Hydralysins, a new category of β-pore-forming toxins in cnidaria

Keyphrases

• Cnidaria 100%
• Sequence Motif 100%
• Pore-forming Toxins 100%
• Pore-forming 100%
• Paralytic Activity 100%
• Stinging 50%
• Cnidarian 50%
• Receptor-mediated 50%
• Molecular Mechanism 50%
• Multiple Sequence Alignment 50%
• Functional Characterization 50%
• Diverse Groups 50%
• Mutagenesis 50%
• Carbohydrates 50%
• Computational Analysis 50%
• Pore Formation 50%
• Nematocytes 50%
• Phospholipids 50%
• Hemolytic Activity 50%
• Actinoporin 50%
• Green Hydra 50%
• Venomous Animals 50%
• Specific Receptor 50%
• Peptide Toxin 50%
• Protein Toxin 50%
• Pore-forming Protein 50%
• Cytolytic 50%
• Aerolysin 50%
• Cytolytic Toxin 50%
• Far-UV Circular Dichroism 50%
• Cytolytic Activity 50%
• Circular Dichroism Spectroscopy 50%
• Conserved Sequence 50%
• Fungal Toxins 50%
• Paralytic Toxins 50%
• Bacterial Toxins 50%
• Cloning Expression 50%
• Erythrocyte Membrane 50%
• Wide Distribution 50%
• Pore Former 50%

Biochemistry, Genetics and Molecular Biology

• Cnidaria 100%
• Sequence Motif 100%
• Pore-Forming Toxin 100%
• Prey 33%
• Isoform 33%
• Sequence Alignment 33%
• Mutagenesis 33%
• Channel Gating 33%
• Poisonous Animal 33%
• Aerolysin 33%
• Pore Forming Protein 33%
• Erythrocyte Membrane 33%
• Erythrocyte Shape 33%
• Conserved Sequence 33%
• Circular Dichroism 33%
• Phospholipid 33%

Pharmacology, Toxicology and Pharmaceutical Science

• Cnidaria 100%
• Pore-Forming Toxin 100%
• Receptor 66%
• Mutagenesis 33%
• Prey 33%
• Polypeptide 33%
• Poisonous Animal 33%
• Monomer 33%
• Phospholipid 33%
• Aerolysin 33%
• Bacterial Toxin 33%
• Mycotoxin 33%