@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{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{silphaduang_colorni_noga_2006, title={Evidence for widespread distribution of piscidin antimicrobial peptides in teleost fish}, volume={72}, ISSN={["1616-1580"]}, DOI={10.3354/dao072241}, abstractNote={Antimicrobial peptides (AMPs) are increasingly recognized as a critical component of the host's defense against infection. Several types of AMPs have been recently identified from mucosal tissues or immune cells of a number of teleosts. Among these are the piscidins, which are 22 residue, alpha-helical AMPs that were originally isolated from mast cells of hybrid striped bass Morone saxatilis male x Morone chrysops female. Using an antibody specific for the conserved N-terminal amino acid sequence of piscidin 1, we used immunohistochemistry to probe skin, gill, and gastrointestinal tract of 39 teleosts representing 7 different orders. Nine fish species were piscidin-positive, with all of these species being in the Perciformes, the largest and most evolutionarily advanced order of teleosts. Piscidin-positive cells were identified in species belonging to the families Moronidae, Serranidae, Sciaenidae, Siganidae and Belontidae. Immunopositive cells were usually most consistent with mast cells, although in some species, the granule appearance and tinctorial properties diverged somewhat from those of a typical piscine mast cell. In addition, rodlet cells were piscidin-positive in one member of the family Cichlidae; to our knowledge, it is the first time that a host-associated chemical biomarker has been identified in rodlet cells. Our data suggest that piscidins are present in many evolutionarily advanced teleosts. Piscidin-immunoreactive cells were most common at sites of pathogen entry, including the skin, gill and gastrointestinal tract. These results strongly suggest that piscidins are a widespread and important component of many fishes' defense against disease.}, number={3}, journal={DISEASES OF AQUATIC ORGANISMS}, author={Silphaduang, U. and Colorni, A. and Noga, E. J.}, year={2006}, month={Oct}, pages={241–252} }
 @misc{noga_silphaduang_2004, title={Antimicrobial peptides isolated from fish}, volume={6,753,407}, number={2004 June 22}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Noga, E. J. and Silphaduang, U.}, year={2004} }
 @article{chinchar_bryan_silphadaung_noga_wade_rollins-smith_2004, title={Inactivation of viruses infecting ectothermic animals by amphibian and piscine antimicrobial peptides}, volume={323}, ISSN={["0042-6822"]}, DOI={10.1016/j.virol.2004.02.029}, abstractNote={The ability of five purified amphibian antimicrobial peptides (dermaseptin-1, temporin A, magainin I, and II, PGLa), crude peptide fractions isolated from the skin of Rana pipiens and R. catesbeiana, and four antimicrobial peptides (AMPs) from hybrid striped bass (piscidin-1N, -1H, -2, and -3) were examined for their ability to reduce the infectivity of channel catfish virus (CCV) and frog virus 3 (FV3). All compounds, with the exception of magainin I, markedly reduced the infectivity of CCV. In contrast to CCV, FV3 was 2- to 4-fold less sensitive to these agents. Similar to an earlier study employing two other amphibian peptides, the agents used here acted rapidly and over a wide, physiologically relevant, temperature range to reduce virus infectivity. These results extend our previous findings and strongly suggest that various amphibian and piscine AMPs may play important roles in protecting fish and amphibians from pathogenic viruses.}, number={2}, journal={VIROLOGY}, author={Chinchar, VG and Bryan, L and Silphadaung, U and Noga, E and Wade, D and Rollins-Smith, L}, year={2004}, month={Jun}, pages={268–275} }
 @article{noga_fan_silphaduang_2002, title={Host site of activity and cytological effects of histone-like proteins on the parasitic dinoflagellate Amyloodinium ocellatum}, volume={52}, ISSN={["0177-5103"]}, DOI={10.3354/dao052207}, abstractNote={Histone-like proteins (HLPs) are broad-spectrum, endogenously produced antibiotics which we have isolated from tissues of rainbow trout Oncorhynchus mykiss and hybrid striped bass (Morone saxatilis male x M. chrysops female). Here, we show that HLP-1, which has high sequence homology to histone H2B, equally inhibited both young and mature trophonts of the important ectoparasite Amyloodinium ocellatum. In addition to direct killing of Amyloodinium trophonts, there was evidence that HLP-1 from both rainbow trout and hybrid striped bass caused severe developmental abnormalities, including delayed development, in both the parasitic trophont stage as well as the reproductive tomont stage. The deleterious effects of HLP-1 also were manifested in what appeared to be 'delayed mortality', where parasites of normal appearance would die later in development. Similar serious damage was also seen with calf histone H2B and the unrelated peptide antibiotic magainin 2. A comparison of the antibiotic activity in mucus versus epidermis compartments of the skin of hybrid striped bass suggested that the majority of antibiotic (including HLP-1) activity resided in the epidermis, although some activity was present in the mucus. These data suggest that normal, nonimmune fish skin contains potent defenses against protozoan ectoparasites and that the effects of these defenses may extend beyond their transient interactions with the parasites, which has important implications for this host-parasite relationship.}, number={3}, journal={DISEASES OF AQUATIC ORGANISMS}, author={Noga, EJ and Fan, ZQ and Silphaduang, U}, year={2002}, month={Dec}, pages={207–215} }
 @article{silphaduang_noga_2001, title={Antimicrobials - Peptide antibiotics in mast cells of fish}, volume={414}, ISSN={["0028-0836"]}, DOI={10.1038/35104690}, number={6861}, journal={NATURE}, author={Silphaduang, U and Noga, EJ}, year={2001}, month={Nov}, pages={268–269} }
 @article{noga_fan_silphaduang_2001, title={Histone-like proteins from fish are lethal to the parasitic dinoflagellate Amyloodinium ocellatum}, volume={123}, number={2001 July}, journal={Parasitology}, author={Noga, E. J. and Fan, Z. Q. and Silphaduang, U.}, year={2001}, pages={57–65} }
 @article{silphaduang_hatai_wada_noga_2000, title={Cladosporiosis in a tomato clownfish (Amphiprion frenatus)}, volume={31}, number={2}, journal={Journal of Zoo and Wildlife Medicine}, author={Silphaduang, U. and Hatai, K. and Wada, S. and Noga, E.}, year={2000}, pages={259–261} }