GoPubMed Proteins lists recent and important papers and reviews for
proteins. Page last changed on 19 Dec 2016.
Niemann-Pick disease, type C2
NPC2, HEI, HE1
This gene encodes a protein containing a lipid recognition domain. The encoded protein may function in regulating the transport of cholesterol through the late endosomal/lysosomal system. Mutations in this gene have been associated with Niemann-Pick disease, type C2 and frontal lobe atrophy. [provided by RefSeq, Jul 2008] (from
NCBI)
Top mentioned proteins:
NPC1, CAN, HAD, ACID, AGE
Papers on
NPC2
Optogenetic Control of Mouse Outer Hair Cells.
New
Ann Arbor, United States. In Biophys J, Feb 2016
Three approaches were compared: 1) adeno-associated virus-mediated in utero transfer of the ChR-2 gene into the developing murine otocyst, 2) expression of ChR-2(H134R) in an auditory cell line (HEI-OC1), and 3) expression of ChR-2 in the OHCs of a mouse line carrying a ChR-2 conditional allele.
miR214-regulated p53-NOX4/p66shc pathway plays a crucial role in the protective effect of Ginkgolide B against cisplatin-induced cytotoxicity in HEI-OC1 cells.
New
Xi'an, China. In Chem Biol Interact, Feb 2016
The results showed that, in HEI-OC1 auditory cells, both NOX4 and p66(shc) expression was increased by cisplatin.
Arylpiperidines as a new class of oxidosqualene cyclase inhibitors.
New
München, Germany. In Eur J Med Chem, Jan 2016
UNASSIGNED: The cyclization of oxidosqualene to lanosterol, catalyzed by the enzyme oxidosqualene cyclase (OSC), goes through a number of carbocationic high energy intermediates (HEI), and mimicking these intermediates is a promising approach for the development of OSC inhibitors.
Gpnmb Is a Potential Marker for the Visceral Pathology in Niemann-Pick Type C Disease.
New
Amsterdam, Netherlands. In Plos One, Dec 2015
Impaired function of NPC1 or NPC2 lysosomal proteins leads to the intracellular accumulation of unesterified cholesterol, the primary defect underlying Niemann-Pick type C (NPC) disease.
[Research advances in diagnosis and therapy of Niemann-Pick disease type C].
Review
New
Beijing, China. In Zhongguo Dang Dai Er Ke Za Zhi, May 2015
Impaired cholesterol trafficking and unesterified cholesterol accumulation in the late endosomes and lysosomals, as a results of mutations in NPC1 or NPC2 genes, are initial for the disease, and defective cellular autophagy, defective lysosomal calcium homeostasis and oxidative stress may all play roles in the physiological processes.
Complex lipid trafficking in Niemann-Pick disease type C.
Review
Lyon, France. In J Inherit Metab Dis, 2015
Niemann-Pick disease type C (NPC) is an atypical lysosomal storage disease resulting from mutations in one of two genes, either NPC1 or NPC2.
Association of lunch meat consumption with nutrient intake, diet quality and health risk factors in U.S. children and adults: NHANES 2007-2010.
United States. In Nutr J, 2014
METHODS: Lunch meat consumers were defined as those consuming any amount of lunch meat during a 24-h recall and association with nutrient intake, diet quality (Healthy Eating Index (HEI)-2010 score) and physiological measures were evaluated using the National Health and Nutrition Examination Survey (NHANES), 2007-2010.
Recent advances in the diagnosis and treatment of niemann-pick disease type C in children: a guide to early diagnosis for the general pediatrician.
Review
Tripoli, Libya. In Int J Pediatr, 2014
It is an autosomal recessive disorder, caused by mutations in the NPC1 or NPC2 genes.
The unique case of the Niemann-Pick type C cholesterol storage disorder.
Review
In Pediatr Endocrinol Rev, 2014
Niemann-Pick type C disease (NPC) is a neurovisceral lysosomal cholesterol storage disorder that arises from loss-of-f unction mutations in either the NPCI or NPC2 genes.
Genetic and laboratory diagnostic approach in Niemann Pick disease type C.
Review
Birmingham, United Kingdom. In J Neurol, 2014
Niemann Pick disease type C (NP-C) is a rare autosomal recessive disorder that results from mutations in either the NPC1 or the NPC2 gene.
Glycine N-methyltransferase deficiency affects Niemann-Pick type C2 protein stability and regulates hepatic cholesterol homeostasis.
GeneRIF
Taipei, Taiwan. In Mol Med, 2011
This is the first report demonstrating that GNMT plays an important role in regulating cholesterol homeostasis via interaction with NPC2
Loss of Niemann Pick type C proteins 1 and 2 greatly enhances HIV infectivity and is associated with accumulation of HIV Gag and cholesterol in late endosomes/lysosomes.
GeneRIF
Nashville, United States. In Virol J, 2011
Loss of Niemann Pick type C proteins 1 and 2 greatly enhances HIV infectivity and is associated with accumulation of HIV Gag and cholesterol in late endosomes/lysosomes.
Sterol transfer between cyclodextrin and membranes: similar but not identical mechanism to NPC2-mediated cholesterol transfer.
GeneRIF
New Brunswick, United States. In Biochemistry, 2011
mechanism of sterol transport by cyclodextrins using in vitro model systems and fluorescence spectroscopy and NPC2-deficient fibroblasts
Endosomal/lysosomal processing of gangliosides affects neuronal cholesterol sequestration in Niemann-Pick disease type C.
GeneRIF
New York City, United States. In Am J Pathol, 2011
NPC1 and NPC2 proteins participate in endosomal/lysosomal processing of both sphingolipids and cholesterol
Loss of Niemann-Pick C1 or C2 protein results in similar biochemical changes suggesting that these proteins function in a common lysosomal pathway.
GeneRIF
United States. In Plos One, 2010
In liver, absence of either NPC1 or NPC2 resulted in similar alterations in the carbohydrate processing of the lysosomal protease, tripeptidyl peptidase I.
Identification of surface residues on Niemann-Pick C2 essential for hydrophobic handoff of cholesterol to NPC1 in lysosomes.
Impact
GeneRIF
Dallas, United States. In Cell Metab, 2010
NPC2 protein interacts N-ternimal domain of NPC1 protein, thereby opening an entry pore on NPC1 protein and allowing cholesterol to transfer without passing through the water phase.
Transfer of cholesterol by the NPC team.
Impact
Edmonton, Canada. In Cell Metab, 2010
In this issue of Cell Metabolism, Wang et al. (2010) identify amino acid residues on the lumenal lysosomal protein Niemann-Pick C2 (NPC2) that are required for intralysosomal transfer of endocytosed cholesterol to membrane-bound NPC1 via a process that avoids movement of hydrophobic cholesterol through the aqueous phase.
Nogo-B receptor stabilizes Niemann-Pick type C2 protein and regulates intracellular cholesterol trafficking.
Impact
GeneRIF
New Haven, United States. In Cell Metab, 2009
Niemann-Pick type C2 protein levels are increased in the presence of Nogo-B receptor, and Nogo-B receptor enhances Niemann-Pick type C2 protein protein stability.
Getting a "Hold" on NPC2.
Impact
Saint Louis, United States. In Cell Metab, 2009
Lipoprotein cholesterol is mobilized from lysosomes by actions of the NPC1 and NPC2 proteins.
Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol.
Impact
Dallas, United States. In Cell, 2009
Exit of cholesterol from lysosomes requires two proteins, membrane-bound Niemann-Pick C1 (NPC1) and soluble NPC2.
