Presenilin-1, nicastrin, amyloid precursor protein, and gamma-secretase activity are co-localized in the lysosomal membrane
about
AIP4/Itch regulates Notch receptor degradation in the absence of ligandThe Amyloid Precursor Protein is rapidly transported from the Golgi apparatus to the lysosome and where it is processed into beta-amyloid.PAR-4 is involved in regulation of beta-secretase cleavage of the Alzheimer amyloid precursor proteinThe cholesterol transporter ABCG1 modulates the subcellular distribution and proteolytic processing of beta-amyloid precursor proteinThe proteome of lysosomesDecreased CALM expression reduces Aβ42 to total Aβ ratio through clathrin-mediated endocytosis of γ-secretaseThe tetraspanin CD63 regulates ESCRT-independent and -dependent endosomal sorting during melanogenesisSyntaxin 5 interacts with presenilin holoproteins, but not with their N- or C-terminal fragments, and affects beta-amyloid peptide productionAssociation of gamma-secretase with lipid rafts in post-Golgi and endosome membranes.Lipoprotein receptors and cholesterol in APP trafficking and proteolytic processing, implications for Alzheimer's diseaseLinking lipids, Alzheimer's and LXRs?Targeting Notch to overcome radiation resistanceLysosomal membrane proteins and their central role in physiologyMIiSR: Molecular Interactions in Super-Resolution Imaging Enables the Analysis of Protein Interactions, Dynamics and Formation of Multi-protein StructuresDevelopment of nanoparticles incorporating a novel liposomal membrane destabilization peptide for efficient release of cargos into cancer cellsLigand binding and calcium influx induce distinct ectodomain/gamma-secretase-processing pathways of EphB2 receptorProteolytic processing of Alzheimer's β-amyloid precursor proteinAssembly, trafficking and function of gamma-secretaseDegradative organelles containing mislocalized alpha-and beta-synuclein proliferate in presenilin-1 null neuronsABCA2 is a marker of neural progenitors and neuronal subsets in the adult rodent brainPresenilin 1 mediates the turnover of telencephalin in hippocampal neurons via an autophagic degradative pathwayTargeting the γ-/β-secretase interaction reduces β-amyloid generation and ameliorates Alzheimer's disease-related pathogenesisEndocytosis and signalling: intertwining molecular networksRapid and direct transport of cell surface APP to the lysosome defines a novel selective pathway.Arf6 controls beta-amyloid production by regulating macropinocytosis of the Amyloid Precursor Protein to lysosomesPresenilin 1 and Presenilin 2 Target γ-Secretase Complexes to Distinct Cellular Compartments.Assembly, maturation, and trafficking of the gamma-secretase complex in Alzheimer's disease.Synaptic and endosomal localization of active gamma-secretase in rat brain.Membrane localization of beta-amyloid 1-42 in lysosomes: a possible mechanism for lysosome labilizationGamma-secretase subunits associate in intracellular membrane compartments in Arabidopsis thaliana.The vacuolar ATPase is required for physiological as well as pathological activation of the Notch receptorCellular distribution of gamma-secretase subunit nicastrin in the developing and adult rat brains.The cell giveth and the cell taketh away: an overview of Notch pathway activation by endocytic trafficking of ligands and receptorsPapillomavirus infection requires gamma secretase.Phosphorylation of nicastrin by SGK1 leads to its degradation through lysosomal and proteasomal pathways.An early specific cell-cell interaction occurs in the production of beta-amyloid in cell cultures.Mitochondrial dysfunction and cellular metabolic deficiency in Alzheimer's diseaseThe low density lipoprotein receptor-related protein 1B retains beta-amyloid precursor protein at the cell surface and reduces amyloid-beta peptide production.Presenilin is necessary for efficient proteolysis through the autophagy-lysosome system in a γ-secretase-independent manner.Endocytic regulation of notch signalling during development.
P2860
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P2860
Presenilin-1, nicastrin, amyloid precursor protein, and gamma-secretase activity are co-localized in the lysosomal membrane
description
2003 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2003
@ast
im Juli 2003 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2003/07/18)
@sk
vědecký článek publikovaný v roce 2003
@cs
wetenschappelijk artikel (gepubliceerd op 2003/07/18)
@nl
наукова стаття, опублікована в липні 2003
@uk
name
Presenilin-1, nicastrin, amylo ...... ized in the lysosomal membrane
@ast
Presenilin-1, nicastrin, amylo ...... ized in the lysosomal membrane
@en
Presenilin-1, nicastrin, amylo ...... ized in the lysosomal membrane
@nl
type
label
Presenilin-1, nicastrin, amylo ...... ized in the lysosomal membrane
@ast
Presenilin-1, nicastrin, amylo ...... ized in the lysosomal membrane
@en
Presenilin-1, nicastrin, amylo ...... ized in the lysosomal membrane
@nl
prefLabel
Presenilin-1, nicastrin, amylo ...... ized in the lysosomal membrane
@ast
Presenilin-1, nicastrin, amylo ...... ized in the lysosomal membrane
@en
Presenilin-1, nicastrin, amylo ...... ized in the lysosomal membrane
@nl
P2093
P2860
P3181
P356
P1476
Presenilin-1, nicastrin, amylo ...... ized in the lysosomal membrane
@en
P2093
Brian J. Pak
Cameron A. Ackerley
Don J. Mahuran
John W. Callahan
Marianne Guiral
Richard D. Bagshaw
Stephen H. Pasternak
Sunqu Zhang
P2860
P304
26687–26694
P3181
P356
10.1074/JBC.M304009200
P407
P577
2003-07-18T00:00:00Z