Identification of a new functional domain in angiopoietin-like 3 (ANGPTL3) and angiopoietin-like 4 (ANGPTL4) involved in binding and inhibition of lipoprotein lipase (LPL). (Q43131473)

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scientific article published on 23 March 2009

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English	Identification of a new functional domain in angiopoietin-like 3 (ANGPTL3) and angiopoietin-like 4 (ANGPTL4) involved in binding and inhibition of lipoprotein lipase (LPL).	scientific article published on 23 March 2009

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24 January 2020

Identification of a new functional domain in angiopoietin-like 3 (ANGPTL3) and angiopoietin-like 4 (ANGPTL4) involved in binding and inhibition of lipoprotein lipase (LPL) (English)

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24 January 2020

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24 January 2020

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E-Chiang Lee

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24 January 2020

Gennady Gololobov

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24 January 2020

Seokjoo Hong

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24 January 2020

Xiao Feng

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24 January 2020

Xuan-Chuan Yu

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24 January 2020

Jason Gay

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24 January 2020

Nat Wilganowski

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24 January 2020

Cuihua Gao

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24 January 2020

Ling-Ling Du

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24 January 2020

Joan Chen

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24 January 2020

Yi Hu

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24 January 2020

Sharon Zhao

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24 January 2020

Laura Kirkpatrick

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24 January 2020

Matthias Schneider

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24 January 2020

Brian P Zambrowicz

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24 January 2020

Greg Landes

17

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24 January 2020

David R Powell

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24 January 2020

William K Sonnenburg

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24 January 2020

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23 March 2009

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24 January 2020

Journal of Biological Chemistry

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24 January 2020

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24 January 2020

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24 January 2020

13735-13745

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Rare loss-of-function mutations in ANGPTL family members contribute to plasma triglyceride levels in humans.

1 reference

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The angiopoietin-like proteins ANGPTL3 and ANGPTL4 inhibit lipoprotein lipase activity through distinct mechanisms

1 reference

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Six new loci associated with blood low-density lipoprotein cholesterol, high-density lipoprotein cholesterol or triglycerides in humans

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Fasting compared with nonfasting triglycerides and risk of cardiovascular events in women

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Lipid-lowering effects of anti-angiopoietin-like 4 antibody recapitulate the lipid phenotype found in angiopoietin-like 4 knockout mice

1 reference

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Population-based resequencing of ANGPTL4 uncovers variations that reduce triglycerides and increase HDL.

1 reference

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Angiopoietin-like protein 4 converts lipoprotein lipase to inactive monomers and modulates lipase activity in adipose tissue

1 reference

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Differential regulation and properties of angiopoietin-like proteins 3 and 4

1 reference

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Protein region important for regulation of lipid metabolism in angiopoietin-like 3 (ANGPTL3): ANGPTL3 is cleaved and activated in vivo.

1 reference

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Lipoprotein lipase: genetics, lipid uptake, and regulation.

1 reference

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Angiopoietin-like protein 4 is a potent hyperlipidemia-inducing factor in mice and inhibitor of lipoprotein lipase

1 reference

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Lipoprotein lipase: the regulation of tissue specific expression and its role in lipid and energy metabolism

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ANGPTL3 decreases very low density lipoprotein triglyceride clearance by inhibition of lipoprotein lipase

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Angptl3 regulates lipid metabolism in mice

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Lipoprotein lipase: physiology, biochemistry, and molecular biology

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15 August 2018

Oligomerization state-dependent hyperlipidemic effect of angiopoietin-like protein 4.

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1 reference

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12 December 2020

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Nonfasting Triglycerides and Risk of Myocardial Infarction, Ischemic Heart Disease, and Death in Men and Women

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https://pubmed.ncbi.nlm.nih.gov/19318355

12 December 2020

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10.1074/JBC.M807899200

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24 January 2020

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