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ProteomicsPeptidome of Bothrops cotiara snake venom
The knowledge regarding toxins diversity, composition, structure, molecular and pharmacological interactions involved in the process of envenomation provide lessons for drug design based on these natural molecular scaffolds and pharmacophores of toxins. This study unravels new toxins sequenced by ma...
ORGANISM(S): Bothrops cotiara 
2023-10-20 | PXD036130 | Pride
Bothrops cotiara Peptidome Snake venoms 
ProteomicsNeuropeptidomic Analysis of a Genetically Defined Cell Type in Mouse Brain and Pituitary
We describe a method to identify neuropeptides in specific cell-types by the conditional disruption of the gene for carboxypeptidase E (Cpe), an essential neuropeptide-processing enzyme. The loss of Cpe led to the accumulation of neuropeptides containing C-terminal basic residues which are used as t...
ORGANISM(S): Mus musculus (Mouse) 
2020-11-20 | PXD020999 | Pride
Neuropeptidomics Pituitary Single-cell Brain 
ProteomicsPhosphosite-specific regulation of the oxidative-stress response of P. brasiliensis: A Shotgun Phosphoproteomic Analysis
Paracoccidioides brasiliensis, a thermally dimorphic fungus, is the causative agent of paracoccidioidomycosis, a systemic mycosis that is widespread in Latin America. P. brasiliensis infection occurs when conidia or mycelial fragments are inhaled by the host, which causes these cells to transition t...
ORGANISM(S): Paracoccidioides brasiliensis (strain Pb18) 
2022-03-03 | PXD001181 | Pride
Paracoccidioides brasiliensis Post-translational modification Cell proliferation Phosphorylation Oxidative stress 
ProteomicsExploring potential virulence regulators in Paracoccidioides brasiliensis isolates of varying virulence through quantitative proteomics
Paracoccidioides brasiliensis is the agent of paracoccidioidomycosis, an important systemic mycosis in Latin America. Few virulence factors have been identified for this pathogen. In this study, we quantitatively evaluated the protein composition of P. brasiliensis in the yeast phase using minimal a...
ORGANISM(S): Paracoccidioides brasiliensis (strain Pb18) 
2014-08-28 | PXD000804 | Pride
Paracoccidioides brasiliensis  pathogenic fungus  proteomic analysis  virulence regulators 
ProteomicsA novel peptide from Bothrops cotiara peptidome
The knowledge regarding toxins diversity, composition, structure, molecular and pharmacological interactions involved in the process of envenomation provide lessons for drug design based on these natural molecular scaffolds and pharmacophores of toxins. This study unravels new toxins sequenced by ma...
ORGANISM(S): Bothrops cotiara 
2023-10-20 | PXD041473 | Pride
Bothrops cotiara Peptidome. 
ProteomicsComparative gender peptidomics of Bothrops atrox venoms: new peptides and evidences of increased disintegrins levels in the venoms of females
Background: Bothrops atrox is known to be the pitviper responsible for most snakebites and human fatalities in the Amazon region. It can be found in a wide geographical area including the northern South America, the east of Andes and the Amazon basin. Possibly due to its wide distribution range and ...
ORGANISM(S): Bothrops atrox 
2020-10-13 | PXD018632 | Pride
Peptidomics Sexual dimorphism Venom Mass spectrometry Bothrops atrox Disintegrins 
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 
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 
ProteomicsA multi-omics approach unravels new toxins with potential antimicrobial, antiviral and antitumoral activities in the venom of Acanthoscurria rondoniae
The Araneae order is considered one of the most successful group among venomous animals in the world. An important factor for this success is the production of venoms, a refined biological fluid rich in proteins, short peptides and cysteine-rich peptides (CRPs). These toxins may present pharmacologi...
ORGANISM(S): Acanthoscurria rondoniae 
2020-07-20 | PXD019343 | Pride
Peptidomics Cysteine-rich peptides Proteomics 33 antimicrobial peptides Antiviral peptides Multi-omics Acanthoscurria rondoniae Antitumoral peptides 
ProteomicsQuantitative proteomics of non hodgkin's
Abstract: ArtinM, a D-mannose-binding lectin from Artocarpus heterophyllus induces the activation of a Mast cell, neutrophils, macrophages, and CD4+ and CD8+ T cells, via carbohydrate recognition. we previously reported, that ArtinM is able to induce IL-17 and IL-12p40 production in murine B cells. ...
ORGANISM(S): Homo sapiens (Human) 
2023-03-11 | PXD029399 | Pride
B cells  artinm  burkitt’s lymphoma  death cells  apoptosis  carbohydrate recognition 
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