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Ajit Varki

Researcher at University of California, San Diego

Publications -  557
Citations -  63836

Ajit Varki is an academic researcher from University of California, San Diego. The author has contributed to research in topics: Sialic acid & SIGLEC. The author has an hindex of 124, co-authored 542 publications receiving 58772 citations. Previous affiliations of Ajit Varki include Emory University & National Institute of Advanced Industrial Science and Technology.

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Structural studies of phosphorylated high mannose-type oligosaccharides.

TL;DR: It is found that the oligosaccharide units of newly synthesized beta-glucuronidase contain phosphate residues in diester linkage between mannose and alpha-linked N-acetylglucosamine residues, and it is demonstrated that phosphorylation can occur at 5 separateMannose residues on the high mannosed-type oligOSaccharides.
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P-selectin mediates the adhesion of sickle erythrocytes to the endothelium

TL;DR: First evidence for the novel adhesion of normal and, to a greater extent, sickle RBCs to endothelial P-selectin is presented, suggesting that P- selectin inhibition be considered as a potential approach to therapy for the treatment of painful vaso-occlusion in sickle cell disease.
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Differential metastasis inhibition by clinically relevant levels of heparins--correlation with selectin inhibition, not antithrombotic activity.

TL;DR: Heparin can attenuate metastasis at clinically relevant doses, likely by inhibiting selectins, and hitherto unsuspected benefits of selectin inhibition in various clinical circumstances may be unwittingly discarded.
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A monoclonal antibody recognizes an O-acylated sialic acid in a human melanoma-associated ganglioside.

TL;DR: Findings suggest that the antigenic epitope defined by antibody D1.1 contains an O-acylated sialic acid and may arise from aberrant O-acetylation occurring in human malignant melanoma cells.
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The spectrum of anionic oligosaccharides released by endo-beta-N-acetylglucosaminidase H from glycoproteins. Structural studies and interactions with the phosphomannosyl receptor.

TL;DR: The findings indicate that the generation of the physiological phosphomannosyl ligand on lysosomal enzymes involves removal of the blocking N-acetylglucosamine residues, trimming of certain mannose residues, and correct positioning of the phosphate esters.