EC Number   |
Title |
Organism |
|---|
   3.4.17.11 | A novel technique to monitor carboxypeptidase G2 expression in suicide gene therapy using (19)F magnetic resonance spectroscopy |
Homo sapiens |
| 3.4.17.11 | A phase I study of single administration of antibody-directed enzyme prodrug therapy with the recombinant anti-carcinoembryonic antigen antibody-enzyme fusion protein MFECP1 and a bis-iodo phenol mustard prodrug |
Pseudomonas aeruginosa |
| 3.4.17.11 | Attenuated Salmonella targets prodrug activating enzyme carboxypeptidase G2 to mouse melanoma and human breast and colon carcinomas for effective suicide gene therapy |
Pseudomonas sp. |
| 3.4.17.11 | Carboxypeptidase displaying differential velocity in hydrolysis of methotrexate, 5-methyltetrahydrofolic acid, and leucovorin |
Flavobacterium sp. |
| 3.4.17.11 | Carboxypeptidase G2 rescue in patients with methotrexate intoxication and renal failure |
Pseudomonas sp. |
| 3.4.17.11 | Carboxypeptidase G: purification and properties |
Pseudomonas sp. |
| 3.4.17.11 | Characterisation of the carboxypeptidase G2 catalytic site and design of new inhibitors for cancer therapy |
Pseudomonas sp. RS-16 |
| 3.4.17.11 | Characterization of a stable form of carboxypeptidase G2 (glucarpidase), a potential biobetter variant, from Acinetobacter sp. 263903-1 |
Acinetobacter sp. 263903-1 |
| 3.4.17.11 | Characterization of a stable form of carboxypeptidase G2 (glucarpidase), a potential biobetter variant, from Acinetobacter sp. 263903-1 |
Pseudomonas sp. RS-16 |
| 3.4.17.11 | Crystal structure of carboxypeptidase G2, a bacterial enzyme with applications in cancer therapy |
Pseudomonas sp. |
