ArticleBMC evolutionary biology2008
Accelerated exchange of exon segments in Viperid three-finger toxin genes (Sistrurus catenatus edwardsii; Desert Massasauga).
Article in BMC evolutionary biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.
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Who cites it
19 citing papers in PubMed, 1 synthesis or guideline pooled it, 52 citations in OpenAlex.
- Pooled it
- Orphan Three-Finger Toxins from Snake Venoms: Unexplored Library of Novel Biological Ligands with Potential New Structures and Functions.International journal of molecular sciences · 2025Review
- Variations in "Functional Site" Residues and Classification of Three-Finger Neurotoxins in Snake Venoms.Toxins · 2025Review
- From birth to bite: the evolutionary ecology of India's medically most important snake venoms.BMC biology · 2024Article
- A Review of Rattlesnake Venoms.Toxins · 2023Review
- Genomic, transcriptomic, and epigenomic analysis of a medicinal snake,Acta pharmaceutica Sinica. B · 2023Article
- What Are the Neurotoxins in Hemotoxic Snake Venoms?International journal of molecular sciences · 2023Review
- Old World Vipers-A Review about Snake Venom Proteomics of Viperinae and Their Variations.Toxins · 2021Review
- Toxinology provides multidirectional and multidimensional opportunities: A personal perspective.Toxicon: X · 2020Article
- Toxin transcripts inJournal of venom research · 2020Article
- A Review and Database of Snake Venom Proteomes.Toxins · 2017Review
- Evaluation of cytotoxic activities of snake venoms toward breast (MCF-7) and skin cancer (A-375) cell lines.Cytotechnology · 2016Article
- Full-Length Venom Protein cDNA Sequences from Venom-Derived mRNA: Exploring Compositional Variation and Adaptive Multigene Evolution.PLoS neglected tropical diseases · 2016Article
- Three-fingered RAVERs: Rapid Accumulation of Variations in Exposed Residues of snake venom toxins.Toxins · 2013Article
- Engineering of three-finger fold toxins creates ligands with original pharmacological profiles for muscarinic and adrenergic receptors.PloS one · 2012Article
- Evolutionary analysis of novel serine proteases in the venom gland transcriptome of Bitis gabonica rhinoceros.PloS one · 2011Article
- Transcriptomic analysis of the venom gland of the red-headed krait (Bungarus flaviceps) using expressed sequence tags.BMC molecular biology · 2010Article
- Evolution of Conus peptide genes: duplication and positive selection in the A-superfamily.Journal of molecular evolution · 2010Article
- Role of accelerated segment switch in exons to alter targeting (ASSET) in the molecular evolution of snake venom proteins.BMC evolutionary biology · 2009Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundSnake venoms consist primarily of proteins and peptides showing a myriad of potent biological activities which have been shaped by both adaptive and neutral selective forces. Venom proteins are encoded by multigene families that have evolved through a process of gene duplication followed by accelerated evolution in the protein coding region.
resultsHere we report five gene structures of three-finger toxins from a viperid snake, Sistrurus catenatus edwardsii. These toxin genes are structured similarly to elapid and hydrophiid three-finger toxin genes, with two introns and three exons. Both introns and exons show distinct patterns of segmentation, and the insertion/deletion of segments may define their evolutionary history. The segments in introns, when present, are highly similar to their corresponding segments in other members of the gene family. In contrast, some segments in the exons show high similarity, while others are often distinctly different among corresponding regions of the isoforms.
conclusionOrdered, conserved exon structure strongly suggests that segments in corresponding regions in exons have been exchanged with distinctly different ones during the evolution of these genes. Such a "switching" of segments in exons may result in drastically altering the molecular surface topology and charge, and hence the molecular targets of these three-finger toxins. Thus the phenomenon of accelerated segment switch in exons to alter targeting (ASSET) may play an important role in the evolution of three-finger toxins, resulting in a family of toxins with a highly conserved structural fold but widely varying biological activities.
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