{"id":694,"date":"2022-02-07T14:22:33","date_gmt":"2022-02-07T19:22:33","guid":{"rendered":"http:\/\/www.loewenlabs.com\/peter\/?page_id=694"},"modified":"2022-02-08T14:24:11","modified_gmt":"2022-02-08T19:24:11","slug":"publications","status":"publish","type":"page","link":"http:\/\/www.loewenlabs.com\/peter\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"\n
Citations >8,900, h index = 47 (Web of Science)
Citations >13,100, h index = 58; i-10 = 147(Google Scholar)
(as of 24 January, 2022)

2020<\/span><\/strong>
181. M. Singh, P. M. De Silva, Y. Al-Saadi, J. Switala, P. C. Loewen, G. Hausner, W. Chen, I. Hernandez, S. Castillo-Ramirez and A. Kumar. 2020. Characterization of extremely drug-resistant and hypervirulent Acinetobacter baumannii<\/em> AB030. Antibiotics. 9:328; doi:10.3390\/antibiotics9060328. View PDF<\/strong><\/a>

2018<\/span><\/strong>
180. P. C. Loewen, J. Switala, J. P. Wells, F, Huang, A. T. Zara, J. S. Allingham and M. C. Loewen. 2018. Structure and function of a lignostilbene-alpha,beta-dioxygenase orthologue from Pseudomonas brassicacearum<\/em>. BMC Biochemistry<\/em> 19: 8. doi.org\/10.1186\/s12858-018-0098-4. View PDF<\/strong><\/a>

179. P. C. Loewen, P. M. De Silva, L. J. Donald, J. Switala, J. Villaneuva, I. Fita and A. Kumar. 2018. KatG-mediated oxidation imparts reduced susceptibility to kanamycin. ACS Omega<\/em> 3: 4213-4219. View PDF<\/strong><\/a> Supplementary Information: View PDF<\/strong><\/a>

178. A. Ivancich and P. C. Loewen. 2018. Electron transfer in catalases and catalase-peroxidases. In Robert, G. and Watts, A., European Biophysical Societies (eds), Encyclopedia of Biophysics<\/em>, Springer, Berlin, Heidelberg. https:\/\/doi.org\/10.1007\/978-3-642-35943-9_51-1. View PDF<\/strong><\/a>

2017<\/span><\/strong>
177. D. Vila-Vicosa, B, Victor, J. Ramos, D. machado, M. Viveiros, J. Switala, P. C. Loewen, R. Leitao, F. Martins and M. Machuqueiro. 2017. Insights on the mechanism of action of INH-C10 as an anti-tubercular pro-drug. Molec. Pharm.<\/em> 14: 4597-4605. View PDF<\/strong><\/a>

176. M. Machuquerio, B. Victor, J. Switala, J. Villanueva, C. Rovira, I. Fita and P. C. Loewen. 2017. Catalase activity of catalase-peroxidases is modulated by changes in pKa of the distal histidine. Biochemistry<\/em> 56: 2271-2281. View PDF<\/strong><\/a>

175. D. M. Fernando, P. Chong, M. Singh, V. Spicer, M. Unger, P. C. Loewen, G. Westmacott, and A. Kumar. 2017. Multi-omics approach to study global changes in a triclosan-resistant mutant strain of Acinetobacter baumannii<\/em> ATCC 17978. Int. J. Antimicrob. Agts.<\/em> 49: 74-80. View PDF<\/strong><\/a>

2016<\/span><\/strong>
174. M. Nandi, C. Berry, A. K. C. Brassinga, M. F. Belmonte, W. G. D. Fernando, P. C. Loewen and T. R. de Kievit. 2016. Pseudomonas brassicacearum<\/em> strain DF41 kills Caenorhaditis elegans<\/em> through biofilm-dependent and biofilm-independent mechanisms. Appl. Environ. Micro.<\/em> 82: 6889-6898. View PDF<\/strong><\/a>

173. J. Wiens, R. Ho, D. Fernando, A. Kumar, P. C. Loewen, A. K. Brassinga and W. G. Anderson. 2016. Complete genome sequence of the Rhodococcus<\/em> species isolated from the winter skate Leucoraja ocellata<\/em>. genomeA<\/em> 4: e00918-16 View PDF<\/strong><\/a>

172. W. Behrens, T. Schweinitzer, J. McMurry, P. C. Loewen, F. Buttner, S. Menz and C. Josenhans. 2016. Localisation and protein-protein interactions of the Helicobacter pylori<\/em> taxis sensor TlpD and their connection to metabolic functions. Scientific Reports<\/em> 6: 23582, doi:10.1038\/srep23582 View PDF<\/strong><\/a>

171. D. Sun, S. A. Crowell, C. M. Harding, P. M. DeSilva, A. Harrison, D. M. Fernando, K. M. Mason, E. Santana, P. C. Loewen, A. Kumar and Y. Liu. 2016. KatG and KatE confer Acinetobacter<\/em> resistance to hydrogen peroxide but sensitize bacteria to killing by phagocytic respiratory burst. Life Sciences<\/em> 148: 31-40. View PDF<\/strong><\/a>

2015<\/span><\/strong>
170. M. M. Galka, N. Rajagopalan, L. M. Buhrow, K. M. Nelson, J. Switala, A. J. Cutler, D. R. J. Palmer, P. C. Loewen, S. R. Abrams and M. C. Loewen. 2015. Identification of interactions between abscisic acid and ribulose-1,5-bisphosphate carboxylase\/oxygenase. PLoS One<\/em> 10(7):e0133033 doi:10.1371\/journal\/pone.0133033 View PDF<\/strong><\/a>

169. I. Fita, X. Carpena and P. C. Loewen. 2015. Catalase-peroxidase (KatG) structure and function. Heme peroxidases<\/em>. ed. E. Raven and B. Dunford

168. M. Nandi, C. Selin, A. K. C. Brassinga, M. F. Belmonte, W. G. D. Fernando, P. C. Loewen and T. R. de Kievit. 2015. Pyrrolnitrin and hydrogen cyanide production by Pseudomonas chlororaphis<\/em> strain PA23 exhibits potent nematicidal and repellent activity against Caenorhabditis elegans<\/em>. PLoS One<\/em> 10(4):e0123184 doi:10.1371\/journal.pone.0123184 View PDF<\/strong><\/a>

167. I. Fita, P. C. Loewen and X. Carpena. 2015. Catalase-peroxidase:KatG. Encyclopedia of Inorganic and Bioinorganic Chemistry<\/em> ed. R. A. Scott, John Wiley: Chichester. DOI: 10.1002\/9781119951438.eibc2273 View PDF<\/strong><\/a>

166. P. C. Loewen, J. Villanueva, J. Switala, L. J. Donald and A. Ivancich. 2015. Unprecedented access of phenolic substrates to the heme active site of a catalase: substrate binding and peroxidase-like reactivity of Bacillus pumilus<\/em> catalase monitored by X-ray crystallography and EPR spectroscopy. Proteins<\/em> 83: 853-866. View PDF<\/strong><\/a>

2014<\/span><\/strong>
165. P. C. Loewen, Y. Alsaadi, D. Fernando and A. Kumar. 2014. Genome sequence of Acinetobacter baumannii<\/em> AB031, a tigecycline-resistant clinical isolate from bloodstream infection. genomeA<\/em> 2: e01036-14 View PDF<\/strong><\/a>

164. P. C. Loewen, Y. Alsaadi, D. Fernando and A. Kumar. 2014. Genome sequence of Acinetobacter baumannii<\/em> AB030, an extreme drug-resistant (XDR) clinical isolate. genomeA<\/em> 2: e01035-14 View PDF<\/strong><\/a>

163. D. Fernando, W. Xu, P. C. Loewen, G. G. Zhanel and A. Kumar. 2014. Triclosan can select for an AdeIJK overexpressing mutant of Acinetobacter baumannii<\/em> ATCC17978 that displays reduced susceptibility to multiple antibiotics. Antimicrob. Agents Chemo.<\/em> 58: 6424-6431. View PDF<\/strong><\/a>

162. P. C Loewen, J. Villanueva, W. G. D. Fernando and T. de Kievit. 2014. Genome sequence of Pseudomonas chlororaphis PA23. genomeA<\/em> 2: e00689-14 View PDF<\/strong><\/a>

161. K. D. Miner, T. D. Pfister, P. Hosseinzadeh, N. Karaduman, L. J. Donald, P. C. Loewen, Y. Lu and A. Ivancich. 2014. Identifying the elusive sites of tyrosyl radicals in cytochrome c peroxidase: implications for oxidation of substrates bound at a site remote from the heme. Biochemistry<\/em> 53: 3781-3789 View PDF<\/strong><\/a>

160. P. C. Loewen, X. Carpena, P. Vidossich, I. Fita and C. Rovira. 2014. An ionizable active site tryptophan imparts catalase activity to a peroxidase core. J. Am. Chem. Soc.<\/em> 136: 7249-7252. View PDF<\/strong><\/a>

159. P. C. Loewen, J. Switala, D. Fernando and T. de Kievit. 2014. Genome sequence of Pseudomonas brassicacearum<\/em> DF41. 2014. genomeA<\/em> 2: e00390-24. View PDF<\/strong><\/a>

158. J. Villanueva, J. Switala, A. Ivancich and P. C. Loewen. 2014. Genome sequence of Bacillus pumilus<\/em> MTCC B6033. genomeA<\/em> 2: e00327-14. View PDF<\/strong><\/a>

157. P. Vidossich, P. C. Loewen, X. Carpena, G. Fiorin, I. Fita, and C. Rovira. 2014. Binding of the anti-tubercular pro-drug isoniazid in the heme access channel of catalase-peroxidase (KatG). A combined structural and metadynamics investigation. J. Phys. Chem. B<\/em> 118: 2924-2931. View PDF<\/strong><\/a>

156. M. M. S. Ismaiel, Y. M. El-Ayouty, P. C. Loewen, M. D. Piercey-Normore. 2014. Characterization of the iron-containing superoxide dismutase and its response to stress in cyanobacterium Spirulina (Arthrospira) platensis<\/em>. J. Appl. Phycology<\/em> DOI 10.1007\/s10811-013-0233-y. View PDF<\/strong><\/a>

155. C. L. Berry, M. Nandi, J. Manuel, A. K. C. Brassinga, W. G. D. Fernando, P. C. Loewen and T. R. de Kievit. 2014. Characterization of the Pseudomonas<\/em> sp. DF41 quorum sensing locus and its role in fungal antagonism. Biol. Control<\/em> 69: 82-89. View PDF<\/strong><\/a>

2013<\/span><\/strong>
154. A. Ivancich, L. J. Donald, J. Villanueva, B. Wiseman, I. Fita, and P. C. Loewen. 2013. Spectroscopic and kinetic investigation of the reactions of peroxyacetic acid with Burkholderia pseudomallei<\/em> catalase-peroxidase, KatG. Biochemistry<\/em> 52: 7271-7282. View PDF<\/strong><\/a>

153. D. Aparicio, R. Perez-Luque, X. Carpena, M. Diaz, J. C. Ferrer, P. C. Loewen and I. Fita. 2013. Structural asymmetry and disulphide bridges amoung subunits modulate the activity of human malonyl-CoA decarboxylase. J. Biol. Chem. <\/em>288: 11907-11919. View PDF<\/strong><\/a>

152. P. C. Loewen, A. L. Didychuk, J. Switala, R. Perez-Luque, I. Fita and M. C. Loewen. 2013. Structure of Pisum sativum rubisco<\/em> with bound ribulose-1,5-bisphosphate. Acta. Crystallog.<\/em> F69: 10-14. View PDF<\/strong><\/a>

2012<\/span><\/strong>
151. D. A. Alarcon, M. Nandi, X. Carpena, I. Fita and P. C. Loewen. 2012. Structure of glycerol-3-phosphate dehydrogenase, GPD1, from Saccharomyces cerevisiae<\/em> at 2.45 \u00c5 resolution. Acta. Crystallog. <\/em> F68 :1279-1283. View PDF<\/strong><\/a>

150. M. Zamocky, Q. Garcia-Fern\u00e1ndez, B. Gasselhuber, C. Jakopitsch, P. G. Furtm\u00fcller, P. C. Loewen, I. Fita, C. Obinger and X. Carpena. 2012. High conformation stability of secreted eukaryotic catalase-peroxidases – answers from the first crystal and unfolding studies. J. Biol. Chem.<\/em> 287: 32254-32262. View PDF<\/strong><\/a>

149. V. Jha, P. Chelikani, X. Carpena, I. Fita and P. C. Loewen. 2012. Influence of main channel structure on H2<\/sub>O2<\/sub> access to the heme cavity of catalase KatE of Escherichia coli<\/em>. Arch. Biochem. Biophys.<\/em> 526: 54-59. View PDF<\/strong><\/a>

148. C. L. Berry, A. K. C. Brassinga, L. J. Donald, W.G. D. Fernando, P. C. Loewen, and T. R. de Kievit. 2012. Investigation of the structure and biological activity of a novel lipopeptide essential for Pseudomonas<\/em> sp. DF41 biocontrol of Sclerotinia sclerotiorum<\/em>. Can. J. Microbiol.<\/em> 58: 1027-1034. View PDF<\/strong><\/a>

147. A. Diaz, P. C. Loewen, I. Fita and X. Carpena. 2012. Thirty years of heme catalase structural biology. Arch. Biochem. Biophys<\/em> 525: 102-110 View PDF<\/strong><\/a>

146. V. Jha, L. J. Donald and P. C. Loewen. 2012. Mutation of Phe413 to Tyr in catalase KatE from Escherichia coli<\/i> leads to side chain damage and main chain cleavage. Arch. Biochem. Biophys<\/em> 525: 207-214 2012. View PDF<\/strong><\/a>

145. A. Ivancich and P. C. Loewen. 2012. Electron transfer in catalases and catalase-peroxidases. In Encyclopedia of Biophysics.<\/em> ed. G. C. K. Roberts Springer-Verlag, Vol. 2, pp 611-614.

144. M. Hafez, M. Iranpour, S.-T. Mullineux, J. Sethuraman, K. Wosnitza, P. Lehn, J. Kroeker, P. C. Loewen, J. Reid, and G. Hausner. 2012. Group I intron-like elements within the SSU rDNA gene in species of Ceratocystiopsis<\/i> and related taxa. Fungal Biol.<\/em> 116:98-111. View PDF<\/strong><\/a>

2011<\/span><\/strong>
143. V. Jha, S. Louis, P. Chelikani, X. Carpena, L. J. Donald, I. Fita and P. C. Loewen. 2011. Modulation of heme orientation and binding by a single residue in catalase HPII of E. coli<\/i>. Biochemistry<\/em> 50: 2101-2110. View PDF<\/strong><\/a>

142. P. Vidossich, X. Carpena, P. C. Loewen, I. Fita and C. Rovira. 2011. Oxygen binding to catalase-peroxidase. J. Phys. Chem. Let.<\/em> 2: 196-200. View PDF<\/strong><\/a>

2010<\/span><\/strong>
141. J. Reid, M. Iranpour, S. M. Rudski, P. C. Loewen and G. Hausner. 2010. A new conifer-inhabiting species of Ceratocystis<\/i> from Norway. Botany<\/em> 88: 971-983. View PDF<\/strong><\/a>

140. C. Berry, W. G. D. Fernando, P. C. Loewen, and T. R. de Kievit. 2010. Lipopeptides are essential for Pseudomonas<\/i> sp. DF41 biocontrol of Sclerotinia sclerotiorum<\/i>. Biological Control<\/em> 55: 211-218. View PDF<\/strong><\/a>

139. B. Wiseman, X. Carpena, M. Feliz, L. J. Donald, M. Pons, I. Fita and P. C. Loewen. 2010. Isonicotinic acid hydrazide (INH) conversion to isonicotinyl-NAD by catalase-peroxidases. J. Biol. Chem.<\/em> 285: 26662-26673. View PDF<\/strong><\/a>

138. P. Vidossich, M. Alfonso-Prieto, X. Carpena, I. Fita, P. C. Loewen and C. Rovira. 2010. The dynamic role of distal side residues in heme hydroperoxidase catalysis. Interplay between X-ray crystallography and ab initio<\/i> MD simulations. Arch. Biochem. Biophys.<\/em> 500: 37-44. View PDF<\/strong><\/a>

2009<\/span><\/strong>
137. J. Colin, B. Wiseman, J. Switala, P. C. Loewen and A. Ivancich. 2009. Distinct role of specific tryptophans in facilitating electron transfer or as [Fe(IV)=O Trpo<\/sup>] intermediates in the peroxidase reaction of Burkholderia pseudomallei<\/em> catalase-peroxidase: a multifrequency EPR spectroscopy investigation. J. Am. Chem. Soc.<\/em> 131:8557-8563 View PDF<\/strong><\/a>

136. B. Wiseman, J. Colin, A. T. Smith, A. Ivancich and P. C. Loewen. 2009. Mechanistic insight into the initiation step of the reaction of Burkholderia pseudomallei<\/em> catalatse-peroxidase with peroxyacetic acid. J. Biol. Inorg. Chem.<\/em> 14: 801-811 View PDF<\/strong><\/a>

135. L. J. Donald, V. M. Collado, J. J. Galka, J. D. O’Neil, H. W. Duckworth, P. C. Loewen and K. G. Standing. 2009. Urea as a protein destabilizing agent in electrospray ionization. Rapid Commun. in Mass Spectrom. <\/em>23: 788-792 View PDF<\/strong><\/a>

2008<\/span><\/strong>
134. M. Alfonso-Prieto, P. Vidossich, A. Rodr\u00edguez-Fortea, X. Carpena, I. Fita, P. C. Loewen and Carme Rovira. 2008. Electronic state of the molecular oxygen released in the catalase reaction. J. Phys. Chem. A<\/em> 112: 12842-12848. View PDF<\/strong><\/a>

133. A. J. Fielding, R. Singh, B. Boscolo, P. C. Loewen, E. M. Ghibaudi, and A. Ivancich. 2008. Intramolecular electron transfer vs. substrate oxidation in lactoperoxidase: investigation of the radical intermediates by stopped-flow absorption spectrophotometry and (9-285 GHz) EPR spectroscopy. Biochemistry<\/em> 47: 9781-9792 View PDF<\/strong><\/a>

132. R. Singh, B. Wiseman, T. Deemagarn, V. Jha, J. Switala and P. C. Loewen. 2008. Comparative study of catalase-peroxidases (KatGs). Arch. Biochem. Biophys.<\/em> 471: 207-214. View PDF<\/strong><\/a>

131. J. Richardson, X. Carpena, J. Switala, P. C. Loewen and I Oresnik. 2008. RhaU of Rhizobium leguminosarum<\/em> is a rhamnose mutarotase. J. Bacteriol. <\/em>190: 2903-2910. View PDF<\/strong><\/a>

130. G. Hausner, J. Reid, G. G. Eyjolfsdottir, M. Iranpour and P. C. Loewen 2008. Basidiopycnides albertensis<\/em> gen. et spec. nov., a new anamporphic fungus whith phylogenetic affinities in the Atractiellales (Basidiomycota)<\/em>. Mycotaxon.<\/em> 103: 279-297. View PDF<\/strong><\/a> <\/a>

2007<\/span><\/strong>
129. R. Singh, J. Switala, P. C. Loewen and A. Ivancich. 2007. Two [Fe(IV)=O Trp\u00b7<\/strong>] intermediates in M. tuberculosis<\/em> catalase-peroxidase discriminated by multifrequency (9-285 GHz) EPR spectroscopy: reactivity towards isoniazid. J. Am. Chem. Soc.<\/em> 129: 15954-15963. View PDF<\/strong><\/a>

128. P. Vidossich, M. Alfonso-Prieto, X. Carpena, P. C. Loewen, I. Fita and C. Rovera. 2007. Versatility of the electronic structure of compound I in catalase-peroxidases (KatGs). J. Am. Chem. Soc.<\/em> 129: 13426-13446. View PDF<\/strong><\/a>

127. G. R. Golding, C. A. Kelly, R. Sparling, P. C. Loewen, and T. Barclay. 2007. Evaluation of mercury toxicity as a predictor of mercury bioavailability. Environ. Sci. Tech<\/em>41: 5685-5692. View PDF<\/strong><\/a>

126. M. Alfonso-Prieto, A. Borovik, X. Carpena, G. Murshudov, W. Melik-Adamyan, I. Fita, C. Rovira and P. C. Loewen. 2007. The structures and electronic configuration of compound I intermediates of Helicobacter pylori<\/em> and Penicillium vitale<\/em> catalases determined by X-Ray crystallography and QM\/MM DFT calculations. J. Am. Chem. Soc.<\/em> 129: 4193-4205. View PDF<\/strong><\/a>

125. C. Jakopitsch, J. Vlasits, B. Wiseman, P. C. Loewen and C. Obinger. 2007. Redox intermediates in the catalase cycle of catalase-peroxidases from Synechocystis<\/em> PCC 6803, Burkholderia pseudomallei<\/em>, and Mycobacterium tuberculosis<\/em>. Biochemistry<\/em> 46: 1183-1193. View PDF<\/strong><\/a>

124. T. Deemagarn, B. Wiseman, X. Carpena, A. Ivancich, I. Fita and P. C. Loewen. 2007. Two alternative substrate paths for compound I formation and reduction in catalase-peroxidase KatG from Burkholderia pseudomallei<\/em>. Proteins<\/em> 66: 219-228. View PDF<\/strong><\/a> <\/a>

2006<\/span><\/strong>
123. X. Carpena, B. Wiseman, T. Deemagarn, B. Herguedas, A. Ivancich, R. Singh, P. C. Loewen, and I. Fita. 2006. Roles for Arg426 and Trp111 in the modulation of NADH oxidase activity of the catalase-peroxidase KatG from Burkholderia pseudomallei<\/em> inferred from pH-induced structural changes. Biochemistry<\/em> 45: 5171-5179. View PDF<\/strong><\/a>

122. C. Rovira, M. Alfonso, X. Biarn\u00e9s, X. Carpena, I. Fita, and P. C. Loewen. 2006. A first principles study of the binding of formic acid in catalase complementing high resolution X-ray structures. Chem. Phys.<\/em> 323: 129-137. View PDF<\/strong><\/a>

121. M. Miller-Williams, P. C. Loewen and I. J. Oresnik. 2006. Isolation of salt sensitive mutants of Sinorhizobium meliloti<\/em> strain Rm1021. Microbiology<\/em> 152: 2049-2059. View PDF<\/strong><\/a>

120. K. Choudhary, V. L. Spicer, L. J. Donald, H. W. Duckworth, W. Ens, P. C. Loewen, and K. G. Standing. 2006. A method for estimating the isotopic distributions of metabolically labeled proteins by MALDI-TOFMS: application to NMR samples. Anal. Chem.<\/em> 78: 5419-5423. View PDF<\/strong><\/a>

<\/a>2005<\/span><\/strong>
119. R. Habibian, J. Dzioba, J. Barrett, M. Y. Galperin, P. C. Loewen and P. Dibrov. 2005. Functional analysis of conserved polar residues in VcNhaD, Na+\/H+ antiporter of Vibrio cholerae<\/em>. J. Biol. Chem.<\/em> 280: 39637-39643. View PDF<\/strong><\/a>

118. X. Carpena, B. Wiseman, T. Deemagarn, R. Singh, J. Switala, A. Ivancich, I. Fita and P.C. Loewen. 2005. A molecular switch and electronic circuit modulate activity in catalase-peroxidases. EMBO Reports<\/em> 6: 1156-1162. View PDF<\/strong><\/a>

117. G. Hausner, M. Iranpour, J.-J. Kim, C. Breuil, C, N. Davis, E. A. Gibb, J. Reid, J., P. C. Loewen, and A. A. Hopkin. 2005. Fungi vectored by the introduced bark beetle Tomicus piniperda<\/em> in Ontario, Canada and comments on the taxonomy of Leptographium lundbergii<\/em>, L. terebrantis<\/em>, L. truncatum<\/em> and L. wingfieldii<\/em>. Can. J. Bot.<\/em> 83: 1222-1237. View PDF<\/strong><\/a>

116. P.Chelikani, X. Carpena, R. Perez-Luque, L. J. Donald, H. W. Duckworth, J. Switala, I. Fita and P. C. Loewen. 2005. Characterization of a large subunit catalase truncated by proteolytic cleavage. Biochemistry<\/em> 44: 5597-5605. View PDF<\/strong><\/a>

115. T. Deemagarn, X. Carpena, R. Singh, B. Wiseman, I. Fita and P. C. Loewen. 2005. Structural characterization of the Ser324Thr variant of the catalase-peroxidase (KatG) from Burkholderia pseudomallei<\/em>. J. Mol. Biol.<\/em> 345: 21-28. View PDF<\/strong><\/a>

<\/a>2004<\/span><\/strong>
114. X. Carpena, W. Melik-Adamyan, P. C. Loewen, and I. Fita. 2004. Crystal structure of the C-terminal domain from the catalase-peroxidase KatG of Escherichia coli<\/em>. Acta Cryst.<\/em> D60: 1824-1832. View PDF<\/strong><\/a>

113. S. H. Cho, P. C. Loewen, and R. R. Marquardt. 2004. A plasmid DNA encoding chicken Interleukin-6 and Escherichia coli<\/em> K88 fimbrial protein FaeG stimulates the production of anti-K88 fimbrial antibodies in chickens. Poultry Sci.<\/em> 83: 1973-1978. View PDF<\/strong><\/a>

112. R. Singh, B. Wiseman, T. Deemagarn, L. J. Donald, H. W. Duckworth, X.Carpena, I. Fita, and P. C. Loewen. 2004. Catalase-peroxidases (KatG) exhibit NADH oxidase activity. J. Biol. Chem.<\/em> 279: 43098-43106. View PDF<\/strong><\/a>

111. P. C. Loewen, X. Carpena, R. Perez-Luque, C. Rovira, A. Ivancich, R. Perez-Luque, R. Haas, S. Odenbreit, P. Nicholls, and I. Fita. 2004. Structure of Helicobacter pylori<\/em> catalase, with and without formic acid bound, at 1.6 \u00c5 resolution. Biochemistry<\/em> 43: 3089-3103. View PDF<\/strong><\/a>

110. P. Chelikani, I. Fita and P. C. Loewen. 2004. Diversity of structures and properties among catalases. Cell Molec. Life Sci.<\/em> 61: 192-208. View PDF<\/strong><\/a>

<\/a>2003<\/span><\/strong>
109. L. J.Donald, O. V. Krokhin, H. W. Duckworth, B.Wiseman, T. Deemagarn, R.Singh, J. Switala, X. Carpena, I. Fita and P. C. Loewen. 2003. Characterization of the catalase-peroxidase KatG from Burkholderia pseudomallei<\/em> by mass spectrometry. J. Biol. Chem.<\/em> 278: 35687-35692. View PDF<\/strong><\/a>

108. P. Chelikani, X. Carpena, I. Fita and P. C. Loewen. 2003. An electrical potential in the access channel of catalases enhances catalysis. J. Biol. Chem.<\/em>278: 31290-31296. View PDF<\/strong><\/a>

107. P. Chelikani, L. J. Donald, H. W. Duckworth and P. C. Loewen. 2003. Hydroperoxidase II of Escherichia coli<\/em> exhibits enhanced resistance to proteolytic cleavage compared to other catalases. Biochemistry<\/em> 42: 5729-5735. View PDF<\/strong><\/a>

106. M. G. Klotz and P. C. Loewen. 2003. The molecular evolution of catalatic hydroperoxidases: Evidence for multiple lateral transfer of genes between prokaryota and from bacteria into eukaryota. Molec. Biol. Evol.<\/em> 20: 1098-1112. View PDF<\/strong><\/a>

105. X. Carpena, S. Loprasert, S. Mongkolsuk, J. Switala, P. C. Loewen and I. Fita. 2003. Catalase-peroxidase KatG of Burkholderia pseudomallei<\/em> at 1.7 \u00c5 resolution. J. Mol. Biol.<\/em> 327: 475-489. View PDF<\/strong><\/a>

104. X. Carpena, M. Soriano, M. G. Klotz, H. W. Duckworth, L. J. Donald, I. Fita and P. C. Loewen. 2003. Structure of the clade 1 catalase, CatF from Pseudomonas syringae<\/em> at 1.7 \u00c5 resolution. Proteins<\/em> 50: 423-436. View PDF<\/strong><\/a>

103. N. Chauvatcharin, P. Vattanaviboon, J. Switala, P. C. Loewen, and S. Mongkolsuk. 2003. Cloning and characterization of katA, encoding the major monofunctional catalase from Xanthomonas campestris<\/em> pv. phaseoli and characterization of the encoded catalase KatA. Curr. Microbiol.<\/em> 46: 83-87. View PDF<\/strong><\/a>

<\/a>2002<\/span><\/strong>
102. X. Carpena, J. Switala, S. Loprasert, S. Mongkolsuk, I. Fita and P. C. Loewen. 2002. Crystallization and preliminary X-ray analysis of the catalase-peroxidase KatG from Burkholderia pseudomallei<\/em>. Acta Cryst.<\/em>D58: 2184-2186. View PDF<\/strong><\/a>

101. E. Ostroumov, J. Dzioba, P. C. Loewen and P. Dibrov. 2002. Asp344 and Thr345 are critical for cation exchange mediated by NhaD, Na+\/H+ antiporter of Vibrio cholerae<\/em>. Biochim. Biophys. Acta.<\/em> 1564: 99-106. View PDF<\/strong><\/a>

100. G. R. Golding, C. A. Kelly, R.Sparling, P. C. Loewen, J. W. M. Rudd, and T. Barkay. 2002. Evidence for facilitated uptake of Hg(II) by Vibrio anguillarum<\/em> and Escherichia coli<\/em> under anaerobic and aerobic conditions. Limnol. Oceanog.<\/em>47: 967-975. View PDF<\/strong><\/a>

99. J. Switala and P. C. Loewen. 2002. Diversity of properties among catalases. Arch. Biochem. Biophys.<\/em> 401:145-154. View PDF<\/strong><\/a>

98. X. Carpena, A. Guarn\u00e9, J. C. Ferrer, P. M. Alzari, I. Fita, and P. C. Loewen. 2002. Crystallization and preliminary X-ray analysis of the hydroperoxidase I C-terminal domain from Eschericia coli<\/em>. Acta Cryst.<\/em> D58: 853-855. View PDF<\/strong><\/a>

<\/a>2001<\/span><\/strong>
97. X. Carpena, R. Perez, W. F. Ochoa, N. Verdaguer, M. Klotz, J. Switala, W. Melik-Adamyan, I. Fita, and P. C. Loewen. 2001. Crystallisation and preliminary X-ray analysis of Clade I catalases from Pseudomonas syringae<\/em> and Listeria seeligeri<\/em>. Acta Cryst.<\/em> D57: 1184-1186. View PDF<\/strong><\/a>

96. G. Regelsberger, C. Jakopitsch, F. R\u00fcker, J. Switala, P. C. Loewen, and C. Obinger. 2001. The role of distal tryptophan in the bifunctional activity of catalase-peroxidases. Biochem. Soc. Trans.<\/em> 29: 99-105. View PDF<\/strong><\/a>

95. W. Melik-Adamyan, J. Bravo, X. Carpena, J. Switala, M. J. Mat\u00e9, I. Fita and P. C. Loewen. 2001. Substrate flow in catalases deduced from the crystal structures of active site variants of HPII from Escherichia coli<\/em>. Proteins<\/em> 44: 270-281. View PDF<\/strong><\/a>

94. L. Powers, A. Hillar and P. C. Loewen. 2001. Active site structure of the catalase-peroxidases from Mycobacterium tuberculosis<\/em> and Escherichia coli by extended X-ray absorption fine structure analysis (EXAFS). Biochim. Biophys. Acta<\/em> 1546: 44-54. View PDF<\/strong><\/a>

93. P. Nicholls, I. Fita and P. C. Loewen. 2001. Enzymology and structure of catalases. Adv. Inorg. Chem.<\/em> 51: 51-106. View PDF<\/strong><\/a>

92. M. J. Mate, G. Murshudov, J. Bravo, W. Melik-Adamyan, P. C. Loewen and I. Fita. 2001. Heme catalases. In: Handbook of Metalloproteins<\/em> pp 486-502, J. Wiley & Sons, New York, NY View PDF<\/strong><\/a>

<\/a>2000<\/span><\/strong>
91. P. C. Loewen, M. G. Klotz, and D. J. Hassett. 2000. Catalase – an ‘old’ enzyme that continues to surprise us. ASM News<\/em> 66: 76-82. View PDF<\/strong><\/a>

90. A. Hillar, B. Peters, R. Pauls, A. Loboda, H. Zhang, A. G. Mauk, and P. C. Loewen. 2000. Modulation of the activities of catalase-peroxidase HPI of Escherichia coli<\/em> by site-directed mutagenesis. Biochemistry<\/em> 39: 5868-5875. View PDF<\/strong><\/a>

<\/a>1999<\/span><\/strong>
89. M. J. Mate, M. S. Sevinc, B. Hu, J. Bujons, J. Bravo, J. Switala, W. Ens, P. C. Loewen, and I. Fita. 1999. Mutants that alter the covalent structure of catalase HPII from Escherichia coli<\/em>. J. Biol. Chem.<\/em> 274: 27717-27725. View PDF<\/strong><\/a>

88. P. C. Loewen. 1999. Catalase. In: The Encyclopedia of Molecular Biology<\/em> ed. T. Creighton, pp 351-353, J. Wiley & Sons, New York, NY View PDF<\/strong><\/a>

87. J. Switala, J. O’Neil, and P. C. Loewen. 1999. Catalase HPII from Escherichia coli<\/em> exhibits enhanced resistance to denaturation. Biochemistry<\/em> 38: 3895-3901. View PDF<\/strong><\/a>

86. A. Hillar, L. Van Caeseele and P. C. Loewen. 1999. Intracellular location of catalase-peroxidase HPI of E. coli<\/em>. FEMS Microbiol. Lett.<\/em> 170: 307-312. View PDF<\/strong><\/a>

85. M. S. Sevinc, M. J. Mate, J. Switala, I. Fita, and P. C. Loewen. 1999. Role of the lateral channel in catalase HPII of Escherichia coli<\/em>. Protein Sci.<\/em> 8: 490-498. View PDF<\/strong><\/a>

84. J. Bravo, M. J. Mate, T. Schneider, J. Switala, K. Wilson, P. C. Loewen, and I. Fita. 1999. Structure of catalase HPII from Escherichia coli<\/em> at 1.9 \u00c5 resolution. Proteins<\/em> 34: 155-166. View PDF<\/strong><\/a>

<\/a>1998<\/span><\/strong>
83. P. C. Loewen, B. Hu, J. Strutinsky and R. Sparling. 1998. Regulation in the rpoS<\/em> regulon of Escherichia coli<\/em>. Can. J. Microbiol.<\/em> 44: 707-717. View PDF<\/strong><\/a>

82. M. S. Sevinc, J. Switala, J. Bravo, I. Fita, and P. C. Loewen. 1998. Truncation and heme pocket mutations reduce the accumulation of functional catalase HPII of Escherichia coli<\/em>. Prot. Eng.<\/em> 11: 549-555. View PDF<\/strong><\/a>

81. M. Maj, P. C. Loewen and P. Nicholls. 1998. E. coli<\/em> HPII catalase interaction with high spin ligands: formate and fluoride as active site probes. Biochim. Biophys. Acta<\/em> 1384: 209-222. View PDF<\/strong><\/a>

<\/a>1997<\/span><\/strong>
80. K. Tanaka, K. Handel, P. C. Loewen and H. Takahashi. 1997. Identification and analysis of the RpoS-dependent promoter of katE<\/em>, encoding catalase HPII in Escherichia coli<\/em>. Biochim. Biophys. Acta<\/em> 1352: 161-166. View PDF<\/strong><\/a>

79. C. Obinger, M. Maj, P. Nicholls and P. C. Loewen. 1997. Activity, peroxide compound formation and heme d synthesis in E. coli<\/em> HPII catalase. Arch. Biochem. Biophys.<\/em> 342: 58-67. View PDF<\/strong><\/a>

78. J. Bravo, I. Fita, J. C. Ferrer, W. Ens, A. Hillar, J. Switala and P. C. Loewen. 1997. Identification of a novel bond between a histidine and the essential tyrosine in catalase HPII of Escherichia coli<\/em>. Protein Science<\/em> 6: 1016-1023. View PDF<\/strong><\/a>

77. M. G. Klotz, G. R. Klassen and P. C. Loewen. 1997. Phylogenetic relationaships among prokaryotic and eukaryotic catalases. Molec. Biol. Evol.<\/em> 14: 951-958. View PDF<\/strong><\/a>

76. P. C. Loewen. 1997. Bacterial catalases. In: Oxidative Stress and the Molecular Biology of Antioxidant Defenses<\/em>. pp.273-308. Cold Spring Harbor Laboratory Press, Cold Spring Harbor NY View PDF<\/strong><\/a>

<\/a>1996<\/span><\/strong>
75. M. Maj, P. Nicholls, C. Obinger, A. Hillar and P. C. Loewen. 1996. Reaction of E. coli<\/em> catalase HPII with cyanide as ligand and as inhibitor. Biochim. Biophys. Acta<\/em> 1298: 241-249. View PDF<\/strong><\/a>

74. P. C. Loewen. 1996. Probing the structure of HPII of Escherichia coli<\/em> – a review. Gene<\/em> 179: 39-44. View PDF<\/strong><\/a>

73. G. N. Murshudov, A. I. Grebenko, V. Barynin, Z. Dauter, K. S. Wilson, B. K. Vainshtein, W. Melik-Adamyan, J. Bravo, J. M. Ferran, J. C. Ferrer, J. Switala, P. C. Loewen, and I. Fita. 1996. Structure of heme d of Penicillium vitale<\/em> and Escherichia coli<\/em> catalases. J. Biol. Chem.<\/em> 271: 8863-8868. View PDF<\/strong><\/a> <\/a>

1995<\/span><\/strong>
72. P. C. Loewen and J. Switala. 1995. Template structure can increase the error frequency of the DNA polymerase from Thermus aquaticus<\/em>. Gene<\/em> 164: 59-63. View PDF<\/strong><\/a>

71. A. Hillar and P. C. Loewen. 1995. Comparison of isoniazid oxidation catalyzed by bacterial catalase-peroxidases and horse radish peroxidase. Arch. Biochem. Biophys.<\/em> 323: 438-446. View PDF<\/strong><\/a>

70. M. S. Sevinc, W. Enns and P. C. Loewen. 1995. The cysteines of catalase HPII of Escherichia coli<\/em>, including Cys438 which is blocked, do not have a catalytic role. Eur. J. Biochem.<\/em> 230: 127-132. View PDF<\/strong><\/a>

69. J. Bravo, N. Verdaguer, J. Tormo, C. Betzel, J. Switala, P. C. Loewen and I. Fita. 1995. Crystal structure of catalase HPII from Escherichia coli<\/em>. Structure<\/em> 3: 491-502. View PDF<\/strong><\/a>

68. N. A. Buchmeier, S. J. Libby, Y. Xu, P. C. Loewen, J. Switala, D. G. Guiney and F. C. Fang. 1995. DNA repair is more important than catalase for Salmonella<\/em> virulence in mice. J. Clin. Invest.<\/em> 95: 1047-1053. View PDF<\/strong><\/a>

<\/a>1994<\/span><\/strong>
67. P. C. Loewen and R. Hengge-Aronis. 1994. The role of the sigma factor sigma-S (KatF) in bacterial global regulation. Annu. Rev. Microbiol.<\/em> 48: 53-80. View PDF<\/strong><\/a>

66. A. Hillar, P. Nicholls, J. Switala and P. C. Loewen. 1994. NADPH binding and control of catalase compound II formation: comparison of bovine, yeast and Escherichia coli<\/em> enzymes. Biochem. J.<\/em> 300: 531-539. View PDF<\/strong><\/a>

65. F. F. Davidson, P. C. Loewen and H. G. Khorana. 1994. Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state. Proc. Natl. Acad. Sci USA<\/em> 91: 4029-4033. View PDF<\/strong><\/a>

64. M. R. Volkert, P. C. Loewen, J. Switala, D. Crowley and M. Conley. 1994. The delta(argF-lacZ<\/em>)205(U169) deletion greatly enhances resistance to hydrogen peroxide in stationary-phase Escherichia coli<\/em>. J. Bacteriol.<\/em> 176: 1297-1302. View PDF<\/strong><\/a>

<\/a>1993<\/span><\/strong>
63. P. C. Loewen, J. Switala, I. von Ossowski, A. Hillar, A. Christie, B. Tattrie and P. Nicholls. 1993. Catalase HPII of Escherichia coli<\/em> catalyzes the conversion of protoheme to cis-heme d. Biochemistry<\/em> 32: 10159-10164. View PDF<\/strong><\/a>

62. I. von Ossowski, G. Hausner, and P. C. Loewen. 1993. Molecular evolutionary analysis based on the amino acid sequence of catalase. J. Mol. Evol.<\/em>37: 71-76. View PDF<\/strong><\/a>

61. P. C. Loewen, I. von Ossowski, J. Switala and M. R. Mulvey. 1993. KatF (sigma-S) synthesis in Escherichia coli<\/em> is subject to post-transcriptional regulation. J. Bacteriol.<\/em> 175: 2150-2153. View PDF<\/strong><\/a>

<\/a>1992<\/span><\/strong>
60. F. C. Fang, S. J. Libby, N. A. Buchmeier, P. C. Loewen, J. Switala, J. Harwood, and D. G. Gurney. 1992. The alternative sigma factor KatF regulates Salmonella virulence<\/em>. Proc. Natl. Acad. Sci. USA <\/em> 89: 11978-11982. View PDF<\/strong><\/a>

59. Q. Pang, R. Timkovich, P. C. Loewen and J. Peterson. 1992. Identification of heme macrocycle type by near-infrared magnetic circular dichroism spectroscopy at cryogenic temperatures. FEBS Lett.<\/em> 309: 157-160. View PDF<\/strong><\/a>

58. P. C. Loewen. 1992. Regulation of bacterial catalase synthesis. In: Molecular Biology of Free Radical Scavenging Systems<\/em>>. pp. 77-115. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y. View PDF<\/strong><\/a>

<\/a>1991<\/span><\/strong>
57. J. H. Dawson, A. M. Bacete, A. M. Huff, S. Kadkhodayan, C. M. Zeitter, M. Sono, C. K. Chang and P. C. Loewen. 1991. The active site structure of E. coli<\/em> HPII catalase. Evidence favoring coordination of a tyrosinate proximal legand to the chlorin iron. FEBS Lett.<\/em> 295: 123-126. View PDF<\/strong><\/a>

56. I. von Ossowski, M. R. Mulvey, P. A. Leco, A. Borys and P. C. Loewen. 1991. Nucleotide sequence of katE<\/em> of Escherichia coli<\/em> encoding catalase HPII. J. Bacteriol.<\/em> 173: 514-520. View PDF<\/strong><\/a>

<\/a>1990<\/span><\/strong>
55. M. R. Mulvey, J. Switala, A. Borys and P. C. Loewen. 1990. Regulation of transcription of katE<\/em> and katF<\/em> in Escherichia coli<\/em>. J. Bacteriol.<\/em> 172: 6713-6720. View PDF<\/strong><\/a>

54. P. C. Loewen and G. V. Stauffer. 1990. Nucleotide sequence of katG<\/em> of Salmonella typhimurium<\/em> LT2 and characterization of its product, hydroperoxidase I. Molec. Gen. Genet.<\/em> 224: 147-151. View PDF<\/strong><\/a>

53. J. Switala, B. L. Triggs-Raine and P. C. Loewen. 1990. Homology among bacterial catalase genes. Canad. J. Microbiol.<\/em> 36: 728-731. View PDF<\/strong><\/a>

52. P. C. Loewen, J. Switala, M. Smolenski and B. L. Triggs-Raine 1990. Molecular characterization of three mutations in katG<\/em>, affecting the activity of hydroperoxidase I of Escherichia coli<\/em>. Biochem. Cell Biol.<\/em> 68: 1037-1044. View PDF<\/strong><\/a>

51. J. Tormo, I. Fita, J. Switala and P. C. Loewen. 1990. Crystallization and preliminary x-ray diffraction analysis of catalase HPII from Escherichia coli<\/em>. J. Mol. Biol.<\/em> 213: 219-220. View PDF<\/strong><\/a>

<\/a>1989<\/span><\/strong>
50. M. R. Mulvey and P. C. Loewen. 1989. Nucleotide sequence of katF<\/em> suggests KatF protein is a novel sigma transcription factor. Nucl. Acids Res.<\/em> 17: 9979-9991. View PDF<\/strong><\/a>

49. J. T. Chiu, P. C. Loewen, J. Switala, R. B. Gennis and R. Timkovich. 1989. Proposed structure for the prosthetic group of the catalase HPII from Escherichia coli<\/em>. J. Am. Chem. Soc.<\/em> 111: 7046-7050. View PDF<\/strong><\/a>

48. P. C. Loewen. 1989. Genetic mapping of katB<\/em>, a locus that affects catalase 2 levels in Bacillus subtilis<\/em>. Can. J. Microbiol.<\/em> 35: 807-810. View PDF<\/strong><\/a>

<\/a>1988<\/span><\/strong>
47. M. R. Mulvey, P. . Sorby, B. L. Triggs-Raine and P. C. Loewen. 1988. Cloning and physical characterization of katE<\/em> and katF<\/em>, required for catalase HPII expression in E. coli<\/em>. Gene<\/em> 73: 337-345. View PDF<\/strong><\/a>

46. B. L. Triggs-Raine, B. W. Doble, M. R. Mulvey, P. A. Sorby and P. C. Loewen. 1988. Nucleotide sequence of katG<\/em> encoding catalase HPI of Escherichia coli<\/em>. J. Bacteriol.<\/em> 170: 4415-4419. View PDF<\/strong><\/a>

45. P. C. Loewen and J. Switala. 1988. Purification and characterization of spore-specific catalase-2 from Bacillus subtilis<\/em>. Biochem. Cell. Biol.<\/em>66: 707-714. View PDF<\/strong><\/a>

44. H. E. Richter, J. Switala and P. C. Loewen. 1988. Effect of ascorbate on oxygen uptake and growth of Escherichia coli B. Can. J. Microbiol.<\/em> 34: 822-824. View PDF<\/strong><\/a>

<\/a>1987<\/span><\/strong>
43. P. C. Loewen and J. Switala. 1987. Genetic mapping of katA<\/em>, a locus that affects the synthesis of catalase-1 in Bacillus subtilis<\/em>. J. Bacteriol.<\/em> 169: 5848-5851. View PDF<\/strong><\/a>

42. P. C. Loewen and J. Switala. 1987. Purification of catalase-1 from Bacillus subtilis<\/em>. Biochem. Cell Biol.<\/em> 65: 939-947. View PDF<\/strong><\/a>

41. P. C. Loewen and J. Switala. 1987. Multiple catalases in Bacillus subtilis<\/em>. J. Bacteriol.<\/em> 169: 3601-3607. View PDF<\/strong><\/a>

40. B. L. Triggs-Raine and P. C. Loewen. 1987. Physical characterization of katG<\/em>, encoding catalase HPI of Escherichia coli<\/em>. Gene<\/em> 52: 121-128. View PDF<\/strong><\/a>

1986<\/span><\/strong>
39. P. C. Loewen and J. Switala. 1986. Purification and characterization of catalase HPII from Escherichia coli<\/em> K12. Can. J. Biochem. Cell Biol.<\/em> 64: 638-646. View PDF<\/strong><\/a> <\/a>

1985<\/span><\/strong>
38. P. C. Loewen, J. Switala and B. L. Triggs-Raine. 1985. Catalases HPI and HPII in Escherichia coli<\/em> are induced independently. Arch. Biochem. Biophys.<\/em> 243: 144-149. View PDF<\/strong><\/a>

37. P. C. Loewen, B. L. Triggs, C. S. George and B. E. Hrabarchuk. 1985. Genetic mapping of katG<\/em>, a locus that affects the synthesis of the bifunctional catalase-peroxidase HPI in Escherichia coli<\/em>. J. Bacteriol.<\/em> 162: 661-667. View PDF<\/strong><\/a>

36. F. C. Wong, J. G. Spearman, M. A. Smolenski and P. C. Loewen. 1985. Equine parvovirus: Initial isolation and partial characterization. Can. J. Comp. Med.<\/em> 49: 50-54. View PDF<\/strong><\/a>

35. P. C. Loewen. 1985. Detection of p-aminobenzoylpoly(gamma-glutamates) using fluorescamine. Methods in Enzymology<\/em> 122: 330-333. View PDF<\/strong><\/a>

<\/a>1984<\/span><\/strong>
34. P. C. Loewen and B. L. Triggs. 1984. Genetic mapping of katF<\/em>, a locus that with katE<\/em> affects the synthesis of a second catalase species in Escherichia coli<\/em>. J. Bacteriol.<\/em> 160: 668-675. View PDF<\/strong><\/a>

33. P. C. Loewen. 1984. Isolation of catalase-deficient Escherichia coli<\/em> mutants and genetic mapping of katE<\/em>, a locus that affects catalase activity. J. Bacteriol.<\/em> 157: 622-626. View PDF<\/strong><\/a>

<\/a>1983<\/span><\/strong>
32. P. C. Loewen, B. L. Triggs, G. R. Klassen and J. H. Weiner. 1983. Identification and physical characterisation of a ColEl hybrid plasmid containing a catalase gene of Escherichia coli<\/em>. Can. J. Biochem.<\/em> 61: 1315-1321. View PDF<\/strong><\/a>

31. P. C. Loewen and H. E. Richter. 1983. Inhibition of sugar uptake by ascorbic acid in Escherichia coli<\/em>. Arch. Biochem. Biophys.<\/em> 226: 657-665. View PDF<\/strong><\/a>

30. W. J. P. Blonski, F. E. Hruska, K. L. Sadana and P. C. Loewen. 1983. Conformational studies of ribo-, 2′-deoxyribo- and arabinonucleotides by carbon 13 NMR. <Biopolymers<\/em> 22: 605-616. View PDF<\/strong><\/a>

<\/a>1982<\/span><\/strong>
29. H. E. Richter and P. C. Loewen. 1982. Rapid inactivation of bacteriophage T7 by ascorbic acid is repairable. Biochem. Biophys. Acta<\/em> 697: 25-30. View PDF<\/strong><\/a>

28. H. E. Richter and P. C. Loewen. 1982. Catalase synthesis in Escherichia coli<\/em> is not controlled by catabolite repression. Arch. Biochem. Biophys.<\/em>215: 72-77. View PDF<\/strong><\/a>

<\/a>1981<\/span><\/strong>
27. K. L. Sadana, F. E. Hruska and P. C. Loewen. 1981. A simplified strategy for the synthesis of dideoxyribonucleotide blocks. Tetrahedron Letters<\/em> 22: 3367-3370. View PDF<\/strong><\/a>

26. R. A. H. Furness and P. C. Loewen. 1981. Detection of p-aminobenzoyl(gamma- glutamates) using fluorescamine. Anal. Biochem.<\/em> 117: 126-135. View PDF<\/strong><\/a>

25. H. E. Richter and P. C. Loewen. 1981. Induction of catalase in Escherichia coli by ascorbic acid involves hydrogen peroxide. Biochem. Biophys. Res. Comm.<\/em> 100: 1039-1046. View PDF<\/strong><\/a>

24. W. P. Niemczura, F. E. Hruska, K. L. Sadana and P. C. Loewen. 1981. Proton magnetic resonance study of nucleosides, nucleotides and dideoxynucleoside monophosphates containing a syn pyrimidine base. Biopolymers<\/em> 20: 1671-1690. View PDF<\/strong><\/a>

23. P. C. Loewen. 1981. Effect of glutathione deficiency on the pool of CoA-glutathione mixed disulfide in Escherichia coli<\/em>. Can. J. Biochem.<\/em> 59: 379-382. View PDF<\/strong><\/a>

<\/a>1979<\/span><\/strong>
22. W. C. H. Bees and P. C. Loewen. 1979. Partial characterization of the mode of inhibition of E. coli<\/em> RNA polymerase by the mixed disulfide, CoASSG. Can. J. Biochem.<\/em> 57: 336-345. View PDF<\/strong><\/a>

21. P.C. Loewen. 1979. Levels of glutathione in E. coli<\/em>. Can. J. Biochem.<\/em> 57: 107-111. View PDF<\/strong><\/a>

<\/a>1978<\/span><\/strong>
20. K. L. Sadana and P. C. Loewen. 1978. A rapid and efficient synthesis of ribonucleotides. Tetrahedron Letters<\/em> 5095-5098. View PDF<\/strong><\/a>

19. P.C. Loewen. 1978. Levels of coenzyme A-glutathione mixed disulfide in Escherichia coli<\/em>. Can. J. Biochem.<\/em> 56: 753-759. View PDF<\/strong><\/a>

18. D. R. McNaughton, G. R. Klassen, P. C. Loewen and H. B. L\u00e9John. 1978. Recharacterization of fungal dinucleoside polyphosphate (HS3). Can. J. Biochem.<\/em>56: 217-226. View PDF<\/strong><\/a>

17. J. Peeling, F. E. Hruska and P. C. Loewen. 1978. Ribo-, 2′-deoxyribo- hybrid dinuclesoide monophosphates. Proton, magnetic resonance studies of 3′, 5′- and 2′,5′-uridylyl-2′-deoxythymidine. Can. J. Chem.<\/em> 56: 522-529. View PDF<\/strong><\/a>

<\/a>1977<\/span><\/strong>
16. P. C. Loewen. l977. Identification of a coenzyme A-glutathione disulfide (DSI), a modified coenzyme A disulfide (DSII) and a NADPH-dependent coenzyme A-glutathione disulfide reductase in E. coli<\/em>. Can. J. Biochem.<\/em> 55: 1019-1027. View PDF<\/strong><\/a>

<\/a>1976<\/span><\/strong>
15. P. C. Loewen. 1976. Partial characterization of an endonuclease activity which appears in nuclease free T4 polynucleotide kinase. Nucl. Acids Res.<\/em> 3: 3133-3141. View PDF<\/strong><\/a>

14. G. R. Klassen, R. A. Furness and P. C. Loewen. 1976. Inhibition of E. coli<\/em> DNA dependent RNA polymerase by novel nucleotides DSI and DSII. Biochem. Biophys. Res. Comm.<\/em> 72: 1056-1062. View PDF<\/strong><\/a>

13. P. C. Loewen 1976. Novel nucleotides from E. coli<\/em> isolated and partially characterized. Biochem. Biophys. Res. Comm.<\/em> 70: 1210-1218. View PDF<\/strong><\/a>

12. R. Kleppe, T. Sekiya, P. C. Loewen, K. Kleppe, A. L. Agarwal, H. Buchi, P. Besmer, M. H. Caruthers, P. J. Cashion, M. Fridkin, E. Jay, A. Kumar, R. C. Miller, K. Minamoto, A. Panet, U. L. RajBhandary, B. Ramamoorthy, N. Siderova, T. Takeya, J. H. van de Sande and H. G. Khorana. 1976. Studies on Polynucleotides CXLI. Total synthesis of the structural gene for the precursor of a tyrosine suppressor transfer RNA from E. coli<\/em>. Enzymatic joining to form the total DNA duplex. J. Biol. Chem.<\/em> 251: 667-675. View PDF<\/strong><\/a>

11. P.C. Loewen, R.C. Miller, A. Panet, T. Sekiya and H.G. Khorana. 1976.Studies on polynucleotides CXXXVIII. Total synthesis of the structural gene for the precursor of a tyrosine suppressor transfer RNA from E. coli<\/i>. Enzymatic joining of the chemically synthesized segments to form DNA duplexes corresponding to the nucleotide sequences 23 to 60 and 23 to 66. J. Biol. Chem.<\/i> 251: 642-650. View PDF<\/b><\/a>

10. H. G. Khorana, K. L. Agarwal, P. Besmer, H. Buchi, M. H. Caruthers, P. J. Cashion, M. Fridkin, E. Jay, K. Kleppe, R. Kleppe, A. Kumar, P. C. Loewen, R. C. Miller, K. Minamoto, A. Panet, U. L. RajBhandary, B. Ramamoorthy, T. Sekiya, T. Takeya and J. H. van de Sande. 1976. Studies on Polynucleotides CXXXI. Total synthesis of the structural gene for the precursor of a tyrosine suppressor transfer from E. coli<\/i>. General introduction. J. Biol. Chem.<\/i> 251: 565-570. View PDF<\/b><\/a>

<\/a>1974<\/span><\/b>
9. P. C. Loewen. 1974. Determination of the sequences of 18 nucleotides from the 5′-end of the 1-strand and 15 nucleotides from the 5′-end of the r-strand of T7 DNA. Nucleic Acids Research<\/i> 2: 839-852. View PDF<\/b><\/a>

8. P. C. Loewen, T. Sekiya and H. G. Khorana. 1974. Studies on Polynucleotides CXXVI. The nucleotide sequence adjoining the CCA end of the E. coli<\/i> tyrosine transfer RNA gene. J. Biol. Chem.<\/i> 249: 217-226. View PDF<\/b><\/a>

<\/a>1973<\/span><\/b>
7. P. C. Loewen and H. G. Khorana. 1973. Studies on Polynucleotides CXXII. Dodecanucleotide sequence adjoining the CCA end of the tyrosine transfer RNA gene. J. Biol. Chem.<\/i> 248: 3489-3499. View PDF<\/b><\/a>

6. A. Panet, J. H. van de Sande, P. C. Loewen, H. G. Khorana, A. J. Raae, J. L. Lillehaug and K. Kleppe. 1973. Studies on Polynucleotides CXXIII. Physical characterisation and simultaneous purification of bacteriophage T4 induced polynucleotide kinase, polynucleotide ligase and DNA polymerase. Biochemistry<\/i> 12: 5045-5050. View PDF<\/b><\/a>

<\/a>1972<\/span><\/b>
5. H. van de Sande, P. C. Loewen and H. G. Khorana. 1972. Studies on Polynucleotides CXVIII. A further study of ribonucleotide incorporation into DNA by DNA polymerase I of E. coli<\/i>. J. Biol. Chem.<\/i> 247: 6140-6148. View PDF<\/b><\/a>

4. P. C. Loewen and R. K. Brown. 1972. 2-Aryloxytetrahydrofurans. Their reductive cleavage by ether solutions of AlH2<\/sub>Cl and their cleavage and rearrangement by ether solutions of AlCl3<\/sub>. Can. J. Chem.<\/i> 50: 3639-3647. View PDF<\/b><\/a>

3. P. C. Loewen, L. P. Makubu and R. K. Brown. 1972. The influence of the 2-alkoxy group and C-5 substituents on the direction of reductive cleavage of 2-alkoxytetrahydrofurans by AlH2<\/sub>Cl in ether solution. Can. J. Chem.<\/i> 50: 1502-1512. View PDF<\/b><\/a>

<\/a>1969<\/span><\/b>
2. P. C. Loewen, W. W. Zajac and R. K. Brown. 1969. Hydrogenolysis of LiAlH4<\/sub>-AlCl3<\/sub> of an ether solution of norcamphor isobutylene ketal. Can. J. Chem.<\/i> 47: 4059-4067. View PDF<\/b><\/a>

<\/a>1965<\/span><\/b>
1. T. L. Richards and P. C. Loewen. 1965. A preliminary investigation of solar radiation over the Great Lakes as compared to adjacent land areas. Proc. Eighth Conf. on Great Lakes Research<\/i> 13: 278-282. View PDF<\/b><\/a><\/td><\/tr><\/tbody><\/table><\/figure>\n","protected":false},"excerpt":{"rendered":"

Citations >8,900, h index = 47 (Web of Science) Citations >13,100, h index = 58; i-10 = 147(Google Scholar) (as of 24 January, 2022) 2020 181. M. Singh, P. M. De Silva, Y. Al-Saadi, J. Switala, P. C. Loewen, G. Hausner, W. Chen, I. Hernandez, S. Castillo-Ramirez and A. Kumar. 2020. Characterization of extremely […]<\/p>\n","protected":false},"author":2,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-694","page","type-page","status-publish","hentry","odd"],"_links":{"self":[{"href":"http:\/\/www.loewenlabs.com\/peter\/wp-json\/wp\/v2\/pages\/694","targetHints":{"allow":["GET"]}}],"collection":[{"href":"http:\/\/www.loewenlabs.com\/peter\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"http:\/\/www.loewenlabs.com\/peter\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"http:\/\/www.loewenlabs.com\/peter\/wp-json\/wp\/v2\/users\/2"}],"replies":[{"embeddable":true,"href":"http:\/\/www.loewenlabs.com\/peter\/wp-json\/wp\/v2\/comments?post=694"}],"version-history":[{"count":8,"href":"http:\/\/www.loewenlabs.com\/peter\/wp-json\/wp\/v2\/pages\/694\/revisions"}],"predecessor-version":[{"id":724,"href":"http:\/\/www.loewenlabs.com\/peter\/wp-json\/wp\/v2\/pages\/694\/revisions\/724"}],"wp:attachment":[{"href":"http:\/\/www.loewenlabs.com\/peter\/wp-json\/wp\/v2\/media?parent=694"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}