2,110 research outputs found

    STATCOM evaluation in electrified railway using V/V and Scott power transformers

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    Rail transport has always been one of the greatest economic boosters of several world nations, allowing the freight and passenger transport. In addition, it is the most secure and economic land transportation mode. From the energetic perspective, the electric locomotives emerge as one of the most efficient land transportation mode, as well as allow a more sustainable development. However, when an electric locomotive is connected to the three-phase power grid, power quality (PQ) deterioration arise, leading to the distortion and unbalance of the three-phase power grid currents and voltages which imply higher operational costs, raising economic and functional issues. In order to overcome the PQ deterioration phenomena, several solutions based power electronics technology have been studied and developed. These solutions vary in terms of control, functionality, implementation costs and complexity. One of the existing solutions is a static synchronous compensator (STATCOM), which compensates the three-phase currents imbalance and harmonics. In this paper, a comprehensive review of the electrified railway systems is carried out, identifying the electric PQ phenomena which may appear due to the non-linear dynamic traction loads. Following this topic, a computational simulation of the STATCOM is presented, making analysis of its behavior regarding the PQ improvement in electrified railway systems. Two case studies are presented: (i) a traction power system fed with V/V power transformer; (ii) a traction power system fed with Scott power transformer.This work has been supported by FCT – Fundação para a Ciência e Tecnologia with-in the Project Scope: UID/CEC/00319/2019. This work has been supported by the FCT Project QUALITY4POWER PTDC/EEI-EEE/28813/2017, and by the FCT Project DAIPESEV PTDC/EEI-EEE/30382/2017. Mr. Luis A. M. Barros is supported by the doctoral scholarship PD/BD/143006/2018 granted by the Portuguese FCT foundation. Mr. Mohamed Tanta was supported by FCT PhD grant with a reference PD/BD/127815/2016

    Targeted online liquid chromatography electron capture dissociation mass spectrometry for the localization of sites of in vivo phosphorylation in human Sprouty2

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    We demonstrate a strategy employing collision-induced dissociation for phosphopeptide discovery, followed by targeted electron capture dissociation (ECD) for site localization. The high mass accuracy and low background noise of the ECD mass spectra allow facile sequencing of coeluting isobaric phosphopeptides, with up to two isobaric phosphopeptides sequenced from a single mass spectrum. In contrast to the previously described neutral loss of dependent ECD method, targeted ECD allows analysis of both phosphotyrosine peptides and lower abundance phosphopeptides. The approach was applied to phosphorylation analysis of human Sprouty2, a regulator of receptor tyrosine kinase signaling. Fifteen sites of phosphorylation were identified, 11 of which are novel

    Repurposing the aldose reductase inhibitor and diabetic neuropathy drug epalrestat for the congenital disorder of glycosylation PMM2-CDG

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    Phosphomannomutase 2 deficiency, or PMM2-CDG, is the most common congenital disorder of glycosylation and affects over 1000 patients globally. There are no approved drugs that treat the symptoms or root cause of PMM2-CDG. To identify clinically actionable compounds that boost human PMM2 enzyme function, we performed a multispecies drug repurposing screen using a novel worm model of PMM2-CDG, followed by PMM2 enzyme functional studies in PMM2-CDG patient fibroblasts. Drug repurposing candidates from this study, and drug repurposing candidates from a previously published study using yeast models of PMM2-CDG, were tested for their effect on human PMM2 enzyme activity in PMM2-CDG fibroblasts. Of the 20 repurposing candidates discovered in the worm-based phenotypic screen, 12 were plant-based polyphenols. Insights from structure-activity relationships revealed epalrestat, the only antidiabetic aldose reductase inhibitor approved for use in humans, as a first-in-class PMM2 enzyme activator. Epalrestat increased PMM2 enzymatic activity in four PMM2-CDG patient fibroblast lines with genotypes R141H/F119L, R141H/E139K, R141H/N216I and R141H/F183S. PMM2 enzyme activity gains ranged from 30% to 400% over baseline, depending on genotype. Pharmacological inhibition of aldose reductase by epalrestat may shunt glucose from the polyol pathway to glucose-1,6-bisphosphate, which is an endogenous stabilizer and coactivator of PMM2 homodimerization. Epalrestat is a safe, oral and brain penetrant drug that was approved 27 years ago in Japan to treat diabetic neuropathy in geriatric populations. We demonstrate that epalrestat is the first small molecule activator ofPMM2 enzyme activity with the potential to treat peripheral neuropathy and correct the underlying enzyme deficiency in a majority of pediatric and adult PMM2-CDG patients
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