Intramembrane-cleaving aspartic proteases and disease: presenilins, signal peptide peptidase and their homologs
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SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 productionThe Fas ligand intracellular domain is released by ADAM10 and SPPL2a cleavage in T-cellsSubstrate requirements for SPPL2b-dependent regulated intramembrane proteolysisγ-Secretase inhibitors and modulators.Structural biology of presenilin 1 complexesPlasmodium falciparum signal peptide peptidase cleaves malaria heat shock protein 101 (HSP101). Implications for gametocytogenesisSignal peptide peptidase is required for dislocation from the endoplasmic reticulumBACE1 and presenilin: two unusual aspartyl proteases involved in Alzheimer's diseaseAn internal signal sequence directs intramembrane proteolysis of a cellular immunoglobulin domain proteinA C-terminal region of signal peptide peptidase defines a functional domain for intramembrane aspartic protease catalysisAssembly, maturation, and trafficking of the gamma-secretase complex in Alzheimer's disease.Identification of cellular genes affecting the infectivity of foot-and-mouth disease virus.Cryoelectron microscopy structure of purified gamma-secretase at 12 A resolution.An update on the amyloid hypothesis.A presenilin-1 mutation identified in familial Alzheimer disease with cotton wool plaques causes a nearly complete loss of gamma-secretase activityCrystal structure of the γ-secretase component nicastrin.Mechanism of intramembrane proteolysis investigated with purified rhomboid proteases.Structure of gamma-secretase and its trimeric pre-activation intermediate by single-particle electron microscopy.A snapshot of the Ixodes scapularis degradomeMembrane-embedded protease poses for photoshoot.Moonlighting activity of presenilin in plants is independent of gamma-secretase and evolutionarily conserved.Membrane proteases in the bacterial protein secretion and quality control pathway.Genetic and molecular aspects of Alzheimer's disease shed light on new mechanisms of transcriptional regulation.Presenilin function and gamma-secretase activity.Signal peptide peptidases and gamma-secretase: cousins of the same protease family?Interactome analyses of mature γ-secretase complexes reveal distinct molecular environments of presenilin (PS) paralogs and preferential binding of signal peptide peptidase to PS2.Studies of the role of ubiquitination in the interaction of ubiquilin with the loop and carboxyl terminal regions of presenilin-2Substrate specificity of gamma-secretase and other intramembrane proteases.Structural and Functional Determinants of gamma-Secretase, an Intramembrane Protease Implicated in Alzheimer's Disease.Presenilins: members of the gamma-secretase quartets, but part-time soloists too.Intramembrane proteolysis by signal peptide peptidases: a comparative discussion of GXGD-type aspartyl proteases.Identification of candidate cancer-causing genes in mouse brain tumors by retroviral taggingSignal peptide peptidase (SPP) dimer formation as assessed by fluorescence lifetime imaging microscopy (FLIM) in intact cells.Interleukin-1 receptor type 1 is a substrate for gamma-secretase-dependent regulated intramembrane proteolysis.Maturation of hepatitis C virus core protein by signal peptide peptidase is required for virus production.Self-organizing molecular fingerprints: a ligand-based view on drug-like chemical space and off-target prediction.Signal peptide peptidase and gamma-secretase share equivalent inhibitor binding pharmacology.C-terminal PAL motif of presenilin and presenilin homologues required for normal active site conformation.Signal peptide peptidase-catalyzed cleavage of hepatitis C virus core protein is dispensable for virus budding but destabilizes the viral capsid.Signal peptide peptidase cleavage of GB virus B core protein is required for productive infection in vivo.
P2860
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P2860
Intramembrane-cleaving aspartic proteases and disease: presenilins, signal peptide peptidase and their homologs
description
2003 nî lūn-bûn
@nan
2003 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Intramembrane-cleaving asparti ...... e peptidase and their homologs
@ast
Intramembrane-cleaving asparti ...... e peptidase and their homologs
@en
Intramembrane-cleaving asparti ...... e peptidase and their homologs
@nl
type
label
Intramembrane-cleaving asparti ...... e peptidase and their homologs
@ast
Intramembrane-cleaving asparti ...... e peptidase and their homologs
@en
Intramembrane-cleaving asparti ...... e peptidase and their homologs
@nl
prefLabel
Intramembrane-cleaving asparti ...... e peptidase and their homologs
@ast
Intramembrane-cleaving asparti ...... e peptidase and their homologs
@en
Intramembrane-cleaving asparti ...... e peptidase and their homologs
@nl
P356
P1476
Intramembrane-cleaving asparti ...... e peptidase and their homologs
@en
P2093
Bruno Martoglio
Todd E Golde
P304
P356
10.1093/HMG/DDG303
P407
P478
12 Spec No 2
P577
2003-10-15T00:00:00Z