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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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Peptidomic analysis of skin secretions from Rana heckscheri and Rana okaloosae provides insight into phylogenetic relationships among frogs of the Aquarana species group.

TL;DR: Cl cladistic analysis based upon a comparison of the amino acid sequences of antimicrobial peptides indicates a sister-group relationship between R. heckscheri and R. grylio and a close, but less well defined, phylogenetic relationship with R. okaloosae.
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Clinical Applications of Amphibian Antimicrobial Peptides

TL;DR: Treatment and prevention of acne and periodontal disease are identified as areas in which frog skin antimicrobial peptides might find future applications.
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Isolation of the opioid peptide Leu-Val-Val-hemorphin-7 from bronchoalveolar lavage fluid of a patient with non-small cell lung cancer.

TL;DR: The ability of LVV-hemorphin-7 to inhibit angiotensin-converting enzyme suggests that its formation may be of pathophysiological significance in the regulation of tumor blood flow in certain patients.
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Identification and localization of neurohypophysial peptides in the brain of a caecilian amphibian, Typhlonectes natans (Amphibia: Gymnophiona).

TL;DR: This caecilian species, therefore, possesses neurohypophysial peptides that are similar in their structure and distribution to the peptides found in anuran and urodele amphibian orders.
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Host-defense peptides from skin secretions of the tetraploid frogs Xenopus petersii and Xenopus pygmaeus, and the octoploid frog Xenopus lenduensis (Pipidae)

TL;DR: Peptidomic analysis of norepinephrine-stimulated skin secretions led to the identification of host-defense peptides belonging to the magainin, peptide glycine-leucine-amide (PGLa), and caerulein precursor fragment (CPF) families from the tetraploid frogs, Xenopus petersii and Xenopus pygmaeus (Bouchia clawed frog), and the octoploid frog Xenopus lenduensis.