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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)
Richard Sadovsky,André Bensadoun +1 more
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.
Anne P. Beigneux,Peter Gin,Brandon S.J. Davies,Michael M. Weinstein,André Bensadoun,Robert O. Ryan,Loren G. Fong,Stephen G. Young +7 more
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
Nathalie Bergeron,Leila Kotite,Marcel Verges,Patricia J. Blanche,Robert L. Hamilton,Ronald M. Krauss,André Bensadoun,Richard J. Havel +7 more
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.
L A Cisar,André Bensadoun +1 more
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.