PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1969657-9	1990	The number and size of its glycosaminoglycan chains vary with changes in cell shape and organization yielding tissue type-specific polymorphic forms of syndecan.	Glycosaminoglycans	27-44	syndecan 1	Homo sapiens	152-160	
1698781-6	1990	Syndecans are known to change their glycosaminoglycan composition yielding tissue-type specific polymorphic forms of syndecan (Sanderson, R., and Bernfield, M. (1988) Proc.	Glycosaminoglycans	36-53	syndecan 1	Homo sapiens	117-125	
2324102-4	1990	108, 1547-1556), the core protein of human syndecan can be divided into three domains: a matrix-interacting ectodomain containing putative glycosaminoglycan attachment sites, a 25-residue hydrophobic membrane-spanning domain, and a 34-residue cytoplasmic domain.	Glycosaminoglycans	139-156	syndecan 1	Homo sapiens	43-51	
25945286-11	2015	The role played by chondroitin sulfate glycosaminoglycan (GAG) chains on the ability of sdc1 to associate with its ligands needs further investigation.	Glycosaminoglycans	58-61	syndecan 1	Homo sapiens	88-92	
25945286-12	2015	At wound sites heparanase can cleave the HS GAG chains of sdc1, alter its ability to bind cytokines, and induce shedding of the ectodomain.	Glycosaminoglycans	44-47	syndecan 1	Homo sapiens	58-62	
23939434-2	2013	Reduced glycosaminoglycan, in endothelial HSPGs syndecan and perlecan, is associated with diabetic cardiovascular complications but changes in core protein remain controversial.	Glycosaminoglycans	8-25	syndecan 1	Homo sapiens	48-56	
22351752-9	2012	In addition, we found that although syndecan-1 interacts exclusively through its glycosaminoglycan chains, syndecan-4 binding relies on both its core protein and its heparan sulfate chains.	Glycosaminoglycans	81-98	syndecan 1	Homo sapiens	36-46	
10027728-1	1999	Syndecan-1 (CD138) is a surface proteoglycan consisting of long unbranched glycosaminoglycan (GAG) chains covalently attached to a protein backbone.	Glycosaminoglycans	75-92	syndecan 1	Homo sapiens	0-10	
21957484-7	2011	Using a mutant CHO-K1 cell line that lacks all glycosaminoglycans (GAGs) on its surface (CHO-745) we demonstrate that the core protein of syndecan-1 possesses the ability to modulate membrane fusion and viral spread.	Glycosaminoglycans	47-65	syndecan 1	Homo sapiens	138-148	
15383330-3	2004	Deletions within the syndecan-1 ectodomain (S1ED) implicate an active site within the core protein between the glycosaminoglycan attachment region and the transmembrane domain.	Glycosaminoglycans	111-128	syndecan 1	Homo sapiens	21-31	
15355933-10	2005	Finally, RANTES forms GAG-dependent complexes with the shed ectodomains of SD-1 and SD-4 as well as with those of CD44.	Glycosaminoglycans	22-25	syndecan 1	Homo sapiens	75-79	
10595940-7	1999	Our results suggest that glycosaminoglycan side chains of the HSPGs agrin, syndecan, and glypican, but not perlecan, may play an important role in the formation of both senile plaques and neurofibrillary tangles.	Glycosaminoglycans	25-42	syndecan 1	Homo sapiens	75-83	
10027728-1	1999	Syndecan-1 (CD138) is a surface proteoglycan consisting of long unbranched glycosaminoglycan (GAG) chains covalently attached to a protein backbone.	Glycosaminoglycans	75-92	syndecan 1	Homo sapiens	12-17	
10027728-1	1999	Syndecan-1 (CD138) is a surface proteoglycan consisting of long unbranched glycosaminoglycan (GAG) chains covalently attached to a protein backbone.	Glycosaminoglycans	94-97	syndecan 1	Homo sapiens	0-10	
10027728-1	1999	Syndecan-1 (CD138) is a surface proteoglycan consisting of long unbranched glycosaminoglycan (GAG) chains covalently attached to a protein backbone.	Glycosaminoglycans	94-97	syndecan 1	Homo sapiens	12-17	
8662979-10	1996	Analysis of a form of syndecan-1 that lacked glycosaminoglycan acceptor sites revealed that covalently attached glycosaminoglycans were not required for cell surface expression, microfilament association, or detergent insolubility.	Glycosaminoglycans	112-130	syndecan 1	Homo sapiens	22-32	
9160685-8	1997	Finally, we have demonstrated by RT-PCR, flow cytometry, and Western blotting that cultured RS cells, of B and undetermined phenotype, express syndecan-1 mRNA and produce a form of syndecan-1, recognized by the B-B4 MoAb, which is predominantly associated with glycosaminoglycans and is present at the cell surface.	Glycosaminoglycans	261-279	syndecan 1	Homo sapiens	181-191	
7890615-6	1995	Using rotation-mediated aggregation assays, we find that aggregation of syndecan-1-transfected cells is dependent on divalent cations and is inhibited by the following: (i) addition of heparin and heparin-like glycosaminoglycans, (ii) removal of heparan sulfate from the cell surface, or (iii) addition of exogenous purified syndecan-1.	Glycosaminoglycans	210-228	syndecan 1	Homo sapiens	72-82