E
E. V. Chandrasekaran
Researcher at Roswell Park Cancer Institute
Publications - 44
Citations - 934
E. V. Chandrasekaran is an academic researcher from Roswell Park Cancer Institute. The author has contributed to research in topics: Sialyltransferase & Glycan. The author has an hindex of 18, co-authored 44 publications receiving 891 citations.
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Journal ArticleDOI
Fluorinated per-acetylated GalNAc metabolically alters glycan structures on leukocyte PSGL-1 and reduces cell binding to selectins
Dhananjay Marathe,Alexander Buffone,E. V. Chandrasekaran,Jun Xue,Robert D. Locke,Mehrab Nasirikenari,Joseph T.Y. Lau,Khushi L. Matta,Sriram Neelamegham +8 more
TL;DR: Overall, the data suggest that 4F-GalNAc may be applied as a metabolic inhibitor to reduce O-linked glycosylation, sialyl Lewis-X formation, and leukocyte adhesion via the selectins.
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The pattern of glycosyl- and sulfotransferase activities in cancer cell lines: a predictor of individual cancer-associated distinct carbohydrate structures for the structural identification of signature glycans
TL;DR: 3'-Sulfo-T-hapten has an apparent relationship to the tumorigenic potential of breast cancer cells and the existence of unique carbohydrate moieties in certain cancer-associated glycolipids is suggested.
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Biologic contribution of P1 promoter-mediated expression of ST6Gal I sialyltransferase.
Michelle M. Appenheimer,Ruea-Yea Huang,E. V. Chandrasekaran,Martin Dalziel,Yi Ping Hu,Paul D. Soloway,Sherry A. Wuensch,Khushi L. Matta,Joseph T.Y. Lau +8 more
TL;DR: Siat1deltaP1 animals are unable to elevate hepatic Siat1 mRNA as part of the inflammatory response induced by turpentine, and serum glycoprotein components exhibit normal extent of sialylation.
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Ovarian cancer alpha 1,3-L-fucosyltransferase. Differentiation of distinct catalytic species with the unique substrate, 3'-sulfo-N-acetyllactosamine in conjunction with other synthetic acceptors.
TL;DR: Several N-acetyllactosamine derivatives were tested as acceptors for alpha 1,3-L-fucosyltransferase present in human ovarian cancer sera and ovarian tumor, indicating the coexistence of alpha 1-3- andalpha 1,4- fucosytransferase.
Journal ArticleDOI
Specificity analysis of three clonal and five non-clonal alpha 1,3-L-fucosyltransferases with sulfated, sialylated, or fucosylated synthetic carbohydrates as acceptors in relation to the assembly of 3'-sialyl-6'-sulfo Lewis x (the L-selectin ligand) and related complex structures.
E. V. Chandrasekaran,Rakesh K. Jain,Robert D. Larsen,Ken Wlasichuk,Richard A. DiCioccio,Khushi L. Matta +5 more
TL;DR: Unique specificities of the cloned alpha 1,3-L-fucosyltransferases (FTs), FT III, FT IV, and FT V (myeloid type), and the alpha 1-3-FTs of Colo 205 (colon carcinoma), HL 60, HL60, B142, EKVX, and calf mesenteric lymph nodes (CMLN) were discerned with sulfated, sialylated, and/or f