EC Number |
Disease |
PubMed ID |
Title of Publication |
Category |
Confidence Level |
---|
2.4.2.29 | Breast Neoplasms |
32182756 |
tRNA Queuosine Modification Enzyme Modulates the Growth and Microbiome Recruitment to Breast Tumors. |
causal interaction diagnostic usage ongoing research unassigned |
4 1 4 0 |
2.4.2.29 | Carcinogenesis |
32182756 |
tRNA Queuosine Modification Enzyme Modulates the Growth and Microbiome Recruitment to Breast Tumors. |
causal interaction diagnostic usage ongoing research unassigned |
4 1 4 0 |
2.4.2.29 | Colonic Neoplasms |
1378304 |
Absence of tRNA-guanine transglycosylase in a human colon adenocarcinoma cell line. |
ongoing research unassigned |
4 0 |
2.4.2.29 | Colonic Neoplasms |
15246567 |
Elevated expression level of 60-kDa subunit of tRNA-guanine transglycosylase in colon cancer. |
causal interaction diagnostic usage unassigned |
2 3 0 |
2.4.2.29 | Dysentery, Bacillary |
11178905 |
A new target for shigellosis: rational design and crystallographic studies of inhibitors of tRNA-guanine transglycosylase. |
therapeutic application unassigned |
4 0 |
2.4.2.29 | Dysentery, Bacillary |
18510366 |
Structure-based drug design: exploring the proper filling of apolar pockets at enzyme active sites. |
causal interaction therapeutic application unassigned |
1 4 0 |
2.4.2.29 | Dysentery, Bacillary |
19199329 |
Crystal structure analysis and in silico pKa calculations suggest strong pKa shifts of ligands as driving force for high-affinity binding to TGT. |
causal interaction unassigned |
1 0 |
2.4.2.29 | Dysentery, Bacillary |
19746363 |
High-Affinity Inhibitors of tRNA-Guanine Transglycosylase Replacing the Function of a Structural Water Cluster. |
therapeutic application unassigned |
1 0 |
2.4.2.29 | Dysentery, Bacillary |
19894214 |
How to replace the residual solvation shell of polar active site residues to achieve nanomolar inhibition of tRNA-guanine transglycosylase. |
therapeutic application unassigned |
4 0 |
2.4.2.29 | Dysentery, Bacillary |
23534552 |
Launching Spiking Ligands into a Protein-Protein Interface: A Promising Strategy to Destabilize and Break Interface Formation in a tRNA Modifying Enzyme. |
therapeutic application unassigned |
3 0 |