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PubMed:22270369 JSON TXT

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GlyCosmos6-Glycan-Motif-Image

Id	Subject	Object	Predicate	Lexical cue	image
T1	524-530	Glycan_Motif	denotes	Neu5Ac	https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY
T2	606-615	Glycan_Motif	denotes	O-mannose	https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ
T3	882-891	Glycan_Motif	denotes	O-mannose	https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ

sentences

Id	Subject	Object	Predicate	Lexical cue
T1	0-151	Sentence	denotes	Absence of post-phosphoryl modification in dystroglycanopathy mouse models and wild-type tissues expressing non-laminin binding form of α-dystroglycan.
T2	152-299	Sentence	denotes	α-Dystroglycan (α-DG) is a membrane-associated glycoprotein that interacts with several extracellular matrix proteins, including laminin and agrin.
T3	300-460	Sentence	denotes	Aberrant glycosylation of α-DG disrupts its interaction with ligands and causes a certain type of muscular dystrophy commonly referred to as dystroglycanopathy.
T4	461-677	Sentence	denotes	It has been reported that a unique O-mannosyl tetrasaccharide (Neu5Ac-α2,3-Gal-β1,4-GlcNAc-β1,2-Man) and a phosphodiester-linked modification on O-mannose play important roles in the laminin binding activity of α-DG.
T5	678-900	Sentence	denotes	In this study, we use several dystroglycanopathy mouse models to demonstrate that, in addition to fukutin and LARGE, FKRP (fukutin-related protein) is also involved in the post-phosphoryl modification of O-mannose on α-DG.
T6	901-1180	Sentence	denotes	Furthermore, we have found that the glycosylation status of α-DG in lung and testis is minimally affected by defects in fukutin, LARGE, or FKRP. α-DG prepared from wild-type lung- or testis-derived cells lacks the post-phosphoryl moiety and shows little laminin-binding activity.
T7	1181-1306	Sentence	denotes	These results show that FKRP is involved in post-phosphoryl modification rather than in O-mannosyl tetrasaccharide synthesis.
T8	1307-1549	Sentence	denotes	Our data also demonstrate that post-phosphoryl modification not only plays critical roles in the pathogenesis of dystroglycanopathy but also is a key determinant of α-DG functional expression as a laminin receptor in normal tissues and cells.

GlyCosmos6-Glycan-Motif-Structure

Id	Subject	Object	Predicate	Lexical cue
T1	524-530	https://glytoucan.org/Structures/Glycans/G81533KY	denotes	Neu5Ac
T2	606-615	https://glytoucan.org/Structures/Glycans/G70323CJ	denotes	O-mannose
T3	882-891	https://glytoucan.org/Structures/Glycans/G70323CJ	denotes	O-mannose

Glycosmos6-MAT

Id	Subject	Object	Predicate	Lexical cue
T1	969-973	http://purl.obolibrary.org/obo/MAT_0000135	denotes	lung
T2	978-984	http://purl.obolibrary.org/obo/MAT_0000132	denotes	testis
T3	1075-1079	http://purl.obolibrary.org/obo/MAT_0000135	denotes	lung
T4	1084-1090	http://purl.obolibrary.org/obo/MAT_0000132	denotes	testis

DisGeNET

Id	Subject	Object	Predicate	Lexical cue
T0	326-330	gene:1605	denotes	α-DG
T1	398-416	disease:C0026850	denotes	muscular dystrophy
R1	T0	T1	associated_with	α-DG,muscular dystrophy

Allie

Id	Subject	Object	Predicate	Lexical cue
SS1_22270369_1_0	152-166	expanded	denotes	α-Dystroglycan
SS2_22270369_1_0	168-172	abbr	denotes	α-DG
AE1_22270369_1_0	SS1_22270369_1_0	SS2_22270369_1_0	abbreviatedTo	α-Dystroglycan,α-DG

PubmedHPO

Id	Subject	Object	Predicate	Lexical cue
T1	398-416	HP_0003560	denotes	muscular dystrophy

NGLY1-deficiency

Id	Subject	Object	Predicate	Lexical cue
PD-NGLY1-deficiency-B_T1	545-551	chem:24139	denotes	GlcNAc

DisGeNET5_gene_disease

Id	Subject	Object	Predicate	Lexical cue
22270369-2#26#30#gene1605	326-330	gene1605	denotes	α-DG
22270369-2#98#116#diseaseC0026850	398-416	diseaseC0026850	denotes	muscular dystrophy
26#30#gene160598#116#diseaseC0026850	22270369-2#26#30#gene1605	22270369-2#98#116#diseaseC0026850	associated_with	α-DG,muscular dystrophy

mondo_disease

Id	Subject	Object	Predicate	Lexical cue	mondo_id
T1	43-61	Disease	denotes	dystroglycanopathy	http://purl.obolibrary.org/obo/MONDO_0018282
T2	398-416	Disease	denotes	muscular dystrophy	http://purl.obolibrary.org/obo/MONDO_0020121
T3	441-459	Disease	denotes	dystroglycanopathy	http://purl.obolibrary.org/obo/MONDO_0018282
T4	708-726	Disease	denotes	dystroglycanopathy	http://purl.obolibrary.org/obo/MONDO_0018282
T5	1420-1438	Disease	denotes	dystroglycanopathy	http://purl.obolibrary.org/obo/MONDO_0018282

Anatomy-MAT

Id	Subject	Object	Predicate	Lexical cue	mat_id
T1	969-973	Body_part	denotes	lung	http://purl.obolibrary.org/obo/MAT_0000135
T2	978-984	Body_part	denotes	testis	http://purl.obolibrary.org/obo/MAT_0000132
T3	1075-1079	Body_part	denotes	lung	http://purl.obolibrary.org/obo/MAT_0000135
T4	1084-1090	Body_part	denotes	testis	http://purl.obolibrary.org/obo/MAT_0000132

HP-phenotype

Id	Subject	Object	Predicate	Lexical cue	hp_id
T1	398-416	Phenotype	denotes	muscular dystrophy	HP:0003560

Glycan-GlyCosmos

Id	Subject	Object	Predicate	Lexical cue	image
T1	524-530	Glycan	denotes	Neu5Ac	https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR

GlyCosmos15-HP

Id	Subject	Object	Predicate	Lexical cue	hp_id
T1	398-416	Phenotype	denotes	muscular dystrophy	HP:0003560

GlyCosmos15-MONDO

Id	Subject	Object	Predicate	Lexical cue	mondo_id
T1	43-61	Disease	denotes	dystroglycanopathy	http://purl.obolibrary.org/obo/MONDO_0018282
T2	398-416	Disease	denotes	muscular dystrophy	http://purl.obolibrary.org/obo/MONDO_0020121
T3	441-459	Disease	denotes	dystroglycanopathy	http://purl.obolibrary.org/obo/MONDO_0018282
T4	708-726	Disease	denotes	dystroglycanopathy	http://purl.obolibrary.org/obo/MONDO_0018282
T5	1420-1438	Disease	denotes	dystroglycanopathy	http://purl.obolibrary.org/obo/MONDO_0018282

GlyCosmos15-NCBITAXON

Id	Subject	Object	Predicate	Lexical cue	db_id
T1	62-67	OrganismTaxon	denotes	mouse	10088\|10090
T3	727-732	OrganismTaxon	denotes	mouse	10088\|10090

GlyCosmos15-UBERON

Id	Subject	Object	Predicate	Lexical cue	uberon_id
T1	179-187	Body_part	denotes	membrane	http://purl.obolibrary.org/obo/GO_0016020\|http://purl.obolibrary.org/obo/UBERON_0000094\|http://purl.obolibrary.org/obo/UBERON_0000158
T4	240-260	Body_part	denotes	extracellular matrix	http://purl.obolibrary.org/obo/GO_0031012
T5	969-973	Body_part	denotes	lung	http://purl.obolibrary.org/obo/UBERON_0002048
T6	978-984	Body_part	denotes	testis	http://purl.obolibrary.org/obo/UBERON_0000473
T7	1075-1079	Body_part	denotes	lung	http://purl.obolibrary.org/obo/UBERON_0002048
T8	1084-1090	Body_part	denotes	testis	http://purl.obolibrary.org/obo/UBERON_0000473

GlyCosmos15-MAT

Id	Subject	Object	Predicate	Lexical cue	mat_id
T1	969-973	Body_part	denotes	lung	http://purl.obolibrary.org/obo/MAT_0000135
T2	978-984	Body_part	denotes	testis	http://purl.obolibrary.org/obo/MAT_0000132
T3	1075-1079	Body_part	denotes	lung	http://purl.obolibrary.org/obo/MAT_0000135
T4	1084-1090	Body_part	denotes	testis	http://purl.obolibrary.org/obo/MAT_0000132

sentences

Id	Subject	Object	Predicate	Lexical cue
T1	0-151	Sentence	denotes	Absence of post-phosphoryl modification in dystroglycanopathy mouse models and wild-type tissues expressing non-laminin binding form of α-dystroglycan.
T2	152-299	Sentence	denotes	α-Dystroglycan (α-DG) is a membrane-associated glycoprotein that interacts with several extracellular matrix proteins, including laminin and agrin.
T3	300-460	Sentence	denotes	Aberrant glycosylation of α-DG disrupts its interaction with ligands and causes a certain type of muscular dystrophy commonly referred to as dystroglycanopathy.
T4	461-677	Sentence	denotes	It has been reported that a unique O-mannosyl tetrasaccharide (Neu5Ac-α2,3-Gal-β1,4-GlcNAc-β1,2-Man) and a phosphodiester-linked modification on O-mannose play important roles in the laminin binding activity of α-DG.
T5	678-900	Sentence	denotes	In this study, we use several dystroglycanopathy mouse models to demonstrate that, in addition to fukutin and LARGE, FKRP (fukutin-related protein) is also involved in the post-phosphoryl modification of O-mannose on α-DG.
T6	901-1180	Sentence	denotes	Furthermore, we have found that the glycosylation status of α-DG in lung and testis is minimally affected by defects in fukutin, LARGE, or FKRP. α-DG prepared from wild-type lung- or testis-derived cells lacks the post-phosphoryl moiety and shows little laminin-binding activity.
T7	1181-1306	Sentence	denotes	These results show that FKRP is involved in post-phosphoryl modification rather than in O-mannosyl tetrasaccharide synthesis.
T8	1307-1549	Sentence	denotes	Our data also demonstrate that post-phosphoryl modification not only plays critical roles in the pathogenesis of dystroglycanopathy but also is a key determinant of α-DG functional expression as a laminin receptor in normal tissues and cells.

GlyCosmos15-Sentences

Id	Subject	Object	Predicate	Lexical cue
T1	0-151	Sentence	denotes	Absence of post-phosphoryl modification in dystroglycanopathy mouse models and wild-type tissues expressing non-laminin binding form of α-dystroglycan.
T2	152-299	Sentence	denotes	α-Dystroglycan (α-DG) is a membrane-associated glycoprotein that interacts with several extracellular matrix proteins, including laminin and agrin.
T3	300-460	Sentence	denotes	Aberrant glycosylation of α-DG disrupts its interaction with ligands and causes a certain type of muscular dystrophy commonly referred to as dystroglycanopathy.
T4	461-677	Sentence	denotes	It has been reported that a unique O-mannosyl tetrasaccharide (Neu5Ac-α2,3-Gal-β1,4-GlcNAc-β1,2-Man) and a phosphodiester-linked modification on O-mannose play important roles in the laminin binding activity of α-DG.
T5	678-900	Sentence	denotes	In this study, we use several dystroglycanopathy mouse models to demonstrate that, in addition to fukutin and LARGE, FKRP (fukutin-related protein) is also involved in the post-phosphoryl modification of O-mannose on α-DG.
T6	901-1180	Sentence	denotes	Furthermore, we have found that the glycosylation status of α-DG in lung and testis is minimally affected by defects in fukutin, LARGE, or FKRP. α-DG prepared from wild-type lung- or testis-derived cells lacks the post-phosphoryl moiety and shows little laminin-binding activity.
T7	1181-1306	Sentence	denotes	These results show that FKRP is involved in post-phosphoryl modification rather than in O-mannosyl tetrasaccharide synthesis.
T8	1307-1549	Sentence	denotes	Our data also demonstrate that post-phosphoryl modification not only plays critical roles in the pathogenesis of dystroglycanopathy but also is a key determinant of α-DG functional expression as a laminin receptor in normal tissues and cells.

GlyCosmos15-Glycan

Id	Subject	Object	Predicate	Lexical cue	image
T1	524-530	Glycan	denotes	Neu5Ac	https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR

NCBITAXON

Id	Subject	Object	Predicate	Lexical cue	db_id
T1	62-67	OrganismTaxon	denotes	mouse	10088\|10090
T3	727-732	OrganismTaxon	denotes	mouse	10088\|10090

Anatomy-UBERON

Id	Subject	Object	Predicate	Lexical cue	uberon_id
T1	179-187	Body_part	denotes	membrane	http://purl.obolibrary.org/obo/GO_0016020\|http://purl.obolibrary.org/obo/UBERON_0000094\|http://purl.obolibrary.org/obo/UBERON_0000158
T4	240-260	Body_part	denotes	extracellular matrix	http://purl.obolibrary.org/obo/GO_0031012
T5	969-973	Body_part	denotes	lung	http://purl.obolibrary.org/obo/UBERON_0002048
T6	978-984	Body_part	denotes	testis	http://purl.obolibrary.org/obo/UBERON_0000473
T7	1075-1079	Body_part	denotes	lung	http://purl.obolibrary.org/obo/UBERON_0002048
T8	1084-1090	Body_part	denotes	testis	http://purl.obolibrary.org/obo/UBERON_0000473