• Publications
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Antimicrobial peptides from ranid frogs: taxonomic and phylogenetic markers and a potential source of new therapeutic agents.
The broad-spectrum antibacterial and antifungal activities of certain peptides, for example esculentin-1, ranalexin-1 and ranatuerin, together with their relatively low hemolytic activity, make them candidates for development into therapeutically useful anti-infective agents. Expand
Activity of antimicrobial skin peptides from ranid frogs against Batrachochytrium dendrobatidis, the chytrid fungus associated with global amphibian declines.
It is shown that 10 peptides representing eight families of peptides derived from North American ranid frogs can effectively inhibit growth of this chytrid fungus, suggesting that the ranidfrogs have, within their repertoire of antimicrobial substances, a number of skin peptides that should be a deterrent to chyTrid infection. Expand
Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris.
The skin secretions of the North American pickerel frog Rana palustris are toxic to both microorganisms and predators. A total of 22 peptides with differential growth-inhibitory activity towardsExpand
Reflections on a systematic nomenclature for antimicrobial peptides from the skins of frogs of the family Ranidae
  • J. Conlon
  • Medicine, Biology
  • Peptides
  • 1 October 2008
Frogs belonging to the extensive family Ranidae represent a valuable source of antimicrobial peptides with therapeutic potential but there is currently no consistent system of nomenclature toExpand
The contribution of skin antimicrobial peptides to the system of innate immunity in anurans
  • J. Conlon
  • Biology, Medicine
  • Cell and Tissue Research
  • 2010
The low potency of many frog skin antimicrobial peptides is consistent with the hypothesis that cutaneous symbiotic bacteria may provide the major system of defense against pathogenic microorganisms in the environment with antimicrobial Peptide assuming a supplementary role in some species. Expand
Antimicrobial peptide defenses of the Tarahumara frog, Rana tarahumarae.
Data clearly show that antimicrobial peptides in the skin secretions of the Tarahumara frog are active against B. dendrobatidis and should provide some protection against infection, causing the observed susceptibility of these frogs to this pathogen in the wild. Expand
Cloning of the cDNA encoding the urotensin II precursor in frog and human reveals intense expression of the urotensin II gene in motoneurons of the spinal cord.
The present study demonstrates that UII, which has long been regarded as a peptide exclusively produced by the urophysis of teleost fish, is actually present in the brain of amphibians and mammals. Expand
Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens.
Despite the close phylogenetic relationship between the various species of Ranid frogs, the distribution and amino-acid sequences of the antimicrobial peptides produced by each species are highly variable and species-specific, suggesting that they may be valuable in taxonomic classification and molecular phylogenetic analysis. Expand
Somatostatin- and urotensin II-related peptides: molecular diversity and evolutionary perspectives
It is speculated that at least two somatostatin genes are expressed in all classes of vertebrates but these genes have evolved at very different rates. Expand
Receptors for glucagon-like peptide-1(7-36) amide on rat insulinoma-derived cells.
Binding of the peptide resulted in a dose-dependent increase in cyclic AMP concentrations and binding sites for GLP-1 (7-36)amide were not present on dispersed enterocytes from porcine small intestine. Expand