EC Number   |
Title |
Organism |
|---|
   2.4.2.29 | Crystal structure of the human tRNA guanine transglycosylase catalytic subunit QTRT1 |
Homo sapiens |
| 2.4.2.29 | An integrative approach combining noncovalent mass spectrometry, enzyme kinetics and X-ray crystallography to decipher Tgt protein-protein and protein-RNA interaction |
Zymomonas mobilis |
| 2.4.2.29 | Crystal structure analysis and in silico pKa calculations suggest strong pKa shifts of ligands as driving force for high-affinity binding to TGT |
Zymomonas mobilis |
| 2.4.2.29 | Crystal structure of tRNA-guanine transglycosylase: RNA modification by base exchange |
Zymomonas mobilis |
| 2.4.2.29 | Crystal structures of tRNA-guanine transglycosylase (TGT) in complex with novel and potent inhibitors unravel pronounced induced-fit adaptations and suggest dimer formation upon substrate binding |
Zymomonas mobilis |
| 2.4.2.29 | Elevated expression level of 60-kDa subunit of tRNA-guanine transglycosylase in colon cancer |
Homo sapiens |
| 2.4.2.29 | From lin-benzoguanines to lin-benzohypoxanthines as ligands for Zymomonas mobilis tRNA-guanine transglycosylase: replacement of protein-ligand hydrogen bonding by importing water clusters |
Zymomonas mobilis |
| 2.4.2.29 | Glutamate versus glutamine exchange swaps substrate selectivity in tRNA-guanine transglycosylase: insight into the regulation of substrate selectivity by kinetic and crystallographic studies |
Zymomonas mobilis |
| 2.4.2.29 | High-affinity inhibitors of tRNA-guanine transglycosylase replacing the function of a structural water cluster |
Zymomonas mobilis |
| 2.4.2.29 | How to replace the residual solvation shell of polar active site residues to achieve nanomolar inhibition of tRNA-guanine transglycosylase |
Zymomonas mobilis |
