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Substrate Affinity Is Not Crucial for Therapeutic L-Asparaginases: Antileukemic Activity of Novel Bacterial Enzymes.
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- Molecules, 2024, v. 29, n. 10, p. 2272, doi. 10.3390/molecules29102272
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Probing the active site of Class 3 L-asparaginase by mutagenesis. I. Tinkering with the zinc coordination site of ReAV.
- Published in:
- Frontiers in Chemistry, 2024, p. 01, doi. 10.3389/fchem.2024.1381032
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- Article
Biochemical characterization of L-asparaginase isoforms from Rhizobium etli--the boosting effect of zinc.
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- Frontiers in Chemistry, 2024, p. 01, doi. 10.3389/fchem.2024.1373312
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Rhizobium etli has two l‐asparaginases with low sequence identity but similar structure and catalytic center.
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- Acta Crystallographica: Section D, Structural Biology, 2023, v. 79, n. 8, p. 775, doi. 10.1107/S2059798323005648
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Identification and partial characterization of proteolytic activity of Enterococcus faecalis relevant to their application in the dairy industry.
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- Acta Biochimica Polonica, 2019, v. 66, n. 1, p. 61, doi. 10.18388/abp.2018_2714
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- Article