T
Ten Feizi
Researcher at Imperial College London
Publications - 387
Citations - 25073
Ten Feizi is an academic researcher from Imperial College London. The author has contributed to research in topics: Antigen & Oligosaccharide. The author has an hindex of 82, co-authored 381 publications receiving 23988 citations. Previous affiliations of Ten Feizi include Northwick Park Hospital & University of Southampton.
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Journal ArticleDOI
Demonstration by Monoclonal Antibodies That Carbohydrate Structures of Glycoproteins and Glycolipids Are Onco-Developmental Antigens
TL;DR: These findings either may reflect limitations in the methods of selection of hybridoma antibodies or point to important roles for the diverse carbohydrate structures as receptors for regulators of cell growth and differentiation.
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A Potent and Broad Neutralizing Antibody Recognizes and Penetrates the HIV Glycan Shield
Robert Pejchal,Katie J. Doores,Katie J. Doores,Laura M. Walker,Reza Khayat,Po-Ssu Huang,Sheng-Kai Wang,Robyn L. Stanfield,Jean-Philippe Julien,Alejandra Ramos,Matthew Crispin,Rafael S. Depetris,Umesh Katpally,Andre Marozsan,Albert Cupo,Sebastien M. Maloveste,Yan Liu,Ryan McBride,Yukishige Ito,Rogier W. Sanders,Cassandra Ogohara,James C. Paulson,Ten Feizi,Christopher N. Scanlan,Chi-Huey Wong,John P. Moore,William C. Olson,Andrew B. Ward,Pascal Poignard,Pascal Poignard,William R. Schief,William R. Schief,Dennis R. Burton,Dennis R. Burton,Ian A. Wilson +34 more
TL;DR: The data suggest that the high neutralization potency of PGT 127 and 128 immunoglobulin Gs may be mediated by cross-linking Env trimers on the viral surface.
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Stage-specific embryonic antigen involves alpha 1 goes to 3 fucosylated type 2 blood group chains.
TL;DR: Evidence is described that the stage-specific embryonic antigen SSEA-1 involves the carbohydrate sequence Galβ1 → 4GlcNAc ↑1,3 Fucα, which is formed by α 1 → 3 fucosylation of blood group I or i antigens, respectively.
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Oligosaccharide microarrays for high-throughput detection and specificity assignments of carbohydrate-protein interactions
TL;DR: In this article, the authors describe microarrays of oligosaccharides as neoglycolipids and their robust display on nitrocellulose, and show that carbohydrate-recognizing proteins single out their ligands not only in arrays of homogeneous oligosACcharides but also in array of heterogeneous oligo-charides.
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Complex-type N-glycan recognition by potent broadly neutralizing HIV antibodies.
Hugo Mouquet,Louise Scharf,Zelda Euler,Yan Liu,Caroline Eden,Johannes F. Scheid,Johannes F. Scheid,Ariel Halper-Stromberg,Priyanthi N. P. Gnanapragasam,Daniel I. R. Spencer,Michael S. Seaman,Hanneke Schuitemaker,Ten Feizi,Michel C. Nussenzweig,Pamela J. Bjorkman +14 more
TL;DR: As HIV envelopes exhibit varying proportions of high-mannose- and complex-type N-glycans, these results suggest promiscuous carbohydrate interactions, an advantageous adaptation ensuring neutralization of all viruses within a given strain.