![Unraveling snake venom phospholipase A2: an overview of its structure, pharmacology, and inhibitors | Pharmacological Reports Unraveling snake venom phospholipase A2: an overview of its structure, pharmacology, and inhibitors | Pharmacological Reports](https://media.springernature.com/m685/springer-static/image/art%3A10.1007%2Fs43440-023-00543-8/MediaObjects/43440_2023_543_Fig4_HTML.png)
Unraveling snake venom phospholipase A2: an overview of its structure, pharmacology, and inhibitors | Pharmacological Reports
![PDF] Active site of bee venom phospholipase A2: the role of histidine-34, aspartate-64 and tyrosine-87. | Semantic Scholar PDF] Active site of bee venom phospholipase A2: the role of histidine-34, aspartate-64 and tyrosine-87. | Semantic Scholar](https://d3i71xaburhd42.cloudfront.net/7ef426ee07eea4da0943d1d40aa551a47f8ba04d/2-Figure1-1.png)
PDF] Active site of bee venom phospholipase A2: the role of histidine-34, aspartate-64 and tyrosine-87. | Semantic Scholar
![Isolation of two basic phospholipases A2 from Bothrops diporus snake venom: Comparative characterization and synergism between Asp49 and Lys49 variants - ScienceDirect Isolation of two basic phospholipases A2 from Bothrops diporus snake venom: Comparative characterization and synergism between Asp49 and Lys49 variants - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S0041010119304076-fx1.jpg)
Isolation of two basic phospholipases A2 from Bothrops diporus snake venom: Comparative characterization and synergism between Asp49 and Lys49 variants - ScienceDirect
![Unraveling snake venom phospholipase A2: an overview of its structure, pharmacology, and inhibitors | Pharmacological Reports Unraveling snake venom phospholipase A2: an overview of its structure, pharmacology, and inhibitors | Pharmacological Reports](https://media.springernature.com/m685/springer-static/image/art%3A10.1007%2Fs43440-023-00543-8/MediaObjects/43440_2023_543_Fig2_HTML.png)
Unraveling snake venom phospholipase A2: an overview of its structure, pharmacology, and inhibitors | Pharmacological Reports
![Exploring and understanding the functional role, and biochemical and structural characteristics of an acidic phospholipase A2, AplTx-I, purified from Agkistrodon piscivorus leucostoma snake venom - ScienceDirect Exploring and understanding the functional role, and biochemical and structural characteristics of an acidic phospholipase A2, AplTx-I, purified from Agkistrodon piscivorus leucostoma snake venom - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S004101011730003X-fx1.jpg)
Exploring and understanding the functional role, and biochemical and structural characteristics of an acidic phospholipase A2, AplTx-I, purified from Agkistrodon piscivorus leucostoma snake venom - ScienceDirect
![Chemists discovered a new mechanism of action of a Vipera nikolskii venom neurotoxin - Press-room - IBCh RAS Chemists discovered a new mechanism of action of a Vipera nikolskii venom neurotoxin - Press-room - IBCh RAS](https://www.ibch.ru/downloads/press/2092/Chemists_has_understood_how_the_viper_venom_works.jpg)
Chemists discovered a new mechanism of action of a Vipera nikolskii venom neurotoxin - Press-room - IBCh RAS
![RCSB PDB - 1POC: CRYSTAL STRUCTURE OF BEE-VENOM PHOSPHOLIPASE A2 IN A COMPLEX WITH A TRANSITION-STATE ANALOGUE RCSB PDB - 1POC: CRYSTAL STRUCTURE OF BEE-VENOM PHOSPHOLIPASE A2 IN A COMPLEX WITH A TRANSITION-STATE ANALOGUE](https://cdn.rcsb.org/images/structures/1poc_assembly-1.jpeg)
RCSB PDB - 1POC: CRYSTAL STRUCTURE OF BEE-VENOM PHOSPHOLIPASE A2 IN A COMPLEX WITH A TRANSITION-STATE ANALOGUE
![Catalytically Active Snake Venom PLA2 Enzymes: An Overview of Its Elusive Mechanisms of Reaction | Journal of Medicinal Chemistry Catalytically Active Snake Venom PLA2 Enzymes: An Overview of Its Elusive Mechanisms of Reaction | Journal of Medicinal Chemistry](https://pubs.acs.org/cms/10.1021/acs.jmedchem.3c00097/asset/images/large/jm3c00097_0009.jpeg)
Catalytically Active Snake Venom PLA2 Enzymes: An Overview of Its Elusive Mechanisms of Reaction | Journal of Medicinal Chemistry
Catalytically Active Snake Venom PLA2 Enzymes: An Overview of Its Elusive Mechanisms of Reaction | Journal of Medicinal Chemistry
In Vivo Neutralization of Myotoxin II, a Phospholipase A2 Homologue from Bothrops asper Venom, Using Peptides Discovered via Phage Display Technology | ACS Omega
![Panacea within a Pandora's box: the antiparasitic effects of phospholipases A2 (PLA2s) from snake venoms: Trends in Parasitology Panacea within a Pandora's box: the antiparasitic effects of phospholipases A2 (PLA2s) from snake venoms: Trends in Parasitology](https://www.cell.com/cms/attachment/9725d2e5-b872-4be0-9e7a-3cf10535b096/gr2_lrg.jpg)
Panacea within a Pandora's box: the antiparasitic effects of phospholipases A2 (PLA2s) from snake venoms: Trends in Parasitology
![Phospholipases A2 from viperidae snake venoms: how do they induce skeletal muscle damage? | Semantic Scholar Phospholipases A2 from viperidae snake venoms: how do they induce skeletal muscle damage? | Semantic Scholar](https://d3i71xaburhd42.cloudfront.net/5b1e47f9c28b2aead109f9026bf4b676fdd90075/6-Figure3-1.png)
Phospholipases A2 from viperidae snake venoms: how do they induce skeletal muscle damage? | Semantic Scholar
![Phospholipase A2 enzyme from the venom of Egyptian honey bee Apis mellifera lamarckii with anti-platelet aggregation and anti-coagulation activities | Journal of Genetic Engineering and Biotechnology | Full Text Phospholipase A2 enzyme from the venom of Egyptian honey bee Apis mellifera lamarckii with anti-platelet aggregation and anti-coagulation activities | Journal of Genetic Engineering and Biotechnology | Full Text](https://media.springernature.com/m685/springer-static/image/art%3A10.1186%2Fs43141-020-00112-z/MediaObjects/43141_2020_112_Fig1_HTML.png)
Phospholipase A2 enzyme from the venom of Egyptian honey bee Apis mellifera lamarckii with anti-platelet aggregation and anti-coagulation activities | Journal of Genetic Engineering and Biotechnology | Full Text
![Crystal Structure of a Complex Formed between a Snake Venom Phospholipase A2 and a Potent Peptide Inhibitor Phe-Leu-Ser-Tyr-Lys at 1.8 Å Resolution - ScienceDirect Crystal Structure of a Complex Formed between a Snake Venom Phospholipase A2 and a Potent Peptide Inhibitor Phe-Leu-Ser-Tyr-Lys at 1.8 Å Resolution - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S0021925819722236-gr1.jpg)