The Niemann-Pick C1 protein resides in a vesicular compartment linked to retrograde transport of multiple lysosomal cargo.
about
Niemann-Pick disease type CMutations in NPC1 highlight a conserved NPC1-specific cysteine-rich domainATPase-defective mammalian VPS4 localizes to aberrant endosomes and impairs cholesterol traffickingTopological analysis of Niemann-Pick C1 protein reveals that the membrane orientation of the putative sterol-sensing domain is identical to those of 3-hydroxy-3-methylglutaryl-CoA reductase and sterol regulatory element binding protein cleavage-actiThe Wilson disease protein ATP7B resides in the late endosomes with Rab7 and the Niemann-Pick C1 proteinThe ABCA1 transporter modulates late endocytic trafficking: insights from the correction of the genetic defect in Tangier diseaseTau deletion exacerbates the phenotype of Niemann-Pick type C mice and implicates autophagy in pathogenesis.Niemann-Pick C variant detection by altered sphingolipid trafficking and correlation with mutations within a specific domain of NPC1.Niemann-Pick C1 disease: correlations between NPC1 mutations, levels of NPC1 protein, and phenotypes emphasize the functional significance of the putative sterol-sensing domain and of the cysteine-rich luminal loop.Niemann-Pick C1 disease: the I1061T substitution is a frequent mutant allele in patients of Western European descent and correlates with a classic juvenile phenotypeCholesterol accumulation sequesters Rab9 and disrupts late endosome function in NPC1-deficient cellsDeficiency of niemann-pick type C-1 protein impairs release of human immunodeficiency virus type 1 and results in Gag accumulation in late endosomal/lysosomal compartmentsThe pathogenesis of Niemann-Pick type C disease: a role for autophagy?The lysosome: from waste bag to potential therapeutic targetOlfactory deficits in Niemann-Pick type C1 (NPC1) diseaseMutagenesis of the putative sterol-sensing domain of yeast Niemann Pick C-related protein reveals a primordial role in subcellular sphingolipid distribution.Telomerase immortalization upregulates Rab9 expression and restores LDL cholesterol egress from Niemann-Pick C1 late endosomesTargeted mutation of the MLN64 START domain causes only modest alterations in cellular sterol metabolismLoss of Niemann-Pick C1 or C2 protein results in similar biochemical changes suggesting that these proteins function in a common lysosomal pathwayAccumulation of glycosphingolipids in Niemann-Pick C disease disrupts endosomal transportThe Niemann-Pick C1 and caveolin-1 proteins interact to modulate efflux of low density lipoprotein-derived cholesterol from late endocytic compartments.Induction of Cell-Cell Fusion by Ebola Virus Glycoprotein: Low pH Is Not a TriggerInteraction between TIM-1 and NPC1 Is Important for Cellular Entry of Ebola Virus.A novel mouse model of Niemann-Pick type C disease carrying a D1005G-Npc1 mutation comparable to commonly observed human mutations.Dynamic movements of organelles containing Niemann-Pick C1 protein: NPC1 involvement in late endocytic eventsSelective stimulation of caveolar endocytosis by glycosphingolipids and cholesterol.Sterol-modulated glycolipid sorting occurs in niemann-pick C1 late endosomes.Site-specific phosphorylation of tau accompanied by activation of mitogen-activated protein kinase (MAPK) in brains of Niemann-Pick type C mice.Neurons in Niemann-Pick disease type C accumulate gangliosides as well as unesterified cholesterol and undergo dendritic and axonal alterations.Identification of a pharmaceutical compound that partially corrects the Niemann-Pick C phenotype in cultured cells.Dynamics of putative raft-associated proteins at the cell surface.The National Niemann-Pick Type C1 Disease Database: correlation of lipid profiles, mutations, and biochemical phenotypes.Pluronic based β-cyclodextrin polyrotaxanes for treatment of Niemann-Pick Type C disease.Cholesterol pathways affected by small molecules that decrease sterol levels in Niemann-Pick type C mutant cells.Niemann-Pick C1 functions independently of Niemann-Pick C2 in the initial stage of retrograde transport of membrane-impermeable lysosomal cargo.Cyclodextrin overcomes the transport defect in nearly every organ of NPC1 mice leading to excretion of sequestered cholesterol as bile acidCholesterol accumulation in Niemann Pick type C (NPC) model cells causes a shift in APP localization to lipid rafts.Accumulation of cholera toxin and GM1 ganglioside in the early endosome of Niemann-Pick C1-deficient cellsModulation of cellular cholesterol transport and homeostasis by Rab11.Late endosome motility depends on lipids via the small GTPase Rab7.
P2860
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P2860
The Niemann-Pick C1 protein resides in a vesicular compartment linked to retrograde transport of multiple lysosomal cargo.
description
1999 nî lūn-bûn
@nan
1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The Niemann-Pick C1 protein re ...... t of multiple lysosomal cargo.
@ast
The Niemann-Pick C1 protein re ...... t of multiple lysosomal cargo.
@en
type
label
The Niemann-Pick C1 protein re ...... t of multiple lysosomal cargo.
@ast
The Niemann-Pick C1 protein re ...... t of multiple lysosomal cargo.
@en
prefLabel
The Niemann-Pick C1 protein re ...... t of multiple lysosomal cargo.
@ast
The Niemann-Pick C1 protein re ...... t of multiple lysosomal cargo.
@en
P2093
P356
P1476
The Niemann-Pick C1 protein re ...... t of multiple lysosomal cargo.
@en
P2093
Blanchette-Mackie EJ
Carstea ED
Incardona JP
Neufeld EB
P304
P356
10.1074/JBC.274.14.9627
P407
P577
1999-04-01T00:00:00Z