GALLERY

Selected Publications


Roelants, K., Fry, B.G., Norman, J.A.,  Clynen, E., Schoofs, L. & F. Bossuyt, 2010 - Identical Skin Toxins by Convergent Molecular Adaptation in Frogs. Current Biology 20: 125-130.


Fry, B.G., Roelants, K., Winter, K., Hodgson, W.C., Griesman, L., Kwok, H.F., Scanlon, D., Karas, J., Shaw, C., Wong, L. & J.A. Norman, 2009 - Novel venom proteins produced by differential domain-expression strategies in Beaded lizards and Gila monsters (genus Heloderma). Mol. Biol. Evol. 27: 395-407.


Fry, B.G., Roelants, K. & J.A. Norman, 2009 - Tentacles of venom: Toxic protein convergence in the Kingdom Animalia.  J. Mol. Evol. 68: 311-321.


Gibbs, G.M., Roelants, K. & M.K. O’Bryan, 2008 - The CAP superfamily: Cysteine-rich secretory proteins, antigen 5 and pathogenesis-related 1 proteins – roles in reproduction, cancer and immune defense. Endocrine Rev. 9: 865-897.


Roelants, K., Gower, D.J., Wilkinson, M., Loader, S.P., Biju, S.D., Guillaume, K., Moriau, L. & F. Bossuyt, 2007 - Global patterns of diversification in the history of modern amphibians. Proc. Natl. Acad. Sci., USA 104 (3): 887-892.


Roelants, K. & F. Bossuyt, 2005 - Archaeobatrachian paraphyly and pangaean diversification of crown-group frogs.

Systematic Biology 54 (1): 111-126.

Kim focused his PhD and early post-doctoral research on phylogenetic patterns of diversification in amphibians. He is now integrating this phylogenetic background with transcriptome and peptidome data to explore the evolution of antimicrobial and anti-predatory skin peptides in various amphibians. Apart from providing an excellent model system for the study of adaptive evolution at a molecular scale, defensive skin peptides represent promising templates for novel bioactive compounds in various therapeutic applications. Identifying novel classes of amphibian skin peptides represents a major aspect of the ERC program TAPAS (Tracing Antimicrobial peptides and Pheromones in the Amphibian Skin).

Kim Roelants

Postdoc

Research

Amphibian toxins and antimicrobial peptides