APOLIPOPROTEIN B: mRNA editing, lipoprotein assembly, and presecretory degradation.
about
Multiple functions of microsomal triglyceride transfer proteinHepatitis C virus nonstructural proteins inhibit apolipoprotein B100 secretionSomatic hypermutation of the AID transgene in B and non-B cellsMouse and other rodent models of C to U RNA editingC-->U editing of neurofibromatosis 1 mRNA occurs in tumors that express both the type II transcript and apobec-1, the catalytic subunit of the apolipoprotein B mRNA-editing enzymeFamilial hypercholesterolemia: present and future managementTranslational control mechanisms in metabolic regulation: critical role of RNA binding proteins, microRNAs, and cytoplasmic RNA granulesIntestinal triacylglycerol synthesis in fat absorption and systemic energy metabolismInduction of body weight loss through RNAi-knockdown of APOBEC1 gene expression in transgenic rabbitsFamilial hypobetalipoproteinemia: a reviewMutagenesis of apobec-1 complementation factor reveals distinct domains that modulate RNA binding, protein-protein interaction with apobec-1, and complementation of C to U RNA-editing activityNovel role for RNA-binding protein CUGBP2 in mammalian RNA editing. CUGBP2 modulates C to U editing of apolipoprotein B mRNA by interacting with apobec-1 and ACF, the apobec-1 complementation factorApolipoprotein B: a clinically important apolipoprotein which assembles atherogenic lipoproteins and promotes the development of atherosclerosisRegulation of hepatic lipogenesis by the transcription factor XBP1Upregulation of apolipoprotein B secretion, but not lipid, by tumor necrosis factor-alpha in rat hepatocyte cultures in the absence of extracellular fatty acidsARP-1/COUP-TF II determines hepatoma phenotype by acting as both a transcriptional repressor of microsomal triglyceride transfer protein and an inducer of CYP7A1Epigallocatechin gallate increases the formation of cytosolic lipid droplets and decreases the secretion of apoB-100 VLDLHepatic secretion of apoB-100 is impaired in hypobetalipoproteinemic mice with an apoB-38.9-specifying alleleMicrosomal triglyceride transfer protein and its role in apoB-lipoprotein assemblyIntegrative analysis of proteomic and transcriptomic data for identification of pathways related to simvastatin-induced hepatotoxicity.A W-test collapsing method for rare-variant association testing in exome sequencing data.Sensing of dietary lipids by enterocytes: a new role for SR-BI/CLA-1Apolipoprotein B100 quality control and the regulation of hepatic very low density lipoprotein secretion.Deficiency in hepatic ATP-citrate lyase affects VLDL-triglyceride mobilization and liver fatty acid composition in miceRegulation of immunoglobulin class-switch recombination: choreography of noncoding transcription, targeted DNA deamination, and long-range DNA repair.AID and mismatch repair in antibody diversification.Lipid-dependent bidirectional traffic of apolipoprotein B in polarized enterocytes.APOBEC-1-mediated RNA editing.Intersection of the unfolded protein response and hepatic lipid metabolismApoB siRNA-induced liver steatosis is resistant to clearance by the loss of fatty acid transport protein 5 (Fatp5)Endoplasmic reticulum stress and lipid metabolism: mechanisms and therapeutic potentialNR2F1 disrupts synergistic activation of the MTTP gene transcription by HNF-4α and HNF-1α.Effects of CETP inhibition on triglyceride-rich lipoprotein composition and apoB-48 metabolism.Acute hypoxia induces hypertriglyceridemia by decreasing plasma triglyceride clearance in mice.Prepartum body condition score and plane of nutrition affect the hepatic transcriptome during the transition period in grazing dairy cows.Cardiomyocyte Regulation of Systemic Lipid Metabolism by the Apolipoprotein B-Containing Lipoproteins in Drosophila.Trans-Golgi proteins participate in the control of lipid droplet and chylomicron formationInsulin suppression of apolipoprotein B in McArdle RH7777 cells involves increased sortilin 1 interaction and lysosomal targeting.Apolipoproteins A-I and B: biosynthesis, role in the development of atherosclerosis and targets for intervention against cardiovascular disease.Nucleotide levels regulate germline proliferation through modulating GLP-1/Notch signaling in C. elegans.
P2860
Q21245057-A7CEAAF6-3247-4451-AB6D-BF980CBC19EBQ24337547-34D5ACF7-7F32-4816-89B0-0DEBF2F22F10Q24535846-142FA14A-95B2-4DF0-88FA-39993612F8FBQ24598767-D9C55FA8-4FD1-4050-B2CB-55E8B22157D2Q24633130-2FAFE9BB-A198-4D37-BD6A-87C0F9270C09Q26828489-1A2EB1AA-329E-4E91-AA32-0AD27E245A48Q27022700-46E00FE0-BB3A-47A4-8F0C-ABC94429FF0DQ27023275-DB239A2C-DA80-4490-B86A-FA8EF65A1CA8Q27312336-B29ABADB-3FE8-40B8-8AE8-08089D28D55CQ28183795-AB3457E7-BA3F-4228-BAA5-AC91399EDAD5Q28188677-391F606D-DEE5-4054-BBA2-6BC481C48D85Q28189260-AA126F48-6257-4D77-9183-159E5B8A4DCCQ28278173-87233579-A9AE-41DE-95A5-20E602905A8BQ28507784-605BDD1D-FAA2-486B-8080-88150BD91F3BQ28564773-79B35EB1-B42E-4BA6-B06E-E4834D3319CBQ28582103-DBB62B0B-BE23-4A73-99CC-70D822918C5DQ28582707-FB3F3E57-C396-40AA-9B05-5C867455140CQ28593031-349FC4D0-F34F-473D-A6AD-201583D94475Q28624200-EE237F12-E9C7-47C5-AE19-D92186E65790Q30586189-49020862-F8D6-423F-A17E-F277B7473CB1Q31121956-45568040-F783-4E5E-AFD7-BC23D1DBEAFDQ33402916-D778A8FD-DD0C-46F4-9E8C-9947C4EBB66EQ33858526-D640F838-F060-43FD-925C-1878DEB7EC71Q34053069-B814236B-035E-441F-B256-4113B03E93E4Q34115234-907637CB-122B-42B5-AD3E-F98568CEEE37Q34770418-CDC63737-B45A-4C42-8C31-23A796744950Q34785828-8DF7A12C-9321-469B-9E93-3F87037BA217Q34910421-281C14D1-D907-4898-814E-B1A7CE4DC4DEQ34985745-8CFFF493-20A2-44D2-B95A-E8CEF47B4853Q35541914-F3378808-3DD5-49C2-AD8E-DC171CE47228Q35614922-A8CDE3DC-3B89-42ED-92D4-B36AADC3559EQ35897027-88C46230-84B2-4AD0-9AC4-8D547F194000Q35958491-3C8B41A9-4D6F-4189-B2CF-D9F7EDD25432Q36175990-35D00E68-E69C-4C0D-A80B-7511BA109D7CQ36180569-79A3AC9E-E132-4763-9921-3DF49FB137BDQ36251148-8F560145-628C-447D-B9D8-C2D4E5CE3A94Q36467350-4729B5FE-69C6-41AA-ACBC-392AB0511AF0Q36532383-42F2F694-940E-4B70-834D-648F6332A17BQ36536256-550FB6C0-121A-499C-9A38-DEBDCD993BD1Q36549516-F44329A9-03B3-464A-BDF8-8AA73DBAD625
P2860
APOLIPOPROTEIN B: mRNA editing, lipoprotein assembly, and presecretory degradation.
description
2000 nî lūn-bûn
@nan
2000 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
APOLIPOPROTEIN B: mRNA editing, lipoprotein assembly, and presecretory degradation.
@ast
APOLIPOPROTEIN B: mRNA editing, lipoprotein assembly, and presecretory degradation.
@en
APOLIPOPROTEIN B: mRNA editing, lipoprotein assembly, and presecretory degradation.
@nl
type
label
APOLIPOPROTEIN B: mRNA editing, lipoprotein assembly, and presecretory degradation.
@ast
APOLIPOPROTEIN B: mRNA editing, lipoprotein assembly, and presecretory degradation.
@en
APOLIPOPROTEIN B: mRNA editing, lipoprotein assembly, and presecretory degradation.
@nl
prefLabel
APOLIPOPROTEIN B: mRNA editing, lipoprotein assembly, and presecretory degradation.
@ast
APOLIPOPROTEIN B: mRNA editing, lipoprotein assembly, and presecretory degradation.
@en
APOLIPOPROTEIN B: mRNA editing, lipoprotein assembly, and presecretory degradation.
@nl
P1476
APOLIPOPROTEIN B: mRNA editing, lipoprotein assembly, and presecretory degradation.
@en
P2093
Davidson NO
Shelness GS
P304
P356
10.1146/ANNUREV.NUTR.20.1.169
P407
P577
2000-01-01T00:00:00Z