ArticleProceedings of the National Academy of Sciences of the United States of America2009
A designer ligand specific for Kv1.3 channels from a scorpion neurotoxin-based library.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
38 citing papers in PubMed, 70 citations in OpenAlex.
- A designer pore-blocking peptide reveals an electrostatic complementation mechanism for the inhibition-resistant Kv1.5 channel.Science advances · 2026Article
- Directed evolution of chlorotoxin enhances MMP-2 recognition and improves CAR-T-cell activity in glioblastoma modelsFrontiers in bioengineering and biotechnology · 2026Article
- Toward the rational design of oncogenic TASK-3 channel inhibitor peptides and nanoconjugate complexes.Frontiers in pharmacology · 2026Review
- C6 peptide blockade of Hv1 channels inhibits neutrophil migration into the lungs to suppress Pseudomonas aeruginosa-induced acute lung injury.Respiratory research · 2025Article
- Amyloid precursor protein and C99 are subunits in human microglial Hv1 channels that enhance current and inflammatory mediator release.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- New High-Affinity Peptide Ligands for Kv1.2 Channel: Selective Blockers and Fluorescent Probes.Cells · 2024Article
- Isoleucine gate blocks KeLife · 2024Article
- Kalium 3.0 is a comprehensive depository of natural, artificial, and labeled polypeptides acting on potassium channels.Protein science : a publication of the Protein Society · 2023Article
- Interactions of the Kv1.1 Channel with Peptide Pore Blockers: A Fluorescent Analysis on Mammalian Cells.Membranes · 2023Article
- Article
- Article
- Atto488-Agitoxin 2-A Fluorescent Ligand with Increased Selectivity for Kv1.3 Channel Binding Site.Bioengineering (Basel, Switzerland) · 2022Article
- Discovery of KMedicinal research reviews · 2021Review
- Peptide Toxins Targeting KV Channels.Handbook of experimental pharmacology · 2021Review
- Review on Biological Characteristics of Kv1.3 and Its Role in Liver Diseases.Frontiers in pharmacology · 2021Review
- N-Terminal Tagging with GFP Enhances Selectivity of Agitoxin 2 to Kv1.3-Channel Binding Site.Toxins · 2020Article
- Tuning Scorpion Toxin Selectivity: Switching From KFrontiers in pharmacology · 2020Article
- General lack of structural characterization of chemically synthesized long peptides.Protein science : a publication of the Protein Society · 2019Review
- Venom-Derived Peptide Modulators of Cation-Selective Channels: Friend, Foe or Frenemy.Frontiers in pharmacology · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors at 3 institutions in 2 countries.
Funding
Abstract
Venomous animals immobilize prey using protein toxins that act on ion channels and other targets of biological importance. Broad use of toxins for biomedical research, diagnosis, and therapy has been limited by inadequate target discrimination, for example, among ion channel subtypes. Here, a synthetic toxin is produced by a new strategy to be specific for human Kv1.3 channels, critical regulators of immune T cells. A phage display library of 11,200 de novo proteins is designed using the alpha-KTx scaffold of 31 scorpion toxin sequences known or predicted to bind to potassium channels. Mokatoxin-1 (moka1) is isolated by affinity selection on purified target. Moka1 blocks Kv1.3 at nanomolar levels that do not inhibit Kv1.1, Kv1.2, or KCa1.1. As a result, moka1 suppresses CD3/28-induced cytokine secretion by T cells without cross-reactive gastrointestinal hyperactivity. The 3D structure of moka1 rationalizes its specificity and validates the engineering approach, revealing a unique interaction surface supported on an alpha-KTx scaffold. This scaffold-based/target-biased strategy overcomes many obstacles to production of selective toxins.
Indexed as
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.