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Agnieszka Bzowska

Researcher at University of Warsaw

Publications -  111
Citations -  2123

Agnieszka Bzowska is an academic researcher from University of Warsaw. The author has contributed to research in topics: Purine nucleoside phosphorylase & Phosphorolysis. The author has an hindex of 23, co-authored 108 publications receiving 1972 citations. Previous affiliations of Agnieszka Bzowska include Tokyo University of Pharmacy and Life Sciences.

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Purine nucleoside phosphorylases: properties, functions, and clinical aspects.

TL;DR: Detailed accounts are presented of design of potent inhibitors, largely nucleosides and acyclonucleosides, their phosphates and phosphonates, particularly of the human erythrocyte enzyme intended for induction of the immunodeficient state for clinical applications, such as prevention of host-versus-graft response in organ transplantations.
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Properties of two unusual, and fluorescent, substrates of purine-nucleoside phosphorylase: 7-methylguanosine and 7-methylinosine.

TL;DR: Measurements of pH-dependence of kinetic constants indicated that the cationic forms are the preferred substrates, whereas the monoanion of inosine appears to be almost as good a substrate as the neutral form.
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Crystal structure of the ternary complex of E. coli purine nucleoside phosphorylase with formycin B, a structural analogue of the substrate inosine, and phosphate (Sulphate) at 2.1 A resolution.

TL;DR: The ternary complex of purine nucleoside phosphorylase from E. coli with formycin B and a sulphate or phosphate ion crystallized in the hexagonal space group P6122 contains a biologically active hexamer formed through 2-fold crystallographic symmetry, constituting a trimer of dimers.
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A Multilaboratory Comparison of Calibration Accuracy and the Performance of External References in Analytical Ultracentrifugation

Huaying Zhao, +123 more
- 21 May 2015 - 
TL;DR: A multi-laboratory study to establish the precision and accuracy of basic data dimensions in AUC and validate previously proposed calibration techniques highlights the necessity and effectiveness of independent calibration of basic AUC data dimensions for reliable quantitative studies.
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Crystal structure of calf spleen purine nucleoside phosphorylase in a complex with hypoxanthine at 2.15 A resolution.

TL;DR: Trimeric calf spleen purine nucleoside phosphorylase isolated form human tissues is a primary target for chemotherapeutic intervention, and the more stable calf enzyme has similar physico-chemical and kinetic properties, as well as response to inhibitors.