Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-94 |
Sentence |
denotes |
Characterization of carbohydrate recognition by langerin, a C-type lectin of Langerhans cells. |
T1 |
0-94 |
Sentence |
denotes |
Characterization of carbohydrate recognition by langerin, a C-type lectin of Langerhans cells. |
TextSentencer_T2 |
95-179 |
Sentence |
denotes |
Langerin is a type II transmembrane cell surface receptor found on Langerhans cells. |
T2 |
95-179 |
Sentence |
denotes |
Langerin is a type II transmembrane cell surface receptor found on Langerhans cells. |
TextSentencer_T3 |
180-343 |
Sentence |
denotes |
The extracellular domain of langerin consists of a neck region containing a series of heptad repeats and a C-terminal C-type carbohydrate-recognition domain (CRD). |
T3 |
180-343 |
Sentence |
denotes |
The extracellular domain of langerin consists of a neck region containing a series of heptad repeats and a C-terminal C-type carbohydrate-recognition domain (CRD). |
TextSentencer_T4 |
344-488 |
Sentence |
denotes |
A role for langerin in processing of glycoprotein antigens has been proposed, but until now there has been little study of the langerin protein. |
T4 |
344-488 |
Sentence |
denotes |
A role for langerin in processing of glycoprotein antigens has been proposed, but until now there has been little study of the langerin protein. |
TextSentencer_T5 |
489-792 |
Sentence |
denotes |
In this study, analytical ultracentrifugation and circular dichroism spectroscopy of recombinant soluble fragments of human langerin have been used to show that the extracellular region of this receptor exists as a stable trimer held together by a coiled coil of alpha-helices formed by the neck region. |
T5 |
489-792 |
Sentence |
denotes |
In this study, analytical ultracentrifugation and circular dichroism spectroscopy of recombinant soluble fragments of human langerin have been used to show that the extracellular region of this receptor exists as a stable trimer held together by a coiled coil of alpha-helices formed by the neck region. |
TextSentencer_T6 |
793-943 |
Sentence |
denotes |
The langerin CRD shows specificity for mannose, GlcNAc, and fucose, but only the trimeric extracellular domain fragment binds to glycoprotein ligands. |
T6 |
793-943 |
Sentence |
denotes |
The langerin CRD shows specificity for mannose, GlcNAc, and fucose, but only the trimeric extracellular domain fragment binds to glycoprotein ligands. |
TextSentencer_T7 |
944-1122 |
Sentence |
denotes |
Langerin extracellular domain binds mammalian high mannose oligosaccharides, as well mannose-containing structures on yeast invertase but does not bind complex glycan structures. |
T7 |
944-1122 |
Sentence |
denotes |
Langerin extracellular domain binds mammalian high mannose oligosaccharides, as well mannose-containing structures on yeast invertase but does not bind complex glycan structures. |
TextSentencer_T8 |
1123-1408 |
Sentence |
denotes |
Full-length langerin stably expressed in rat fibroblast transfectants mediates efficient uptake and degradation of a mannosylated neoglycoprotein ligand. pH-dependent ligand release appears to involve interactions between the CRDs or between the CRDs and the neck region in the trimer. |
T8 |
1123-1408 |
Sentence |
denotes |
Full-length langerin stably expressed in rat fibroblast transfectants mediates efficient uptake and degradation of a mannosylated neoglycoprotein ligand. pH-dependent ligand release appears to involve interactions between the CRDs or between the CRDs and the neck region in the trimer. |
TextSentencer_T9 |
1409-1527 |
Sentence |
denotes |
The results are consistent with a role for langerin in internalization of both self and nonself glycoprotein antigens. |
T9 |
1409-1527 |
Sentence |
denotes |
The results are consistent with a role for langerin in internalization of both self and nonself glycoprotein antigens. |