem. (2014) 289(6):3639-3651.
\nPubMed Abstract<\/a><\/p>\n

94. J.J. Tanner, L. Boechi L, J.A. McCammon, and P. Sobrado
\nStructure, Mechanism, and Dynamics of UDP-galactopyranose mutase.
\nArch. Biochem. Biophys. (2014) 544: 128-141
\nArticle featured on journal cover<\/a>
\nPubMed Abstract<\/a><\/p>\n

\n

2013<\/strong><\/p>\n

93.\u00a0 Boechi L, de Oliveira CA, Da Fonseca I, Kizjakina K, Sobrado P, Tanner JJ, McCammon JA.
\nSubstrate-dependent dynamics of UDP-galactopyranose mutase: Implications for drug design.
\nProtein Sci. (2013) 22(11):1490-501.
\nPubMed Abstract<\/a><\/p>\n

92.\u00a0 T.A. Pemberton and J.J. Tanner
\nStructural basis of substrate selectivity of \u03941-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): Semialdehyde chain length.
\nArch. Biochem. Biophys. (2013) 538(1):34-40.
\nPubMed Abstract<\/a><\/p>\n

91. Min Luo, R.K. Singh, and J.J. Tanner
\nStructural Determinants of Oligomerization of 1-Pyrroline-5-Carboxylate Dehydrogenase: Identification of a Hexamerization Hot Spot.
\nJ. Mol. Biol. (2013) 425(17):3106-3120.
\nPubMed Abstract<\/a><\/p>\n

90. Zhu W, Haile AM, Singh R, Larson JD, Smithen D, Chan JY, Tanner JJ, Becker DF.
\nInvolvement of the \u03b23-\u03b13 loop of the Proline Dehydrogenase Domain in Allosteric Regulation of Membrane Association of Proline Utilization A.
\nBiochemistry (2013) 52(26):4482-9.
\nPubMed Abstract<\/a><\/p>\n

89. K. Kizjakina, J. J. Tanner, and P. Sobrado
\nTargeting UDP-Galactopyranose Mutases from Eukaryotic Human Pathogens.
\nCurrent Pharmaceutical Design (2013) 19(14):2561-73.
\nPubMed Abstract<\/a><\/p>\n

88. J.J. Tanner and D.F. Becker
\nPutA and Proline Metabolism
\nChapter 2 of Handbook of Flavoproteins Volume 1 Oxidases, Dehydrogenases and Related Systems.
\nEdited by Russ Hille, Susan Miller, and Bruce Palfey (2013)
\nPage 1 of Chapter 2: PutA and Proline Metabolism<\/a>
\nTable of Contents<\/a>
\nAmazon link<\/a>
\nPublisher’s link<\/a><\/p>\n

87. Henzl MT, Sirianni AG, Wycoff WG, Tan A,\u00a0Tanner JJ
\nSolution structures of polcalcin phl p 7 in three ligation states: Apo-, hemi-mg2+-bound, and fully ca+-bound.
\nProteins (2013) 81(2):300-15.
\nPubMed Abstract<\/a><\/p>\n

\n

2012<\/strong><\/p>\n

86. Luo M, Arentson BW,\u00a0 Srivastava D, Becker DF, and Tanner JJ
\nCrystal Structures and Kinetics of Monofunctional Proline Dehydrogenase Provide Insight into Substrate Recognition and Conformational Changes Associated With Flavin Reduction and Product Release.
\nBiochemistry (2012) 51(50):10099-108).
\nPubMed Abstract<\/a><\/p>\n

85. Dhatwalia R, Singh H, Solano LM, Oppenheimer M, Robinson RM, Ellerbrock JF, Sobrado P,\u00a0Tanner JJ
\nIdentification of the NAD(P)H Binding Site of Eukaryotic UDP-Galactopyranose Mutase.
\nJ Am Chem Soc. (2012) 134(43):18132-8.
\nPubMed Abstract<\/a><\/p>\n

84. Luebbering EK, Mick J, Singh RK,\u00a0Tanner JJ, Mehra-Chaudhary R, Beamer LJ.
\nConservation of Functionally Important Global Motions in an Enzyme Superfamily across Varying Quaternary Structures.
\nJ Mol Biol. (2012) 423(5):831-46
\nPubMed Abstract<\/a><\/p>\n

83. T. A. Pemberton, B. R. Still, E. M. Christensen, H. Singh, D. Srivastava, and J. J. Tanner
\nProline: Mother Nature’s cryoprotectant applied to protein crystallography.
\nActa Cryst. D: Biological Crystallography (2012) 68(Pt 8):1010-8.
\nPubMed Abstract<\/a><\/p>\n

82.\u00a0R. Dhatwalia, H. Singh, Oppenheimer M, Sobrado P, and J. J. Tanner
\nCrystal Structures of Trypanosoma cruzi UDP-Galactopyranose Mutase Implicate Flexibility of the Histidine Loop in Enzyme Activation
\nBiochemistry, (2012), 51 (24), 4968-4979.
\nPubMed Abstract<\/a><\/p>\n

81. D. Srivastava, R.K. Singh, M.A. Moxley, M.T. Henzl, D. F. Becker, and J. J. Tanner
\nThe three-dimensional structural basis of type II hyperproinemia
\nJ. Mol. Biol<\/span>. (2012) 420(3):176-89.
\nPubMed Abstract<\/a><\/p>\n

80. R. Dhatwalia, H. Singh, Oppenheimer M, Karr DB, Nix JC, Sobrado P, Tanner JJ.
\nCrystal structures and small-angle X-ray scattering analysis of UDP-galactopyranose mutase from the pathogenic fungus Aspergillus fumigatus
\nJ. Biol. Chem<\/span>. (2012) 287, 9041-9051.
\nPubMed Abstract<\/a><\/p>\n

79. R. K. Singh and J.J. Tanner
\nUnique structural features and sequence motifs of proline utilization A (PutA)
\nFrontiers in Bioscience (2012) 17, 556-568.
\nPubMed Abstract<\/a><\/p>\n

\n

2011<\/strong><\/p>\n

78. M. A. Moxley, J.J. Tanner and D.F. Becker
\nSteady-State Kinetic Mechanism of the Proline:Ubiquinone Oxidoreductase Activity of Proline Utilization A (PutA) from Escherichia coli
\n<\/i>Arch. Biochem. Biophys. (2011) 516 (2) 113-120.
\nPubMed Abstract<\/a><\/p>\n

77.\u00a0 Ranjan K. Singh, John D. Larson, Weidong Zhu, Robert P. Rambo, Greg L. Hura, Donald F. Becker, and John J. Tanner
\nSmall-Angle X-ray Scattering Studies of the Oligomeric State and Quaternary Structure of the Trifunctional Proline Utilization A (PutA) Flavoprotein from Escherichia coli
\nJ. Biol. Chem. (2011) 286 (50) 43144-53.
\nPubMed Abstract<\/a><\/p>\n

76. Singh H, Reilly TJ, Tanner JJ.
\nStructural basis of the inhibition of class C acid phosphatases by adenosine 5′-phosphorothioate.
\nFEBS J. (2011) 278(22):4374-81.
\nPubMed Abstract<\/a><\/p>\n

75. Zhou H, Singh H, Parsons ZD, Lewis SM, Bhattacharya S, Seiner DR, LaButti JN, Reilly TJ, Tanner JJ, Gates KS.
\nThe biological buffer bicarbonate\/CO2 potentiates H2O2-mediated inactivation of protein tyrosine phosphatases.
\nJ. Am. Chem. Soc. ( 2011) 133(40):15803-5
\nPubMed Abstract<\/a><\/p>\n

74. H. Singh, T. J. Reilly, M. J. Calcutt and J. J. Tanner
\nExpression, purification and crystallization of an atypical class C acid phosphatase from Mycoplasma bovis
\nActa Cryst. (2011) F67, 1296-1299.
\nPubMed Abstract<\/a><\/p>\n

73. Mehra-Chaudhary R, Mick J, Tanner JJ, Beamer LJ.
\nQuaternary structure, conformational variability and global motions of phosphoglucosamine mutase.
\nFEBS J. (2011) 278(18):3298-307.
\nPubMed Abstract<\/a><\/p>\n

72. Tanner JJ, Parsons ZD, Cummings AH, Zhou H, and Gates KS.
\nRedox regulation of protein tyrosine phosphatases: Structural and Chemical Aspects.
\nAntioxid Redox Signal<\/span>. (2011) 15(1):77-97.<\/span>
\nPubMed Abstract<\/a><\/p>\n

71.\u00a0 Singh H, Malinski, T J, Reilly TJ, Henzl, MT,\u00a0 Tanner JJ.
\nCrystal structure and immunogenicity of the class C acid phosphatase from Pasteurella multocida
\nArch. Biochem. Biophys. (2011) 509:76-81.
\nPubMed Abstract<\/a><\/p>\n

70. Mehra-Chaudhary R, Mick J, Tanner JJ, Henzl MT, Beamer LJ.
\nCrystal structure of a bacterial phosphoglucomutase, an enzyme involved in the virulence of multiple human pathogens.
\nProteins. (2011) 79(4):1215-29.
\nPubMed Abstract<\/a><\/p>\n

69. Henzl MT, Tanner JJ, Tan A.
\nSolution Structures of Chicken Parvalbumin 3 in the Ca2+-free and Ca2+-bound States.
\nProteins. (2011) 79(3):752-64<\/span>.
\nPubMed Abstract<\/a><\/p>\n

\n

2010<\/strong><\/p>\n

68. Singh H, Schuermann JP, Reilly TJ, Calcutt MJ, Tanner JJ.
\nRecognition of Nucleoside Monophosphate Substrates by Haemophilus influenzae Class C Acid Phosphatase.
\nJ. Mol. Biol. (2010) 404(4):639-649.
\nPubMed Abstract<\/a><\/p>\n

67. Schuermann JP, Tan A, Tanner JJ, Henzl MT.
\nStructure of Avian Thymic Hormone, a High-affinity Avian beta-parvalbumin, in the Ca(2+)-free and Ca(2+)-bound States.
\nJ. Mol. Biol. (2010) 397(4):991-1002.
\n<\/a>PubMed Abstract<\/a><\/p>\n

66. Srivastava D, Schuermann JP, White TA, Krishnan N, Sanyal N, Hura GL, Tan A, Henzl MT, Becker DF, Tanner JJ.
\nCrystal structure of the bifunctional proline utilization A flavoenzyme from Bradyrhizobium japonicum.
\nProc. Natl. Acad. Sci. U. S. A. (2010) 107(7):2878-83.
\n<\/a>PubMed Abstract<\/a><\/p>\n

65. D. Srivastava, W. Zhu, W.H. Johnson, Jr., C. P.\u00a0 Whitman, D.F. Becker, and J.J. Tanner.
\nStructure of the Proline Utilization A Proline Dehydrogenase Domain Inactivated by N-propargylglycine Provides Insight into Conformational Changes Induced by Substrate Binding and Flavin Reduction
\nBiochemistry (2010) 49 (3): 560-569.
\n<\/a>PubMed Abstract<\/a><\/p>\n

\n

2009<\/strong><\/p>\n

64.\u00a0 H. Singh, R.L. Felts, J.P. Schuermann, T.J. Reilly, and J.J. Tanner.
\nCrystal Structures of the Histidine Acid Phosphatase from Francisella tularensis Provide Insight into Substrate Recognition
\nJ. Mol. Biol. (2009) 394(5):893-904.
\n<\/a>PubMed Abstract<\/a><\/p>\n

63.\u00a0 Lee MN, Takawira D, Nikolova AP, Ballou DP, Furtado VC, Phung NL, Still BR, Thorstad MK, Tanner JJ, Trimmer EE.
\nA Functional Role for the Conformationally Mobile Phenylalanine 223 in the Reaction of Methylenetetrahydrofolate Reductase from E. coli.
\nBiochemistry (2009) 48(32):7673-85
\nPubMed Abstract<\/a><\/p>\n

62. Reilly TJ, Chance DL, Calcutt MJ, Tanner JJ, Felts RL, Waller SC, Henzl MT, Mawhinney TP, Ganjam IK, Fales WH.
\nCharacterization of a unique class C acid phosphatase from Clostridium perfringens
\nAppl Environ Microbiol. (2009) 75(11):3745-54.
\nPubMed Abstract<\/a><\/p>\n

61. H. Singh, R.L. Felts, L. Ma, T.J. Malinsky, M.J. Calcutt, T.J. Reilly, and J.J. Tanner
\nExpression, purification and crystallization of class C acid phosphatases from Francisella tularensis and Pasteurella multocida
\nActa Crystallogr. (2009) F65, 226-231.
\nPubMed Abstract<\/a><\/p>\n

60. E. L. Ostrander, J.D. Larson, J.P. Schuermann and J.J. Tanner
\nA Conserved Active Site Tyrosine Residue of Proline Dehydrogenase Helps Enforce the Preference for Proline over Hydroxyproline as the Substrate.
\nBiochemistry (2009) 48(5):951-959.
\nPubMed Abstract<\/a><\/p>\n

\n

2008<\/strong><\/p>\n

59. J.P. Schuermann, T.A. White, D. Srivastava, D.B. Karr and J.J. Tanner
\nThree Crystal Forms of the Bifunctional Enzyme Proline Utilization A (PutA) from Bradyrhizobium japonicum
\nActa Crystallogr. (2008)\u00a0 F64, 949-953.
\n<\/a>PubMed Abstract<\/a><\/p>\n

58. J.J. Tanner
\nReview article: Structural biology of proline catabolism
\nAmino Acids (2008) 35(4), 719-30.
\n<\/a>PubMed Abstract<\/a><\/p>\n

57.\u00a0 Y. Zhou, J.D. Larson, C.A. Bottoms, E.C. Arturo, M.T. Henzl, J.L. Jenkins, J.C. Nix, D.F. Becker, and J.J. Tanner
\nStructural Basis of Transcriptional Regulation of the Proline Utilization Regulon by Multifunctional PutA
\nJ. Mol. Biol. (2008) 381(1):174-88.
\n<\/a>PubMed Abstract<\/a><\/p>\n

56.\u00a0 T.A. White, W.H. Johnson, Jr., C.P. Whitman and J.J. Tanner
\nStructural basis for the inactivation of Thermus thermophilus proline dehydrogenase by N-propargylglycine
\nBiochemistry (2008) 47(20):5573-80.
\n<\/a>PubMed Abstract<\/a><\/p>\n

55. A. Tan, J. J. Tanner and M. T. Henzl
\nEnergetics of OCP1-OCP2 complex formation
\nBiophys. Chem. (2008) 134(1-2):64-71.
\nPubMed Abstract<\/a><\/p>\n

54. M. T. Henzl and J. J. Tanner
\nSolution structure of calcium-free rat alpha parvalbumin
\nProtein Sci. (2008) 17(3):431-8.
\nPubMed Abstract<\/a><\/p>\n

\n

2007<\/strong><\/p>\n

53. Z. Ou, C.A. Bottoms, M.T. Henzl and J. J. Tanner
\nImpact of DNA Hairpin Folding Energetics on Antibody – ssDNA Association
\nJ. Mol. Biol. (2007) 374, 1029-1040.
\nPubMed Abstract<\/a><\/p>\n

52. R.L. Felts, Z. Ou, T.J. Reilly, and J. J. Tanner
\nStructure of recombinant Haemophilus influenzae e (P4) acid phosphatase reveals a new member of the haloacid dehalogenase superfamily
\nBiochemistry (2007) 46 (39), 11110 -11119.
\nPubMed Abstract<\/a><\/p>\n

51. M. T. Henzl and J. J. Tanner
\nSolution Structure of Ca2+-free Rat \u03b2-Parvalbumin (Oncomodulin)
\nProtein Sci. (2007) Sep;16(9):1914-26.
\nPubMed Abstract\u00a0<\/a><\/p>\n

50. A.J. DiMauro, D. Lin, S. Guo, D. B. Karr, J. J. Tanner, and P. Guo
\nCrystallization of Phi29 Spindle-Shaped Nano-Bar Anti-Receptor with Glycosidase Domain
\nJournal of Nanoscience and Nanotechnology (2007) 7, 1-7.
\nPubMed Abstract
\n<\/a>
\n49. T.A. White, N. Krishnan, D.F. Becker and J.J. Tanner
\nStructure and Kinetics of Monofunctional Proline Dehydrogenase from Thermus thermophilus.
\nJ. Biol. Chem. (2007) 282(19):14316-14327.
\nPubMed Abstract<\/a><\/p>\n

48. W. Zhang, M. Zhang, W. Zhu, Y. Zhou, S. Wanduragala, D. Rewinkel, J.J. Tanner and D.F. Becker
\nRedox-induced changes in flavin structure and roles of the flavin N(5) and the ribityl 2′-OH group in regulating PutA-membrane binding
\nBiochemistry (2007) 46(2):483-491.
\nPubMed Abstract<\/a><\/p>\n

\n

2006<\/strong><\/p>\n

47. J.D. Larson, J.L. Jenkins, J.P. Schuermann, Y. Zhou, D.F. Becker and John J. Tanner
\nCrystal structures of the DNA-binding domain of Escherichia coli proline utilization A flavoprotein and analysis of the role of Lys9 in DNA recognition
\nProtein Sci. (2006), 15:1-12.
\nPubMed Abstract<\/a><\/p>\n

46. R.L. Felts, T.J. Reilly and J.J. Tanner
\nSructure of Francisella tularensis ACPA: Prototype of a unique superfamily of acid phosphatases and phospholipases C
\nJ. Biol. Chem.\u00a0 (2006) Oct 6;281(40):30289-98.
\n<\/a>PubMed Abstract<\/a><\/p>\n

45. R.L. Felts, T.J. Reilly, M.J. Calcutt and J.J. Tanner
\nCloning, purification and crystallization of Bacillus anthracis class C acid phosphatase
\nActa Crytallographica F (2006) F62:705-8.
\n<\/a>PubMed abstract<\/a><\/p>\n

44. C.A. Bottoms, T.A. White and J.J. Tanner
\nExploring Structurally Conserved Sovent Sites in Protein Families
\nProteins (2006) 64(2):404-421.
\n<\/a>PubMed abstract<\/a><\/p>\n

43. M.V. Pattarkine, J.J. Tanner, C.A. Bottoms, Y.-H. Lee and J.D. Wall
\nDesulfovibrio desulfuricans G20 tetraheme cytochrome structure at 1.5 \u00c5 and cytochrome interaction with metal complexes
\nJ. Mol. Biol. (2006) 358(5):1314-1327.
\n<\/a>PubMed abstract<\/a><\/p>\n

42. Z. Ou, R.L. Felts, T.J. Reilly, J.C. Nix and J.J. Tanner
\nCrystallization of recombinant Haemophilus influenzae e (P4) acid phosphatase
\nActa Crytallographica F (2006) F62, 464-466.
\nPubMed abstract<\/a><\/p>\n

41. J.L. Jenkins and J.J. Tanner
\nHigh Resolution Crystal Structure of Human D Glyceraldehyde-3-Phosphate Dehydrogenase
\nActa Crytallographica D (2006) 62(Pt 3):290-301.
\nPubMed abstract<\/a><\/p>\n

40. R.L. Felts, T.J. Reilly, M.J. Calcutt and J.J. Tanner
\nCrystallization of a newly discovered histidine acid phosphatase from Francisella tularensis
\nActa Crytallographica F (2006) F62, 32-35.
\nPubMed abstract<\/a><\/p>\n

39. T.J. Reilly, R.L. Felts, M.T. Henzl, M.J. Calcutt and J.J. Tanner
\nCharacterization of recombinant Francisella tularensis acid phosphatase
\nProt. Exp. Purif. (2006) 45, 132-141.
\nPubMed abstract<\/a><\/p>\n<\/div>\n

\n

2005<\/strong><\/p>\n

38. White, T. A. & Tanner, J. J.
\nCloning, purification and crystallization of Thermus thermophilus proline dehydrogenase.
\nActa Crystallogr. (2005) F61, 737-739.
\nPubMed abstract
\n<\/a>
\n37. Tanner, J. J., Agah, S., Lee, Y. H. & Henzl, M. T.
\nCrystal Structure of the D94S\/G98E Variant of Rat alpha-Parvalbumin. An Explanation for the Reduced Divalent Ion Affinity.
\nBiochemistry (2005) 44, 10966-76.
\nPubMed abstract
\n<\/a>
\n36. R.L. Felts, T.J. Reilly and J.J. Tanner
\nCrystallization of AcpA, a respiratory burst-inhibiting acid phosphatase from Francisella tularensis.
\nBiochim. Biophys. Acta. (2005) 1752, 107-10.
\nPubMed abstract
\n<\/a>
\n35. J.P. Schuermann, S.P. Prewitt, C. Davies, S.L. Deutscher, and J. J. Tanner
\nEvidence for Structural Plasticity of Heavy Chain Complementarity-Determining Region 3 in Antibody-ssDNA Recognition
\nJ. Mol. Biol. (2005) 347(5), 965-78.
\nPubMed abstract<\/a><\/p>\n

\n

2004<\/strong><\/p>\n

34.\u00a0M. Zhang, T.A. White, J.P. Schuermann, B.A. Baban, D.F. Becker, and J. J. Tanner
\nStructures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors.
\nBiochemistry (2004) 43(39) 12539-48.
\nPubMed abstract<\/a><\/p>\n

33. B. Baban, M.P. Vinod, J.J. Tanner, and D.F. Becker
\nProbing a hydrogen bond pair and the FAD redox properties in the proline dehydrogenase domain of Escherichia coli PutA
\nBiochem. Biophys. Acta (2004) 1701, 49-59.
\nPubMed abstract
\n<\/a>
\n32. Y.-H. Lee, J.J. Tanner, J.D. Larson, and M.T. Henzl
\nCrystal Structure of a High-Affinity Variant of Rat alpha-Parvalbumin
\nBiochemistry (2004), 43(31):10008-10017.
\nPubMed abstract
\n<\/a>
\n31. D. Gu, Y.Zhou, V. Kallhoff, B. Baban, J. J. Tanner, and D. Becker
\nIdentification and Characterization of the DNA-binding Domain of the Multifunctional PutA Flavoenzyme
\nJ. Biol. Chem. (2004), 279(30):31171-31176.
\nPubMed abstract<\/a><\/p>\n

30. J.P. Schuermann, M.T. Henzl, S.L. Deutscher, and J.J. Tanner
\nStructure of an anti-DNA Fab complexed with a non-DNA ligand provides insights into cross-reactivity and molecular mimicry.
\nProteins (2004) 57, 269-278.
\nPubMed abstract
\n<\/a>
\n29. C.A. Bottoms, J.P. Schuermann, S. Agah, M.T. Henzl, and J.J. Tanner
\nCrystal structure of rat alpha-parvalbumin at 1.05 Angstrom resolution.
\nProtein Sci. (2004) 13(7):1724-1734 .
\nPubMed abstract
\n<\/a>
\n28. M. Zhang and J.J. Tanner
\nDetection of L-lactate in polyethylene glycol solutions confirms the identity of the active-site ligand in a proline dehydrogenase structure.
\nActa Crystallogr.\u00a0 (2004) D60, 985-986.
\nPubMed abstract<\/a><\/p>\n

\n

2003<\/strong><\/p>\n

27. J.P. Schuermann and J.J. Tanner
\nMRSAD: using anomalous dispersion from S atoms collected at Cu Kalpha wavelength in molecular-replacement structure determination.
\nActa Crystallogr. (2003) D59, 1731-1736.
\nPubMed abstract
\n<\/a>
\n26. Y.-H. Lee, S. Nadaraia, D. Gu, D. F. Becker, and\u00a0 J. J. Tanner
\nStructure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein
\nNature Structural Biology (2003) 10, 109-114.
\nPubMed abstract
\n<\/a><\/p>\n

\n

2002<\/strong><\/p>\n

25.\u00a0 C. A. Bottoms, P. E. Smith, and J. J. Tanner
\nA structurally conserved water molecule in Rossmann dinucleotide-binding domains
\nProtein Sci. (2002) 11, 2125-2137.
\nPubMed abstract
\n<\/a><\/p>\n

\n

2001<\/strong><\/p>\n

24.\u00a0 S. Nadaraia, Y.-H. Lee, D. F. Becker, and J. J. Tanner
\nCrystallization and Preliminary Crystallographic Analysis of the Proline Dehydrogenase Domain of the Multifunctional PutA Flavoprotein from Escherichia coli
\nActa Crystallogr. D Biol Crystallogr. (2001) D57,1925-1927.
\nPubMed abstract
\n<\/a><\/p>\n

23.\u00a0 J.J. Tanner, A.A. Komissarov, and S.L. Deutscher
\nCrystal Structure of an Antigen-Binding Fragment Bound to Single-Stranded DNA
\nJ. Mol. Biol. (2001) 314, 807-22.
\nPubMed abstract<\/a><\/p>\n

\n

2000<\/strong><\/p>\n

22. Crystallization and Molecular Replacement Studies of a Recombinant Antigen-Binding Fragment Complexed with Single-stranded DNA<\/a>
\nS. P. Prewitt, A.A. Komissarov, S.L. Deutscher, SL, and J.J. Tanner
\nActa Cryst. (2000), D56, 1007-1011.<\/p>\n

21. Conformations of Nicotinamide Adenine Dinucleotide (NAD+) in Various Environments.<\/a>
\nP.E. Smith and J.J. Tanner, J. J.
\nJ. Mol. Recognit. (2000)13, 27-34<\/p>\n

\n

1999<\/strong><\/p>\n

20. Molecular dynamics simulations of NAD+ in solution.<\/a>
\nP.E. Smith and J.J. Tanner
\nJ. Amer. Chem. Soc. (1999)121, 8637-8644.<\/p>\n

\n

Dr. Tanner’s Postdoctoral Research at University of Houston<\/strong><\/p>\n

19. Unusual Folded Conformation of NAD+ Bound to Flavin Reductase P.
\nJ.J. Tanner, S.-C. Tu,\u00a0 L.J. Barbour, C.L. Barnes, & K.L. Krause
\nProtein Science (1999) 8, 1725-1732.
\nPubMed Abstract <\/a><\/p>\n

18. Structure of bacterial luciferase beta2 homodimer: Implications for flavin binding.
\nJ.J. Tanner, M.D. Miller, K.S. Wilson, S.-C. Tu & K.L. Krause
\nBiochemistry (1997) 36, 665.
\nPubMed Abstract<\/a><\/p>\n

17.\u00a0 Crystal structure of flavin reductase P – a dimeric enzyme that provides reduced flavin in Vibrio harveyi.
\nK.L. Krause, M.D. Miller & J.J. Tanner
\nIn Proceedings:\u00a0 Bioluminescence and Chemiluminescence.\u00a0 Molecular reporting with photons.
\nEds.\u00a0 J. W. Hastings, L. J. Kricka, & P. E. Stanley.\u00a0 J. Wiley & Sons, Sussex, (1997) p. 42-49.<\/p>\n

16.\u00a0 Molecular mechanics
\nJ.J. Tanner
\nMacmillan Encyclopedia of Chemistry (1997) p. 959, Simon & Schuster Macmillan.<\/p>\n

15. Flavin reductase P: Structure of a dimeric enzyme that reduces flavin.<\/a>
\nJ.J. Tanner, B. Lei, S.-C. Tu & K.L. Krause
\nBiochemistry (1996) 35, 13531.<\/p>\n

14.\u00a0 Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticusD-glyceraldehyde-3-phosphate dehydrogenase at 2.5 Angstrom resolution.<\/a>
\nJ.J. Tanner, R.M. Hecht,\u00a0 & K.L. Krause
\nBiochemistry (1996) 35, 2597.<\/p>\n

13.\u00a0 Preliminary crystallographic analysis of glyceraldehyde 3-phosphate dehydrogenase from the extreme thermophile Thermus aquaticus.<\/a>
\nJ. Tanner, R. M.Hecht, M.Pisegna, D. M. Seth & K. L. Krause
\nActa Cryst. (1994) D50, 744.<\/p>\n

12.\u00a0 Crystallization and preliminary crystallographic analysis of NADPH:FMN oxidoreductase from Vibrio harveyi.<\/a>
\nJ. Tanner, B. Lei, M. Liu, S.-C. Tu\u00a0 & Krause, K. L.
\nJ. Mol. Biol. (1994) 241, 283.<\/p>\n

11.\u00a0 2.1 Angstrom structure of Serratia endonuclease suggests a mechanism for binding to double-stranded DNA.<\/a>
\nM. D. Miller, J. Tanner,\u00a0 M. Alpaugh, M. J. Benedik & K. L. Krause
\nNature Struct. Biol. (1994) 1, 461.<\/p>\n

10. A practical approach to data collection using the R-axis II.
\nJ. Tanner, & K. L. Krause
\nThe Rigaku Journal (1994) 11, 4.<\/p>\n

9.\u00a0 Molecular dynamics simulations and rigid body (TLS) analysis of aspartate carbamoyltransferase: Evidence for an uncoupled R state.<\/a>
\nJ.J. Tanner, P.E. Smith, & K. L. Krause
\nProtein Science (1993) 2, 927.<\/p>\n

8.\u00a0 Anti-insulin antibody structure and conformation. II. Molecular dynamics with explicit solvent.<\/a>
\nJ.J. Tanner, L.J. Nell & J.A. McCammon
\nBiopolymers (1992) 32, 23.<\/p>\n

7.\u00a0 A comparative study of time dependent quantum mechanical wave packet evolution methods.<\/a>
\nT. N. Truong, , J.J. Tanner, P. Bala, J.A. McCammon, D.J.\u00a0 Kouri, B. Lesyng & D. K. Hoffman
\nJ. Chem. Phys. (1992) 96, 2077.<\/p>\n

6.\u00a0 Ab Initio study of proton transfer in [H3N-H-NH3]+ and [H3N-H-OH2]+.<\/a>
\nL. Jaroszewski,\u00a0 B.L. Lesyng, J.J. Tanner & J.A. McCammon
\nChem. Phys. Letters (1990) 175, 282.<\/p>\n

5.\u00a0 A computer-based approach to teaching quantum dynamics.<\/a>
\nJ.J. Tanner
\nJ. Chem. Ed. (1990) 67, 917.<\/p>\n

\n

Dr. Tanner’s Dissertation Research at\u00a0Brown University<\/strong><\/p>\n

4. Floquet analysis of the far-infrared dissociation of a Morse oscillator.<\/a>
\nJ.J. Tanner & M.M. Maricq
\nPhys. Rev. (1989) A40, 4054<\/p>\n

3. Far IR dissociation of a highly excited Morse oscillator.<\/a>
\nJ.J. Tanner & M.M. Maricq
\nChem. Phys. Letters (1988) 149, 503.<\/p>\n

2.\u00a0 The role of rotation in the vibrational relaxation of diatomic molecules.<\/a>
\nJ.J. Tanner & M.M. Maricq
\nChem. Phys.\u00a0 (1988) 119, 307.<\/p>\n

1.\u00a0 A modified Landau-Teller model for vibrational relaxation of small molecular ions.<\/a>
\nJ.J. Tanner & M.M. Maricq
\nChem. Phys. Letters (1987) 138, 495.<\/p>\n","protected":false},"excerpt":{"rendered":"

Tanner Lab publication list in PubMed 2026 185. Targeting a unique cysteine residue to achieve isoform-selective inhibition of the proline biosynthetic enzyme pyrroline-5-carboxylate reductase 2. T.C. Rossman, K.R. Meeks, G. Purohit, M.J. Naldret, J.J. Tanner,\u00a0 & D. F. Becker ACS Chemical Biology, Accepted 04\/14\/2026 184. Structural Principles of Covalent Flavin Modification in Oxidoreductases John J. […]<\/p>\n","protected":false},"author":8,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-7","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/cafnrfaculty.missouri.edu\/tannerlab\/wp-json\/wp\/v2\/pages\/7","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/cafnrfaculty.missouri.edu\/tannerlab\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/cafnrfaculty.missouri.edu\/tannerlab\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/cafnrfaculty.missouri.edu\/tannerlab\/wp-json\/wp\/v2\/users\/8"}],"replies":[{"embeddable":true,"href":"https:\/\/cafnrfaculty.missouri.edu\/tannerlab\/wp-json\/wp\/v2\/comments?post=7"}],"version-history":[{"count":333,"href":"https:\/\/cafnrfaculty.missouri.edu\/tannerlab\/wp-json\/wp\/v2\/pages\/7\/revisions"}],"predecessor-version":[{"id":667,"href":"https:\/\/cafnrfaculty.missouri.edu\/tannerlab\/wp-json\/wp\/v2\/pages\/7\/revisions\/667"}],"wp:attachment":[{"href":"https:\/\/cafnrfaculty.missouri.edu\/tannerlab\/wp-json\/wp\/v2\/media?parent=7"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}