Publications by authors named "Rebecca Tavares e Silva"
Article Synopsis
- A retrospective study analyzed the factors contributing to bacteremia caused by multidrug-resistant and extensively drug-resistant Pseudomonas aeruginosa, focusing on overexpressed efflux pumps and changes in porin structures.
- Molecular techniques like Pulsed Field Gel Electrophoresis and PCR were utilized to assess strain typing and identify key resistance genes, revealing a strong link between prior carbapenem use and bacteremia development.
- Among non-Metallo-β-Lactamase isolates, there was a notable prevalence of AmpC overproduction and alterations in OprD porin, indicating that intrinsic resistance mechanisms play a significant role in promoting multi-drug resistance.
A successful strategy for the recovering of active P21, an insoluble recombinant protein of Trypanosoma cruzi.
Marlus Alves dos Santos Francesco Brugnera Teixeira Heline Hellen Teixeira Moreira Adele Aud Rodrigues Fabrício Castro Machado Rebecca Tavares e Silva Claudio Vieira da Silva
Sci Rep
March 2014
Structural studies of proteins normally require large quantities of pure material that can only be obtained through heterologous expression systems and recombinant technique. In these procedures, large amounts of expressed protein are often found in the insoluble fraction, making protein purification from the soluble fraction inefficient, laborious, and costly. Usually, protein refolding is avoided due to a lack of experimental assays that can validate correct folding and that can compare the conformational population to that of the soluble fraction.
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