3.4.23.B24: signal peptide peptidase
This is an abbreviated version!
For detailed information about signal peptide peptidase, go to the full flat file.
Word Map on EC 3.4.23.B24
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3.4.23.B24
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aspartyl
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presenilins
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intramembrane-cleaving
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gamma-secretase
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sppl2a
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medicine
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gxgd-type
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spp-mediated
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bri2
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i-clips
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presenilin-like
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site-2
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pharmacology
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analysis
- 3.4.23.B24
-
aspartyl
-
presenilins
-
intramembrane-cleaving
- gamma-secretase
- sppl2a
- medicine
-
gxgd-type
-
spp-mediated
- bri2
- i-clips
-
presenilin-like
-
site-2
- pharmacology
- analysis
Reaction
intramembrane cleavage of signal peptides =
Synonyms
ANID_08681, aspartic intramembrane protease, Hm13, hSPP, minor histocompatibility antigen H13, PF3D7_1457000, PlSPP, signal peptide peptidase like 2a, signal peptide peptidase-like 2a, signal peptide peptidase-like 2B, signal peptide peptidase-like 2C, signal peptide peptidase-like 3, SPP, SPP-like 2A, SPP-like 2B, SPP-like 2C, SPP-like 3, SPP1, SppA, SPPL, SPPL2a, SPPL2b, SPPL2c, UMAG_02729
ECTree
3.4.23.B24 signal peptide peptidaseAdvanced search results
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Application on EC 3.4.23.B24 - signal peptide peptidase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
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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
medicine
pharmacology
mechanism of SPP inhibitors in Plasmodium falciparum, overview. PlSPP is an attractive target for the treatment of malaria
medicine
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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
medicine
malaria heat shock protein 101 is a substrate, and partial inhibition of Plasmodium falciparum signal peptide peptidase correlates with the emergence of gametocytes
medicine
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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
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
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
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
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
medicine
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the signal peptide peptidase hSPP is a biomedically important protease implicated as therapeutic target for hepatitis C
medicine
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the signal peptide peptidase pSPP is a biomedically important protease implicated as therapeutic target for treatement of Plasmodia and malaria
medicine
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the signal peptide peptidase SPPL2a is a biomedically important protease implicated as therapeutic target for B-cell immunomodulation and neoplasia
