Manganese-dependent inhibition of human liver arginase by borate
Author:
Publisher
Elsevier BV
Subject
Inorganic Chemistry,Biochemistry
Reference33 articles.
1. Altering the Binuclear Manganese Cluster of Arginase Diminishes Thermostability and Catalytic Function
2. Interaction of arginase with metal ions: studies of the enzyme from human liver and comparison with other arginases
3. Nuclear Magnetic Resonance Studies of Manganese Binding of Rat Liver Arginase
4. Purification of Human Hepatic Arginase and Its Manganese (II)-Dependent and pH-Dependent Interconversion between Active and Inactive Forms: A Possible pH-Sensing Function of the Enzyme on the Ornithine Cycle
5. Effect of manganese on the quaternary structure of human liver arginase
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2. Illuminating the structure–function landscape of an evolutionary nonconserved motif in the arginases of Helicobacter gastric pathogens;IUBMB Life;2023-04-22
3. Chemical similarities and differences among inhibitors of nitric oxide synthase, arginase and dimethylarginine dimethylaminohydrolase-1: Implications for the design of novel enzyme inhibitors modulating the nitric oxide pathway;Bioorganic & Medicinal Chemistry;2022-10
4. An Update on Arginase Inhibitors and Inhibitory Assays;Mini-Reviews in Medicinal Chemistry;2021-12-29
5. An evolutionary non-conserved motif in Helicobacter pylori arginase mediates positioning of the loop containing the catalytic residue for catalysis;Biochemical Journal;2021-02-24
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