Apolipoproteins C-I and C-III inhibit lipoprotein lipase activity by displacement of the enzyme from lipid droplets.
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Triglyceride-Rich Lipoproteins and Remnants: Targets for Therapy?The crucial roles of apolipoproteins E and C-III in apoB lipoprotein metabolism in normolipidemia and hypertriglyceridemiaNew Era of Lipid-Lowering DrugsPlasma apolipoprotein C-III levels, triglycerides, and coronary artery calcification in type 2 diabetics.Associations of the APOC3 rs5128 polymorphism with plasma APOC3 and lipid levels: a meta-analysisApolipoprotein C-III: a potent modulator of hypertriglyceridemia and cardiovascular disease.Apoc2 loss-of-function zebrafish mutant as a genetic model of hyperlipidemia.Identification of Apolipoprotein C-I Peptides as a Potential Biomarker and its Biological Roles in Breast CancerTryptophan probes reveal residue-specific phospholipid interactions of apolipoprotein C-IIIApolipoprotein CIII overexpression exacerbates diet-induced obesity due to adipose tissue higher exogenous lipid uptake and retention and lower lipolysis rates.D25V apolipoprotein C-III variant causes dominant hereditary systemic amyloidosis and confers cardiovascular protective lipoprotein profile.The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain.Apolipoproteins as Differentiating and Predictive Markers for Assessing Clinical Outcomes in Patients with Small Cell Lung Cancer.Persimmon (Diospyros kaki) fruit: hidden phytochemicals and health claims.WAT apoC-I secretion: role in delayed chylomicron clearance in vivo and ex vivo in WAT in obese subjects.18O proteomics reveal increased human apolipoprotein CIII in Hispanic HIV-1+ women with HAART that use cocaineDiagnostic and prognostic significance of serum apolipoprotein C-I in triple-negative breast cancer based on mass spectrometryAPOC3 induces endothelial dysfunction through TNF-α and JAM-1Serum Protein KNG1, APOC3, and PON1 as Potential Biomarkers for Yin-Deficiency-Heat Syndrome.Unusual Dyslipidemia in Patients with Chronic Kidney Diseases.A human APOC3 missense variant and monoclonal antibody accelerate apoC-III clearance and lower triglyceride-rich lipoprotein levels.Endothelial cell-cardiomyocyte crosstalk in diabetic cardiomyopathy.Emerging strategies of targeting lipoprotein lipase for metabolic and cardiovascular diseases.ApoC-III inhibits clearance of triglyceride-rich lipoproteins through LDL family receptors.Aromatic residues in the C terminus of apolipoprotein C-III mediate lipid binding and LPL inhibition.A Pressure-dependent Model for the Regulation of Lipoprotein Lipase by Apolipoprotein C-II.The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 counteracts this unfolding.Multidimensional regulation of lipoprotein lipase: impact on biochemical and cardiovascular phenotypes.Lipoprotein lipase reaches the capillary lumen in chickens despite an apparent absence of GPIHBP1.Hepatitis B virus inhibits the in vivo and in vitro synthesis and secretion of apolipoprotein C3.Evaluation of the immediate vascular stability of lipoprotein lipase-generated 2-monoacylglycerol in mice.Apolipoprotein C-III inhibits triglyceride hydrolysis by GPIHBP1-bound LPL.Lipoprotein lipase activity and interactions studied in human plasma by isothermal titration calorimetry.HDL Subspecies Defined by Presence of Apolipoprotein C-III and Incident Coronary Heart Disease in Four Cohorts.Impaired thermogenesis and sharp increases in plasma triglyceride levels in GPIHBP1-deficient mice during cold exposure.Apolipoprotein C-II: New findings related to genetics, biochemistry, and role in triglyceride metabolism.Knockout of a difficult-to-remove CHO host cell protein, lipoprotein lipase, for improved polysorbate stability in monoclonal antibody formulations.Proteomic Profiles of Adipose and Liver Tissues from an Animal Model of Metabolic Syndrome Fed Purple Vegetables.Core lipid, surface lipid and apolipoprotein composition analysis of lipoprotein particles as a function of particle size in one workflow integrating asymmetric flow field-flow fractionation and liquid chromatography-tandem mass spectrometry.
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Apolipoproteins C-I and C-III inhibit lipoprotein lipase activity by displacement of the enzyme from lipid droplets.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 11 October 2013
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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
Apolipoproteins C-I and C-III ...... he enzyme from lipid droplets.
@en
Apolipoproteins C-I and C-III ...... he enzyme from lipid droplets.
@nl
type
label
Apolipoproteins C-I and C-III ...... he enzyme from lipid droplets.
@en
Apolipoproteins C-I and C-III ...... he enzyme from lipid droplets.
@nl
prefLabel
Apolipoproteins C-I and C-III ...... he enzyme from lipid droplets.
@en
Apolipoproteins C-I and C-III ...... he enzyme from lipid droplets.
@nl
P2093
P2860
P356
P1476
Apolipoproteins C-I and C-III ...... he enzyme from lipid droplets.
@en
P2093
Aivar Lookene
Evelina Vorrsjö
Mikael Larsson
P2860
P304
33997-34008
P356
10.1074/JBC.M113.495366
P407
P577
2013-10-11T00:00:00Z