Gilbert Ashwell
National Institutes of Health
109 Papers
5.2K Citations
Gilbert Ashwell is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Asialoglycoproteins & Sialic acid. The author has an hindex of 48, co-authored 109 publications. Previous affiliations of Gilbert Ashwell include Albert Einstein College of Medicine & United States Public Health Service.
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Papers
The Role of Sialic Acid in Determining the Survival of Glycoproteins in the Circulation
TL;DR: Evidence is presented to indicate a generalized role for the terminal sialic acid residues of circulating glycoproteins of desialylated plasma proteins inducers of gonadotropic hormones and follicle-stimulating hormone.
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Architecture of the yeast cell wall. Beta(1-->6)-glucan interconnects mannoprotein, beta(1-->)3-glucan, and chitin.
Roman Kollár,Bruce B. Reinhold,Eva Petráková,Herman J. C. Yeh,Gilbert Ashwell,Jana Drgonová,J. C. Kapteyn,Frans M. Klis,Enrico Cabib +8 more
TL;DR: It is concluded that the latter polysaccharide has a central role in the organization of the yeast cell wall and the possible mechanism of synthesis and physiological significance of the cross-links is discussed.
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The isolation and properties of a rabbit liver binding protein specific for asialoglycoproteins.
Roger L. Hudgin,Roger L. Hudgin,W.E. Pricer,W.E. Pricer,Gilbert Ashwell,Gilbert Ashwell,Richard J. Stockert,Richard J. Stockert,A G Morell,A G Morell +9 more
TL;DR: The purification, by affinity chromatography, of an hepatic protein which retains the characteristic binding properties associated with the membranes is described, which indicates a high degree of aggregation in the final, water-soluble preparation.
608
Receptor-mediated endocytosis of transferrin in K562 cells
Richard D. Klausner,J van Renswoude,Gilbert Ashwell,C. Kempf,Alan N. Schechter,A Dean,Kenneth Bridges +6 more
TL;DR: Human diferric transferrin binds to the surface of K562 cells, a human leukemic cell line, and the loss of surface receptors upon internalization never exceeds 60-70% of the initial binding capacity suggests that receptors enter the cell with ligand but are replaced so as to maintain a constant, albeit reduced, receptor number on the cell surface.
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