Coquet, L., Kolodziejek, J., Jouenne, T., Nowotny, N., King, J.D., and Conlon, J.M. 2016. Peptidomic analysis of the extensive array of host-defense peptides in skin secretions of the dodecaploid frog Xenopus ruwenzoriensis (Pipidae). Comp. Biochem. Physiol. D. 19:18-24. |
|
Conlon, J.M., Mechkarska, M., Lukic, M.L., and Flatt, P.R. 2014. Potential therapeutic applications of multifunctional host-defense peptides from frog skin as anti-cancer, antiviral, immunomodulatory, and anti-diabetic agents. Peptides. 57:67-77. |
|
King, J.D., Mechkarska, M., Meetani, M.A., and Conlon, J.M. 2013. Peptidomic analysis of skin secretions provides insight into the taxonomic status of the African clawed frogs Xenopus victorianus and Xenopus laevis sudanensis (Pipidae). Comp. Biochem. Physiol. D. 8:250-254. |
|
King, J.D., Mechkarska, M., Coquet, L., Leprince, J., Jouenne, T., Vaudry, H., Takada, K., and Conlon, J.M. 2012. Host-defense peptides from skin secretions of the tetraploid frogs Xenopus petersii and Xenopus pygmaeus, and the octoploid frog Xenopus lenduensis (Pipidae). Peptides. 33:35-43. |
|
Conlon, J.M., Mechkarska, M., Ahmed, E., Leprince, J., Vaudry, H., King, J.D., and Takada, K. 2011c. Purification and properties of antimicrobial peptides from skin secretions of the Eritrea clawed frog Xenopus clivii (Pipidae). Comp. Biochem. Physiol. C. 153:350-354. |
|
Mechkarska, M., Ahmed, E., Coquet, L., Leprince, J., Jouenne, T., Vaudry, H., King, J.D., and Conlon, J.M. 2011c. Peptidomic analysis of skin secretions demonstrates that the allopatric populations of Xenopus muelleri (Pipidae) are not conspecific. Peptides. 32:1502-1508. |
|
Mechkarska, M., Eman, A., Coquet, L., Jerome, L., Jouenne, T., Vaudry, H., King, J.D., Takada, K., and Conlon, J.M. 2011b. Genome duplications within the Xenopodinae do not increase the multiplicity of antimicrobial peptides in Silurana paratropicalis and Xenopus andrei skin secretions. Comp. Biochem. Physiol. D. 6:206-212. |
|
Hou, F., Li, J., Pan, P., Xu, J., Liu, L., Liu, W., Song, B., Li, N., Wan, J., and Gao, H. 2011. Isolation and characterisation of a new antimicrobial peptide from the skin of Xenopus laevis. Int. J. Antimicrob. Agents. 38:510. |
|
Zahid, O.K., Mechkarska, M., Ojo, O.O., Abdel-Wahab, Y.H., Flatt, P.R., Meetani, M.A., and Conlon, J.M. 2011. Caerulein-and xenopsin-related peptides with insulin-releasing activities from skin secretions of the clawed frogs, Xenopus borealis and Xenopus amieti (Pipidae). Gen. Comp. Endocrinol. 172:314-320 |
|
Conlon, J.M., Al-Ghaferi, N., Ahmed, E., Meetani, M.A., Leprince, J., and Nielsen, P.F. 2010b. Orthologs of magainin, PGLa, procaerulein-derived, and proxenopsin-derived peptides from skin secretions of the octoploid frog Xenopus amieti (Pipidae). Peptides. 31:989-994. |
|
Mechkarska, M., Ahmed, E., Coquet, L., Leprince, J., Jouenne, T., Vaudry, H., King, J.D., and Conlon, J.M. 2010. Antimicrobial peptides with therapeutic potential from skin secretions of the Marsabit clawed frog Xenopus borealis (Pipidae). Comp. Biochem. Physiol. C. 152:467-472. |
|
Roseghini, M., Erspamer, G.F., and Severini, C. 1988. Biogenic amines and active peptides in the skin of fifty-two African amphibian species other than bufonids. Comp. Biochem. Physiol. C. 91:281-228. |
|
Zasloff, M. 1987. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. USA. 84:5449-5453. |
|
Gibson, B.W., Poulter, L., Williams, D.H., and Maggio, J.E. 1986. Novel peptide fragments originating from PGLa and the caerulein and xenopsin precursors from Xenopus laevis. J. Biol. Chem. 261:5341-5349. |
|
Croce, G., and Bolognani, L. 1975. Lipid components in the skin secretions of amphibia. I. Cholesterol. Comp. Biochem. Physiol. B. 52:307-309. |
|
Anastasi, A., Bertaccini, G., Cei, J.M., De Caro, G., Erspamer, V., Impicciatore, M., and Roseghini, M. 1970. Presence of caerulein in extracts of the skin of Leptodactylus pentadactylus labyrinthicus and of Xenopus laevis. British J. Pharmacol. 38:221-228. |
|