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Bruce S. Seal

Researcher at Oregon State University

Publications -  127
Citations -  6156

Bruce S. Seal is an academic researcher from Oregon State University. The author has contributed to research in topics: Virus & Newcastle disease. The author has an hindex of 43, co-authored 126 publications receiving 5664 citations. Previous affiliations of Bruce S. Seal include Agricultural Research Service & United States Department of Agriculture.

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Development of a Real-Time Reverse-Transcription PCR for Detection of Newcastle Disease Virus RNA in Clinical Samples

TL;DR: A positive correlation was obtained between the RRT-PCR results and virus isolation for NDV from clinical samples, and a real-time reverse-transcription PCR test was developed to detect avian paramyxovirus 1 (APMV-1) RNA in clinical samples from birds.
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Isolation of a Lactobacillus salivarius Strain and Purification of Its Bacteriocin, Which Is Inhibitory to Campylobacter jejuni in the Chicken Gastrointestinal System

TL;DR: Bacteriocin from L. salivarius NRRL B-30514 appears potentially very useful to reduce C. jejuni in poultry prior to processing, and had sequence similarity, even in the C-terminal region, to acidocin A, which was previously identified fromL.
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Characterization of Newcastle disease virus isolates by reverse transcription PCR coupled to direct nucleotide sequencing and development of sequence database for pathotype prediction and molecular epidemiological analysis.

TL;DR: Differences in the fusion protein cleavage sequence that correlated genotypically with virulence among various NDV pathotypes were detected and lentogenic viruses were grouped phylogenetically separate from other pathotypes by using sequences generated from the matrix protein gene coding for the nuclear localization signal.
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Isolation and Purification of Enterocin E-760 with Broad Antimicrobial Activity against Gram-Positive and Gram-Negative Bacteria

TL;DR: The proteinaceous nature of purified enterocin E-760 was demonstrated upon treatment with various proteolytic enzymes, and the antimicrobial peptide was found to be sensitive to beta-chymotrypsin, proteinase K, and papain, while it was resistant to lysozyme and lipase.