cysteine and lewis x antigen

cysteine has been researched along with lewis x antigen in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's3 (100.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Chai, W; Combarnous, Y; Feizi, T; Jankovic, M; Leteux, C; Loveless, RW; Maric, SC; Misulovin, Z; Nussenzweig, MC; Uhlin-Hansen, L; Yuen, CT1
Bjorkman, PJ; Liu, Y; Misulovin, Z1
Baenziger, JU; Roseman, DS1

Other Studies

3 other study(ies) available for cysteine and lewis x antigen

ArticleYear
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 molecular mechanism of sulfated carbohydrate recognition by the cysteine-rich domain of mannose receptor.
    Journal of molecular biology, 2001, Jan-19, Volume: 305, Issue:3

    Topics: Acetylglucosamine; Animals; Binding Sites; Carbohydrate Metabolism; Carbohydrates; Crystallography, X-Ray; Cysteine; Fluorescence; Hydrogen-Ion Concentration; Lectins; Lectins, C-Type; Lewis Blood Group Antigens; Lewis X Antigen; Ligands; Mannose Receptor; Mannose-Binding Lectins; Mice; Models, Molecular; Oligosaccharides; Protein Conformation; Protein Structure, Tertiary; Receptors, Cell Surface; Substrate Specificity; Sulfates; Thermodynamics

2001
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