ArticleActa naturae2014
Cobra cytotoxins: structural organization and antibacterial activity.
Article in Acta naturae, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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Who cites it
13 citing papers in PubMed.
- Profiling cytotoxicity of nanofractionated elapid snake venoms in human cell lines representing different tissues.Journal of pharmaceutical analysis · 2026Article
- Targeting cobra venom cytotoxin: a linear 40-mer ssDNA aptamer-based antivenom confers neutralisation potentials against cobra venom-induced cytotoxicity.Archives of toxicology · 2026Article
- Review
- Unveiling the functional epitopes of cobra venom cytotoxin by immunoinformatics and epitope-omic analyses.Scientific reports · 2023Article
- Membrane-Disrupting Activity of Cobra Cytotoxins Is Determined by Configuration of the N-Terminal Loop.Toxins · 2022Article
- Article
- Article
- An Appraisal of Antidotes' Effectiveness: Evidence of the Use of Phyto-Antidotes and Biotechnological Advancements.Molecules (Basel, Switzerland) · 2020Review
- Mechanisms underpinning the permanent muscle damage induced by snake venom metalloprotease.PLoS neglected tropical diseases · 2019Article
- Review
- Engineered nanoparticles bind elapid snake venom toxins and inhibit venom-induced dermonecrosis.PLoS neglected tropical diseases · 2018Article
- Article
- Latarcins: versatile spider venom peptides.Cellular and molecular life sciences : CMLS · 2015Review
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cardiotoxins (cytotoxins, CT) are β-structured proteins isolated from the venom of cobra. They consist of 59-61 amino acid residues, whose antiparallel chains form three 'fingers'. In contrast to neurotoxins with an overall similar fold, CTs are amphiphilic. The amphiphilicity is caused by positively charged lysine and arginine residues flanking the tips of the loops that consist primarily of hydrophobic amino acids. A similar distribution of amino acid residues is typical for linear (without disulfide bonds) cationic cytolytic peptides from the venoms of other snakes and insects. Many of them are now considered to be lead compounds in combatting bacterial infections and cancer. In the present review, we summarize the data on the antibacterial activity of CTs and compare it to the activity of linear peptides.
Indexed as
Identifiers
25349711PMC4207557What 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.