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ProteomicsComparative proteomics and biochemical analysis of venom of thirteen Bothrops moojeni specimens reveal several individual variations
Snake venoms are complex protein mixtures with different biological activities that can act in both their preys and human victims. Many of these proteins play a role in prey capture and in the digestive process of these animals. It is known that some snakes are resistant to the toxicity of their own...
ORGANISM(S): Bothrops moojeni 
2019-09-26 | PXD012585 | Pride
Bothrops moojeni  snake venom  envenomation  intraspecific venom variability  snake plasma 
ProteomicsOntogenetic study of the composition of snake venom inhibitors and evaluation of the neutralizing activity of the gamma-type phospholipase inhibitor (γPLI) present in the plasma of Bothrops jararaca snake
Snake venom inhibitors have been studied for over a century. Among them are the plasma proteins of some mammals and of non-venomous and venomous snakes, which have the ability to promote resistance to the venom. These proteins have aroused biotechnological interest, as they are an excellent alternat...
ORGANISM(S): Bothrops jararaca (Jararaca) (Bothrops jajaraca) 
2024-05-21 | PXD034977 | Pride
Phospholipases a2  envenomation  pla2 inhibitor venomous snake 
ProteomicsFrom birth to adulthood: An analysis of Bothrops moojeni snake venom at different life stages
Bothrops moojeni has a wide distribution in Brazil and represents a serious medical concern at some localities. Previous works reported that the manifestations of snakebites caused by B. moojeni juveniles were mainly related to coagulation, while those caused by adults had more prominent local damag...
ORGANISM(S): Crotalus durissus terrificus Bothrops moojeni 
2021-06-24 | PXD024447 | Pride
Snake venom  bothrops moojeni  ontogeny  hdmse 
ProteomicsSnake venom color and LAAO: an evidence of long-term captive Crotalus durissus terrificus venom plasticity
The venom color variation of C. d. terrificus (Cdt) is attributed to the presence of the toxin LAAO. However, the driving mechanisms of such variability have not been studied and identified so far. During the venom milking routine at Butantan Institute, we have noticed that most of the venoms of cap...
ORGANISM(S): Crotalus durissus terrificus 
2023-10-23 | PXD019730 | Pride
Snake venom  crotalus durissus terrificus  snake venom plasticity  intraspecific venom variability  captivity maintenance  l-amino acid oxidase. 
ProteomicsEnhancing the bothropic antivenom through a reverse antivenomics approach
Antivenoms are the only effective treatment for snakebite envenomation and have saved countless lives over more than a century. Despite its value, antivenoms often present risks of adverse reactions. Current formulations contain a substantial fraction of non-specific antibodies and serum proteins th...
ORGANISM(S): Equus Caballus (ncbitaxon:9796) 
2024-11-07 | MSV000096324 | MassIVE
ProteomicsVenom proteomics of the Amazonian spider Acanthoscurria juruenicola
Acanthoscurria juruenicola is an Amazonian tarantula spider described for the first time a century ago. Specimens of both genders are similar in size and in most morphological aspects, but ecological behavior and their venom composition remained unknown to date. Here we present the trascriptomics, p...
ORGANISM(S): Acanthoscurria Juruenicola 
2021-07-08 | MSV000087777 | MassIVE
ProteomicsAnalysis of the yeast peptidome and comparison with the human peptidome
Peptides function as signaling molecules in species as diverse as humans and yeast. Mass spectrometry-based peptidomics techniques provide a relatively unbiased method to assess the peptidome of biological samples. In the present study, we used a quantitative peptidomic technique to characterize the...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2020-06-02 | PXD004800 | Pride
Mass spectrometry Saccharomyces cerevisiae Proteasome Peptidome 
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