Despite the increasing number of placenta accreta spectrum (PAS) cases in recent years, its impact on neonatal outcomes and respiratory morbidity, as well as the underlying pathogenetic mechanism, has not yet been extensively studied. Moreover, no study has yet demonstrated the effectiveness of antenatal corticosteroid therapy (CT) for the prevention of respiratory distress syndrome (RDS) in newborns of mothers with PAS at the molecular level. In this regard, microRNA (miRNA) profiling by small RNA deep sequencing and quantitative real-time PCR was performed on 160 blood plasma samples from preterm infants (gestational age: 33-36 weeks) and their mothers who had been diagnosed with or without PAS depending on the timing of the antenatal RDS prophylaxis.
View Article and Find Full Text PDFIn this Letter, a two-term formalism for constructing protein solubility curves in thermal proteome profiling (TPP) is considered, which takes into account the efficiency of the drug-protein binding reaction. When the reaction is incomplete, this results in distortion of the otherwise sigmoidal shape of the curve after drug treatment, which is often observed in experiments. This distortion may be significant enough to disqualify the corresponding protein from the list of drug target candidates, thus negatively affecting the results of TPP data analysis.
View Article and Find Full Text PDFUnderstanding the properties of molecular nitrogen N2 at extreme conditions is the fundamental problem for atomistic theory and the important benchmark for the capabilities of first-principles molecular dynamics (FPMD) methods. In this work, we focus on the connection between the dynamics of ions and electronic excitations in warm dense N2. The restricted open-shell Kohn-Sham method gives us the possibility to reach relevant time and length scales for FPMD modeling of an isolated exciton dynamics in warm dense N2.
View Article and Find Full Text PDFCurrent stage of proteomic research in the field of biology, medicine, development of new drugs, population screening, or personalized approaches to therapy dictates the need to analyze large sets of samples within the reasonable experimental time. Until recently, mass spectrometry measurements in proteomics were characterized as unique in identifying and quantifying cellular protein composition, but low throughput, requiring many hours to analyze a single sample. This was in conflict with the dynamics of changes in biological systems at the whole cellular proteome level upon the influence of external and internal factors.
View Article and Find Full Text PDFAdvances in high-throughput high-resolution mass spectrometry and the development of thermal proteome profiling approach (TPP) have made it possible to accelerate a drug target search. Since its introduction in 2014, TPP quickly became a method of choice in chemical proteomics for identifying drug-to-protein interactions on a proteome-wide scale and mapping the pathways of these interactions, thus further elucidating the unknown mechanisms of action of a drug under study. However, the current TPP implementations based on tandem mass spectrometry (MS/MS), associated with employing lengthy peptide separation protocols and expensive labeling techniques for sample multiplexing, limit the scaling of this approach for the ever growing variety of drug-to-proteomes.
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