CPQ, carboxypeptidase Q, 10404

N. diseases: 87; N. variants: 1
Disease: Primary malignant neoplasm ×
Source: ALL
Disease Score gda Association Type Type Original DB Sentence supporting the association PMID PMID Year
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm 		0.050 Biomarker group BEFREE It is the only known aminopeptidase in the family and is reported to be involved in cancer and other major diseases. 30044821 2018
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm 		0.050 Biomarker group BEFREE These properties suggested that Ec-LDP-TRAIL and Ec-LDP-TRAIL-AE may be promising candidates for targeted cancer therapy. 25122444 2015
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm 		0.050 Biomarker group BEFREE This review focuses on the function and subcellular location of five key aminopeptidases (aminopeptidase N, leucine aminopeptidase, puromycin-sensitive aminopeptidase, leukotriene A4 hydrolase and endoplasmic reticulum aminopeptidase 1/2) and their association with different diseases, in particular cancer and their current position as target for therapeutic intervention by aminopeptidase inhibitors. 24385243 2014
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm 		0.050 Biomarker group BEFREE This metallo-aminopeptidase has been identified as a potential target for cancer chemotherapy. 23428964 2013
CUI: C1306459
Disease: Primary malignant neoplasm
Primary malignant neoplasm 		0.050 Biomarker group BEFREE The potential efficacy of hlFVII-LDP-AE for cancer therapy was examined in vitro by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assays and in vivo with a BALB/c nude mouse xenograft model of the human lung cancer line NCI-H292. hlFVII-LDP-AE caused chromatin condensation and cleavage of genomic DNA in NCI-H292 cells. 22108624 2012