ArticleFrontiers in pharmacology2019
From Synthetic Fragments of Endogenous Three-Finger Proteins to Potential Drugs.
Article in Frontiers in pharmacology, 2019. 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.
- Scalable production of recombinant three-finger proteins: from inclusion bodies to high quality molecular probes.Microbial cell factories · 2024Article
- Comparison of Conformations and Interactions with Nicotinic Acetylcholine Receptors forInternational journal of molecular sciences · 2023Article
- Genomic, transcriptomic, and epigenomic analysis of a medicinal snake,Acta pharmaceutica Sinica. B · 2023Article
- α7- and α9-Containing Nicotinic Acetylcholine Receptors in the Functioning of Immune System and in Pain.International journal of molecular sciences · 2023Review
- Inhibition of nicotinic acetylcholine receptors by oligoarginine peptides and polyamine-related compounds.Frontiers in pharmacology · 2023Article
- Article
- Biophysical characterization of lynx-nicotinic receptor interactions using atomic force microscopy.FASEB bioAdvances · 2021Article
- α9-Containing Nicotinic Receptors in Cancer.Frontiers in cellular neuroscience · 2021Review
- Spatial Structure and Activity of Synthetic Fragments of Lynx1 and of Nicotinic Receptor Loop C Models.Biomolecules · 2020Article
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The proteins of the Ly6 family have a three-finger folding as snake venom α-neurotoxins, targeting nicotinic acetylcholine receptors (nAChRs), and some of them, like mammalian secreted Ly6/uPAR protein (SLURP1) and membrane-attached Ly-6/neurotoxin (Lynx1), also interact with distinct nAChR subtypes. We believed that synthetic fragments of these endogenous proteins might open new ways for drug design because nAChRs are well-known targets for developing analgesics and drugs against neurodegenerative diseases. Since interaction with nAChRs was earlier shown for synthetic fragments of the α-neurotoxin central loop II, we synthesized a 15-membered fragment of human Lynx1, its form with two Cys residues added at the N- and C-termini and forming a disulfide, as well as similar forms of human SLURP1, SLURP2, and of
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