@article{zahran_manning_seo_noga_2016, title={The effect of Ochratoxin A on antimicrobial polypeptide expression and resistance to water mold infection in channel catfish (Ictalurus punctatus)}, volume={57}, journal={Fish & Shellfish Immunology}, author={Zahran, E. and Manning, B. and Seo, J. K. and Noga, E. J.}, year={2016}, pages={60–67} }
 @article{zahran_seo_noga_2012, title={The effect of adjuvant and microbial challenge on the expression of antimicrobial polypeptides in channel catfish (Ictalurus punctatus)}, volume={33}, number={2}, journal={Fish & Shellfish Immunology}, author={Zahran, E. and Seo, J. K. and Noga, E. J.}, year={2012}, pages={168–173} }
 @article{noga_borron_hinshaw_gordon_gordon_seo_2011, title={Identification of histones as endogenous antibiotics in fish and quantification in rainbow trout (Oncorhynchus mykiss) skin and gill}, volume={37}, ISSN={["1573-5168"]}, DOI={10.1007/s10695-010-9422-7}, abstractNote={Antimicrobial polypeptides (AMPPs) are increasingly recognized as a critical component of innate host defense. Among the AMPPs, polypeptides related to histones have been identified from many animals. Using peptide mapping, we further confirm the identity of two histone-like proteins from fish as members of the H2B (sunshine bass) and H1 (rainbow trout) histone groups. We optimized the conditions for measuring rainbow trout HLP-1/H2B via sandwich ELISA. We used two antibodies, one to the amino terminus and one to the carboxyl terminus, of trout histone H2B, as the capture antibodies, and we used peroxidase-labeled antibody raised to calf histone H2B as the secondary antibody. Specificity of the detecting antibody was confirmed by specific reactivity with histone H2B in tissue extracts via western blotting. The test was reproducible and capable of detecting as little as 5 ng of histone H2B (0.05 μg/ml). Histone H2B levels expressed in gill tissue of juvenile, healthy rainbow trout were well within concentrations that are lethal to important fish pathogens. However, there was a significant, age (size)-dependent decline in histone H2B concentrations as fish matured, until levels became virtually undetectable in market-size fish. In contrast, levels in skin appeared to remain high and unchanged in small versus large fish. Antibacterial activity in skin and gill tissues was closely correlated with histone H2B concentration measured via ELISA, which supports our previous finding that histones are the major AMPPs in rainbow trout skin and gill.}, number={1}, journal={FISH PHYSIOLOGY AND BIOCHEMISTRY}, author={Noga, Edward J. and Borron, Paul J. and Hinshaw, Jeffrey and Gordon, William C. and Gordon, Linda J. and Seo, Jung-Kil}, year={2011}, month={Mar}, pages={135–152} }
 @article{seo_stephenson_noga_2011, title={Multiple antibacterial histone H2B proteins are expressed in tissues of American oyster}, volume={158}, number={3}, journal={Comparative Biochemistry and Physiology. B, Biochemistry & Molecular Biology}, author={Seo, J. K. and Stephenson, J. and Noga, E. J.}, year={2011}, pages={223–229} }
 @article{park_silphaduang_moon_seo_corrales_noga_2011, title={Structure-activity relationships of piscidin 4, a piscine antimicrobial peptide}, volume={50}, number={16}, journal={Biochemistry}, author={Park, N. G. and Silphaduang, U. and Moon, H. S. and Seo, J. K. and Corrales, J. and Noga, E. J.}, year={2011}, pages={3288–3299} }
 @article{seo_stephenson_crawford_stone_noga_2010, title={American oyster, Crassostrea virginica, expresses a potent antibacterial histone H2B protein}, volume={12}, number={5}, journal={Marine Biotechnology (New York, N.Y.)}, author={Seo, J. K. and Stephenson, J. and Crawford, J. M. and Stone, K. L. and Noga, E. J.}, year={2010}, pages={543–551} }
 @article{noga_silphaduang_park_seo_stephenson_kozowicz_2009, title={Piscidin 4, a novel member of the piscidin family of antimicrobial peptides}, volume={152}, ISBN={1096-4959}, number={4}, journal={Comparative Biochemistry and Physiology. B, Biochemistry & Molecular Biology}, author={Noga, E. J. and Silphaduang, U. and Park, N. G. and Seo, J. K. and Stephenson, J. and Kozowicz, S.}, year={2009}, pages={299–305} }
 @article{srinivasulu_syvitski_seo_mattatall_knickle_douglas_2008, title={Expression, purification and structural characterization of recombinant hepcidin, an antimicrobial peptide identified in Japanese flounder, Paralichthys olivaceus}, volume={61}, ISSN={["1096-0279"]}, DOI={10.1016/j.pep.2008.05.012}, abstractNote={The cysteine-rich peptide hepcidin is an antimicrobial peptide and iron transport regulator that has been found in vertebrates including birds, fish and mammals. To elucidate the structure and biological function of fish hepcidin, which is difficult to produce synthetically, we have cloned several plasmid constructs encoding hepcidin from Japanese flounder, Paralichthys olivaceus, and tested expression of recombinant peptides, each with an N-terminal hexahistidine (6xHis) tag, in inclusion bodies or the periplasmic space of Escherichia coli. Hepcidin expressed in inclusion bodies was reduced, and subsequently refolded using a dilution technique with a cysteine redox system. The oxidized His-hepcidin monomer was separated from protein multimers and mass spectrometry analysis showed that the peptide was of the predicted size and contained four disulfide bonds. Removal of the 6xHis tag was attempted using enzymatic cleavage by Factor Xa and tobacco etch virus (TEV) protease or chemical cleavage by hydroxylamine. The Factor Xa cleavage was unsuccessful and hydroxylamine cleavage resulted in aggregation of cleaved peptide. TEV protease cleavage was successful but immediately resulted in hexamer formation despite varying reaction conditions (redox, non-redox, pH, temperature, target protein concentration, type of buffer). However, the recombinant His-hepcidin fusion peptide monomer showed considerable antimicrobial activity. NMR-based studies showed that hepcidin contained a rare vicinal disulfide linkage at the top of a loop structure and a short beta-sheet structure encompassing residues 7-13 and 19-25 that is stabilized by three disulfide bonds.}, number={1}, journal={PROTEIN EXPRESSION AND PURIFICATION}, author={Srinivasulu, B. and Syvitski, R. and Seo, J. -K. and Mattatall, N. R. and Knickle, L. C. and Douglas, S. E.}, year={2008}, month={Sep}, pages={36–44} }
 @article{seo_crawford_stone_noga_2005, title={Purification of a novel arthropod defensin from the American oyster, Crassostrea virginica}, volume={338}, ISSN={["1090-2104"]}, DOI={10.1016/j.bbrc.2005.11.013}, abstractNote={An antimicrobial peptide was purified from acidified gill extract of a bivalve mollusk, the American oyster (Crassostrea virginica), by preparative acid-urea–polyacrylamide gel electrophoresis and reversed-phase high performance liquid chromatography. The 4265.0 Da peptide had 38 amino acids, including 6 cysteines. It showed strongest activity against Gram-positive bacteria (Lactococcus lactis subsp. lactis and Staphylococcus aureus; minimum effective concentrations [MECs] 2.4 and 3.0 μg/ml, respectively) but also had significant activity against Gram-negative bacteria (Escherichia coli D31 and Vibrio parahemolyticus; MECs 7.6 and 15.0 μg/ml, respectively). Comparison of the amino acid sequence with those of other known antimicrobial peptides revealed that the novel peptide had high sequence homology to arthropod defensins, including those from other bivalves, the mussels Mytilus edulis and Mytilus galloprovincialis. This is the first antimicrobial peptide to be isolated from any oyster species and we have named it American oyster defensin (AOD).}, number={4}, journal={BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS}, author={Seo, JK and Crawford, JM and Stone, KL and Noga, EJ}, year={2005}, month={Dec}, pages={1998–2004} }