A5074122622- Prion Diseases and Protein Misfolding
- Trace Elements in Health
- Neurological diseases and metabolism
- RNA regulation and disease
- RNA Research and Splicing
- Bacteriophages and microbial interactions
- Alzheimer's disease research and treatments
- Seed Germination and Physiology
- Enzyme Structure and Function
- Microbial bioremediation and biosurfactants
- Fern and Epiphyte Biology
- Biofuel production and bioconversion
- Plant tissue culture and regeneration
- Microbial Metabolic Engineering and Bioproduction
- Biotin and Related Studies
Universidade Federal do Rio de Janeiro
2010-2025
Yale University
2020
Harvard University
2020
Rockefeller University
2020
National Institutes of Health
2020
Universitat Autònoma de Barcelona
2016
Structural conversion of cellular prion protein (PrPC) into scrapie PrP (PrPSc) and subsequent aggregation are key events associated with the onset transmissible spongiform encephalopathies (TSEs). Experimental evidence supports role nucleic acids (NAs) in assisting this conversion. Here, we asked whether undergoes liquid-liquid phase separation (LLPS) if process is modulated by NAs. To end, two 25-mer DNA aptamers, A1 A2, were selected against globular domain recombinant murine (rPrP90-231)...
A misfolded form of the prion protein (PrP) is primary culprit in mammalian diseases. It has been shown that nucleic acids catalyze misfolding cellular PrP into a scrapie-like conformer. also observed interaction with nonspecific and complex can be toxic to cultured cells. No direct correlation yet drawn between changes structure toxicity due acid binding. Here we asked whether different aggregation, stability, effects are detected when nonrelated DNA sequences interact recombinant PrP....
The prion protein (PrP) is implicated in the Transmissible Spongiform Encephalopathies (TSEs), which comprise a group of fatal neurodegenerative diseases affecting humans and other mammals. Conversion cellular PrP (PrPC) into scrapie form (PrPSc) hallmark TSEs. Once formed, PrPSc aggregates catalyzes PrPC misfolding new molecules. Although many compounds have been shown to inhibit conversion process, so far there no effective therapy for Besides, most previously evaluated failed vivo due...
Bioremediation using microorganisms offers a sustainable approach to addressing hydrocarbon contamination. This study explores biosurfactant production by Yarrowia lipolytica IMUFRJ 50682 during crude oil and asphaltene-free fraction biodegradation in corn steep liquor (CSL)-based media. By evaluating CSL concentrations (5–30 g/L) combinations with glucose, molasses, oil, this demonstrates that is an effective nutrient source for supporting microbial growth production. The highest...
An increasing number of proteins are being shown to assemble into amyloid structures that lead pathological states. Among them, mammalian prions outstand due their ability transmit the pathogenic conformation, becoming thus infectious. The structural conversion cellular prion protein (PrPC), its misfolded form (PrPSc) is central event prion-driven pathologies. study properties intracellular aggregates in general and prion-like ones particular a challenging task. In this context, evidence...
ABSTRACT Structural conversion of cellular prion protein (PrP C ) into scrapie PrP Sc and subsequent aggregation are key events for the onset Transmissible Spongiform Encephalopathies (TSEs). Experimental evidences support role nucleic acids (NAs) in assisting process. Here, we used SELEX methodology to identify two 25-mer DNA aptamers against globular domain recombinant murine (rPrP 90-231 ), namely A1 A2. High-affinity binding A2 rPrP was verified by ITC. Aptamers structure characterized...
Mammalian prion proteins (PrPs) that cause transmissible spongiform encephalopathies are misfolded conformations of the host cellular PrP. The form, scrapie PrP (PrP(Sc)), can aggregate into amyloid fibrils progressively accumulate in brain, evolving to a pathological phenotype. A particular characteristic PrP(Sc) is be found as different strains, related diversity conformational states it adopt. Prion strains responsible for multiple phenotypes observed diseases, presenting incubation times...