Journal ArticleDOI
I-type lectins.
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TLDR
The I- type lectins are a subset of the immunoglobulin superfamily that are capable of carbohydrate-protein interactions and there are I-type lectins recognizing sialic acids, other sugars and glycosaminoglycans.About:
This article is published in Biochimica et Biophysica Acta.The article was published on 2002-09-19. It has received 174 citations till now. The article focuses on the topics: Immunoglobulin superfamily & SIGLEC.read more
Citations
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Journal ArticleDOI
Siglecs and their roles in the immune system
TL;DR: The postulated functions of the recently discovered CD33-related Siglecs are discussed and the factors that seem to be driving their rapid evolution are considered.
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Biological Roles of Glycans
TL;DR: It is time for the diverse functional roles of glycans to be fully incorporated into the mainstream of biological sciences, as they are no different from other major macromolecular building blocks of life, simply more rapidly evolving and complex.
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Siglecs--the major subfamily of I-type lectins.
Ajit Varki,Takashi Angata +1 more
TL;DR: Siglecs as mentioned in this paper is a family of I-type lectins with sialic acid (Sia)-binding properties and characteristic amino-terminal structural features, which appear to have evolved by convergent evolution.
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Multifarious roles of sialic acids in immunity
Ajit Varki,Pascal Gagneux +1 more
TL;DR: This overview surveys examples of biological roles of sialic acids in immunity, with emphasis on an evolutionary perspective, given the breadth of the subject.
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Chemical biology of the sugar code.
Hans-Joachim Gabius,Hans-Christian Siebert,Sabine André,Jesús Jiménez-Barbero,Harold Rüdiger +4 more
TL;DR: This review sketches the concept of the sugar code, with a solid description of the historical background, and places emphasis on a distinctive feature of the code, that is, the potential of a carbohydrate ligand to adopt various defined shapes, each with its own particular ligand properties (differential conformer selection).
References
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The Immunological Synapse: A Molecular Machine Controlling T Cell Activation
Arash Grakoui,Shannon K. Bromley,Cenk Sumen,Mark M. Davis,Andrey S. Shaw,Paul M. Allen,Michael L. Dustin +6 more
TL;DR: Immunological synapse formation is now shown to be an active and dynamic mechanism that allows T cells to distinguish potential antigenic ligands and was a determinative event for T cell proliferation.
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Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor.
TL;DR: It is demonstrated that free heparin and heparan sulfate can reconstitute a low affinity receptor that is, in turn, required for the high affinity binding of bFGF.
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Advanced glycation end-products: a review.
TL;DR: The chemistry of advanced glycated end-product formation and their patho-biochemistry particularly in relation to the diabetic microvascular complications of retinopathy, neuropathy and nephropathy as well as their role in the accelerated vasculopathy observed in diabetes are discussed.
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The Immunoglobulin Superfamily—Domains for Cell Surface Recognition
and A F Williams,A N Barclay +1 more
TL;DR: The domain hypothesis was firmly established when the structures of V and C domains were determined to reveal a common fold forming a sandwich of two p-sheets that was stabilized by the conserved disulfide bond.
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Receptor specificity of the fibroblast growth factor family.
David M. Ornitz,Jingsong Xu,Jennifer S. Colvin,Donald G. McEwen,Craig A. MacArthur,François Coulier,Guangxia Gao,Mitchell Goldfarb +7 more
TL;DR: It is demonstrated that FGF 1 is the only FGF that can activate all FGF receptor splice variants and the relative activity of all the other members of the FGF family is determined.