ArticlePharmaceuticals (Basel, Switzerland)2010
Imperatoxin A, a Cell-Penetrating Peptide from Scorpion Venom, as a Probe of Ca-Release Channels/Ryanodine Receptors.
Article in Pharmaceuticals (Basel, Switzerland), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
26 citing papers in PubMed, 53 citations in OpenAlex.
- Review
- Deciphering Scorpion Toxin-Induced Pain: Molecular Mechanisms and Ion Channel Dynamics.International journal of biological sciences · 2025Review
- Exploring the Chemical Features and Biomedical Relevance of Cell-Penetrating Peptides.International journal of molecular sciences · 2024Review
- The Significant Therapeutic Effects of Chinese Scorpion: Modern Scientific Exploration of Ion Channels.Pharmaceuticals (Basel, Switzerland) · 2024Review
- OpiCa1-PEG-PLGA nanomicelles antagonize acute heart failure induced by the cocktail of epinephrine and caffeine.Materials today. Bio · 2023Article
- Cryo-EM analysis of scorpion toxin binding to Ryanodine Receptors reveals subconductance that is abolished by PKA phosphorylation.Science advances · 2023Article
- Scorpion Peptides and Ion Channels: An Insightful Review of Mechanisms and Drug Development.Toxins · 2023Review
- The Sarcoplasmic Reticulum of Skeletal Muscle Cells: A Labyrinth of Membrane Contact Sites.Biomolecules · 2022Review
- Structural Insight Into Ryanodine Receptor Channelopathies.Frontiers in pharmacology · 2022Review
- Review
- Australian ScorpionBiomolecules · 2020Article
- Miniproteins as a Powerful Modality in Drug Development.Trends in biochemical sciences · 2020Review
- Venoms of Iranian Scorpions (Arachnida, Scorpiones) and Their Potential for Drug Discovery.Molecules (Basel, Switzerland) · 2019Review
- CPP-Ts: a new intracellular calcium channel modulator and a promising tool for drug delivery in cancer cells.Scientific reports · 2018Article
- Co-Localization of Crotamine with Internal Membranes and Accentuated Accumulation in Tumor Cells.Molecules (Basel, Switzerland) · 2018Article
- Mammalian display screening of diverse cystine-dense peptides for difficult to drug targets.Nature communications · 2017Article
- Toxin bioportides: exploring toxin biological activity and multifunctionality.Cellular and molecular life sciences : CMLS · 2017Review
- Article
- Approaching ryanodine receptor therapeutics from the calcin angle.The Journal of general physiology · 2016Article
- Structure-function relationships of peptides forming the calcin family of ryanodine receptor ligands.The Journal of general physiology · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Scorpion venoms are rich in ion channel-modifying peptides, which have proven to be invaluable probes of ion channel structure-function relationship. We previously isolated imperatoxin A (IpTxa), a 3.7 kDa peptide activator of Ca(2+)-release channels/ryanodine receptors (RyRs) [1,2,3] and founding member of the calcin family of scorpion peptides. IpTxa folds into a compact, mostly hydrophobic molecule with a cluster of positively-charged, basic residues polarized on one side of the molecule that possibly interacts with the phospholipids of cell membranes. To investigate whether IpTxa permeates external cellular membranes and targets RyRs in vivo, we perfused IpTxa on intact cardiomyocytes while recording field-stimulated intracellular Ca(2+) transients. To further investigate the cell-penetrating capabilities of the toxin, we prepared thiolated, fluorescent derivatives of IpTxa. Biological activity and spectroscopic properties indicate that these derivatives retain high affinity for RyRs and are only 5- to 10-fold less active than native IpTxa. Our results demonstrate that IpTxa is capable of crossing cell membranes to alter the release of Ca(2+)in vivo, and has the capacity to carry a large, membrane-impermeable cargo across the plasma membrane, a finding with exciting implications for novel drug delivery.
Identifiers
What OpenQuestion holds
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.