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Discovery of six families of fungal defensin-like peptides provides insights into origin and evolution of the CSαβ defensins
Computational identification of six families of fungal DLPs in which three known defensin types (antibacterial ancient invertebrate-type defensins (AITDs), antibacterial classical insect-type DEFs, and antifungal plant/insect- types (PITDs) can be clearly assigned helps establish a paralogous relationship between AITDs and CITDs. Expand
The defensin gene family expansion in the tick Ixodes scapularis.
Computational identification of two multigene families of defensin-like peptides (DLPs) in the Ixodid ticks genome, one corresponding to scapularisin and the other named scasin, finding of extensive gene expansion of DLPs in a vector arachnida may be valuable in the understanding of its role in pathogen transmission. Expand
Four Novel Tarantula Toxins as Selective Modulators of Voltage-Gated Sodium Channel Subtypes
Molecular modeling indicates that subtle differences in toxin surfaces may relate to their different pharmacological profiles, and an evolutionary trace analysis of these toxins and other structurally related three-disulfide spider toxins provides clues for the exploration of toxin-channel interaction and future structure-function research. Expand
Structural and functional characterization of two genetically related meucin peptides highlights evolutionary divergence and convergence in antimicrobial peptides
Structural and functional characterization of two genetically related meucin peptides highlights evolutionary divergence and convergence in antimicrobial peptides and provides new insights into an evolutionary link among AMPs from invertebrates and vertebrates and clues for evolutionary convergence between AMPs and virus fusion domains. Expand
Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold
Comparisons in precursor organization, exon–intron structure, 3D-fold and function suggest that scorpion venom ICK-type K+ channel inhibitors and Ca2+ release channel activators share a common ancestor and their divergence occurs after speciation between buthidae and non-buthids. Expand
Dermatophytic defensin with antiinfective potential
17 new fungal defensin-like peptide (fDLP) genes are reported and the detailed characterization of a corresponding synthetic fDLP (micasin) from a dermatophyte in terms of its structure, activity and therapeutic potential are described. Expand
Did cathelicidins, a family of multifunctional host-defense peptides, arise from a cysteine protease inhibitor?
  • Shunyi Zhu
  • Biology, Medicine
  • Trends in microbiology
  • 1 August 2008
A gradual evolution model is proposed to explain how the AMD evolved from the ancestral cystatin scaffold, and conserved gene structure and related function provide new evidence in favor of a common ancestral origin for cystatins and CLDs. Expand
Nrf2/Maf-binding-site-containing functional Cyp6a2 allele is associated with DDT resistance in Drosophila melanogaster.
The results suggest that the Nrf2/Maf binding-site-containing functional Cyp6a2 allele is associated with DDT resistance in the D. melanogaster strains under study. Expand
Activation of cathepsin L by the cathelin-like domain of protegrin-3.
The results provide new insights into deeper understanding of the immune-related biological activity of this so-called pro-domain of the cathelicidin family. Expand
Mesomartoxin, a new K(v)1.2-selective scorpion toxin interacting with the channel selectivity filter.
Electrophysiological experiments showed that MMTX exhibits high affinity for the Drosophila Shaker K(+) channel but differential selectivity on different members of the rat voltage-gated K()+ channel (Kv) family, and site-directed mutagenesis of the channel pore identified a key site located on the selectivity filter of the pore, which is directly implicated in toxin binding and controls target's selectivity of the toxin. Expand