ArticleInternational journal of molecular sciences2018
Oxidative Alteration of Trp-214 and Lys-199 in Human Serum Albumin Increases Binding Affinity with Phenylbutazone: A Combined Experimental and Computational Investigation.
Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 16 citations in OpenAlex.
- Albumin-on-a-chip: binding profiling of circulating human albumin via selective immunocapture and real-time SPR analysis.Scientific reports · 2026Article
- Ligand-human serum albumin analysis: the near-UV CD and UV-Vis spectroscopic studies.Naunyn-Schmiedeberg's archives of pharmacology · 2025Article
- Quenching of Protein Fluorescence by Fullerenol CInternational journal of molecular sciences · 2022Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
Human serum albumin (HSA) is a target for reactive oxygen species (ROS), and alterations of its physiological functions caused by oxidation is a current issue. In this work, the amino-acid residues Trp-214 and Lys-199, which are located at site I of HSA, were experimentally and computationally oxidized, and the effect on the binding constant with phenylbutazone was measured. HSA was submitted to two mild oxidizing reagents, taurine monochloramine (Tau-NHCl) and taurine dibromamine (Tau-NBr₂). The oxidation of Trp-214 provoked spectroscopic alterations in the protein which were consistent with the formation of
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