Purified NPC1 protein: II. Localization of sterol binding to a 240-amino acid soluble luminal loop. - Wikidata - wikimedia - TriplyDB

Purified NPC1 protein: II. Localization of sterol binding to a 240-amino acid soluble luminal loop.

Purified NPC1 protein: II. Localization of sterol binding to a 240-amino acid soluble luminal loop.

http://www.wikidata.org/entity/Q38296620

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The structure of the NPC1L1 N-terminal domain in a closed conformation Membrane topology of human NPC1L1, a key protein in enterohepatic cholesterol absorption NPC2 facilitates bidirectional transfer of cholesterol between NPC1 and lipid bilayers, a step in cholesterol egress from lysosomes Nogo-B receptor stabilizes Niemann-Pick type C2 protein and regulates intracellular cholesterol trafficking Regulation of sterol transport between membranes and NPC2 Erlins restrict SREBP activation in the ER and regulate cellular cholesterol homeostasis Ebola virus entry requires the host-programmed recognition of an intracellular receptor Deficiency of niemann-pick type C-1 protein impairs release of human immunodeficiency virus type 1 and results in Gag accumulation in late endosomal/lysosomal compartments NPC1/NPC2 function as a tag team duo to mobilize cholesterol The LDL receptor Structure of N-Terminal Domain of NPC1 Reveals Distinct Subdomains for Binding and Transfer of Cholesterol Pathogen-Related Yeast (PRY) proteins and members of the CAP superfamily are secreted sterol-binding proteins.Characterization of the Niemann-Pick C pathway in alveolar type II cells and lamellar bodies of the lung Loss of Niemann-Pick C1 or C2 protein results in similar biochemical changes suggesting that these proteins function in a common lysosomal pathway Niemann-Pick type C 1 function requires lumenal domain residues that mediate cholesterol-dependent NPC2 binding Translocator protein 2 is involved in cholesterol redistribution during erythropoiesis The Niemann-Pick C1 and caveolin-1 proteins interact to modulate efflux of low density lipoprotein-derived cholesterol from late endocytic compartments.Proteins that bind and move lipids: MsbA and NPC1.The National Niemann-Pick Type C1 Disease Database: correlation of lipid profiles, mutations, and biochemical phenotypes.Oxysterols and their cellular effectors.Niemann-Pick C disease and mobilization of lysosomal cholesterol by cyclodextrin Cholesterol, the central lipid of mammalian cells Genetic connections between neurological disorders and cholesterol metabolism Therapeutic potential of cyclodextrins in the treatment of Niemann-Pick type C disease.Deficiency of a Niemann-Pick, type C1-related protein in toxoplasma is associated with multiple lipidoses and increased pathogenicity.Structure and mechanism of RND-type multidrug efflux pumps Early steps in steroidogenesis: intracellular cholesterol trafficking.Absence of Nceh1 augments 25-hydroxycholesterol-induced ER stress and apoptosis in macrophages Scientific side trips: six excursions from the beaten path.Insights into the mechanisms of sterol transport between organelles.Npc1 haploinsufficiency promotes weight gain and metabolic features associated with insulin resistance.Identification of surface residues on Niemann-Pick C2 essential for hydrophobic handoff of cholesterol to NPC1 in lysosomes Mechanisms of RND multidrug efflux pumps Defining structural and evolutionary modules in proteins: a community detection approach to explore sub-domain architecture.Altered vitamin E status in Niemann-Pick type C disease.Gene-diet interactions in childhood obesity.The N-terminal domain of NPC1L1 protein binds cholesterol and plays essential roles in cholesterol uptake.The role of the Niemann-Pick disease, type C1 protein in adipocyte insulin action.Endosomal/lysosomal processing of gangliosides affects neuronal cholesterol sequestration in Niemann-Pick disease type C.Amino acid substitution in NPC1 that abolishes cholesterol binding reproduces phenotype of complete NPC1 deficiency in mice.

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P2860

Purified NPC1 protein: II. Localization of sterol binding to a 240-amino acid soluble luminal loop.

http://www.wikidata.org/entity/Q38296620

description

2007 nî lūn-bûn

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Purified NPC1 protein: II. Loc ...... ino acid soluble luminal loop.

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Purified NPC1 protein: II. Loc ...... ino acid soluble luminal loop.

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Lina Abi-Mosleh

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Lisa N Kinch

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Michael L Wang

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Michael S Brown

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Rodney E Infante

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P2860

Topological 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-acti

Identification of HE1 as the second gene of Niemann-Pick C disease

NPC1 and NPC2 regulate cellular cholesterol homeostasis through generation of low density lipoprotein cholesterol-derived oxysterols

NPC2, the protein deficient in Niemann-Pick C2 disease, consists of multiple glycoforms that bind a variety of sterols

Niemann-Pick C1 disease gene: homology to mediators of cholesterol homeostasis

Structure of a cholesterol-binding protein deficient in Niemann-Pick type C2 disease

Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: oxysterols block transport by binding to Insig

Structural Basis of Sterol Binding by NPC2, a Lysosomal Protein Deficient in Niemann-Pick Type C2 Disease

Regulated cleavage of sterol regulatory element binding proteins requires sequences on both sides of the endoplasmic reticulum membrane

Genetic evidence for nonredundant functional cooperativity between NPC1 and NPC2 in lipid transport

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10.1074/JBC.M707944200

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283

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Nick V. Grishin

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2007-11-06T00:00:00Z

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5857785

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