Clues to the mechanism of cholesterol transfer from the structure of NPC1 middle lumenal domain bound to NPC2.
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Pathogenic mycobacteria achieve cellular persistence by inhibiting the Niemann-Pick Type C disease cellular pathwayIdentifying the structure-activity relationship of leelamine necessary for inhibiting intracellular cholesterol transport.Crystal structure of the DNA-binding domain of Myelin-gene Regulatory FactorLysosomal membrane glycoproteins bind cholesterol and contribute to lysosomal cholesterol export.Triazoles inhibit cholesterol export from lysosomes by binding to NPC1.Characterization of cholesterol homeostasis in sphingosine-1-phosphate lyase-deficient fibroblasts reveals a Niemann-Pick disease type C-like phenotype with enhanced lysosomal Ca2+ storage.3.3 Å structure of Niemann-Pick C1 protein reveals insights into the function of the C-terminal luminal domain in cholesterol transport.Histone deacetylase inhibitors correct the cholesterol storage defect in most Niemann-Pick C1 mutant cells.Exacerbating and reversing lysosomal storage diseases: from yeast to humans.Mechanisms of Filovirus Entry.Quantitative Analysis of the Proteome Response to the Histone Deacetylase Inhibitor (HDACi) Vorinostat in Niemann-Pick Type C1 disease.Human TRPML1 channel structures in open and closed conformations.Concerted regulation of npc2 binding to endosomal/lysosomal membranes by bis(monoacylglycero)phosphate and sphingomyelin.Mechanisms of action of Coxiella burnetii effectors inferred from host-pathogen protein interactions.The extending spectrum of NPC1-related human disorders: from Niemann-Pick C1 Disease to obesity.Niemann-Pick C2 Proteins: A New Function for an Old Family.Large-scale computational drug repositioning to find treatments for rare diseases.Emerging Roles for the Lysosome in Lipid Metabolism.Recent neuroimaging, neurophysiological, and neuropathological advances for the understanding of NPC.Prospective Turkish Cohort Study to Investigate the Frequency of Niemann-Pick Disease Type C Mutations in Consanguineous Families with at Least One Homozygous Family Member.Lysosomal cholesterol export reconstituted from fragments of Niemann-Pick C1Simulations of NPC1(NTD):NPC2 Protein Complex Reveal Cholesterol Transfer PathwaysOdorant-Binding Proteins as Sensing Elements for Odour Monitoring
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P2860
Clues to the mechanism of cholesterol transfer from the structure of NPC1 middle lumenal domain bound to NPC2.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 22 August 2016
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Clues to the mechanism of chol ...... lumenal domain bound to NPC2.
@en
Clues to the mechanism of chol ...... lumenal domain bound to NPC2.
@nl
type
label
Clues to the mechanism of chol ...... lumenal domain bound to NPC2.
@en
Clues to the mechanism of chol ...... lumenal domain bound to NPC2.
@nl
prefLabel
Clues to the mechanism of chol ...... lumenal domain bound to NPC2.
@en
Clues to the mechanism of chol ...... lumenal domain bound to NPC2.
@nl
P2093
P2860
P356
P1476
Clues to the mechanism of chol ...... lumenal domain bound to NPC2.
@en
P2093
Piyali Saha
Suzanne R Pfeffer
Xiaochun Li
P2860
P304
10079-10084
P356
10.1073/PNAS.1611956113
P407
P577
2016-08-22T00:00:00Z