n-acetylgalactosamine 4-sulfate and lewis x antigen

n-acetylgalactosamine 4-sulfate has been researched along with lewis x antigen in 2 studies

Compound Research Comparison

Studies (n-acetylgalactosamine 4-sulfate)	Trials (n-acetylgalactosamine 4-sulfate)	Recent Studies (post-2010) (n-acetylgalactosamine 4-sulfate)	Studies (lewis x antigen)	Trials (lewis x antigen)	Recent Studies (post-2010) (lewis x antigen)
18	0	3	2,147	29	438

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Chai, W; Combarnous, Y; Feizi, T; Jankovic, M; Leteux, C; Loveless, RW; Maric, SC; Misulovin, Z; Nussenzweig, MC; Uhlin-Hansen, L; Yuen, CT	1
Baenziger, JU; Roseman, DS	1

Other Studies

2 other study(ies) available for n-acetylgalactosamine 4-sulfate and lewis x antigen

Article	Year
The cysteine-rich domain of the macrophage mannose receptor is a multispecific lectin that recognizes chondroitin sulfates A and B and sulfated oligosaccharides of blood group Lewis(a) and Lewis(x) types in addition to the sulfated N-glycans of lutropin. The Journal of experimental medicine, 2000, Apr-03, Volume: 191, Issue:7 Topics: Acetylgalactosamine; Animals; Binding Sites; Carbohydrate Sequence; Chondroitin Sulfates; Cysteine; Dermatan Sulfate; Humans; Lectins; Lectins, C-Type; Lewis Blood Group Antigens; Lewis X Antigen; Luteinizing Hormone; Macrophages; Mannose Receptor; Mannose-Binding Lectins; Mice; Molecular Sequence Data; Oligosaccharides; Polysaccharides; Proteoglycans; Receptors, Cell Surface; Sialyl Lewis X Antigen; Spleen; Staining and Labeling	2000
The mannose/N-acetylgalactosamine-4-SO4 receptor displays greater specificity for multivalent than monovalent ligands. The Journal of biological chemistry, 2001, May-18, Volume: 276, Issue:20 Topics: Acetylgalactosamine; Animals; Binding Sites; Binding, Competitive; Carbohydrate Sequence; Cattle; Cell Membrane; Cysteine; Entropy; Kinetics; Lewis X Antigen; Ligands; Mannose; Mannose-Binding Lectins; Molecular Sequence Data; Oligosaccharides; Receptors, Cell Surface; Serum Albumin, Bovine; Substrate Specificity; Surface Plasmon Resonance; Trisaccharides	2001

Article

Year

The cysteine-rich domain of the macrophage mannose receptor is a multispecific lectin that recognizes chondroitin sulfates A and B and sulfated oligosaccharides of blood group Lewis(a) and Lewis(x) types in addition to the sulfated N-glycans of lutropin.

The Journal of experimental medicine, 2000, Apr-03, Volume: 191, Issue:7

Topics: Acetylgalactosamine; Animals; Binding Sites; Carbohydrate Sequence; Chondroitin Sulfates; Cysteine; Dermatan Sulfate; Humans; Lectins; Lectins, C-Type; Lewis Blood Group Antigens; Lewis X Antigen; Luteinizing Hormone; Macrophages; Mannose Receptor; Mannose-Binding Lectins; Mice; Molecular Sequence Data; Oligosaccharides; Polysaccharides; Proteoglycans; Receptors, Cell Surface; Sialyl Lewis X Antigen; Spleen; Staining and Labeling

2000

The mannose/N-acetylgalactosamine-4-SO4 receptor displays greater specificity for multivalent than monovalent ligands.

The Journal of biological chemistry, 2001, May-18, Volume: 276, Issue:20

Topics: Acetylgalactosamine; Animals; Binding Sites; Binding, Competitive; Carbohydrate Sequence; Cattle; Cell Membrane; Cysteine; Entropy; Kinetics; Lewis X Antigen; Ligands; Mannose; Mannose-Binding Lectins; Molecular Sequence Data; Oligosaccharides; Receptors, Cell Surface; Serum Albumin, Bovine; Substrate Specificity; Surface Plasmon Resonance; Trisaccharides

2001