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MetabolomicsOrganic and Peptidyl Constituents of Snake Venoms: The Picture Is Vastly More Complex Than We Imagined
Small metabolites and peptides in 17 snake venoms (Elapidae, Viperinae, and Crotalinae), were quantified using liquid chromatography-mass spectrometry. Each venom contains >900 metabolites and peptides. Many small organic compounds are present at levels that are probably significant in prey envenoma...
2023-01-11 | MTBLS755 | MetaboLights
ProteomicsSystemic toxicity of snake venom metalloproteinases: proteomics analyses of kidney injury and blood plasma disturbances in a mouse model
Metalloproteinases are abundant in viperid venoms and are implicated in several envenomation effects. Bothrops jararaca venom is reported to induce kidney injury and coagulopathy. HF3 is an extremely hemorrhagic metalloproteinase from B. jararaca venom and participates in the local pathogenesis of e...
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2023-01-20 | MSV000091101 | MassIVE
ProteomicsLachesis muta snake venom peptidome
Snake venoms are known to be major sources of peptides with different pharmacological properties. In this study, we comprehensively explored the venom peptidomes of three specimens of Lachesis muta, the largest venomous snake in South America, using mass spectrometry techniques. The analysis reveale...
ORGANISM(S): Lachesis muta 
2023-10-23 | PXD045732 | Pride
Peptidomics Bradykinin potentiating peptides Mass spectrometry Lachesis muta Snake venom Snake venom metalloproteinases 
ProteomicsVipera ammodytes ammodytes venom proteomics
The nose-horned viper, its nominotypical subspecies Vipera ammodytes ammodytes (Vaa) in particular is, medically, the most relevant snake in Europe. The local and systemic clinical manifestations of poisoning by the venom of this snake are the result of the pathophysiological effects inflicted by en...
ORGANISM(S): Vipera ammodytes ammodytes 
2019-05-06 | PXD012752 | Pride
2-de Vipera ammodytes ammodytes Snake venom Lc-ms/ms 
ProteomicsA systemic view of active site specificity profiling of the snake venom metalloprotease HF3 using Proteomic Identification of Cleavage Sites and N-terminomics TAILS
Snake venom metalloproteinases play important roles in the pathological effects of Viperidae venoms including severe local tissue damage, hemorrhage and coagulopathy. Hemorrhagic Factor 3 (HF3), a metalloproteinase isolated from Bothrops jararaca venom, induces severe local hemorrhage. Previous prot...
ORGANISM(S): Mus musculus (Mouse) 
2019-07-29 | PXD009201 | Pride
N-terminome Snake venom metalloprotease Snake venom Hf3 Tails Degradomics 
UnknownVenom-related transcripts from Bothrops jararaca tissues provide novel molecular insights into the production and evolution of snake venom.
Not available
S-EPMC4327157 | biostudies-literature
ProteomicsEarly response of C2C12 myotubes to a sub-cytotoxic dose of hemorrhagic metalloproteinase HF3 from Bothrops jararaca venom
Manifestations of local tissue damage, such as hemorrhage and myonecrosis, are among the most dramatic effects of envenomation by viperid snakes. Snake venom metalloproteinases (SVMPs) of the P-III class are main players of the hemorrhagic effect due to their activities in promoting blood vessel dis...
ORGANISM(S): Mus musculus (Mouse) 
2019-02-25 | PXD011274 | Pride
C2c12 myotubes  hf3  snake venom metalloproteinase  peptidomics  proteomics 
UnknownSnakebite drug discovery: high-throughput screening to identify novel snake venom metalloproteinase toxin inhibitors.
Not available
S-EPMC10808794 | biostudies-literature
UnknownIdentification of new snake venom metalloproteinase inhibitors using compound screening and rational Peptide design.
Not available
S-EPMC4025828 | biostudies-literature
UnknownP-I snake venom metalloproteinase is able to activate the complement system by direct cleavage of central components of the cascade.
Not available
S-EPMC3814341 | biostudies-literature
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