PubMed:18621992
Annnotations
Glycan-Motif
{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":47,"end":54},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T2","span":{"begin":151,"end":158},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T3","span":{"begin":224,"end":231},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T4","span":{"begin":410,"end":417},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T5","span":{"begin":594,"end":601},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
GlyCosmos600-Glycan-Motif-Structure
{"project":"GlyCosmos600-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":47,"end":54},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T2","span":{"begin":151,"end":158},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T3","span":{"begin":224,"end":231},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T4","span":{"begin":410,"end":417},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T5","span":{"begin":594,"end":601},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
GlyCosmos600-CLO
{"project":"GlyCosmos600-CLO","denotations":[{"id":"T1","span":{"begin":568,"end":577},"obj":"http://purl.obolibrary.org/obo/GO_0005764"},{"id":"T2","span":{"begin":666,"end":674},"obj":"http://purl.obolibrary.org/obo/GO_0005764"},{"id":"T3","span":{"begin":717,"end":725},"obj":"http://purl.obolibrary.org/obo/GO_0005764"},{"id":"T4","span":{"begin":870,"end":874},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
GlyCosmos6-Glycan-Motif-Image
{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":47,"end":54},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":151,"end":158},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":224,"end":231},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":410,"end":417},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":594,"end":601},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
PMID_GLOBAL
{"project":"PMID_GLOBAL","denotations":[{"id":"T1","span":{"begin":181,"end":183},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T2","span":{"begin":762,"end":764},"obj":"DiseaseOrPhenotypicFeature"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"0016063"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"0016063"}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
sentences
{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":77},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":78,"end":427},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":428,"end":675},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":676,"end":883},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":884,"end":1083},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1084,"end":1255},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":77},"obj":"Sentence"},{"id":"T2","span":{"begin":78,"end":427},"obj":"Sentence"},{"id":"T3","span":{"begin":428,"end":675},"obj":"Sentence"},{"id":"T4","span":{"begin":676,"end":883},"obj":"Sentence"},{"id":"T5","span":{"begin":884,"end":1083},"obj":"Sentence"},{"id":"T6","span":{"begin":1084,"end":1255},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
GlyCosmos6-Glycan-Motif-Structure
{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":47,"end":54},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T2","span":{"begin":151,"end":158},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T3","span":{"begin":224,"end":231},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T4","span":{"begin":410,"end":417},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T5","span":{"begin":594,"end":601},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
ICD10
{"project":"ICD10","denotations":[{"id":"T1","span":{"begin":503,"end":511},"obj":"http://purl.bioontology.org/ontology/ICD10/O80-O84.9"}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
uniprot-human
{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":181,"end":187},"obj":"http://www.uniprot.org/uniprot/P20645"},{"id":"T2","span":{"begin":762,"end":768},"obj":"http://www.uniprot.org/uniprot/P20645"},{"id":"T3","span":{"begin":184,"end":200},"obj":"http://www.uniprot.org/uniprot/P11717"},{"id":"T4","span":{"begin":254,"end":260},"obj":"http://www.uniprot.org/uniprot/P11717"},{"id":"T5","span":{"begin":742,"end":748},"obj":"http://www.uniprot.org/uniprot/P11717"}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
uniprot-mouse
{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":181,"end":187},"obj":"http://www.uniprot.org/uniprot/P24668"},{"id":"T2","span":{"begin":762,"end":768},"obj":"http://www.uniprot.org/uniprot/P24668"},{"id":"T3","span":{"begin":184,"end":200},"obj":"http://www.uniprot.org/uniprot/Q07113"},{"id":"T4","span":{"begin":254,"end":260},"obj":"http://www.uniprot.org/uniprot/Q07113"},{"id":"T5","span":{"begin":742,"end":748},"obj":"http://www.uniprot.org/uniprot/Q07113"},{"id":"T6","span":{"begin":888,"end":892},"obj":"http://www.uniprot.org/uniprot/Q6A009"}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
GlycoBiology-NCBITAXON
{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":67,"end":76},"obj":"http://purl.bioontology.org/ontology/STY/T192"},{"id":"T2","span":{"begin":254,"end":256},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/245896"},{"id":"T3","span":{"begin":742,"end":744},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/245896"},{"id":"T4","span":{"begin":1052,"end":1055},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/604139"},{"id":"T5","span":{"begin":1156,"end":1165},"obj":"http://purl.bioontology.org/ontology/STY/T192"},{"id":"T6","span":{"begin":1170,"end":1177},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/353209"}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
GO-BP
{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":395,"end":409},"obj":"http://purl.obolibrary.org/obo/GO_0016310"}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
GO-MF
{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":910,"end":917},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T2","span":{"begin":1075,"end":1082},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
GO-CC
{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":568,"end":577},"obj":"http://purl.obolibrary.org/obo/GO_0005764"},{"id":"T2","span":{"begin":666,"end":674},"obj":"http://purl.obolibrary.org/obo/GO_0005764"},{"id":"T3","span":{"begin":717,"end":725},"obj":"http://purl.obolibrary.org/obo/GO_0005764"},{"id":"T4","span":{"begin":695,"end":708},"obj":"http://purl.obolibrary.org/obo/GO_0005622"},{"id":"T5","span":{"begin":870,"end":874},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T6","span":{"begin":870,"end":882},"obj":"http://purl.obolibrary.org/obo/GO_0009986"},{"id":"T7","span":{"begin":896,"end":909},"obj":"http://purl.obolibrary.org/obo/GO_0005576"}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
GlyCosmos600-FMA
{"project":"GlyCosmos600-FMA","denotations":[{"id":"T1","span":{"begin":15,"end":27},"obj":"Body_part"},{"id":"T2","span":{"begin":47,"end":54},"obj":"Body_part"},{"id":"T3","span":{"begin":151,"end":158},"obj":"Body_part"},{"id":"T4","span":{"begin":224,"end":231},"obj":"Body_part"},{"id":"T5","span":{"begin":410,"end":417},"obj":"Body_part"},{"id":"T6","span":{"begin":568,"end":577},"obj":"Body_part"},{"id":"T7","span":{"begin":594,"end":601},"obj":"Body_part"},{"id":"T8","span":{"begin":642,"end":658},"obj":"Body_part"},{"id":"T9","span":{"begin":666,"end":674},"obj":"Body_part"},{"id":"T10","span":{"begin":717,"end":725},"obj":"Body_part"},{"id":"T11","span":{"begin":870,"end":882},"obj":"Body_part"},{"id":"T12","span":{"begin":870,"end":874},"obj":"Body_part"},{"id":"T13","span":{"begin":1024,"end":1032},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"fma_id","subj":"T1","obj":"http://purl.org/sig/ont/fma/fma82737"},{"id":"A2","pred":"fma_id","subj":"T2","obj":"http://purl.org/sig/ont/fma/fma82801"},{"id":"A3","pred":"fma_id","subj":"T3","obj":"http://purl.org/sig/ont/fma/fma82801"},{"id":"A4","pred":"fma_id","subj":"T4","obj":"http://purl.org/sig/ont/fma/fma82801"},{"id":"A5","pred":"fma_id","subj":"T5","obj":"http://purl.org/sig/ont/fma/fma82801"},{"id":"A6","pred":"fma_id","subj":"T6","obj":"http://purl.org/sig/ont/fma/fma63836"},{"id":"A7","pred":"fma_id","subj":"T7","obj":"http://purl.org/sig/ont/fma/fma82801"},{"id":"A8","pred":"fma_id","subj":"T8","obj":"http://purl.org/sig/ont/fma/fma82742"},{"id":"A9","pred":"fma_id","subj":"T9","obj":"http://purl.org/sig/ont/fma/fma63836"},{"id":"A10","pred":"fma_id","subj":"T10","obj":"http://purl.org/sig/ont/fma/fma63836"},{"id":"A11","pred":"fma_id","subj":"T11","obj":"http://purl.org/sig/ont/fma/fma67653"},{"id":"A12","pred":"fma_id","subj":"T12","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A13","pred":"fma_id","subj":"T13","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
glycosmos-test-glycan-structure
{"project":"glycosmos-test-glycan-structure","denotations":[{"id":"PD-GlycanStructures-B_T1","span":{"begin":47,"end":54},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T2","span":{"begin":151,"end":158},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T3","span":{"begin":224,"end":231},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T4","span":{"begin":410,"end":417},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T5","span":{"begin":594,"end":601},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
glycosmos-test-structure-v1
{"project":"glycosmos-test-structure-v1","denotations":[{"id":"PD-GlycanStructures-B_T1","span":{"begin":47,"end":54},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T2","span":{"begin":151,"end":158},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T3","span":{"begin":224,"end":231},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T4","span":{"begin":410,"end":417},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T5","span":{"begin":594,"end":601},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
GlyCosmos600-GlycoProteins
{"project":"GlyCosmos600-GlycoProteins","denotations":[{"id":"PD-GlycoProteins-B_T1","span":{"begin":134,"end":179},"obj":"https://acgg.asia/db/gpdb/id/GPDB0003510"},{"id":"PD-GlycoProteins-B_T2","span":{"begin":205,"end":252},"obj":"https://acgg.asia/db/gpdb/id/GPDB0003923"}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
pubmed-enju-pas
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for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
Lectin
{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":615,"end":618},"obj":"https://acgg.asia/db/lfdb/LfDB0217"},{"id":"Lectin_T2","span":{"begin":1005,"end":1008},"obj":"https://acgg.asia/db/lfdb/LfDB0217"},{"id":"Lectin_T3","span":{"begin":1056,"end":1059},"obj":"https://acgg.asia/db/lfdb/LfDB0217"},{"id":"Lectin_T4","span":{"begin":181,"end":187},"obj":"https://acgg.asia/db/lfdb/LfDB0096"},{"id":"Lectin_T5","span":{"begin":762,"end":768},"obj":"https://acgg.asia/db/lfdb/LfDB0096"},{"id":"Lectin_T6","span":{"begin":254,"end":260},"obj":"https://acgg.asia/db/lfdb/LfDB0097"},{"id":"Lectin_T7","span":{"begin":742,"end":748},"obj":"https://acgg.asia/db/lfdb/LfDB0097"}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
GlyTouCan-IUPAC
{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G41652MJ\""},{"id":"GlycanIUPAC_T2","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G20761YC\""},{"id":"GlycanIUPAC_T3","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G19807HM\""},{"id":"GlycanIUPAC_T4","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G20351TE\""},{"id":"GlycanIUPAC_T5","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G71957MR\""},{"id":"GlycanIUPAC_T6","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G59040AE\""},{"id":"GlycanIUPAC_T7","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G14987PW\""},{"id":"GlycanIUPAC_T8","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G95064PC\""},{"id":"GlycanIUPAC_T9","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G39143AQ\""},{"id":"GlycanIUPAC_T10","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G65149OO\""},{"id":"GlycanIUPAC_T11","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G02766SY\""},{"id":"GlycanIUPAC_T12","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G26019KJ\""},{"id":"GlycanIUPAC_T13","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G36429CZ\""},{"id":"GlycanIUPAC_T14","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G89633TP\""},{"id":"GlycanIUPAC_T15","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G28494FO\""},{"id":"GlycanIUPAC_T16","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G06219CP\""},{"id":"GlycanIUPAC_T17","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G44237SM\""},{"id":"GlycanIUPAC_T18","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G57948RL\""},{"id":"GlycanIUPAC_T19","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G64016DN\""},{"id":"GlycanIUPAC_T20","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G14536PC\""},{"id":"GlycanIUPAC_T21","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G14356FW\""},{"id":"GlycanIUPAC_T22","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G34565UO\""},{"id":"GlycanIUPAC_T23","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G67124MW\""},{"id":"GlycanIUPAC_T24","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G71457ZU\""},{"id":"GlycanIUPAC_T25","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G55228VZ\""},{"id":"GlycanIUPAC_T26","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G31034MJ\""},{"id":"GlycanIUPAC_T27","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G25776IP\""},{"id":"GlycanIUPAC_T28","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G64442BV\""},{"id":"GlycanIUPAC_T29","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G57018LE\""},{"id":"GlycanIUPAC_T30","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G61761GX\""},{"id":"GlycanIUPAC_T31","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G76318UX\""},{"id":"GlycanIUPAC_T32","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G61906ER\""},{"id":"GlycanIUPAC_T33","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G68723GR\""},{"id":"GlycanIUPAC_T34","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G19540LE\""},{"id":"GlycanIUPAC_T35","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G74944PO\""},{"id":"GlycanIUPAC_T36","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G89489ZJ\""},{"id":"GlycanIUPAC_T37","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G04434YU\""},{"id":"GlycanIUPAC_T38","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G21450PB\""},{"id":"GlycanIUPAC_T39","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G93629QY\""},{"id":"GlycanIUPAC_T40","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G02603TR\""},{"id":"GlycanIUPAC_T41","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G40280JP\""},{"id":"GlycanIUPAC_T42","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G95259IC\""},{"id":"GlycanIUPAC_T43","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G26900FE\""},{"id":"GlycanIUPAC_T44","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G21346KK\""},{"id":"GlycanIUPAC_T45","span":{"begin":347,"end":350},"obj":"\"http://rdf.glycoinfo.org/glycan/G62509FF\""},{"id":"GlycanIUPAC_T46","span":{"begin":347,"end":350},"obj"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6,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G45970UX\""},{"id":"GlycanIUPAC_T183","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G93661NW\""},{"id":"GlycanIUPAC_T184","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G93661NW\""},{"id":"GlycanIUPAC_T185","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G93661NW\""},{"id":"GlycanIUPAC_T186","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G04988XL\""},{"id":"GlycanIUPAC_T187","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G04988XL\""},{"id":"GlycanIUPAC_T188","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G04988XL\""},{"id":"GlycanIUPAC_T189","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G85800UH\""},{"id":"GlycanIUPAC_T190","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G85800UH\""},{"id":"GlycanIUPAC_T191","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G85800UH\""},{"id":"GlycanIUPAC_T192","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G96338GZ\""},{"id":"GlycanIUPAC_T193","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G96338GZ\""},{"id":"GlycanIUPAC_T194","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G96338GZ\""},{"id":"GlycanIUPAC_T195","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G96296PU\""},{"id":"GlycanIUPAC_T196","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G96296PU\""},{"id":"GlycanIUPAC_T197","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G96296PU\""},{"id":"GlycanIUPAC_T198","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G59124WZ\""},{"id":"GlycanIUPAC_T199","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G59124WZ\""},{"id":"GlycanIUPAC_T200","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G59124WZ\""},{"id":"GlycanIUPAC_T201","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G57275GR\""},{"id":"GlycanIUPAC_T202","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G57275GR\""},{"id":"GlycanIUPAC_T203","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G57275GR\""},{"id":"GlycanIUPAC_T204","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G46105MZ\""},{"id":"GlycanIUPAC_T205","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G46105MZ\""},{"id":"GlycanIUPAC_T206","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G46105MZ\""},{"id":"GlycanIUPAC_T207","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G76001GO\""},{"id":"GlycanIUPAC_T208","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G76001GO\""},{"id":"GlycanIUPAC_T209","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G76001GO\""},{"id":"GlycanIUPAC_T210","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G89599ML\""},{"id":"GlycanIUPAC_T211","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G89599ML\""},{"id":"GlycanIUPAC_T212","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G89599ML\""},{"id":"GlycanIUPAC_T213","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G85872BD\""},{"id":"GlycanIUPAC_T214","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G85872BD\""},{"id":"GlycanIUPAC_T215","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G85872BD\""},{"id":"GlycanIUPAC_T216","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G69460YK\""},{"id":"GlycanIUPAC_T217","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G69460YK\""},{"id":"GlycanIUPAC_T218","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G69460YK\""},{"id":"GlycanIUPAC_T219","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G25240JV\""},{"id":"GlycanIUPAC_T220","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G25240JV\""},{"id":"GlycanIUPAC_T221","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G25240JV\""},{"id":"GlycanIUPAC_T222","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G80489OS\""},{"id":"GlycanIUPAC_T223","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G80489OS\""},{"id":"GlycanIUPAC_T224","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G80489OS\""},{"id":"GlycanIUPAC_T225","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G35726XK\""},{"id":"GlycanIUPAC_T226","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G35726XK\""},{"id":"GlycanIUPAC_T227","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G35726XK\""},{"id":"GlycanIUPAC_T228","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G11002JA\""},{"id":"GlycanIUPAC_T229","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G11002JA\""},{"id":"GlycanIUPAC_T230","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G11002JA\""},{"id":"GlycanIUPAC_T231","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G85388FO\""},{"id":"GlycanIUPAC_T232","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G85388FO\""},{"id":"GlycanIUPAC_T233","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G85388FO\""},{"id":"GlycanIUPAC_T234","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G20221JL\""},{"id":"GlycanIUPAC_T235","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G20221JL\""},{"id":"GlycanIUPAC_T236","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G20221JL\""},{"id":"GlycanIUPAC_T237","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G39026SP\""},{"id":"GlycanIUPAC_T238","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G39026SP\""},{"id":"GlycanIUPAC_T239","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G39026SP\""},{"id":"GlycanIUPAC_T240","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G66979UZ\""},{"id":"GlycanIUPAC_T241","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G66979UZ\""},{"id":"GlycanIUPAC_T242","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G66979UZ\""},{"id":"GlycanIUPAC_T243","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G68566EA\""},{"id":"GlycanIUPAC_T244","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G68566EA\""},{"id":"GlycanIUPAC_T245","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G68566EA\""},{"id":"GlycanIUPAC_T246","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G20255ZD\""},{"id":"GlycanIUPAC_T247","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G20255ZD\""},{"id":"GlycanIUPAC_T248","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G20255ZD\""},{"id":"GlycanIUPAC_T249","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G68860MF\""},{"id":"GlycanIUPAC_T250","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G68860MF\""},{"id":"GlycanIUPAC_T251","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G68860MF\""},{"id":"GlycanIUPAC_T252","span":{"begin":615,"end":618},"obj":"\"http://rdf.glycoinfo.org/glycan/G50413KD\""},{"id":"GlycanIUPAC_T253","span":{"begin":1005,"end":1008},"obj":"\"http://rdf.glycoinfo.org/glycan/G50413KD\""},{"id":"GlycanIUPAC_T254","span":{"begin":1056,"end":1059},"obj":"\"http://rdf.glycoinfo.org/glycan/G50413KD\""},{"id":"GlycanIUPAC_T255","span":{"begin":1052,"end":1055},"obj":"\"http://rdf.glycoinfo.org/glycan/G02780QX\""},{"id":"GlycanIUPAC_T256","span":{"begin":1052,"end":1055},"obj":"\"http://rdf.glycoinfo.org/glycan/G18425DX\""},{"id":"GlycanIUPAC_T257","span":{"begin":1052,"end":1055},"obj":"\"http://rdf.glycoinfo.org/glycan/G18630JE\""},{"id":"GlycanIUPAC_T258","span":{"begin":1052,"end":1055},"obj":"\"http://rdf.glycoinfo.org/glycan/G01004IT\""},{"id":"GlycanIUPAC_T259","span":{"begin":1052,"end":1055},"obj":"\"http://rdf.glycoinfo.org/glycan/G87301QZ\""},{"id":"GlycanIUPAC_T260","span":{"begin":1052,"end":1055},"obj":"\"http://rdf.glycoinfo.org/glycan/G39790GW\""},{"id":"GlycanIUPAC_T261","span":{"begin":1052,"end":1055},"obj":"\"http://rdf.glycoinfo.org/glycan/G42928BB\""},{"id":"GlycanIUPAC_T262","span":{"begin":1052,"end":1055},"obj":"\"http://rdf.glycoinfo.org/glycan/G51134HC\""},{"id":"GlycanIUPAC_T263","span":{"begin":1052,"end":1055},"obj":"\"http://rdf.glycoinfo.org/glycan/G68183GR\""},{"id":"GlycanIUPAC_T264","span":{"begin":1052,"end":1055},"obj":"\"http://rdf.glycoinfo.org/glycan/G46883FA\""},{"id":"GlycanIUPAC_T265","span":{"begin":1052,"end":1055},"obj":"\"http://rdf.glycoinfo.org/glycan/G54702VY\""}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
Lectin-Jamboree-Sentence
{"project":"Lectin-Jamboree-Sentence","blocks":[{"id":"T1","span":{"begin":0,"end":77},"obj":"Sentence"},{"id":"T2","span":{"begin":78,"end":427},"obj":"Sentence"},{"id":"T3","span":{"begin":428,"end":675},"obj":"Sentence"},{"id":"T4","span":{"begin":676,"end":883},"obj":"Sentence"},{"id":"T5","span":{"begin":884,"end":1083},"obj":"Sentence"},{"id":"T6","span":{"begin":1084,"end":1255},"obj":"Sentence"}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}
Anatomy-UBERON
{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":666,"end":674},"obj":"Body_part"},{"id":"T2","span":{"begin":695,"end":708},"obj":"Body_part"},{"id":"T3","span":{"begin":717,"end":725},"obj":"Body_part"},{"id":"T4","span":{"begin":896,"end":909},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0005764"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/GO_0005622"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/GO_0005764"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/GO_0005576"}],"text":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors.\nThe two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The best-characterized function of the MPRs is their ability to direct the delivery of approximately 60 different newly synthesized soluble lysosomal enzymes bearing mannose 6-phosphate (Man-6-P) on their N-linked oligosaccharides to the lysosome. In addition to its intracellular role in lysosome biogenesis, the CI-MPR, but not the CD-MPR, participates in a number of other biological processes by interacting with various molecules at the cell surface. The list of extracellular ligands recognized by this multifunctional receptor has grown to include a diverse spectrum of Man-6-P-containing proteins as well as several non-Man-6-P-containing ligands. Recent structural studies have given us a clearer view of how these two receptors use related, but yet distinct, approaches in the recognition of phosphomannosyl residues."}