EC Number |
Disease |
PubMed ID |
Title of Publication |
Category |
Confidence Level |
---|
3.4.21.B12 | Carcinoma |
28743213 |
Kallikrein-related peptidase 4 contributes to the tumor metastasis of oral squamous cell carcinoma. |
causal interaction unassigned |
4 0 |
3.4.21.B12 | Neoplasms |
18308730 |
Kallikrein-related peptidase 4 (KLK4) initiates intracellular signaling via protease-activated receptors (PARs). KLK4 and PAR-2 are co-expressed during prostate cancer progression. |
causal interaction unassigned |
2 0 |
3.4.21.B12 | Neoplasms |
28743213 |
Kallikrein-related peptidase 4 contributes to the tumor metastasis of oral squamous cell carcinoma. |
causal interaction unassigned |
4 0 |
3.4.21.B12 | Neoplasms |
31829025 |
MiR-378a-5p inhibits angiogenesis of oral squamous cell carcinoma by targeting KLK4. |
causal interaction unassigned |
4 0 |
3.4.21.B12 | Neoplasms |
32400148 |
Kallikrein-related peptidase 4 promotes migration and invasion of endometrial stromal cells in endometriosis by inducing epithelial-mesenchymal transition. |
causal interaction ongoing research unassigned |
4 4 0 |
3.4.21.B12 | Neoplasms |
34373558 |
A KLK4 proteinase substrate capture approach to antagonize PAR1. |
causal interaction unassigned |
3 0 |
3.4.21.B12 | Pancreatic Neoplasms |
26546433 |
PRSS1 mutations and the proteinase/antiproteinase imbalance in the pathogenesis of pancreatic cancer. |
causal interaction diagnostic usage ongoing research unassigned |
4 4 3 0 |
3.4.21.B12 | Prostatic Neoplasms |
18308730 |
Kallikrein-related peptidase 4 (KLK4) initiates intracellular signaling via protease-activated receptors (PARs). KLK4 and PAR-2 are co-expressed during prostate cancer progression. |
causal interaction unassigned |
2 0 |
3.4.21.B12 | Prostatic Neoplasms |
19549601 |
Substrate-guided design of a potent and selective kallikrein-related peptidase inhibitor for kallikrein 4. |
causal interaction therapeutic application unassigned |
3 4 0 |
3.4.21.B12 | Prostatic Neoplasms |
21556330 |
Mastering the canonical loop of serine protease inhibitors: enhancing potency by optimising the internal hydrogen bond network. |
causal interaction therapeutic application unassigned |
3 4 0 |