Targeting presenilin-type aspartic protease signal peptide peptidase with gamma-secretase inhibitors. - Wikidata - wikimedia - TriplyDB

Targeting presenilin-type aspartic protease signal peptide peptidase with gamma-secretase inhibitors.

Targeting presenilin-type aspartic protease signal peptide peptidase with gamma-secretase inhibitors.

http://www.wikidata.org/entity/Q44350630

about

A gamma-secretase-like intramembrane cleavage of TNFalpha by the GxGD aspartyl protease SPPL2b SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 production Human CRB2 inhibits gamma-secretase cleavage of amyloid precursor protein by binding to the presenilin complex Intramembrane processing by signal peptide peptidase regulates the membrane localization of hepatitis C virus core protein and viral propagation Targeting γ-secretase in breast cancer Toward the structure of presenilin/γ-secretase and presenilin homologs Core protein cleavage by signal peptide peptidase is required for hepatitis C virus-like particle assembly Requirement of the proteasome for the trimming of signal peptide-derived epitopes presented by the nonclassical major histocompatibility complex class I molecule HLA-E An internal signal sequence directs intramembrane proteolysis of a cellular immunoglobulin domain protein A C-terminal region of signal peptide peptidase defines a functional domain for intramembrane aspartic protease catalysis Identification of an archaeal presenilin-like intramembrane protease Differential Inhibition of Signal Peptide Peptidase Family Members by Established γ-Secretase Inhibitors Gamma-secretase composed of PS1/Pen2/Aph1a can cleave notch and amyloid precursor protein in the absence of nicastrin Cellular functions of gamma-secretase-related proteins.A small molecule inhibitor of signal peptide peptidase inhibits Plasmodium development in the liver and decreases malaria severity.γ-Secretase Inhibitors and Modulators Induce Distinct Conformational Changes in the Active Sites of γ-Secretase and Signal Peptide Peptidase Inhibitors of signal peptide peptidase (SPP) affect HSV-1 infectivity in vitro and in vivo.Foamy virus envelope protein is a substrate for signal peptide peptidase-like 3 (SPPL3).Structure, mechanism and inhibition of gamma-secretase and presenilin-like proteases Targeting the ERAD pathway via inhibition of signal peptide peptidase for antiparasitic therapeutic design Drosophila signal peptide peptidase is an essential protease for larval development.Visualizing active enzyme complexes using a photoreactive inhibitor for proximity ligation--application on γ-secretase.A role for Notch signaling in trophoblast endovascular invasion and in the pathogenesis of pre-eclampsia.Three-dimensional structure of the signal peptide peptidase Mechanisms of hepatitis C virus infection.Membrane proteases in the bacterial protein secretion and quality control pathway.Presenilin function and gamma-secretase activity.Protease inhibitors as potential disease-modifying therapeutics for Alzheimer's disease.Current experimental therapy for Alzheimer's disease TRC8-dependent degradation of hepatitis C virus immature core protein regulates viral propagation and pathogenesis Distinct pharmacological effects of inhibitors of signal peptide peptidase and gamma-secretase.Substrate specificity of gamma-secretase and other intramembrane proteases.Intraneuronal aggregation of the β-CTF fragment of APP (C99) induces Aβ-independent lysosomal-autophagic pathology.Intramembrane proteolysis Presenilins: members of the gamma-secretase quartets, but part-time soloists too.Presenilins, Notch dose control the fate of pancreatic endocrine progenitors during a narrow developmental window.Intramembrane proteolysis by signal peptide peptidases: a comparative discussion of GXGD-type aspartyl proteases.Pigment epithelium-derived factor maintains retinal pigment epithelium function by inhibiting vascular endothelial growth factor-R2 signaling through gamma-secretase Plasmodium falciparum signal peptide peptidase is a promising drug target against blood stage malaria.Structural biology of presenilins and signal peptide peptidases.

P2860

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P2860

Targeting presenilin-type aspartic protease signal peptide peptidase with gamma-secretase inhibitors.

http://www.wikidata.org/entity/Q44350630

description

2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

@wuu

2003年学术文章

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2003年学术文章

@zh-cn

2003年学术文章

@zh-hans

2003年学术文章

@zh-my

2003年学术文章

@zh-sg

2003年學術文章

@yue

2003年學術文章

@zh-hant

name

Targeting presenilin-type aspa ...... th gamma-secretase inhibitors.

@en

Targeting presenilin-type aspa ...... th gamma-secretase inhibitors.

@nl

type

label

Targeting presenilin-type aspa ...... th gamma-secretase inhibitors.

@en

Targeting presenilin-type aspa ...... th gamma-secretase inhibitors.

@nl

prefLabel

Targeting presenilin-type aspa ...... th gamma-secretase inhibitors.

@en

Targeting presenilin-type aspa ...... th gamma-secretase inhibitors.

@nl

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Journal of Biological Chemistry

P1476

Targeting presenilin-type aspa ...... th gamma-secretase inhibitors.

@en

P2093

Albert Schmitz

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Andreas Weihofen

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Bruno Martoglio

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Elena Friedmann

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Giorgio Rovelli

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Heinrich Rueeger

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Paolo Paganetti

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16528-16533

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scholarly article

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10.1074/JBC.M301372200

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19

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278

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Marius K Lemberg

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2003-03-05T00:00:00Z

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12621027

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