Publications by authors named "A I Denisiuk"

Data sharing is central to the rapid translation of research into advances in clinical medicine and public health practice. In the context of COVID-19, there has been a rush to share data marked by an explosion of population-specific and discipline-specific resources for collecting, curating, and disseminating participant-level data. We conducted a scoping review and cross-sectional survey to identify and describe COVID-19-related platforms and registries that harmonise and share participant-level clinical, omics (eg, genomic and metabolomic data), imaging data, and metadata.

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Molecular catalysts can promote ammonia oxidation, providing mechanistic insights into the electrochemical N cycle for a carbon-free fuel economy. We report the ammonia oxidation activity of carbon anodes functionalized with the oligomer {[Ru(bda-κ- )(4,4'-bpy)](4,4'-bpy)}, , where bda is [2,2'-bipyridine]-6,6'-dicarboxylate and 4,4'-bpy is 4,4'-bipyridine. Electrocatalytic studies in propylene carbonate demonstrate that the Ru-based hybrid anode used in a 3-electrode configuration transforms NH to N and H in a 1:3 ratio with near-unity faradaic efficiency at an applied potential of 0.

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Herein, we describe the redox chemistry of bi- and mononuclear α-diimine-Mn(CO) complexes with an internal proton source in close proximity to the metal centers and their catalytic activity in the electrochemically driven CO reduction reactions. In order to address the impact of the two metal sites and of the proton source, we investigate a binuclear complex with phenol moiety, , a binuclear Mn complex with methoxyphenol unit instead, , and the mononuclear analogue with a phenol unit, . Spectroelectrochemical investigation of the complexes in dmf under a nitrogen atmosphere indicates that and undergo a reductive H formation forming [Mn(HL)(CO)Br] and [Mn(HL)(CO)], respectively, which is redox neutral for the complex and equivalent to a deprotonation of the phenol unit.

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Expansion of the structural diversity of peptide antibiotics was performed through two different methods. Supplementation-based incorporation (SPI) and stop-codon suppression (SCS) approaches were used for co-translational incorporation of isostructural and orthogonal noncanonical amino acids (ncAAs) into the lasso peptide capistruin. Two ncAAs were employed for the SPI method and five for the SCS method; each of them probing the incorporation of ncAAs in strategic positions of the molecule.

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