EC Number   |
Application |
Reference |
|---|
   3.4.23.B24 | analysis |
application of the photophore walking technique for probing the active sites of SPP. Nontransition state gamma-secretase inhibitors inhibit labeling of gamma-secretase by activity-based probes but enhance labeling of SPP. The opposite is true of gamma secretase modulators, which have little effect on the labeling of gamma-secretase but diminish labeling of SPP |
732987 |
| 3.4.23.B24 | medicine |
herpes simplex virus type 1 glycoprotein specifically binds to signal peptide peptidase SPP. SPP dominant negative mutants and shRNA against SPP significantly reduce herpes simplex virus type 1 replication in vitro. SPP also affects lysosomes and endoplasmic reticulum responses to herpes simplex virus type 1 infection |
735133 |
| 3.4.23.B24 | medicine |
malaria heat shock protein 101 is a substrate, and partial inhibition of Plasmodium falciparum signal peptide peptidase correlates with the emergence of gametocytes |
733269 |
| 3.4.23.B24 | medicine |
signal peptide peptidase SPP catalyzes the intramembrane cleavage of heme oxygenase HO-1. Coexpression of HO-1 with wild-type SPP promotes the nuclear localization of HO-1 in cells. Two adjacent intramembrane cleavage sites are located after S275 and F276 within the trans membrane segment. Mutations of S275F276 to A275L276 significantly hinder SPP-mediated cleavage and nuclear localization. Nuclear heme oxygenase-1 is detected in A549 and DU145 cancer cell lines expressing high levels of endogenous HO-1 and SPP. SPP knockdown or inhibition significantly reduces nuclear HO-1 localization in A549 and DU145 cells. The positive nuclear HO-1 stain is also evident in lung cancer tissues expressing high levels of HO-1 and SPP. Overexpression of a truncated HO-1 lacking the trans membrane segment in HeLa and H1299 cells promotes cell proliferation and migration/invasion |
734814 |
| 3.4.23.B24 | medicine |
specific inhibition of distinct SPP/SPPL proteases is proposed as a therapeutic concept e.g. for the treatment of autoimmunity and viral or protozoal infections |
752819 |
| 3.4.23.B24 | medicine |
specific inhibition of distinct SPP/SPPL proteases is proposed as a therapeutic concept e.g. for the treatment of autoimmunity and viral or protozoal infections. Scheme for potential applications of SPPL2a inhibitors, overview |
752819 |
| 3.4.23.B24 | medicine |
the signal peptide peptidase hSPP is a biomedically important protease implicated as therapeutic target for hepatitis C |
755089 |
| 3.4.23.B24 | medicine |
the signal peptide peptidase pSPP is a biomedically important protease implicated as therapeutic target for treatement of Plasmodia and malaria |
755089 |
| 3.4.23.B24 | medicine |
the signal peptide peptidase SPPL2a is a biomedically important protease implicated as therapeutic target for B-cell immunomodulation and neoplasia |
755089 |
| 3.4.23.B24 | pharmacology |
mechanism of SPP inhibitors in Plasmodium falciparum, overview. PlSPP is an attractive target for the treatment of malaria |
752819 |
