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ProteomicsSnake Venom Extracellular vesicles (SVEVs) reveal wide molecular and functional proteome diversity
This study aimed at characterizing the snake venom extracellular vesicles (SVEVs).Shotgun proteomics analysis of SVEVs was performed to identify the proteome content of these vesicles. TEM, DLS, biochemical activity and cellular assays were performed to characterize the morphology and functionality ...
ORGANISM(S): Crotalus viridis Crotalus atrox Agkistrodon Crotalus cerberus 
2022-03-07 | PXD009506 | Pride
Snake venom Proteomics Extracellular vesicles 
ProteomicsA snapshot of Bothrops jararaca snake venom gland subcellular proteome
The synthesis of snake venom proteins is subjected to finely regulated processes in the specialized secretory epithelium within the venom gland. Such processes occur within a defined time frame in the cell and at specific cellular locations. Thus, the determination of subcellular proteomes allows th...
ORGANISM(S): Bothrops jararaca (Jararaca) (Bothrops jajaraca) 
2023-09-30 | PXD040239 | Pride
Bothrops jararaca Snake venom Snake venom gland Proteome Subcellular fractionation 
ProteomicsAssessing Target Specificity of the Small Molecule Inhibitor Marimastat to Snake Venom Toxins: A Novel Application of Thermal Proteome Profiling
New treatments that circumvent the pitfalls of traditional antivenom therapies are critical to address the problem of snakebite globally. Numerous snake venom toxin inhibitors have shown promising cross-species neutralization of medically significant venom toxins in vivo and in vitro. The developmen...
ORGANISM(S): Crotalus atrox 
2024-06-22 | PXD046399 | Pride
Thermal proteome profiling Snake venom Metalloprotease 
ProteomicsProteomic Investigations of Two Pakistani Naja Snake Venoms Species Unravel the Venom Complexity, Posttranslational Modifications and Presence of Extracellular Vesicles
Latest advancement of omics technologies allows in-depth characterization of venom compositions. In the present work we present a proteomic study of two snake venoms of the genus Naja i.e. Naja naja (black cobra) and Naja oxiana (brown cobra), of Pakistani origin. The present study has shown that th...
ORGANISM(S): Naja naja Naja oxiana 
2020-10-29 | PXD018726 | Pride
Naja naja  naja oxiana  venom proteome 
ProteomicsSnake Venom LC/MSE - Post-transcriptional Mechanisms Contribute Little to Phenotypic Variation in Snake Venoms
Protein expression is a major link in the genotype-phenotype relationship, and processes affecting protein abundances, such as rates of transcription and translation, could contribute to phenotypic evolution if they generate heritable variation. Recent work has suggested that mRNA abundances do not ...
ORGANISM(S): Micrurus fulvius (Eastern coral snake) (Coluber fulvius) Sistrurus miliarius barbouri (Dusky pigmy rattlesnake) (Sistrurus barbouri) Crotalus horridus (Timber rattlesnake) Crotalus adamanteus (Eastern diamondback rattlesnake) Hypsiglena jani Sistrurus catenatus (massasauga) Agkistrodon contortrix Boiga irregularis (Brown tree snake) Micrurus tener (Texas coral snake) Agkistrodon piscivorus (cottonmouth) 
2015-11-09 | PXD002837 | Pride
Snake venom Lc/mse 
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. 
ProteomicsQualitative and quantitative analysis of Bothrops jararaca venom gland proteome
While cellular transcripts encode rich information that provide key features to understand the molecular basis of snake venom variation, their presence/ abundance does not necessary imply/correlate in the translation of a functional (protein) product. In this study we carried out an analysis of the ...
ORGANISM(S): Bothrops jararaca (Jararaca) (Bothrops jajaraca) 
2016-09-28 | PXD004186 | Pride
Venom gland proteome Snake venom proteome Bothrops jararaca Venom variability 
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 of the snake Bothrops bilineatus (Peru)
Venom proteome of the viperid snake Bothrops bilineatus from Peru
ORGANISM(S): Bothrops bilineatus 
2020-08-20 | PXD020013 | Pride
Snake venom  bothrops  bilineatus 
ProteomicsThe still puzzling role of venom composition in snake adaptation to different environments and foraging
Snake venoms have evolved in a few families of Caenophidae, and their toxins have been fine-tuned over the evolutive process into highly effective biochemical weapons with a particular role as a trophic adaptation. However, there are many outstanding questions on how venom contributes to the success...
ORGANISM(S): Bothrops bilineatus Bothrocophias hyoprora Bothrops atrox Bothrops taeniatus Bothrops brazili 
2024-05-24 | PXD046872 | Pride
Transcriptome Venom variability Proteome 
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