EC Number   |
Application |
Reference |
|---|
   3.4.17.22 | medicine |
CpD is part of an autoregulatory feedback loop in which it is both upstream and downstream of transforming growth factor-beta signaling |
683703 |
| 3.4.17.22 | medicine |
CpD is part of the transforming growth factor-beta pathway and is dysregulated in patients with Lupus erythematosus and other autoimmune diseases |
683703 |
| 3.4.17.22 | medicine |
CpD is significantly downregulated in CD14 positive cells isolated from patients with lupus erythematosus. Moreover, it is shown that downregulation of CpD leads to downmodulation of TGF-beta itself, suggesting a role for CpD in a positive feedback loop, providing further evidence for a role of this enzyme in lupus erythematosus |
683703 |
| 3.4.17.22 | medicine |
CPD, nitrotyrosine, and proliferation marker Ki67 levels are higher in prostate cancer than in benign tissue and tend to colocalize, along with phospho-Stat5. The CPD-Arg-NO pathway may be involved in the regulation of prostate cancer cell proliferation |
755287 |
| 3.4.17.22 | medicine |
CPE, probably in combination with CPD, has a functional role in normal placental development, specifically in control of giant cell and glycogen cell growth. In addition, Cpe together with Cpd is an upstream determinant of interspecies hybrid placental dysplasia, whose lack produces placental phenotypes reminiscent of interspecies hybrid placental dysplasia. Pathways regulated by these enzymes are not only important in placentation, but potentially also for speciation in the genus Mus |
683398 |
| 3.4.17.22 | medicine |
essential for duck hepatitis B virus infection. PreS-induced CPD conformational changes may play an important role in the fusion of the viral and cellular membrane |
684108 |
| 3.4.17.22 | medicine |
for duck hepatitis B virus and probably all other avian hepadnaviruses, carboxypeptidase D (CPD) is shown to be indispensable for infection. The striking correlation of the infection competition activity of duck hepatitis B virus-preS polypeptides with their ability to bind duck carboxypeptidase D suggests that it is this molecule which is addressed and inactivated at the surface of hepatocytes |
684108 |
| 3.4.17.22 | medicine |
for infection of primary duck hepatocytes with duck hepatitis B virus, binding of the pre-S domain of the large surface protein to the cellular glycoprotein gp180 as a ubiquitous carboxypeptidase is required |
688729 |
| 3.4.17.22 | medicine |
is not involved in hepatitis B virus infection |
684108 |
| 3.4.17.22 | medicine |
knocking out CpD gene expression provides one solution to eliminating C-terminal lysine heterogeneity for therapeutic antibody production |
753046 |
