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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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Glycosylation Changes in Cancer
TL;DR: In this paper, the authors discuss glycan biosynthetic pathways that are frequently altered in cancer cells, correlations between altered glycosylation, diagnosis, and clinical prognosis; the genetic bases of some of these changes; and studies indicating their pathological importance.
Journal ArticleDOI
A red meat-derived glycan promotes inflammation and cancer progression.
Annie N. Samraj,Oliver M. T. Pearce,Heinz Läubli,Alyssa N. Crittenden,Anne K. Bergfeld,Kalyan Banda,Christopher J. Gregg,Andrea E. Bingman,Patrick Secrest,Sandra Diaz,Nissi Varki,Ajit Varki +11 more
TL;DR: An improved method is used to survey common foods for free and glycosidically bound forms of the nonhuman sialic acid N-glycolylneuraminic acid (Neu5Gc), showing that it is highly and selectively enriched in red meat and is bioavailable, undergoing metabolic incorporation into human tissues, despite being a foreign antigen.
Journal ArticleDOI
Comparing the human and chimpanzee genomes: Searching for needles in a haystack
Ajit Varki,Tasha K. Altheide +1 more
TL;DR: The chimpanzee genome sequence is a long-awaited milestone, providing opportunities to explore primate evolution and genetic contributions to human physiology and disease, and both genome-wide analyses and candidate gene studies should be considered complementary.
Journal ArticleDOI
Loss of N-glycolylneuraminic acid in humans: Mechanisms, consequences, and implications for hominid evolution.
TL;DR: Evidence that the human condition can explain differences in susceptibility or resistance to certain microbial pathogens and a markedly reduced expression of hydroxylase in the brains of other mammals raises the possibility that thehuman‐specific mutation of this enzyme could have played a role in human brain evolution.
Journal ArticleDOI
Fibroblasts from patients with I-cell disease and pseudo-Hurler polydystrophy are deficient in uridine 5'-diphosphate-N-acetylglucosamine: glycoprotein N-acetylglucosaminylphosphotransferase activity.
TL;DR: It is demonstrated that fibroblasts from patients with the lysosomal enzyme storage diseases, I-cell disease and pseudo-Hurler polydystrophy, are severely deficient in UDP-N-acetylglucosamine:glycoprotein N-acetyglucOSaminylphosphotransferase, the first enzyme of the sequence.