A molecular biology-based approach to resolve the subunit orientation of lipoprotein lipase. - Wikidata - wikimedia - TriplyDB

A molecular biology-based approach to resolve the subunit orientation of lipoprotein lipase.

A molecular biology-based approach to resolve the subunit orientation of lipoprotein lipase.

http://www.wikidata.org/entity/Q36151990

about

GPIHBP1 stabilizes lipoprotein lipase and prevents its inhibition by angiopoietin-like 3 and angiopoietin-like 4 The angiopoietin-like proteins ANGPTL3 and ANGPTL4 inhibit lipoprotein lipase activity through distinct mechanisms Angiopoietin-like protein 4 inhibition of lipoprotein lipase: evidence for reversible complex formation Direct interaction between the Arabidopsis disease resistance signaling proteins, EDS1 and PAD4 Interaction of lipoprotein lipase and receptor-associated protein Comparative studies of vertebrate lipoprotein lipase: a key enzyme of very low density lipoprotein metabolism Identification of the active form of endothelial lipase, a homodimer in a head-to-tail conformation.Quarternary structure and enzymological properties of the different hormone-sensitive lipase (HSL) isoforms.Mechanisms of lipase maturation.The lipase gene family.Identification of a lipoprotein lipase cofactor-binding site by chemical cross-linking and transfer of apolipoprotein C-II-responsive lipolysis from lipoprotein lipase to hepatic lipase.Structure-function relationships of hormone-sensitive lipase.Lipase maturation factor 1 is required for endothelial lipase activity.Lipoprotein lipase: from gene to obesity.Severity of diabetes governs vascular lipoprotein lipase by affecting enzyme dimerization and disassembly Chylomicronemia mutations yield new insights into interactions between lipoprotein lipase and GPIHBP1 Biochemistry and pathophysiology of intravascular and intracellular lipolysis.Lipase maturation factor 1: structure and role in lipase folding and assembly.Calcium triggers folding of lipoprotein lipase into active dimers.GPIHBP1 and Plasma Triglyceride Metabolism.Emerging strategies of targeting lipoprotein lipase for metabolic and cardiovascular diseases.The GPIHBP1-LPL complex is responsible for the margination of triglyceride-rich lipoproteins in capillaries.Substrate specificity of lipoprotein lipase and endothelial lipase: studies of lid chimeras.Purification, cellular levels, and functional domains of lipase maturation factor 1.Mice expressing only covalent dimeric heparin binding-deficient lipoprotein lipase: muscles inefficiently secrete dimeric enzyme.Subdomain chimeras of hepatic lipase and lipoprotein lipase. Localization of heparin and cofactor binding.We FRET so You Don't Have To: New Models of the Lipoprotein Lipase Dimer.Lipoprotein Lipase Expression in Chronic Lymphocytic Leukemia: New Insights into Leukemic Progression.

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P2860

A molecular biology-based approach to resolve the subunit orientation of lipoprotein lipase.

http://www.wikidata.org/entity/Q36151990

description

1997 nî lūn-bûn

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1997年の論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年论文

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1997年论文

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1997年论文

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A molecular biology-based appr ...... ntation of lipoprotein lipase.

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A molecular biology-based appr ...... ntation of lipoprotein lipase.

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A molecular biology-based appr ...... ntation of lipoprotein lipase.

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A molecular biology-based appr ...... ntation of lipoprotein lipase.

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Proceedings of the National Academy of Sciences of the United States of America

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A molecular biology-based appr ...... ntation of lipoprotein lipase.

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D Yang

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H Wong

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J Nikazy

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J S Hill

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M C Schotz

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R C Davis

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P2860

Lipoprotein lipase enhances the binding of chylomicrons to low density lipoprotein receptor-related protein

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

A hepatic lipase gene mutation associated with heritable lipolytic deficiency

Human lipoprotein lipase: relationship of activity, heparin affinity, and conformation as studied with monoclonal antibodies

The low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor binds and mediates catabolism of bovine milk lipoprotein lipase.

The carboxyl-terminal domain of lipoprotein lipase binds to the low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor (LRP) and mediates binding of normal very low density lipoproteins to LRP.

Mutagenesis in four candidate heparin binding regions (residues 279-282, 291-304, 390-393, and 439-448) and identification of residues affecting heparin binding of human lipoprotein lipase.

A carboxyl-terminal fragment of lipoprotein lipase binds to the low density lipoprotein receptor-related protein and inhibits lipase-mediated uptake of lipoprotein in cells.

Lipoprotein lipase domain function.

Properties of permease dimer, a fusion protein containing two lactose permease molecules from Escherichia coli.

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