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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.
Papers
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Journal ArticleDOI
On the apparent rarity of epithelial cancers in captive chimpanzees.
Nissi Varki,Ajit Varki +1 more
TL;DR: It is concluded that while relative carcinoma risk is a likely difference between humans and chimpanzees (and possibly other ‘great apes’), a more systematic survey of available data is required for validation of this claim.
Journal ArticleDOI
Detection of accessory spleens with indium 111‐labeled autologous platelets
TL;DR: In two patients with recurrent immune thrombocytopenia, accessory splenic tissue was demonstrated by radionuclide imaging following administration of indium 111‐labeled autologous platelets, and this new technique provides a simple means for demonstrating accessory spleens and simultaneously evaluating the life‐span of autologious platelets.
Book ChapterDOI
The Major Glycosylation Pathways of Mammalian Membranes A Summary
Ajit Varki,Hudson H. Freeze +1 more
TL;DR: This chapter will broadly scan the subject of structure and biosynthesis of Oligosaccharides on glycoconjugates, primarily in higher animal cells, based on the type of linkage that joins them to the nonsugar component (aglycone), rather than on the types of sugars found in the chains.
Journal ArticleDOI
Redox-Controlled Site-Specific α2–6-Sialylation
Na Lu,Jinfeng Ye,Jiansong Cheng,Aniruddha Sasmal,Chang-Cheng Liu,Wenlong Yao,Jun Yan,Naazneen Khan,Wen Yi,Ajit Varki,Hongzhi Cao +10 more
TL;DR: A general redox-controlled site-specific sialylation strategy using Pd2,6ST is described, which features site- specific enzymatic oxidation of galactose units to mask the unwanted sIALylation sites and precisely controlling the site- Specific α2-6-sialylations at intact galactOSE or N-acetylgalactosamine units.
Purification and Characterization of Rat Liver a-N-Acetylglucosaminyl Phosphodiesterase*
Ajit Varki,Stuart Kornfeld +1 more
TL;DR: The enzyme has no activity toward p-nitrophenyl-alpha-N-acetylglucosamine but is capable of cleaving phosphodiester-linked N-acetelglucOSamine in molecules such as UDP-N -acetyl glucosamines, indicating that it can only hydrolyze N- acetylglUCosamine residues that are alpha-linked to a phosphate group.