Sort   by:  
 Page size 
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
ProteomicsVenom proteomic analysis of two medically important Nigerian viperidae (Echis ocellatus and Bitis arietans) snake species
Hydrophilic interaction liquid chromatography coupled with LC- MS/MS was used to analyze the crude venom extracts of Echis ocellatus (Carpet viper) and Bitis arietans (Puff adder). The gel-free proteomic analysis of the crude venom extracts from E. ocellatus and B. arietans yielded the identificatio...
ORGANISM(S): Echis ocellatus Bitis arietans 
2021-03-11 | PXD024638 | Pride
Bitis arietans Viperidae Echi ocellatus Snake venom Neglected tropical disease Snakebite Proteomic Mass spectrometry. 
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 
ProteomicsNaja annulifera Snake: New Insights into the Venom Components and Pathogenesis of Envenomation
Naja annulifera is a dangerous snake that belongs to the Elapidae family. It is found in some of the countries in Sub-Saharan Africa and has caused several accidents in humans and dogs. In this study, we characterized some of the biochemical, toxic and immunogenic properties of N. annulifera venom. ...
ORGANISM(S): Naja annulifera 
2019-02-25 | PXD010962 | Pride
Antivenom Inflammation Ibaq Naja annulifera snake venom Toxins Lc-ms/ms 
ProteomicsComparative analysis of high molecular mass subproteomes of Bothrops snake venoms
Snake venoms are extremely active biological secretions containing primarily various classes of enzymes. The genus Bothrops comprises various pit viper species that represent the most medically significant taxa in Central and South America, accounting for more human envenomations and fatalities than...
ORGANISM(S): Bothrops neuwiedi Bothrops moojeni Bothrops insularis Bothrops cotiara Bothrops jararacussu Bothrops leucurus Acyrthosiphon pisum (Pea aphid) Bothrops jararaca (Jararaca) (Bothrops jajaraca) Bothrops brazili 
2019-03-05 | PXD012088 | Pride
Snake venom Mass spectrometry Enzymes Proteome 
UnknownSnake Venom Metalloproteinases and Their Peptide Inhibitors from Myanmar Russell's Viper Venom.
Not available
S-EPMC5308247 | biostudies-literature
UnknownSnake Venom Metalloproteinases (SVMPs): A structure-function update.
Not available
S-EPMC7399193 | biostudies-literature
ProteomicsSystemic effects of hemorrhagic snake venom metalloproteinases: untargeted peptidomics to explore the pathodegradome of plasma proteins
In this study we investigated the proteolysis of human plasma proteins by HF3, an hemorrhagic metalloproteinase from B. jararaca venom. For this purpose, approaches for the depletion of the most abundant proteins and for the enrichment of low abundant proteins of human plasma were used to minimize t...
ORGANISM(S): Homo sapiens (Human) 
2022-02-17 | PXD027997 | Pride
Bothrops  snake venom  hemorrhagic factor 3 (hf3)  human plasma  degradome 
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 
Sort   by:  
 Page size