@article{noar_loveless_luis navarro-herrero_olson_bruno-barcena_2015, title={Aerobic Hydrogen Production via Nitrogenase in Azotobacter vinelandii CA6}, volume={81}, ISSN={["1098-5336"]}, url={http://europepmc.org/abstract/med/25911479}, DOI={10.1128/aem.00679-15}, abstractNote={ABSTRACT}, number={13}, journal={APPLIED AND ENVIRONMENTAL MICROBIOLOGY}, author={Noar, Jesse and Loveless, Telisa and Luis Navarro-Herrero, Jose and Olson, Jonathan W. and Bruno-Barcena, Jose M.}, year={2015}, month={Jul}, pages={4507–4516} }
 @article{taliercio_loveless_turano_kim_2014, title={Identification of epitopes of the beta subunit of soybean beta-conglycinin that are antigenic in pigs, dogs, rabbits and fish}, volume={94}, ISSN={["1097-0010"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-84903579784&partnerID=MN8TOARS}, DOI={10.1002/jsfa.6556}, abstractNote={BACKGROUND
β-Conglycinin (conglycinin) is one of the major seed storage proteins of soybean. Conglycinin is a 7S trimer composed of different combinations of β, α and α' subunits. All subunits of conglycinin have been reported to be allergenic in humans. The goal of this research is to identify epitopes of the β subunit of conglycinin that are antigenic in multiple animal species.


RESULTS
Sera from pigs, dogs, rabbits and hybrid striped bass that had antibodies against soybean conglycinin were identified by ELISA. Most of these sera recognized peptides that represent the β subunit of conglycinin. One antigenic region of the β subunit of conglycinin had considerable overlap among all species tested. One region that was similar to a peanut allergenic epitope in humans overlapped with a region that binds IgE from dogs. One region was antigenic in multiple rabbits and pigs, suggesting it may play a role in the response of pigs to soybean in the diet.


CONCLUSION
One region of the β subunit of conglycinin is an important antigen across species and abuts a region similar to the peanut allergen ARA h 1. A second region is particularly antigenic in pigs and rabbits. Variants of these antigenic regions of the β subunit of conglycinin may be useful in determining the role these regions play in the health of animals fed soybean. Published 2014. This article is a U.S. Government work and is in the public domain in the USA.}, number={11}, journal={JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE}, author={Taliercio, Earl and Loveless, Telisa M. and Turano, Marc J. and Kim, Sung Woo}, year={2014}, month={Aug}, pages={2289–2294} }
 @article{betancourt_loveless_brown_bishop_2008, title={Characterization of diazotrophs containing Mo-independent nitrogenases, isolated from diverse natural environments}, volume={74}, ISSN={["1098-5336"]}, DOI={10.1128/AEM.02694-07}, abstractNote={ABSTRACT}, number={11}, journal={APPLIED AND ENVIRONMENTAL MICROBIOLOGY}, author={Betancourt, Doris A. and Loveless, Telisa M. and Brown, James W. and Bishop, Paul E.}, year={2008}, month={Jun}, pages={3471–3480} }
 @article{loveless_bishop_1999, title={Identification of genes unique to Mo-independent nitrogenase systems in diverse diazotrophs}, volume={45}, ISSN={["1480-3275"]}, DOI={10.1139/w99-007}, abstractNote={A number of nitrogen-fixing bacteria were screened using PCR for genes (vnfG and anfG) unique to the V-containing nitrogenase (vnf) and the Fe-only nitrogenase (anf) systems. Products with sequences similar to that of vnfG were obtained from Azotobacter paspali and Azotobacter salinestris genomic DNAs, and products with sequences similar to that of anfG were obtained from Azomonas macrocytogenes, Rhodospirillum rubrum, and Azotobacter paspali DNAs. Phylogenetic analysis of the deduced amino acid sequences of anfG and vnfG genes shows that each gene product forms a distinct cluster. Furthermore, amplification of an internal 839-bp region in anfD and vnfD yielded a product similar to anfD from Heliobacterium gestii and a product similar to vnfD from Azotobacter paspali and Azotobacter salinestris. Phylogenetic analysis of NifD, VnfD, and AnfD amino acid sequences indicates that AnfD and VnfD sequences are more closely related to each other than either is to NifD. The results of this study suggest that Azotobacter salinestris possesses the potential to express the vanadium (V)-containing nitrogenase (nitrogenase 2) and that R. rubrum, Azomonas macrocytogenes, and H. gestii possess the potential to express the Fe-only nitrogenase (nitrogenase 3). Like Azotobacter vinelandii, Azotobacter paspali appears to have the potential to express both the V-containing nitrogenase and the Fe-only nitrogenase.Key words: Mo-independent nitrogenase systems, diverse diazotrophs, vnfG, anfG.}, number={4}, journal={CANADIAN JOURNAL OF MICROBIOLOGY}, author={Loveless, TM and Bishop, PE}, year={1999}, month={Apr}, pages={312–317} }
 @article{loveless_saah_bishop_1999, title={Isolation of nitrogen-fixing bacteria containing molybdenum-independent nitrogenases from natural environments}, volume={65}, number={9}, journal={Applied and Environmental Microbiology}, author={Loveless, T. M. and Saah, J. R. and Bishop, P. E.}, year={1999}, pages={4223–4226} }