EC Number   |
Application |
Reference |
|---|
   2.3.2.26 | analysis |
application of ubiquitin-activity-based probes such as ubiquitin-vinyl methylester, ubiquitin-propargylamide to label HECT domains. E2-Ub-activity-based probes can label the catalytic HECT domains of NEDD4, UBE3C, and HECTD1 |
756451 |
| 2.3.2.26 | analysis |
development of ubiquitin variants that inhibit or activate HECT E3 enzymes. Ubiquitin variant inhibitors block the E2-binding site, and activators occupy a ubiquitin-binding exosite. Ubiquitin variants reveal regulation mechanisms among NEDD4 subfamily HECTs and are useful for modulating therapeutically relevant targets of HECT E3s in cells and intestinal organoids. Ubiquitin variant activators bind to the N-lobe exosite and differentially modulate related HECT E3 ligases |
757655 |
| 2.3.2.26 | medicine |
antidepressant drug clomipramine specifically blocks ITCH auto-ubiquitylation, as well as p73 ubiquitylation. Treating a panel of breast, prostate and bladder cancer cell lines with clomipramine, or its homologs, leads to reduced cancer cell growth, and synergize with gemcitabine or mitomycin in killing cancer cells by blocking autophagy |
733627 |
| 2.3.2.26 | medicine |
functional interaction of NEDD4-like ubiquitin protein ligase NEDL1 with p53 might contribute to the induction of apoptosis in cancerous cells bearing wild-type p53 |
694490 |
| 2.3.2.26 | medicine |
high-risk human papilloma virus E6 oncoproteins interact with the ubiquitin ligase E6AP and target several cellular proteins, including p53 and proteins of the MAGI family, towards ubiquitin-mediated degradation. E6 oncoproteins from major high-risk risk human papilloma virus types 16, 18, 33 and 58 bind to a 15-mer peptide containing the LxxphiLsh motif of E6AP, where L indicates conserved leucine residues, phi is a hydrophobic residue, h is an amino acid residue with a side-chain capable of accepting hydrogen bonds, s represents a small amino acid residue and xx is a dipeptide where one of the residues is Asp, Asn, Glu or Gln. The equilibrium dissociation constants are in the low micromolar range. Low-risk risk human papilloma virus 11 E6 does not interact with E6AP. The two zinc-binding domains of E6 are required for E6AP recognition |
728134 |
| 2.3.2.26 | synthesis |
construcution of a soluble HECT domain truncation of isoform WWP2 which is amendable for preparation scale expression in Escherichia coli. A relatively simple purification process achieves highly pure protein by employing immobilized metal-affinity chromatography followed by salting out, ion exchange chromatography and finally, size exclusion chromatography. Procedure allows to obtain about 60 mg/L of the soluble protein |
735207 |
