Publications by authors named "T Agback"

The recent COVID-19 pandemic has set a strong quest for advanced understanding of possible tracks in abating and eliminating viral infections. In the view that several families of "pristine" small oxide nanoparticles (NPs) have demonstrated viricidal activity against SARS-CoV-2, we studied the effect of two NPs, with presumably different reactivity, on two viruses aiming to evaluate two "primary suspect" routes of their antiviral activity, either specific blocking of surface proteins or causing membrane disruption. The chosen NPs were non-photoactive 3.

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Structural- and functional heterogeneity, as well as allosteric regulation, in homo-monomeric enzymes is a highly active area of research. One such enzyme is human nuclear-associated deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase), which has emerged as an interesting drug target in combination therapy with traditional nucleotide analogue treatment of cancer. We report, for the first time, a full structural dynamics study of human dUTPase by NMR.

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Mucosa-associated lymphoid tissue lymphoma-translocation protein 1 (MALT1) is an attractive target for the development of modulatory compounds in the treatment of lymphoma and other cancers. While the three-dimensional structure of MALT1 has been previously determined through X-ray analysis, its dynamic behaviour in solution has remained unexplored. We present here dynamic analyses of the apo MALT1 form along with the E549A mutation.

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Article Synopsis
  • Tryptophan (TRP) oxidation is essential for both plant growth and animal behavior, influencing factors like hunger and sleep.
  • Interactions with metal oxide nanoparticles (NPs) can significantly affect TRP oxidation, providing opportunities for various biomedical and agricultural innovations.
  • Advanced techniques like NMR, optical spectroscopy, and X-ray studies revealed detailed mechanisms of TRP-NP interactions, highlighting how different oxides can oxidize TRP and produce important organic compounds.
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Biocatalytic degradation with the use of enzymes has gained great attention in the past few years due to its advantages of high efficiency and environmental friendliness. Novel, cost-effective, and green nanoadsorbents were produced in this study, using natural silicates as an enzyme host matrix for core-shell immobilization technique. With the natural silicate as a core and silica layer as a shell, it was possible to encapsulate two different enzymes: horseradish peroxidase (HRP) and laccase, for removal and degradation of three pharmaceuticals: diclofenac (DFC), carbamazepine (CBZ), and paracetamol (PC).

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