B
Bartosz Sekula
Researcher at Argonne National Laboratory
Publications - 20
Citations - 384
Bartosz Sekula is an academic researcher from Argonne National Laboratory. The author has contributed to research in topics: Serum albumin & Serine. The author has an hindex of 8, co-authored 17 publications receiving 267 citations. Previous affiliations of Bartosz Sekula include Lodz University of Technology.
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Structural studies of bovine, equine, and leporine serum albumin complexes with naproxen.
TL;DR: A comparison of the structurally investigated complexes with the analogous complex of human serum albumin (HSA‐NPS) revealed surprising differences in the number and distribution of naproxen binding sites.
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Crystallographic studies of the complexes of bovine and equine serum albumin with 3,5-diiodosalicylic acid.
TL;DR: Two crystal structures of the complexes of equine and bovine serum albumins with 3,5-diiodosalicylic acid (DIS) are presented and results with the HSA binding ability of DIS and other structurally similar ligands are compared.
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Structural Investigations of N-carbamoylputrescine Amidohydrolase from Medicago truncatula: Insights into the Ultimate Step of Putrescine Biosynthesis in Plants.
TL;DR: The key residues, highly conserved among the plant kingdom, responsible for the activity and selectivity of MtCPA toward N-carbamoylputrescine are highlighted.
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Structural Insights into the Competitive Binding of Diclofenac and Naproxen by Equine Serum Albumin
Bartosz Sekula,Anna Bujacz +1 more
TL;DR: Results suggest that combined application of both drugs may result in increased concentration of free diclofenac in plasma.
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Structural analysis of phosphoserine aminotransferase (isoform 1) from Arabidopsis thaliana- the enzyme involved in the phosphorylated pathway of serine biosynthesis
TL;DR: The structural characterization of PSAT isoform 1 from Arabidopsis thaliana is presented, a dimeric S-shaped protein that truncated of its 71-residue-long chloroplast-targeting signal peptide to present detailed architecture of AtPSAT1 and allow for the comparison of this plant enzyme with other PSATs.