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J. Michael Conlon

Researcher at Ulster University

Publications -  363
Citations -  12143

J. Michael Conlon is an academic researcher from Ulster University. The author has contributed to research in topics: Peptide & Antimicrobial peptides. The author has an hindex of 51, co-authored 356 publications receiving 11461 citations. Previous affiliations of J. Michael Conlon include University of New South Wales & University of Rouen.

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Avoidance of strongly chaotropic eluents for immunoaffinity chromatography by chemical modification of immobilized ligand.

TL;DR: Treatment of immobilized antibodies with 2-hydroxy-5-nitrobenzyl bromide facilitates the elution of glucagon during immunoaffinity chromatography and the general implications of these results are discussed.
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Antimicrobial peptides of the brevinin-2 family isolated from gastric tissue of the frog, Rana esculenta

TL;DR: The data demonstrate that certain peptides of the brevinin-2 family, like the magainins in the toad, Xenopus laevis, may play an important role in protecting the gastrointestinal tract of Ranid frogs against microbial invasion.
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Activities of the frog skin peptide, ascaphin-8 and its lysine-substituted analogs against clinical isolates of extended-spectrum β-lactamase (ESBL) producing bacteria

TL;DR: The Lys4- and Lys8-substituted analogs were generally the most potent against bacteria but showed the highest hemolytic activity, while the Lys10, Lys14, and Lys18 analogs also displayed potent antibacterial activity while showing very low hemolytics activity.
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Purification, structural characterization, and myotropic activity of endothelin from trout, Oncorhynchus mykiss.

TL;DR: A single molecular form of trout ET with 21-amino acid residues was isolated in pure fo... as mentioned in this paper, which is the only known trace of ET from a nontetrapod species.
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An immunomodulatory peptide related to frenatin 2 from skin secretions of the Tyrrhenian painted frog Discoglossus sardus (Alytidae).

TL;DR: A peptidomic analysis of the secretions revealed the presence of an abundant peptide with structural similarity to frenatin 2, previously isolated from the Australian frog Litoria infrafrenata (Hylidae).