Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway
about
Familial Alzheimer disease-linked mutations specifically disrupt Ca2+ leak function of presenilin 1Protease regulation: the Yin and Yang of neural development and diseaseEarly etiology of Alzheimer's disease: tipping the balance toward autophagy or endosomal dysfunction?The crystal structure of GXGD membrane protease FlaKStructural investigation of the C-terminal catalytic fragment of presenilin 1Transmembrane topology and signal peptide prediction using dynamic bayesian networksChanged membrane integration and catalytic site conformation are two mechanisms behind the increased Aβ42/Aβ40 ratio by presenilin 1 familial Alzheimer-linked mutations.Assembly, maturation, and trafficking of the gamma-secretase complex in Alzheimer's disease.Signal peptide peptidase and its homologs in Arabidopsis thaliana--plant tissue-specific expression and distinct subcellular localization.The large hydrophilic loop of presenilin 1 is important for regulating gamma-secretase complex assembly and dictating the amyloid beta peptide (Abeta) Profile without affecting Notch processing.Novel presenilin 1 variant (P117A) causing Alzheimer's disease in the fourth decade of life.Mutagenesis mapping of the presenilin 1 calcium leak conductance pore.Quantitative proteomic analysis of mitochondria in aging PS-1 transgenic mice.Role of presenilins in neuronal calcium homeostasisRegulation of Ca2+ signaling with particular focus on mast cells.Presenilin is necessary for efficient proteolysis through the autophagy-lysosome system in a γ-secretase-independent manner.Sorting nexin 27 regulates Aβ production through modulating γ-secretase activity.Polyphenols as therapeutic molecules in Alzheimer's disease through modulating amyloid pathways.Generation and characterization of monoclonal antibodies specific to Drosophila presenilin.Putting presenilins centre stage. Introduction to the Talking Point on the role of presenilin mutations in Alzheimer disease.Presenilins and γ-secretase: structure, function, and role in Alzheimer Disease.Lack of evidence for presenilins as endoplasmic reticulum Ca2+ leak channelsThe topology of pen-2, a γ-secretase subunit, revisited: evidence for a reentrant loop and a single pass transmembrane domain.Lysosomal calcium homeostasis defects, not proton pump defects, cause endo-lysosomal dysfunction in PSEN-deficient cells.Effect of Presenilin Mutations on APP Cleavage; Insights into the Pathogenesis of FADInteractome analyses of mature γ-secretase complexes reveal distinct molecular environments of presenilin (PS) paralogs and preferential binding of signal peptide peptidase to PS2.Global topology analysis of pancreatic zymogen granule membrane proteins.Histopathological and molecular heterogeneity among individuals with dementia associated with Presenilin mutationsSubstrate specificity of gamma-secretase and other intramembrane proteases.Structural and Functional Determinants of gamma-Secretase, an Intramembrane Protease Implicated in Alzheimer's Disease.Toward structural elucidation of the gamma-secretase complex.Familial Alzheimer's disease mutations in presenilins: effects on endoplasmic reticulum calcium homeostasis and correlation with clinical phenotypes.Molecular genetics of Alzheimer's disease: an update.Presenilin: RIP and beyond.Presenilins: members of the gamma-secretase quartets, but part-time soloists too.Golgi function and dysfunction in the first COG4-deficient CDG type II patientMutations in amyloid precursor protein affect its interactions with presenilin/gamma-secretase.Protein quality control by Rer1p in the early secretory pathway: from mechanism to implication in Alzheimer's disease.Control of intracellular calcium signaling as a neuroprotective strategyPresenilins function in ER calcium leak and Alzheimer's disease pathogenesis.
P2860
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P2860
Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway
description
2006 nî lūn-bûn
@nan
2006 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
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2006年学术文章
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2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
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2006年学术文章
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2006年學術文章
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name
Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway
@ast
Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway
@en
Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway
@nl
type
label
Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway
@ast
Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway
@en
Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway
@nl
prefLabel
Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway
@ast
Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway
@en
Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway
@nl
P2093
P2860
P356
P1476
Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway
@en
P2093
Alexandra Tolia
Dragana Spasic
Katleen Dillen
Stefan Vrijens
Veerle Baert
Wim Annaert
P2860
P304
P356
10.1074/JBC.M600592200
P407
P577
2006-09-08T00:00:00Z