ArticleBMC evolutionary biology2009
Role of accelerated segment switch in exons to alter targeting (ASSET) in the molecular evolution of snake venom proteins.
Article in BMC evolutionary biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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22 citing papers in PubMed, 65 citations in OpenAlex.
- Venom Variation as a Window into the Ecology and Evolution of Snakes.Integrative and comparative biology · 2026Review
- 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
- Exploring the Diversity and Function of Serine Proteases in Toxicofera Reptile Venoms: A Comprehensive Overview.Toxins · 2024Review
- Domain loss enabled evolution of novel functions in the snake three-finger toxin gene superfamily.Nature communications · 2023Article
- Genomic, transcriptomic, and epigenomic analysis of a medicinal snake,Acta pharmaceutica Sinica. B · 2023Article
- Three-Finger Toxins from Brazilian Coral Snakes: From Molecular Framework to Insights in Biological Function.Toxins · 2021Article
- Toxinology provides multidirectional and multidimensional opportunities: A personal perspective.Toxicon: X · 2020Article
- Subproteome ofThe journal of venomous animals and toxins including tropical diseases · 2019Article
- Receptor variability-driven evolution of snake toxins.Zoological research · 2018Article
- Article
- Adaptive evolution of distinct prey-specific toxin genes in rear-fanged snake venom.Proceedings. Biological sciences · 2018Article
- Orphan Three-Finger Toxins Bind at Tissue Factor-Factor VIIa Interface to Inhibit Factor X Activation: Identification of Functional Site by Docking.TH open : companion journal to thrombosis and haemostasis · 2018Article
- A Review and Database of Snake Venom Proteomes.Toxins · 2017Review
- The Molecular Basis of Toxins' Interactions with Intracellular Signaling via Discrete Portals.Toxins · 2017Review
- Gene duplications are extensive and contribute significantly to the toxic proteome of nematocysts isolated from Acropora digitifera (Cnidaria: Anthozoa: Scleractinia).BMC genomics · 2015Article
- Three-fingered RAVERs: Rapid Accumulation of Variations in Exposed Residues of snake venom toxins.Toxins · 2013Article
- Molecular evolution of α-latrotoxin, the exceptionally potent vertebrate neurotoxin in black widow spider venom.Molecular biology and evolution · 2013Article
- Sequence and phylogenetic analysis of viper venom serine proteases.Bioinformation · 2012Article
- Engineering of three-finger fold toxins creates ligands with original pharmacological profiles for muscarinic and adrenergic receptors.PloS one · 2012Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundSnake venom toxins evolve more rapidly than other proteins through accelerated changes in the protein coding regions. Previously we have shown that accelerated segment switch in exons to alter targeting (ASSET) might play an important role in its functional evolution of viperid three-finger toxins. In this phenomenon, short sequences in exons are radically changed to unrelated sequences and hence affect the folding and functional properties of the toxins.
resultsHere we analyzed other snake venom protein families to elucidate the role of ASSET in their functional evolution. ASSET appears to be involved in the functional evolution of three-finger toxins to a greater extent than in several other venom protein families. ASSET leads to replacement of some of the critical amino acid residues that affect the biological function in three-finger toxins as well as change the conformation of the loop that is involved in binding to specific target sites.
conclusionASSET could lead to novel functions in snake venom proteins. Among snake venom serine proteases, ASSET contributes to changes in three surface segments. One of these segments near the substrate binding region is known to affect substrate specificity, and its exchange may have significant implications for differences in isoform catalytic activity on specific target protein substrates. ASSET therefore plays an important role in functional diversification of snake venom proteins, in addition to accelerated point mutations in the protein coding regions. Accelerated point mutations lead to fine-tuning of target specificity, whereas ASSET leads to large-scale replacement of multiple functionally important residues, resulting in change or gain of functions.
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