ArticleScientific reports2017
Ancestral protein resurrection and engineering opportunities of the mamba aminergic toxins.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Resurrecting Full-Length Ancestral Schizorhodopsins and Heliorhodopsins with Structure-Guided, Indel-Aware Sequence Reconstruction.ACS omega · 2026Article
- Article
- Proteomic Investigations of Two PakistaniToxins · 2020Article
- The Indian cobra reference genome and transcriptome enables comprehensive identification of venom toxins.Nature genetics · 2020Article
- Revenant: a database of resurrected proteins.Database : the journal of biological databases and curation · 2020Article
- Last decade update for three-finger toxins: Newly emerging structures and biological activities.World journal of biological chemistry · 2019Review
- Highly thermostable carboxylic acid reductases generated by ancestral sequence reconstruction.Communications biology · 2019Article
- From Synthetic Fragments of Endogenous Three-Finger Proteins to Potential Drugs.Frontiers in pharmacology · 2019Article
- Article
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Authors and funding
9 authors.
Funding
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Abstract
Mamba venoms contain a multiplicity of three-finger fold aminergic toxins known to interact with various α-adrenergic, muscarinic and dopaminergic receptors with different pharmacological profiles. In order to generate novel functions on this structural scaffold and to avoid the daunting task of producing and screening an overwhelming number of variants generated by a classical protein engineering strategy, we accepted the challenge of resurrecting ancestral proteins, likely to have possessed functional properties. This innovative approach that exploits molecular evolution models to efficiently guide protein engineering, has allowed us to generate a small library of six ancestral toxin (AncTx) variants and associate their pharmacological profiles to key functional substitutions. Among these variants, we identified AncTx1 as the most α
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