EC Number   |
Disease |
PubMed ID |
Title of Publication |
Category |
Confidence Level |
|---|
    2.7.7.23 | Cysts |
10799561 |
UDP-N-acetylglucosamine pyrophosphorylase, a key enzyme in encysting Giardia, is allosterically regulated. |
unassigned |
0 |
| 2.7.7.23 | Cysts |
16169849 |
Kinetic and physical characterization of the inducible UDP-N-acetylglucosamine pyrophosphorylase from Giardia intestinalis. |
unassigned |
0 |
| 2.7.7.23 | Cysts |
16277981 |
mummy/cystic encodes an enzyme required for chitin and glycan synthesis, involved in trachea, embryonic cuticle and CNS development--analysis of its role in Drosophila tracheal morphogenesis. |
therapeutic application
unassigned |
1
0 |
| 2.7.7.23 | Hepatitis B |
31204557 |
Glucosamine promotes hepatitis B virus replication through its dual effects in suppressing autophagic degradation and inhibiting MTORC1 signaling. |
diagnostic usage
unassigned |
3
0 |
| 2.7.7.23 | Infections |
26489015 |
Depletion of M. tuberculosis GlmU from Infected Murine Lungs Effects the Clearance of the Pathogen. |
causal interaction
ongoing research
therapeutic application
unassigned |
2
2
4
0 |
| 2.7.7.23 | Influenza, Human |
31204557 |
Glucosamine promotes hepatitis B virus replication through its dual effects in suppressing autophagic degradation and inhibiting MTORC1 signaling. |
diagnostic usage
unassigned |
3
0 |
| 2.7.7.23 | Neoplasms |
33269005 |
Expression and Bioinformatics-Based Functional Analysis of UAP1 in Lung Adenocarcinoma. |
ongoing research
unassigned |
2
0 |
| 2.7.7.23 | Prostatic Neoplasms |
25241896 |
UAP1 is overexpressed in prostate cancer and is protective against inhibitors of N-linked glycosylation. |
diagnostic usage
unassigned |
3
0 |
| 2.7.7.23 | Trypanosomiasis, African |
23834437 |
A Novel Allosteric Inhibitor of the Uridine Diphosphate N-Acetylglucosamine Pyrophosphorylase from Trypanosoma brucei. |
therapeutic application
unassigned |
1
0 |
| 2.7.7.23 | Tuberculosis |
18573680 |
Expression, essentiality, and a microtiter plate assay for mycobacterial GlmU, the bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase. |
causal interaction
ongoing research
therapeutic application
unassigned |
3
2
4
0 |
