ArticleFrontiers in pharmacology2018
Secreted Cysteine-Rich Repeat Proteins "SCREPs": A Novel Multi-Domain Architecture.
Article in Frontiers in pharmacology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Conkazal-M1 from the MKAVA family of conotoxins: A dual-function protease inhibitor and neuroactive peptide.Protein science : a publication of the Protein Society · 2026Article
- Ancient origin and dynamic evolution of bivalent spider toxins.Molecular biology and evolution · 2026Article
- Conkazal-M1 from the MKAVA family of conotoxins - a dual-function protease inhibitor and neuroactive peptide.bioRxiv : the preprint server for biology · 2025Article
- Signal peptides restrict genome evolution and A-to-I RNA editing.NAR genomics and bioinformatics · 2025Article
- The proteotranscriptomic characterization of venom in the white seafanOpen biology · 2025Article
- Structural Basis of the Bivalency of the TRPV1 Agonist DkTx.Angewandte Chemie (International ed. in English) · 2024Article
- A bivalent remipede toxin promotes calcium release via ryanodine receptor activation.Nature communications · 2023Article
- ScrepYard: An online resource for disulfide-stabilized tandem repeat peptides.Protein science : a publication of the Protein Society · 2023Article
- Emerging Computational Approaches for Antimicrobial Peptide Discovery.Antibiotics (Basel, Switzerland) · 2022Review
- Chemical synthesis ofRSC chemical biology · 2022Article
- Venom Peptide Toxins Targeting the Outer Pore Region of Transient Receptor Potential Vanilloid 1 in Pain: Implications for Analgesic Drug Development.International journal of molecular sciences · 2022Review
- Evaluation of Efficient Non-reducing Enzymatic and Chemical Ligation Strategies for Complex Disulfide-Rich Peptides.Bioconjugate chemistry · 2021Article
- Enzymatic Ligation of Disulfide-Rich Animal Venom Peptides: Using Sortase A to Form Double-Knotted Peptides.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Structure, function, and evolution ofProceedings of the National Academy of Sciences of the United States of America · 2020Article
- From quantum-derived principles underlying cysteine reactivity to combating the COVID-19 pandemic.Wiley interdisciplinary reviews. Computational molecular scienceArticle
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peptide toxins isolated from animal venom secretions have proven to be useful pharmacological tools for probing the structure and function of a number of molecular receptors. Their molecular structures are stabilized by posttranslational formation of multiple disulfide bonds formed between sidechain thiols of cysteine residues, resulting in high thermal and chemical stability. Many of these peptides have been found to be potent modulators of ion channels, making them particularly influential in this field. Recently, several peptide toxins have been described that have an unusual tandem repeat organization, while also eliciting a unique pharmacological response toward ion channels. Most of these are two-domain peptide toxins from spider venoms, such as the double-knot toxin (DkTx), isolated from the Earth Tiger tarantula (
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