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André Bensadoun

Researcher at Cornell University

Publications -  151
Citations -  11432

André Bensadoun is an academic researcher from Cornell University. The author has contributed to research in topics: Lipoprotein lipase & GPIHBP1. The author has an hindex of 53, co-authored 151 publications receiving 10986 citations. Previous affiliations of André Bensadoun include University of California, San Diego & University of California, San Francisco.

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Journal ArticleDOI

Thyroid lodohormones in the plasma of the rooster (Gallus domesticus)

TL;DR: The plasma iodohormones exhibit a diurnal rhythm in the rooster and T3 was the predominant hormone at all times investigated.
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Glycosylation of Asn-76 in mouse GPIHBP1 is critical for its appearance on the cell surface and the binding of chylomicrons and lipoprotein lipase.

TL;DR: GPIHBP1 is a glycosylphosphatidylinositol-anchored protein in the lymphocyte antigen 6 (Ly-6) family that recently was identified as a platform for the lipolytic processing of triglyceride-rich lipoproteins as mentioned in this paper.
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Lamellar Lipoproteins Uniquely Contribute to Hyperlipidemia in Mice Doubly Deficient in Apolipoprotein E and Hepatic Lipase

TL;DR: It is shown that the doubly deficient mice manifest a unique lamellar hyperlipoproteinemia, characterized by vesicular particles 600 A-1,300 A in diameter, which are particularly rich in apo A-IV, and it is proposed that cholesteryl esters are removed from spherical lipoproteins of these mice by scavenger receptor B1, leaving behind polar lipid-rich particles that fuse to form vesicle lipoproteinins.
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Enzyme-linked immunosorbent assay for rat hepatic triglyceride lipase.

TL;DR: A noncompetitive enzyme-linked immunosorbent assay to measure rat hepatic triglyceride lipase (H-T GL) was developed and a linear relationship was obtained between absorbance at 490 nm and the amount of highly purified rat H-TGL used as a standard.
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Identification of the epitope of a monoclonal antibody that inhibits heparin binding of lipoprotein lipase: new evidence for a carboxyl-terminal heparin-binding domain.

TL;DR: Experiments indicate that lipoprotein lipase contains a heparin-binding domain, in addition to Arg 281-Arg 284, that can be blocked by xCAL 3-6a, which is found to inhibit the binding to primary avian adipocytes.