Author
Y. T. Oester
Bio: Y. T. Oester is an academic researcher from Loyola University Chicago. The author has contributed to research in topics: Human serum albumin & Manganese. The author has an hindex of 6, co-authored 7 publications receiving 183 citations.
Papers
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TL;DR: The in vitro binding of warfarin by human serum albumin was studied at various temperatures and at pH 7.4 by a frontal gel filtration technique and showed that, for the therapeutic concentration range, Warfarin was over 99% bound to albumin present in physiological concentration.
53 citations
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TL;DR: Frontal analysis gel filtration, which previously has been shown to provide superior reproducibility, critical temperature control and improved accuracy for two-site resolution, was used and postulated that the binding of salicylate involves both hydrophobic and ionic contributions.
44 citations
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TL;DR: The purpose of this paper is to compare non-dialyzable levels of copper and manganese in the blood serum of patients with various diseases to the levels observed in normal subjects.
36 citations
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26 citations
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19 citations
Cited by
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TL;DR: A generic model for the prediction of drug association constants to HSA is reported, which uses a pharmacophoric similarity concept and partial least square analysis (PLS) to construct a quantitative structure-activity relationship.
510 citations
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378 citations
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TL;DR: Using warfarin as a test system, the application of BIACORE SPR biosensors are validated to reliably determine binding constants for drug/HSA interactions and it is shown that the % bound values determined by SPR correlate with thevalues determined by solution-based methods.
249 citations
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TL;DR: The qualitative and quantitative aspects of capillary electrophoretic methods used to study drug-protein interactions, viz.
223 citations
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TL;DR: In this paper, the pH dependence of warfarin binding to human serum albumin has been studied by circular dichroism, fluorescence, and equilibrium dialysis, showing that albumin complexes at low drug to protein ratios parallel the neutral to base transition, occurring in the protein over the pH range 6 to 9.
215 citations