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António E. N. Ferreira

Researcher at University of Lisbon

Publications -  42
Citations -  1346

António E. N. Ferreira is an academic researcher from University of Lisbon. The author has contributed to research in topics: Methylglyoxal & Lactoylglutathione lyase. The author has an hindex of 16, co-authored 40 publications receiving 1178 citations. Previous affiliations of António E. N. Ferreira include University of Porto & Medical University of South Carolina.

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Metrics for GO based protein semantic similarity: a systematic evaluation

TL;DR: A systematic evaluation of GO-based semantic similarity measures using the relationship with sequence similarity as a means to quantify their performance, and assessed the influence of electronic annotations by testing the measures in the presence and absence of these annotations.
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The glyoxalase pathway: the first hundred years... and beyond.

TL;DR: The aim of the present review is to show the evolution of thought regarding the glyoxalase pathway since its discovery 100 years ago, the current knowledge on the glyxalase enzymes and their recognized role in the control of glycation processes.
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Yeast protein glycation in vivo by methylglyoxal Molecular modification of glycolytic enzymes and heat shock proteins

TL;DR: Using Saccharomyces cerevisiae cells with different glycation phenotypes and MALDI‐TOF peptide mass fingerprints, enolase’2 is identified as the primary methylglyoxal glycation target in yeast and two other glycolytic enzymes are also glycated, aldolase and phosphoglycerate mutase.
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Protein glycation in vivo: functional and structural effects on yeast enolase.

TL;DR: Yeast was shown to be an ideal model to investigate glycation in vivo since it shows different glycation phenotypes and presents specific protein glycation targets, and all effects regarding structure and stability changes were enhanced when the protein was glycated in vitro.
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Quantitative assessment of the glyoxalase pathway in Leishmania infantum as a therapeutic target by modelling and computer simulation.

TL;DR: The sensitivity analysis of the glyoxalase pathway revealed that the most critical parameters for controlling the intracellular concentration of methylglyoxal are its formation rate and the concentration of trypanothione.