Structural Basis for Selective Recognition of Oligosaccharides by DC-SIGN and DC-SIGNR

By H. Feinberg, D. Mitchell, K. Drickamer, William I. Weis. Science, 2001

688 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/89684da7a19b7f36093e68be36241c8b9ec078d8

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Immunology

In Molecular Biology

Y. Kooyk

Citations in the corpus

Mycobacteria Target DC-SIGN to Suppress Dendritic Cell Function (2003, background): “The Ca2 at site 1, the so-called auxiliary site, coordinates the correct positioning of the primary binding site (19, 22), and loss of this Ca2 by mutating Asp320, Glu324 (E324A), Asn350, or Asp355 into Ala residues resulted in complete loss of both M.”
DC-SIGN: escape mechanism for pathogens (2003, background): “, which could explain their distinct carbohydrate-binding specificitie”
From carbohydrate leads to glycomimetic drugs (2009, background): “Thus, E, P and lselectin cocrystallized with sle x or PSGl1 (Pselectin glycoprotein ligand 1) 126 , siaload hesin cocrystallized with 3′sialyl lactose 127 , or DCSIGn cocrystallized with the pentasaccharide GlcNAc 2 Man 3 (REF. 128) hold valuable information for the rational design of glycomimetics.”
DC-SIGN Is the Major Mycobacterium tuberculosis Receptor on Human Dendritic Cells (2003, background): “These additional receptors include the recently identified DC-SIGN (15), a calcium-dependent (C-type) lectin, containing a carbohydrate recognition domain (CRD) at its extracellular COOH-terminal end, that recognizes mannose-rich molecules (16).”
Characterization of β-Glucan Recognition Site on C-Type Lectin, Dectin 1 (2004, background): “saccharides also interact with the surface of DC-SIGN (18).”
Weak Ergodicity Breaking of Receptor Motion in Living Cells Stemming from Random Diffusivity (2014, background): “, a ligand-binding domain; (ii) a long-neck region; and (iii) and a transmembrane part followed by a cytoplasmic tail that allows interactions with inner cell components and facilitates the uptake and internalization of pathogens [46,47].”