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The structure of siglec-7 in complex with sialosides: leads for rational structure-based inhibitor designGalactose 6-O-sulfotransferases are not required for the generation of Siglec-F ligands in leukocytes or lung tissueDevelopmental, malignancy-related, and cross-species analysis of eosinophil, mast cell, and basophil siglec-8 expressionSiglec-F antibody administration to mice selectively reduces blood and tissue eosinophilsAntigen delivery to macrophages using liposomal nanoparticles targeting sialoadhesin/CD169High resolution crystal structures of Siglec-7. Insights into ligand specificity in the Siglec familyStructure-guided design of sialic acid-based Siglec inhibitors and crystallographic analysis in complex with sialoadhesinEnhancing the Receptor Affinity of the Sialic Acid-binding Domain of Vibrio cholerae Sialidase through MultivalencyGanglioside GD3 expression on target cells can modulate NK cell cytotoxicity via siglec-7-dependent and -independent mechanismsProbing sialic acid binding Ig-like lectins (siglecs) with sulfated oligosaccharidesAnalysis of the CD33-related siglec family reveals that Siglec-9 is an endocytic receptor expressed on subsets of acute myeloid leukemia cells and absent from normal hematopoietic progenitorsMouse Siglec-F and human Siglec-8 are functionally convergent paralogs that are selectively expressed on eosinophils and recognize 6'-sulfo-sialyl Lewis X as a preferred glycan ligandCrystallographic and in silico analysis of the sialoside-binding characteristics of the Siglec sialoadhesinSiglecs and their roles in the immune systemMyelin-associated glycoprotein interacts with neurons via a sialic acid binding site at ARG118 and a distinct neurite inhibition siteCharacterization of Siglec-H as a novel endocytic receptor expressed on murine plasmacytoid dendritic cell precursorsHuman Siglec-10 can bind to vascular adhesion protein-1 and serves as its substrateSiglec-9 is a novel leukocyte ligand for vascular adhesion protein-1 and can be used in PET imaging of inflammation and cancer.Siglec-9, a novel sialic acid binding member of the immunoglobulin superfamily expressed broadly on human blood leukocytes.Chemoenzymatic synthesis of sialooligosaccharides on arrays for studies of cell surface adhesionGlycopeptides as oligosaccharide mimics: high affinity sialopeptide ligands for sialoadhesin from combinatorial libraries.Probing the cis interactions of the inhibitory receptor Siglec-7 with alpha2,8-disialylated ligands on natural killer cells and other leukocytes using glycan-specific antibodies and by analysis of alpha2,8-sialyltransferase gene expression.A versatile gold surface approach for fabrication and interrogation of glycoarrays.The M/GP(5) glycoprotein complex of porcine reproductive and respiratory syndrome virus binds the sialoadhesin receptor in a sialic acid-dependent manner.Siglecs facilitate HIV-1 infection of macrophages through adhesion with viral sialic acids.New functions for the sialic acid-binding adhesion molecule CD22, a member of the growing family of Siglecs.Sialoadhesin-deficient mice exhibit subtle changes in B- and T-cell populations and reduced immunoglobulin M levels.Siglec-5 (CD170) can mediate inhibitory signaling in the absence of immunoreceptor tyrosine-based inhibitory motif phosphorylation.Siglecs: sialic-acid-binding immunoglobulin-like lectins in cell-cell interactions and signalling.Early murine T-lymphocyte activation is accompanied by a switch from N-Glycolyl- to N-acetyl-neuraminic acid and generation of ligands for siglec-ESiglec-E is a negative regulator of acute pulmonary neutrophil inflammation and suppresses CD11b β2-integrin-dependent signaling.An expression system for screening of proteins for glycan and protein interactions.Sialoadhesin deficiency does not influence the severity of lupus nephritis in New Zealand black x New Zealand white F1 mice.Evolution of CD33-related siglecs: regulating host immune functions and escaping pathogen exploitation?CD33-related siglecs as potential modulators of inflammatory responses.Sialoadhesin in recognition of self and non-self.The amino-terminal immunoglobulin-like domain of sialoadhesin contains the sialic acid binding site. Comparison with CD22.A small region of the natural killer cell receptor, Siglec-7, is responsible for its preferred binding to alpha 2,8-disialyl and branched alpha 2,6-sialyl residues. A comparison with Siglec-9.Neoglycolipid probes prepared via oxime ligation for microarray analysis of oligosaccharide-protein interactions.Siglec-7 undergoes a major conformational change when complexed with the alpha(2,8)-disialylganglioside GT1b.
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P50
description
hulumtues
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հետազոտող
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name
Paul R Crocker
@nl
Paul R Crocker
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Paul R. Crocker
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Paul R. Crocker
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Paul R. Crocker
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type
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Paul R Crocker
@nl
Paul R Crocker
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Paul R. Crocker
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Paul R. Crocker
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Paul R. Crocker
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Richard
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Paul R Crocker
@nl
Paul R Crocker
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Paul R. Crocker
@de
Paul R. Crocker
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Paul R. Crocker
@es
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