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Disease on EC 3.4.23.B24 - signal peptide peptidase

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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Alzheimer Disease
Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins.
Signal peptide peptidase dependent cleavage of type II transmembrane substrates releases intracellular and extracellular signals.
Breast Neoplasms
Intramembrane proteolysis of an extracellular serine protease, epithin/PRSS14, enables its intracellular nuclear function.
Carcinoma, Hepatocellular
A small molecule inhibitor of signal Peptide peptidase inhibits Plasmodium development in the liver and decreases malaria severity.
Classical Swine Fever
Core protein of pestiviruses is processed at the C terminus by signal peptide peptidase.
Dehydration
Physiological and molecular responses for long term salinity stress in common fig (Ficus carica L.).
Dementia
The ?-Helical Content of the Transmembrane Domain of the British Dementia Protein-2 (Bri2) Determines Its Processing by Signal Peptide Peptidase-like 2b (SPPL2b).
Glioblastoma
Signal Peptide Peptidase, Encoded by HM13, Contributes to Tumor Progression by Affecting EGFRvIII Secretion Profiles in Glioblastoma.
Hepatitis C
Characterization of SPP inhibitors suppressing propagation of HCV and protozoa.
Characterization of the cleavage of signal peptide at the C-terminus of hepatitis C virus core protein by signal peptide peptidase.
Core protein cleavage by signal peptide peptidase is required for hepatitis C virus-like particle assembly.
Efficient cleavage by signal peptide peptidase requires residues within the signal peptide between the core and E1 proteins of hepatitis C virus strain J1.
Hepatitis C virus core protein: carboxy-terminal boundaries of two processed species suggest cleavage by a signal peptide peptidase.
Hepatitis C virus modulates signal peptide peptidase to alter host protein processing.
Intramembrane processing by signal peptide peptidase regulates the membrane localization of hepatitis C virus core protein and viral propagation.
Maturation of hepatitis C virus core protein by signal peptide peptidase is required for virus production.
Membrane binding properties and terminal residues of the mature hepatitis C virus capsid protein in insect cells.
Sequential processing of hepatitis C virus core protein by host cell signal peptidase and signal peptide peptidase: a reassessment.
Signal peptide peptidase dependent cleavage of type II transmembrane substrates releases intracellular and extracellular signals.
Signal peptide peptidase promotes the formation of hepatitis C virus non-enveloped particles and is captured on the viral membrane during assembly.
Structural analysis of hepatitis C virus core-E1 signal peptide and requirements for cleavage of the genotype 3a signal sequence by signal peptide peptidase.
The potential of signal peptide peptidase as a therapeutic target for hepatitis C.
Herpes Simplex
Inhibitors of signal peptide peptidase (SPP) affect HSV-1 infectivity in vitro and in vivo.
Infections
HIV protease inhibitors block parasite signal peptide peptidases and prevent growth of Babesia microti parasites in erythrocytes.
Plasmodium falciparum signal peptide peptidase cleaves malaria heat shock protein 101 (HSP101). Implications for gametocytogenesis.
Signal Peptide Peptidase Cleavage of GB Virus B Core Protein Is Required for Productive Infection in Vivo.
Signal peptide peptidase dependent cleavage of type II transmembrane substrates releases intracellular and extracellular signals.
Malaria
A small molecule inhibitor of signal Peptide peptidase inhibits Plasmodium development in the liver and decreases malaria severity.
HIV protease inhibitors block parasite signal peptide peptidases and prevent growth of Babesia microti parasites in erythrocytes.
Intramembrane proteolytic cleavage by human signal peptide peptidase like 3 and malaria signal peptide peptidase.
Malaria Parasite Signal Peptide Peptidase is an ER-Resident Protease Required for Growth but not for Invasion.
Plasmodium falciparum signal peptide peptidase cleaves malaria heat shock protein 101 (HSP101). Implications for gametocytogenesis.
Plasmodium falciparum signal peptide peptidase is a promising drug target against blood stage malaria.
Neoplasms
A gamma-secretase-like intramembrane cleavage of TNFalpha by the GxGD aspartyl protease SPPL2b.
Intramembrane proteolysis of GXGD-type aspartyl proteases is slowed by a familial Alzheimer disease-like mutation.
Novel biomarkers of mercury-induced autoimmune dysfunction: a cross-sectional study in Amazonian Brazil.
Recent Advances in Lung Cancer Immunotherapy: Input of T-Cell Epitopes Associated With Impaired Peptide Processing.
Signal peptide peptidase promotes tumor progression via facilitating FKBP8 degradation.
Signal Peptide Peptidase, Encoded by HM13, Contributes to Tumor Progression by Affecting EGFRvIII Secretion Profiles in Glioblastoma.
SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 production.
Parkinson Disease
STK39, But Not BST1, HLA-DQB1, and SPPL2B Polymorphism, Is Associated With Han-Chinese Parkinson's Disease in Taiwan.
Virus Diseases
Signal Peptide Peptidase Cleavage of GB Virus B Core Protein Is Required for Productive Infection in Vivo.