PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
32122513-4	2020	DS can anchor to the surface of the chitosan nanocarrier (CNP) by forming amide bond.	Dermatan Sulfate	0-2	2',3'-cyclic nucleotide 3' phosphodiesterase	Homo sapiens	58-61
32413091-5	2020	We found that OspC binds to the extracellular matrix (ECM) components fibronectin and/or dermatan sulfate in an OspC variant-dependent manner.	Dermatan Sulfate	89-105	OspC	Borreliella burgdorferi	14-18
32413091-5	2020	We found that OspC binds to the extracellular matrix (ECM) components fibronectin and/or dermatan sulfate in an OspC variant-dependent manner.	Dermatan Sulfate	89-105	OspC	Borreliella burgdorferi	112-116
32413091-6	2020	Murine infection by isogenic B. burgdorferi strains differing only in their ospC coding region revealed that two OspC variants capable of binding dermatan sulfate promoted colonization of all tissues tested, including joints.	Dermatan Sulfate	146-162	OspC	Borreliella burgdorferi	113-117
32413091-8	2020	Moreover, a strain producing an OspC altered to recognize neither fibronectin nor dermatan sulfate displayed dramatically reduced levels of tissue colonization that were indistinguishable from a strain entirely deficient in OspC.	Dermatan Sulfate	82-98	OspC	Borreliella burgdorferi	32-36
32122513-6	2020	The functionalization of DS not only promoted the specific uptake behavior of melanoma cells, but also up-regulated cleaved caspase-3 and PARP promote tumor cell apoptosis.	Dermatan Sulfate	25-27	caspase 3	Homo sapiens	124-133
32122513-6	2020	The functionalization of DS not only promoted the specific uptake behavior of melanoma cells, but also up-regulated cleaved caspase-3 and PARP promote tumor cell apoptosis.	Dermatan Sulfate	25-27	poly(ADP-ribose) polymerase 1	Homo sapiens	138-142
32130795-1	2020	BACKGROUND: Musculocontractural Ehlers-Danlos Syndrome (mcEDS) is a rare connective tissue disorder caused by biallelic loss-of-function variants in CHST14 (mcEDS-CHST14) or DSE (mcEDS-DSE), both of which result in defective dermatan sulfate biosynthesis.	Dermatan Sulfate	225-241	carbohydrate sulfotransferase 14	Homo sapiens	149-155
31679559-2	2020	IDUA degrades heparan and dermatan sulfates, two types of glycosaminoglycan (GAG), important signalling and structural molecules of the extracellular matrix.	Dermatan Sulfate	26-43	iduronidase, alpha-L	Mus musculus	0-4
32162173-2	2020	IDUA degrades two types of glycosaminoglycans (GAGs): heparan and dermatan sulfates, important components of extracellular matrix, with signaling and structural functions.	Dermatan Sulfate	66-83	iduronidase, alpha-L	Mus musculus	0-4
32188113-0	2020	Mucopolysaccharidosis Type I. Mucopolysaccharidosis type I (MPS I) is caused by the deficiency of alpha-l-iduronidase, leading to the storage of dermatan and heparan sulfate.	Dermatan Sulfate	145-153	alpha-L-iduronidase	Homo sapiens	98-117
31705726-5	2020	CSGALNACT1 encodes CSGalNAcT-1, a key enzyme in the biosynthesis of sulfated glycosaminoglycans chondroitin and dermatan sulfate.	Dermatan Sulfate	112-128	chondroitin sulfate N-acetylgalactosaminyltransferase 1	Homo sapiens	0-10
31705726-5	2020	CSGALNACT1 encodes CSGalNAcT-1, a key enzyme in the biosynthesis of sulfated glycosaminoglycans chondroitin and dermatan sulfate.	Dermatan Sulfate	112-128	chondroitin sulfate N-acetylgalactosaminyltransferase 1	Homo sapiens	19-30
33073008-1	2020	The glycosaminoglycans (GAGs), dermatan sulfate (DS) and heparan sulfate (HS) are both substrates for alpha-l-iduronidase (IDUA).	Dermatan Sulfate	31-47	alpha-L-iduronidase	Homo sapiens	123-127
33073008-1	2020	The glycosaminoglycans (GAGs), dermatan sulfate (DS) and heparan sulfate (HS) are both substrates for alpha-l-iduronidase (IDUA).	Dermatan Sulfate	49-51	alpha-L-iduronidase	Homo sapiens	123-127
31834922-2	2019	IDUA codes for alpha-L-iduronidase (IDUA), a lysosomal hydrolase that degrades glycosaminoglycans (GAGs): heparan sulphate and dermatan sulphate.	Dermatan Sulfate	127-144	iduronidase, alpha-L	Mus musculus	36-40
31705151-8	2020	For the p21 analysis as a differentiation marker on the functional (differentiation) layer, the difference between IR alone and IR + DS arms was significant, indicating that DS inhibited the differentiation process.	Dermatan Sulfate	174-176	cyclin-dependent kinase inhibitor 1A (P21)	Mus musculus	8-11
31834922-2	2019	IDUA codes for alpha-L-iduronidase (IDUA), a lysosomal hydrolase that degrades glycosaminoglycans (GAGs): heparan sulphate and dermatan sulphate.	Dermatan Sulfate	127-144	iduronidase, alpha-L	Mus musculus	0-4
30553867-1	2019	Musculocontractural Ehlers-Danlos syndrome (mcEDS) due to CHST14/D4ST1 deficiency (mcEDS-CHST14) is a recently delineated type of EDS caused by biallelic loss-of-function mutations in CHST14, which results in the depletion of dermatan sulfate (DS).	Dermatan Sulfate	226-242	carbohydrate sulfotransferase 14	Homo sapiens	58-64
31193135-1	2019	Iduronate-2-sulfatase (IDS) is a lysosomal enzyme involved in the metabolism of the glycosaminoglycans heparan (HS) and dermatan (DS) sulfate.	Dermatan Sulfate	120-130	iduronate 2-sulfatase	Mus musculus	0-21
31193135-1	2019	Iduronate-2-sulfatase (IDS) is a lysosomal enzyme involved in the metabolism of the glycosaminoglycans heparan (HS) and dermatan (DS) sulfate.	Dermatan Sulfate	120-130	iduronate 2-sulfatase	Mus musculus	23-26
31544795-1	2019	IDUA contributes to the degradation of the glycosaminoglycans, including heparan sulphate and dermatan sulphate.	Dermatan Sulfate	94-111	alpha-L-iduronidase	Homo sapiens	0-4
31242852-3	2019	We have previously found that dermatan sulfate (DS) can form complexes with molecules of apoptotic cells and stimulate autoreactive CD5+ B cells to produce autoantibodies.	Dermatan Sulfate	30-46	CD5 antigen	Mus musculus	132-135
31242852-3	2019	We have previously found that dermatan sulfate (DS) can form complexes with molecules of apoptotic cells and stimulate autoreactive CD5+ B cells to produce autoantibodies.	Dermatan Sulfate	48-50	CD5 antigen	Mus musculus	132-135
30869126-0	2019	Recombinant dermatan sulfate is a potent activator of heparin cofactor II-dependent inhibition of thrombin.	Dermatan Sulfate	12-28	coagulation factor II, thrombin	Homo sapiens	98-106
30869126-1	2019	The glycosaminoglycan dermatan sulfate (DS) is a well-known activator of heparin cofactor II-dependent inactivation of thrombin.	Dermatan Sulfate	22-38	coagulation factor II, thrombin	Homo sapiens	119-127
30869126-1	2019	The glycosaminoglycan dermatan sulfate (DS) is a well-known activator of heparin cofactor II-dependent inactivation of thrombin.	Dermatan Sulfate	40-42	coagulation factor II, thrombin	Homo sapiens	119-127
30869126-5	2019	Importantly, the recombinant highly 2,4-O-sulfated DS inhibits thrombin via heparin cofactor II, approximately 20 times better than heparin, enabling manipulation of vascular and extravascular coagulation.	Dermatan Sulfate	51-53	coagulation factor II, thrombin	Homo sapiens	63-71
31006321-9	2019	Dermatan sulphate treatment was associated with increased tPA levels versus controls and the fibrosis group.	Dermatan Sulfate	0-17	plasminogen activator, tissue	Mus musculus	58-61
30553867-1	2019	Musculocontractural Ehlers-Danlos syndrome (mcEDS) due to CHST14/D4ST1 deficiency (mcEDS-CHST14) is a recently delineated type of EDS caused by biallelic loss-of-function mutations in CHST14, which results in the depletion of dermatan sulfate (DS).	Dermatan Sulfate	226-242	carbohydrate sulfotransferase 14	Homo sapiens	89-95
30553867-1	2019	Musculocontractural Ehlers-Danlos syndrome (mcEDS) due to CHST14/D4ST1 deficiency (mcEDS-CHST14) is a recently delineated type of EDS caused by biallelic loss-of-function mutations in CHST14, which results in the depletion of dermatan sulfate (DS).	Dermatan Sulfate	47-49	carbohydrate sulfotransferase 14	Homo sapiens	58-64
30553867-1	2019	Musculocontractural Ehlers-Danlos syndrome (mcEDS) due to CHST14/D4ST1 deficiency (mcEDS-CHST14) is a recently delineated type of EDS caused by biallelic loss-of-function mutations in CHST14, which results in the depletion of dermatan sulfate (DS).	Dermatan Sulfate	47-49	carbohydrate sulfotransferase 14	Homo sapiens	89-95
30553867-9	2019	McEDS-CHST14 provides a critical example of the importance of DS in GAG side chains of decorin-PG during assembly of collagen fibrils in maintenance of connective tissues.	Dermatan Sulfate	3-5	carbohydrate sulfotransferase 14	Homo sapiens	6-12
30775257-7	2019	Post-HSCT patients with MPS II showed that IL-1beta and IL-6 were normalized as HS and DS levels decreased.	Dermatan Sulfate	87-89	interleukin 1 beta	Homo sapiens	43-51
30853887-4	2019	It has been reported that dermatan 4-O-sulfotransferase-1 (Chst14/D4st1) specific for DS, but not chondroitin 4-O-sulfotransferase-1 (Chst11/C4st1) specific for CS, regulates proliferation and neurogenesis of neural stem cells (NSCs), indicating that CS and DS play distinct roles in the self-renewal and differentiation of NSCs.	Dermatan Sulfate	86-88	carbohydrate sulfotransferase 14	Mus musculus	59-65
30853887-4	2019	It has been reported that dermatan 4-O-sulfotransferase-1 (Chst14/D4st1) specific for DS, but not chondroitin 4-O-sulfotransferase-1 (Chst11/C4st1) specific for CS, regulates proliferation and neurogenesis of neural stem cells (NSCs), indicating that CS and DS play distinct roles in the self-renewal and differentiation of NSCs.	Dermatan Sulfate	86-88	carbohydrate sulfotransferase 14	Mus musculus	66-71
30853887-4	2019	It has been reported that dermatan 4-O-sulfotransferase-1 (Chst14/D4st1) specific for DS, but not chondroitin 4-O-sulfotransferase-1 (Chst11/C4st1) specific for CS, regulates proliferation and neurogenesis of neural stem cells (NSCs), indicating that CS and DS play distinct roles in the self-renewal and differentiation of NSCs.	Dermatan Sulfate	258-260	carbohydrate sulfotransferase 14	Mus musculus	59-65
30853887-11	2019	Together, this study reveals that specific sulfation of DS is critical in synaptic plasticity of the hippocampus and learning and memory, which might be associated with the changes in the expression of glutamate receptors and other synaptic proteins though Akt/mTOR pathway.	Dermatan Sulfate	56-58	thymoma viral proto-oncogene 1	Mus musculus	257-260
30853887-11	2019	Together, this study reveals that specific sulfation of DS is critical in synaptic plasticity of the hippocampus and learning and memory, which might be associated with the changes in the expression of glutamate receptors and other synaptic proteins though Akt/mTOR pathway.	Dermatan Sulfate	56-58	mechanistic target of rapamycin kinase	Mus musculus	261-265
30775257-7	2019	Post-HSCT patients with MPS II showed that IL-1beta and IL-6 were normalized as HS and DS levels decreased.	Dermatan Sulfate	87-89	interleukin 6	Homo sapiens	56-60
30740185-3	2019	Methods: In this study, we examine the targeting of E-selectin by an engineered peptide moiety bound to a dermatan sulfate backbone.	Dermatan Sulfate	106-122	selectin E	Homo sapiens	52-62
30906633-2	2019	Here we report that DSE, the enzyme that catalyzes the conversion of chondroitin sulfate (CS) to dermatan sulfate (DS), is a critical mediator of malignant character in HCC, through regulation of CCL5 signaling.	Dermatan Sulfate	97-113	dermatan sulfate epimerase	Mus musculus	20-23
30906633-2	2019	Here we report that DSE, the enzyme that catalyzes the conversion of chondroitin sulfate (CS) to dermatan sulfate (DS), is a critical mediator of malignant character in HCC, through regulation of CCL5 signaling.	Dermatan Sulfate	97-113	chemokine (C-C motif) ligand 5	Mus musculus	196-200
30906633-2	2019	Here we report that DSE, the enzyme that catalyzes the conversion of chondroitin sulfate (CS) to dermatan sulfate (DS), is a critical mediator of malignant character in HCC, through regulation of CCL5 signaling.	Dermatan Sulfate	20-22	chemokine (C-C motif) ligand 5	Mus musculus	196-200
30339470-7	2019	From these and previous observations, we drew the conclusion that different CS and DS expression patterns can be growth permitting, growth inhibiting, or neutral for regrowing or sprouting axons, depending on the tissue environment of a particular animal species.-Sahu, S., Li, R., Loers, G., Schachner, M. Knockdown of chondroitin-4-sulfotransferase-1, but not of dermatan-4-sulfotransferase-1, accelerates regeneration of zebrafish after spinal cord injury.	Dermatan Sulfate	83-85	carbohydrate (chondroitin 4) sulfotransferase 11	Danio rerio	320-352
30339470-7	2019	From these and previous observations, we drew the conclusion that different CS and DS expression patterns can be growth permitting, growth inhibiting, or neutral for regrowing or sprouting axons, depending on the tissue environment of a particular animal species.-Sahu, S., Li, R., Loers, G., Schachner, M. Knockdown of chondroitin-4-sulfotransferase-1, but not of dermatan-4-sulfotransferase-1, accelerates regeneration of zebrafish after spinal cord injury.	Dermatan Sulfate	83-85	carbohydrate (N-acetylgalactosamine 4-0) sulfotransferase 14	Danio rerio	365-394
30335002-1	2018	RATIONALE: Mucopolysaccharidosis type VI (MPS VI) or Maroteaux-Lamy syndrome is produced by the deficiency of the enzyme arylsulfatase B, responsible for the hydrolysis of N-acetyl-D-galactosamine, chondroitin sulfate, and dermatan sulfate.	Dermatan Sulfate	223-239	arylsulfatase B	Homo sapiens	121-136
31787635-3	2019	Glycobiological approaches revealed that mutations in CS- and DS-biosynthetic enzymes led to reductions in their enzymatic activities and in the levels of CS and DS.	Dermatan Sulfate	62-64	citrate synthase	Homo sapiens	155-157
31787635-3	2019	Glycobiological approaches revealed that mutations in CS- and DS-biosynthetic enzymes led to reductions in their enzymatic activities and in the levels of CS and DS.	Dermatan Sulfate	162-164	citrate synthase	Homo sapiens	54-56
30064964-1	2018	Mucopolysaccharidosis type II (MPS II or Hunter syndrome) is a lysosomal storage disorder caused by a deficiency of iduronate-2-sulfatase (IDS), an enzyme that catabolizes glycosaminoglycans (GAGs) including heparan sulfate (HS) and dermatan sulfate (DS).	Dermatan Sulfate	233-249	iduronate 2-sulfatase	Mus musculus	139-142
30524696-2	2018	The enzymatic defect of ARSB leads to progressive lysosomal storage disorder and accumulation of glycosaminoglycan (GAG) dermatan sulfate (DS), which causes harmful effects on various organs and tissues and short stature.	Dermatan Sulfate	139-141	arylsulfatase B	Homo sapiens	24-28
29976758-1	2018	During the biosynthesis of chondroitin/dermatan sulfate (CS/DS), a variable fraction of glucuronic acid is converted to iduronic acid through the activities of two epimerases, dermatan sulfate epimerases 1 (DS-epi1) and 2 (DS-epi2).	Dermatan Sulfate	39-55	dermatan sulfate epimerase	Homo sapiens	207-221
29794138-2	2018	ARSB removes 4-sulfate groups from the nonreducing end of dermatan sulfate and chondroitin 4-sulfate (C4S), and its decreased expression has previously been reported to inhibit the activity of the ubiquitous protein-tyrosine phosphatase, nonreceptor type 11 (SHP2 or PTPN11).	Dermatan Sulfate	58-74	arylsulfatase B	Homo sapiens	0-4
29884617-1	2018	The pediatric lysosomal storage disorder mucopolysaccharidosis type II is caused by mutations in IDS, resulting in accumulation of heparan and dermatan sulfate, causing severe neurodegeneration, skeletal disease, and cardiorespiratory disease.	Dermatan Sulfate	143-159	iduronate 2-sulfatase	Homo sapiens	97-100
29081414-1	2017	BACKGROUND: Arylsulfatase B (ARSB) removes the 4-sulfate group from chondroitin 4-sulfate (C4S) and dermatan sulfate and is required for their degradation.	Dermatan Sulfate	100-116	arylsulfatase B	Homo sapiens	12-27
29063236-9	2018	WIKIPATHWAYS, REACTOME, PID_NCI and KEGG pathway analysis showed the down-regulated DEGs were enriched endochondral ossification, TGF beta signalling pathway, integrin cell surface interactions, beta1 integrin cell surface interactions, malaria and glycosaminoglycan biosynthesis-chondroitin sulfate/dermatan sulphate.	Dermatan Sulfate	300-317	transforming growth factor beta 1	Homo sapiens	130-138
29063236-9	2018	WIKIPATHWAYS, REACTOME, PID_NCI and KEGG pathway analysis showed the down-regulated DEGs were enriched endochondral ossification, TGF beta signalling pathway, integrin cell surface interactions, beta1 integrin cell surface interactions, malaria and glycosaminoglycan biosynthesis-chondroitin sulfate/dermatan sulphate.	Dermatan Sulfate	300-317	UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2	Homo sapiens	195-200
29206923-3	2018	Carbohydrate sulfotransferase 14/dermatan 4-O-sulfotransferase-1 (CHST14/D4ST1) is a critical enzyme for biosynthesis of dermatan sulfate, a side chain of various proteoglycans including biglycan that regulates collagen fibrils through their interaction.	Dermatan Sulfate	121-137	carbohydrate sulfotransferase 14	Mus musculus	0-64
29206923-3	2018	Carbohydrate sulfotransferase 14/dermatan 4-O-sulfotransferase-1 (CHST14/D4ST1) is a critical enzyme for biosynthesis of dermatan sulfate, a side chain of various proteoglycans including biglycan that regulates collagen fibrils through their interaction.	Dermatan Sulfate	121-137	carbohydrate sulfotransferase 14	Mus musculus	66-72
29206923-3	2018	Carbohydrate sulfotransferase 14/dermatan 4-O-sulfotransferase-1 (CHST14/D4ST1) is a critical enzyme for biosynthesis of dermatan sulfate, a side chain of various proteoglycans including biglycan that regulates collagen fibrils through their interaction.	Dermatan Sulfate	121-137	carbohydrate sulfotransferase 14	Mus musculus	73-78
29146595-6	2018	We also noted that CLEC3A can be modified with chondroitin/dermatan sulfate side chains and tends to oligomerize to form higher aggregates.	Dermatan Sulfate	59-75	C-type lectin domain family 3 member A	Homo sapiens	19-25
29671225-2	2018	Deficiency of the lysosomal enzyme, iduronate-2-sulfatase (EC 3.1.6.13) results in deposition of the glycosaminoglycans, dermatan, and heparan sulfate in various tissues.	Dermatan Sulfate	121-129	iduronate 2-sulfatase	Homo sapiens	36-57
29081414-1	2017	BACKGROUND: Arylsulfatase B (ARSB) removes the 4-sulfate group from chondroitin 4-sulfate (C4S) and dermatan sulfate and is required for their degradation.	Dermatan Sulfate	100-116	arylsulfatase B	Homo sapiens	29-33
29111696-0	2017	Sequencing the Dermatan Sulfate Chain of Decorin.	Dermatan Sulfate	15-31	decorin	Homo sapiens	41-48
29111696-6	2017	By utilizing sophisticated separation methods followed by compositional analysis, domain mapping, and tandem mass spectrometry coupled with analysis by a modified genetic algorithm approach, the structural motif for the decorin dermatan sulfate chain was determined.	Dermatan Sulfate	228-244	decorin	Homo sapiens	220-227
28593992-1	2017	Hunter syndrome is a rare but devastating childhood disease caused by mutations in the IDS gene encoding iduronate-2-sulfatase, a crucial enzyme in the lysosomal degradation pathway of dermatan sulfate and heparan sulfate.	Dermatan Sulfate	185-201	iduronate 2-sulfatase	Homo sapiens	87-90
28676128-1	2017	BACKGROUND: Mucopolysaccharidosis type I (MPS I) is an autosomal recessive disease due to deficiency of alpha-L-iduronidase (IDUA), a lysosomal enzyme that degrades glycosaminoglycans (GAG) heparan and dermatan sulfate.	Dermatan Sulfate	202-218	alpha-L-iduronidase	Homo sapiens	104-123
28676128-1	2017	BACKGROUND: Mucopolysaccharidosis type I (MPS I) is an autosomal recessive disease due to deficiency of alpha-L-iduronidase (IDUA), a lysosomal enzyme that degrades glycosaminoglycans (GAG) heparan and dermatan sulfate.	Dermatan Sulfate	202-218	alpha-L-iduronidase	Homo sapiens	125-129
28437084-0	2017	Affinity Binding of EMR2 Expressing Cells by Surface-Grafted Chondroitin Sulfate B.	Dermatan Sulfate	61-82	adhesion G protein-coupled receptor E2	Homo sapiens	20-24
29245974-1	2017	The chondroitin sulfatases N-acetylgalactosamine-4-sulfatase (ARSB) and galactosamine-N-acetyl-6-sulfatase (GALNS) remove either the 4-sulfate group at the non-reducing end of chondroitin 4-sulfate (C4S) and dermatan sulfate, or the 6-sulfate group of chondroitin 6-sulfate, chondroitin 4,6-disulfate (chondroitin sulfate E), or keratan sulfate.	Dermatan Sulfate	208-224	arylsulfatase B	Homo sapiens	62-66
29245974-1	2017	The chondroitin sulfatases N-acetylgalactosamine-4-sulfatase (ARSB) and galactosamine-N-acetyl-6-sulfatase (GALNS) remove either the 4-sulfate group at the non-reducing end of chondroitin 4-sulfate (C4S) and dermatan sulfate, or the 6-sulfate group of chondroitin 6-sulfate, chondroitin 4,6-disulfate (chondroitin sulfate E), or keratan sulfate.	Dermatan Sulfate	208-224	galactosamine (N-acetyl)-6-sulfatase	Homo sapiens	72-106
29245974-1	2017	The chondroitin sulfatases N-acetylgalactosamine-4-sulfatase (ARSB) and galactosamine-N-acetyl-6-sulfatase (GALNS) remove either the 4-sulfate group at the non-reducing end of chondroitin 4-sulfate (C4S) and dermatan sulfate, or the 6-sulfate group of chondroitin 6-sulfate, chondroitin 4,6-disulfate (chondroitin sulfate E), or keratan sulfate.	Dermatan Sulfate	208-224	galactosamine (N-acetyl)-6-sulfatase	Homo sapiens	108-113
28593992-1	2017	Hunter syndrome is a rare but devastating childhood disease caused by mutations in the IDS gene encoding iduronate-2-sulfatase, a crucial enzyme in the lysosomal degradation pathway of dermatan sulfate and heparan sulfate.	Dermatan Sulfate	185-201	iduronate 2-sulfatase	Homo sapiens	105-126
28588666-1	2017	Hunter syndrome (or mucopolysaccharidosis type II, MPS II) is an X-linked recessive disorder induced by a deficiency of the iduronate 2-sulfatase (IDS) enzyme, resulting in the accumulation of glycosaminoglycan substrates, heparan sulfate and dermatan sulfate, in the lysosomes.	Dermatan Sulfate	243-259	iduronate 2-sulfatase	Homo sapiens	124-145
28588666-1	2017	Hunter syndrome (or mucopolysaccharidosis type II, MPS II) is an X-linked recessive disorder induced by a deficiency of the iduronate 2-sulfatase (IDS) enzyme, resulting in the accumulation of glycosaminoglycan substrates, heparan sulfate and dermatan sulfate, in the lysosomes.	Dermatan Sulfate	243-259	iduronate 2-sulfatase	Homo sapiens	147-150
28412940-0	2017	Absence of the dermatan sulfate chain of decorin does not affect mouse development.	Dermatan Sulfate	15-31	decorin	Mus musculus	41-48
27744520-4	2017	In this study, we employed a siRNA knockdown approach for heparan sulphate (EXT1) and heparan/chondroitin/dermatan sulphate-biosynthetic enzymes (beta4GalT7) in the aggressive human breast cancer cell line MDA-MB-231 to study the impact on cell behaviour and hyaluronan biosynthesis.	Dermatan Sulfate	106-123	beta-1,4-galactosyltransferase 7	Homo sapiens	146-156
28401457-1	2017	IDS is responsible for the lysosomal degradation of heparan sulfate and dermatan sulfate and linked to an X-linked lysosomal storage disease, mucopolysaccharidosis 2 (MPS2), resulting in neurological damage and early death.	Dermatan Sulfate	72-88	iduronate 2-sulfatase	Homo sapiens	0-3
28412940-1	2017	BACKGROUND: In vitro studies suggest that the multiple functions of decorin are related to both its core protein and its dermatan sulfate chain.	Dermatan Sulfate	121-137	decorin	Mus musculus	68-75
28207863-1	2017	Severe mucopolysaccharidosis type II (MPS II) is a progressive lysosomal storage disease caused by mutations in the IDS gene, leading to a deficiency in the iduronate-2-sulfatase enzyme that is involved in heparan sulphate and dermatan sulphate catabolism.	Dermatan Sulfate	227-244	iduronate 2-sulfatase	Mus musculus	116-119
28207863-1	2017	Severe mucopolysaccharidosis type II (MPS II) is a progressive lysosomal storage disease caused by mutations in the IDS gene, leading to a deficiency in the iduronate-2-sulfatase enzyme that is involved in heparan sulphate and dermatan sulphate catabolism.	Dermatan Sulfate	227-244	iduronate 2-sulfatase	Mus musculus	157-178
28199387-0	2017	Dermatan sulfate is a player in the transglutaminase 2 interaction network.	Dermatan Sulfate	0-16	transglutaminase 2	Homo sapiens	36-54
28199387-3	2017	The enhanced extracellular expression of TG2 is associated with processes such as wound healing, fibrosis or vascular remodeling that are also characterized by a high deposition of dermatan sulfate (DS) proteoglycans in the ECM.	Dermatan Sulfate	181-197	transglutaminase 2	Homo sapiens	41-44
28199387-3	2017	The enhanced extracellular expression of TG2 is associated with processes such as wound healing, fibrosis or vascular remodeling that are also characterized by a high deposition of dermatan sulfate (DS) proteoglycans in the ECM.	Dermatan Sulfate	199-201	transglutaminase 2	Homo sapiens	41-44
28199387-4	2017	However, it is unknown whether DS may bind to TG2 or affect its function.	Dermatan Sulfate	31-33	transglutaminase 2	Homo sapiens	46-49
28199387-5	2017	Using the plasmon surface resonance method, we showed that DS chains, especially those of biglycan, are good binding partners for TG2.	Dermatan Sulfate	59-61	biglycan	Homo sapiens	90-98
28199387-5	2017	Using the plasmon surface resonance method, we showed that DS chains, especially those of biglycan, are good binding partners for TG2.	Dermatan Sulfate	59-61	transglutaminase 2	Homo sapiens	130-133
28199387-7	2017	The competitive effect of heparin on DS binding to TG2 suggests that both glycosaminoglycans occupy the same binding site(s) on the protein molecule.	Dermatan Sulfate	37-39	transglutaminase 2	Homo sapiens	51-54
28199387-8	2017	An occurrence of the DS-TG2 interaction was confirmed by the co-immunoprecipitation of this protein with native decorin that is a DS-bearing proteoglycan rather than with the decorin core protein.	Dermatan Sulfate	21-23	transglutaminase 2	Homo sapiens	24-27
28199387-9	2017	Moreover, in vivo DS is responsible for both TG2 binding and the regulation of the location of this protein in the ECM as can be suggested from an increased extraction of TG2 from the human fascia only when an enzymatic degradation of the tissue DS was conducted in the presence of the anti-collagen type I antiserum.	Dermatan Sulfate	18-20	transglutaminase 2	Homo sapiens	45-48
28199387-9	2017	Moreover, in vivo DS is responsible for both TG2 binding and the regulation of the location of this protein in the ECM as can be suggested from an increased extraction of TG2 from the human fascia only when an enzymatic degradation of the tissue DS was conducted in the presence of the anti-collagen type I antiserum.	Dermatan Sulfate	18-20	transglutaminase 2	Homo sapiens	171-174
28199387-10	2017	In addition, DS with a low affinity for TG2 exerted an inhibitory effect on the protein transamidating activity most probably via the control of the accessibility of a substrate.	Dermatan Sulfate	13-15	transglutaminase 2	Homo sapiens	40-43
28199387-11	2017	Our data show that DS can affect several aspects of TG2 biology in both physiological and pathological conditions.	Dermatan Sulfate	19-21	transglutaminase 2	Homo sapiens	52-55
27898729-2	2016	The GAG family includes sulfated heparin, heparan sulfate (HS), dermatan sulfate (DS), chondroitin sulfate (CS), keratan sulfate, and non-sulfated hyaluronan.	Dermatan Sulfate	64-80	melanoma antigen	Mus musculus	4-7
27926479-6	2017	Since the only known function of ARSB is to remove 4-sulfate groups from the N-acetylgalactosamine 4-sulfate residue at the non-reducing end of chondroitin 4-sulfate (C4S) or dermatan sulfate, experiments were performed to determine the transcriptional mechanisms by which expression of CSPG4 and MMP2 increased.	Dermatan Sulfate	175-191	arylsulfatase B	Homo sapiens	33-37
27826022-1	2017	MPS VI is an autosomal recessive disorder which occurs due to the deficiency of N-acetyl galactosamine-4-sulfatase (Arylsulfatase B - ARSB) involved in catabolism of dermatan sulfate resulting from disease-causing variations in the ARSB gene.	Dermatan Sulfate	166-182	arylsulfatase B	Homo sapiens	116-131
27826022-1	2017	MPS VI is an autosomal recessive disorder which occurs due to the deficiency of N-acetyl galactosamine-4-sulfatase (Arylsulfatase B - ARSB) involved in catabolism of dermatan sulfate resulting from disease-causing variations in the ARSB gene.	Dermatan Sulfate	166-182	arylsulfatase B	Homo sapiens	134-138
27826022-1	2017	MPS VI is an autosomal recessive disorder which occurs due to the deficiency of N-acetyl galactosamine-4-sulfatase (Arylsulfatase B - ARSB) involved in catabolism of dermatan sulfate resulting from disease-causing variations in the ARSB gene.	Dermatan Sulfate	166-182	arylsulfatase B	Homo sapiens	232-236
27898729-2	2016	The GAG family includes sulfated heparin, heparan sulfate (HS), dermatan sulfate (DS), chondroitin sulfate (CS), keratan sulfate, and non-sulfated hyaluronan.	Dermatan Sulfate	82-84	melanoma antigen	Mus musculus	4-7
27445159-3	2016	The expressed serglycin was also decorated with chondroitin/dermatan sulfate chains and the relative abundance of these glycosaminoglycan chains changed under different concentrations of glucose in the culture medium.	Dermatan Sulfate	60-76	serglycin	Homo sapiens	14-23
27564657-5	2016	METHODS: TAFI activation by thrombin or plasmin was studied in the presence of physiological anionic molecules (polyphosphate, heparin, hyaluronan, DNA and dermatan sulfate) and the non-physiological sodium dodecyl sulfate (SDS).	Dermatan Sulfate	156-172	carboxypeptidase B2	Homo sapiens	9-13
27564657-8	2016	Dermatan sulfate and polyphosphates with sodium as counter ion (Na-PolyP700, Na-PolyP100 and Na-PolyP70) enhanced plasmin-mediated but not thrombin-mediated TAFI activation.	Dermatan Sulfate	0-16	plasminogen	Homo sapiens	114-121
27564657-8	2016	Dermatan sulfate and polyphosphates with sodium as counter ion (Na-PolyP700, Na-PolyP100 and Na-PolyP70) enhanced plasmin-mediated but not thrombin-mediated TAFI activation.	Dermatan Sulfate	0-16	carboxypeptidase B2	Homo sapiens	157-161
27605497-5	2016	ARSB is the enzyme that removes 4-sulfate groups from the non-reducing end of chondroitin 4-sulfate and dermatan sulfate.	Dermatan Sulfate	104-120	arylsulfatase B	Homo sapiens	0-4
27547834-1	2016	BACKGROUND: Chondroitin/dermatan sulfate (CS/DS) rich in N-acetylgalactosamine 4,6-bissulfate (GalNAc(4,6SO4)) residues is present as decorin and/or biglycan in mouse liver, and GalNAc(4,6SO4) residues disappeared completely in N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) knockout (KO) mice.	Dermatan Sulfate	24-40	carbohydrate sulfotransferase 15	Mus musculus	228-280
27547834-1	2016	BACKGROUND: Chondroitin/dermatan sulfate (CS/DS) rich in N-acetylgalactosamine 4,6-bissulfate (GalNAc(4,6SO4)) residues is present as decorin and/or biglycan in mouse liver, and GalNAc(4,6SO4) residues disappeared completely in N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) knockout (KO) mice.	Dermatan Sulfate	24-40	carbohydrate sulfotransferase 15	Mus musculus	282-294
27101845-0	2016	Musculocontractural Ehlers-Danlos syndrome and neurocristopathies: dermatan sulfate is required for Xenopus neural crest cells to migrate and adhere to fibronectin.	Dermatan Sulfate	67-83	fibronectin 1 S homeolog	Xenopus laevis	152-163
27699273-1	2016	Mucopolysaccharidosis type II (MPSII) is an X-linked lysosomal storage disease characterized by severe neurologic and somatic disease caused by deficiency of iduronate-2-sulfatase (IDS), an enzyme that catabolizes the glycosaminoglycans heparan and dermatan sulphate.	Dermatan Sulfate	249-266	iduronate 2-sulfatase	Mus musculus	158-179
27699273-1	2016	Mucopolysaccharidosis type II (MPSII) is an X-linked lysosomal storage disease characterized by severe neurologic and somatic disease caused by deficiency of iduronate-2-sulfatase (IDS), an enzyme that catabolizes the glycosaminoglycans heparan and dermatan sulphate.	Dermatan Sulfate	249-266	iduronate 2-sulfatase	Mus musculus	181-184
27101845-3	2016	Musculocontractural Ehlers-Danlos syndrome (MCEDS) is a heritable connective tissue disorder with distinct craniofacial features; this syndrome comprises multiple congenital malformations that are caused by dysfunction of dermatan sulfate (DS) biosynthetic enzymes, including DS epimerase-1 (DS-epi1; also known as DSE).	Dermatan Sulfate	222-238	dermatan sulfate epimerase	Homo sapiens	292-299
27101845-3	2016	Musculocontractural Ehlers-Danlos syndrome (MCEDS) is a heritable connective tissue disorder with distinct craniofacial features; this syndrome comprises multiple congenital malformations that are caused by dysfunction of dermatan sulfate (DS) biosynthetic enzymes, including DS epimerase-1 (DS-epi1; also known as DSE).	Dermatan Sulfate	47-49	dermatan sulfate epimerase	Homo sapiens	292-299
26235607-1	2016	Mucopolysaccharidosis type I (MPS I) is a rare autosomal recessive disease caused by alpha-L-iduronidase deficiency in which heparan and dermatan sulfate degradation is compromised.	Dermatan Sulfate	137-153	iduronidase, alpha-L	Mus musculus	85-104
27100626-12	2016	NF-kappaB activation by HARE-mediated uptake of Hep, HA, dermatan sulfate or acetylated LDL was unaffected in single-motif deletion mutants lacking M1, M2 or M4.	Dermatan Sulfate	57-73	nuclear factor kappa B subunit 1	Homo sapiens	0-9
27100626-12	2016	NF-kappaB activation by HARE-mediated uptake of Hep, HA, dermatan sulfate or acetylated LDL was unaffected in single-motif deletion mutants lacking M1, M2 or M4.	Dermatan Sulfate	57-73	stabilin 2	Homo sapiens	24-28
26812032-7	2016	Moreover, we studied the expression of the chondroitin sulfate proteoglycan (CSPG) dermatan sulfate-dependent proteoglycan-1 (DSD-1-PG), an interaction partner of TN-C.	Dermatan Sulfate	83-99	protein tyrosine phosphatase, receptor type Z, polypeptide 1	Mus musculus	126-134
26812032-7	2016	Moreover, we studied the expression of the chondroitin sulfate proteoglycan (CSPG) dermatan sulfate-dependent proteoglycan-1 (DSD-1-PG), an interaction partner of TN-C.	Dermatan Sulfate	83-99	tenascin C	Mus musculus	163-167
27078017-1	2016	Arylsulfatase B (B-acetylgalactosamine 4-sulfatase; ARSB) is the enzyme that removes 4-sulfate groups from the non-reducing end of the glycosaminoglycans chondroitin 4-sulfate and dermatan sulfate.	Dermatan Sulfate	180-196	arylsulfatase B	Homo sapiens	0-15
27078017-1	2016	Arylsulfatase B (B-acetylgalactosamine 4-sulfatase; ARSB) is the enzyme that removes 4-sulfate groups from the non-reducing end of the glycosaminoglycans chondroitin 4-sulfate and dermatan sulfate.	Dermatan Sulfate	180-196	arylsulfatase B	Homo sapiens	52-56
27009190-4	2016	Halo-FGF1, Halo-FGF2 and Halo-FGF6 bound to HS, whereas Halo-FGF10 also interacted with chondroitin sulfate/dermatan sulfate, and FGF20 did not bind detectably.	Dermatan Sulfate	108-124	fibroblast growth factor 10	Rattus norvegicus	61-66
26909334-1	2016	INTRODUCTION: Maroteaux-Lamy syndrome, or mucopolysaccharidosis (MPS) type VI, is an autosomal recessive lysosomal storage disease caused by a deficient activity of the enzyme arylsulfatase B (ARSB), required to degrade dermatan sulfate.	Dermatan Sulfate	220-236	arylsulfatase B	Homo sapiens	176-191
26373698-3	2016	Thirty-one and three patients have been reported with MC-EDS so far with bi-allelic mutations identified in CHST14 and DSE, respectively, encoding two enzymes necessary for dermatan sulfate (DS) biosynthesis.	Dermatan Sulfate	173-189	carbohydrate sulfotransferase 14	Homo sapiens	108-114
26373698-3	2016	Thirty-one and three patients have been reported with MC-EDS so far with bi-allelic mutations identified in CHST14 and DSE, respectively, encoding two enzymes necessary for dermatan sulfate (DS) biosynthesis.	Dermatan Sulfate	58-60	carbohydrate sulfotransferase 14	Homo sapiens	108-114
26407983-1	2015	BACKGROUND: Mucopolysaccharidosis type I (MPS I) is caused by the deficiency of alpha-L-iduronidase (IDUA), which is involved in the degradation of glycosaminoglycans (GAGs), such as heparan sulfate and dermatan sulfate in the lysosome.	Dermatan Sulfate	203-219	iduronidase, alpha-L	Mus musculus	101-105
27326280-2	2012	Part of a group of clinically progressive disorders, it is caused by the deficiency of the lysosomal enzyme, alpha-L -iduronidase, which results in intralysosomal accumulation of dermatan sulfate and heparan sulfate and in turn causes cell dysfunction.	Dermatan Sulfate	179-195	alpha-L-iduronidase	Homo sapiens	109-129
26349001-4	2015	RESULTS: DS injections prevented thrombus formation and decreased P-selectin expression after 3 days of the injury.	Dermatan Sulfate	9-11	selectin, platelet	Mus musculus	66-76
25703627-5	2015	The glycanation of the dermal DS proteoglycan decorin is impaired in fibroblasts from D4ST1- as well as DS-epi1-deficient patients.	Dermatan Sulfate	30-32	carbohydrate sulfotransferase 14	Homo sapiens	86-91
25751597-6	2015	In addition, the affinity constant values determined could be compared with those obtained in our previous studies for the interactions between apoE isoforms and another important GAG chain of PGs - dermatan sulfate (DS).	Dermatan Sulfate	199-215	apolipoprotein E	Homo sapiens	144-148
25751597-6	2015	In addition, the affinity constant values determined could be compared with those obtained in our previous studies for the interactions between apoE isoforms and another important GAG chain of PGs - dermatan sulfate (DS).	Dermatan Sulfate	217-219	apolipoprotein E	Homo sapiens	144-148
25703627-3	2015	DS-epi1 and D4ST1 are crucial for biosynthesis of dermatan sulfate (DS) moieties in the hybrid chondroitin sulfate (CS)/DS glycosaminoglycans (GAGs).	Dermatan Sulfate	50-66	dermatan sulfate epimerase	Homo sapiens	0-7
25703627-3	2015	DS-epi1 and D4ST1 are crucial for biosynthesis of dermatan sulfate (DS) moieties in the hybrid chondroitin sulfate (CS)/DS glycosaminoglycans (GAGs).	Dermatan Sulfate	50-66	carbohydrate sulfotransferase 14	Homo sapiens	12-17
25703627-5	2015	The glycanation of the dermal DS proteoglycan decorin is impaired in fibroblasts from D4ST1- as well as DS-epi1-deficient patients.	Dermatan Sulfate	30-32	dermatan sulfate epimerase	Homo sapiens	104-111
25797215-1	2015	Mucopolysaccharidosis type VI (MPS VI) is a rare autosomal recessive disorder caused by a deficiency of N-acetylgalactosamine-4-sulfatase (ARSB), one of the enzymes required for the degradation of dermatan sulfate (DS).	Dermatan Sulfate	197-213	arylsulfatase B	Homo sapiens	104-137
25892708-1	2015	Mucopolysaccharidosis VI (MPS VI, Maroteaux-Lamy syndrome) is caused by deficient activity of the enzyme, N-acetylgalactosamine-4-sulfatase, resulting in impaired degradation of the glycosaminoglycan dermatan sulfate.	Dermatan Sulfate	200-216	arylsulfatase B	Homo sapiens	106-139
25797215-1	2015	Mucopolysaccharidosis type VI (MPS VI) is a rare autosomal recessive disorder caused by a deficiency of N-acetylgalactosamine-4-sulfatase (ARSB), one of the enzymes required for the degradation of dermatan sulfate (DS).	Dermatan Sulfate	197-213	arylsulfatase B	Homo sapiens	139-143
25797215-1	2015	Mucopolysaccharidosis type VI (MPS VI) is a rare autosomal recessive disorder caused by a deficiency of N-acetylgalactosamine-4-sulfatase (ARSB), one of the enzymes required for the degradation of dermatan sulfate (DS).	Dermatan Sulfate	215-217	arylsulfatase B	Homo sapiens	104-137
25797215-1	2015	Mucopolysaccharidosis type VI (MPS VI) is a rare autosomal recessive disorder caused by a deficiency of N-acetylgalactosamine-4-sulfatase (ARSB), one of the enzymes required for the degradation of dermatan sulfate (DS).	Dermatan Sulfate	215-217	arylsulfatase B	Homo sapiens	139-143
25558755-3	2014	These are caused by the deficiency or absence of alpha-L-iduronidase, essential to the metabolism of both dermatan and heparan sulfate, and it is encoded by the lDUA gene.	Dermatan Sulfate	106-114	alpha-L-iduronidase	Homo sapiens	49-68
25622168-2	2015	Mucopolysaccharidosis type II (MPS II) is an X-linked recessive disorder characterized by a deficiency of the enzyme iduronate-2-sulfatase leading to a multisystem involvement by tissue accumulation of glycosaminoglycans heparan and dermatan sulfate.	Dermatan Sulfate	233-249	iduronate 2-sulfatase	Homo sapiens	117-138
26937388-6	2015	The expression of eNOS in HPAECs is reduced up to two thirds in the presence of DS.	Dermatan Sulfate	80-82	nitric oxide synthase 3	Homo sapiens	18-22
26937388-8	2015	The expression of VEGFA decreases with increasing DS concentrations and absence of elastin, and increases with increasing DS in the presence of elastin.	Dermatan Sulfate	50-52	vascular endothelial growth factor A	Homo sapiens	18-23
26937388-8	2015	The expression of VEGFA decreases with increasing DS concentrations and absence of elastin, and increases with increasing DS in the presence of elastin.	Dermatan Sulfate	122-124	vascular endothelial growth factor A	Homo sapiens	18-23
26937388-8	2015	The expression of VEGFA decreases with increasing DS concentrations and absence of elastin, and increases with increasing DS in the presence of elastin.	Dermatan Sulfate	122-124	elastin	Homo sapiens	144-151
25646802-0	2015	Effects of enzyme replacement therapy started late in a murine model of mucopolysaccharidosis type I. Mucopolysaccharidosis type I (MPS I) is a progressive disorder caused by deficiency of alpha-L-iduronidase (IDUA), which leads to storage of heparan and dermatan sulphate.	Dermatan Sulfate	255-272	iduronidase, alpha-L	Mus musculus	189-208
25480151-2	2015	Fgf2 requires glycosaminoglycans, like chondroitin and dermatan sulfates (hereafter denoted CS/DS) as co-receptors.	Dermatan Sulfate	55-72	fibroblast growth factor 2	Cricetulus griseus	0-4
25359774-1	2014	Idua(-/-) mice share similar clinical pathology with patients, including the accumulation of the undegraded glycosaminoglycans (GAGs) heparan sulfate (HS), and dermatan sulfate (DS), progressive neurodegeneration, and dysostosis multiplex.	Dermatan Sulfate	160-176	iduronidase, alpha-L	Mus musculus	0-4
25359774-1	2014	Idua(-/-) mice share similar clinical pathology with patients, including the accumulation of the undegraded glycosaminoglycans (GAGs) heparan sulfate (HS), and dermatan sulfate (DS), progressive neurodegeneration, and dysostosis multiplex.	Dermatan Sulfate	178-180	iduronidase, alpha-L	Mus musculus	0-4
24842928-1	2014	Decorin-binding protein A (DbpA) of Borrelia burgdorferi mediates bacterial adhesion to heparin and dermatan sulfate associated with decorin.	Dermatan Sulfate	100-116	Y box protein 3	Mus musculus	27-31
24240681-1	2014	Arylsulfatase B (N-acetylgalactosamine-4-sulfatase; ARSB) removes 4-sulfate groups from chondroitin-4-sulfate (C4S) and dermatan sulfate and is required for their degradation.	Dermatan Sulfate	120-136	arylsulfatase B	Homo sapiens	0-15
24240681-1	2014	Arylsulfatase B (N-acetylgalactosamine-4-sulfatase; ARSB) removes 4-sulfate groups from chondroitin-4-sulfate (C4S) and dermatan sulfate and is required for their degradation.	Dermatan Sulfate	120-136	arylsulfatase B	Homo sapiens	17-50
24240681-1	2014	Arylsulfatase B (N-acetylgalactosamine-4-sulfatase; ARSB) removes 4-sulfate groups from chondroitin-4-sulfate (C4S) and dermatan sulfate and is required for their degradation.	Dermatan Sulfate	120-136	arylsulfatase B	Homo sapiens	52-56
25459762-1	2014	Human alpha-L-iduronidase (IDUA) is a member of glycoside hydrolase family and is involved in the catabolism of glycosaminoglycans (GAGs), heparan sulfate (HS) and dermatan sulfate (DS).	Dermatan Sulfate	164-180	alpha-L-iduronidase	Homo sapiens	6-25
25459762-1	2014	Human alpha-L-iduronidase (IDUA) is a member of glycoside hydrolase family and is involved in the catabolism of glycosaminoglycans (GAGs), heparan sulfate (HS) and dermatan sulfate (DS).	Dermatan Sulfate	164-180	alpha-L-iduronidase	Homo sapiens	27-31
25459762-1	2014	Human alpha-L-iduronidase (IDUA) is a member of glycoside hydrolase family and is involved in the catabolism of glycosaminoglycans (GAGs), heparan sulfate (HS) and dermatan sulfate (DS).	Dermatan Sulfate	182-184	alpha-L-iduronidase	Homo sapiens	6-25
25459762-1	2014	Human alpha-L-iduronidase (IDUA) is a member of glycoside hydrolase family and is involved in the catabolism of glycosaminoglycans (GAGs), heparan sulfate (HS) and dermatan sulfate (DS).	Dermatan Sulfate	182-184	alpha-L-iduronidase	Homo sapiens	27-31
25186462-2	2014	A distinct feature of DS is the presence of iduronic acid, produced by the two enzymes, DS-epimerase 1 and 2, which are encoded by Dse and Dsel, respectively.	Dermatan Sulfate	22-24	dermatan sulfate epimerase-like	Mus musculus	139-143
24942734-0	2014	A hyaluronan receptor for endocytosis (HARE) link domain N-glycan is required for extracellular signal-regulated kinase (ERK) and nuclear factor-kappaB (NF-kappaB) signaling in response to the uptake of hyaluronan but not heparin, dermatan sulfate, or acetylated low density lipoprotein (LDL).	Dermatan Sulfate	231-247	stabilin 2	Homo sapiens	2-37
24942734-11	2014	We conclude that a Link domain complex N-glycan is required specifically for HARE HA-mediated activation of ERK1/2 and NF-kappaB-mediated gene expression and that this initial activation mechanism is different from and independent of the initial mechanisms for HARE-mediated signaling in response to Hep, AcLDL, or DS uptake.	Dermatan Sulfate	315-317	mitogen-activated protein kinase 3	Homo sapiens	108-114
27896125-1	2014	Mucopolysaccharidosis type I (MPSI) is a rare autosomal recessive disorder caused by mutations in the gene encoding the lysosomal enzyme alpha-l-iduronidase (IDUA), which is instrumental in the hydrolysis of the glycosaminoglycans, dermatan and heparan sulfate.	Dermatan Sulfate	232-240	alpha-L-iduronidase	Homo sapiens	137-156
27896125-1	2014	Mucopolysaccharidosis type I (MPSI) is a rare autosomal recessive disorder caused by mutations in the gene encoding the lysosomal enzyme alpha-l-iduronidase (IDUA), which is instrumental in the hydrolysis of the glycosaminoglycans, dermatan and heparan sulfate.	Dermatan Sulfate	232-240	alpha-L-iduronidase	Homo sapiens	158-162
24842928-4	2014	In vitro binding experiments confirmed that recombinant DbpA proteins with mutations in K82, K163, or K170 did not bind decorin, which was due to an inability to interact with dermatan sulfate.	Dermatan Sulfate	176-192	Y box protein 3	Mus musculus	56-60
24842928-9	2014	Taken together, these data showed that lysines K82, K163, and K170 potentiate the binding of DbpA to dermatan sulfate and that an interaction(s) mediated by these lysines is essential for B. burgdorferi murine infection.	Dermatan Sulfate	101-117	Y box protein 3	Mus musculus	93-97
25190157-1	2014	OBJECTIVE: Mucopolysaccharidosis type VI (MPS VI) or Maroteaux-Lamy syndrome is an autosomal recessive lysosomal storage disease caused by a deficiency of arylsulfatase B(ARSB), which is required in the degradation of dermatan sulfate and chondroitin sulfate.	Dermatan Sulfate	218-234	arylsulfatase B	Homo sapiens	171-175
25079227-4	2014	The attachment of microbial pathogens to cells or to the extracellular matrix of target tissues may promote colonization and disease, and the Lyme disease spirochete encodes several surface proteins, including the decorin- and dermatan sulfate-binding adhesin DbpA, which vary among strains and have been postulated to contribute to strain-specific differences in tissue tropism.	Dermatan Sulfate	227-243	Y box protein 3	Mus musculus	260-264
24788890-5	2014	The interactions studied are of interest because, in vivo, apolipoprotein E localizes on DS-containing regions in the extracellular matrix of human vascular subendothelium.	Dermatan Sulfate	89-91	apolipoprotein E	Homo sapiens	59-75
25190157-2	2014	The deficiency of ARSB leads to an accumulation of dermatan sulfate and chondroitin sulfate in lysosomes and gross excretion in the urine.Few articles about clinical study and ARSB gene mutation analysis of Chinese MPS VI patients were published.	Dermatan Sulfate	51-67	arylsulfatase B	Homo sapiens	18-22
24046088-4	2014	HIV-1 gp120 prefers heparin and heparan sulfate (with at least 16 monomers in length) over chondroitin and dermatan.	Dermatan Sulfate	107-115	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	6-11
24221504-1	2014	Mucopolysaccharidosis type VI (Maroteaux-Lamy syndrome, MPS VI, OMIM 253200) is caused by mutations in the gene coding for N-acetylgalactosamine-4-sulfatase (4-sulfatase, arylsulfatase B, ARSB, EC 3.1.6.12), a lysosomal enzyme involved in the degradation of dermatan sulfate (DS).	Dermatan Sulfate	258-274	arylsulfatase B	Homo sapiens	123-156
24221504-1	2014	Mucopolysaccharidosis type VI (Maroteaux-Lamy syndrome, MPS VI, OMIM 253200) is caused by mutations in the gene coding for N-acetylgalactosamine-4-sulfatase (4-sulfatase, arylsulfatase B, ARSB, EC 3.1.6.12), a lysosomal enzyme involved in the degradation of dermatan sulfate (DS).	Dermatan Sulfate	258-274	arylsulfatase B	Homo sapiens	145-156
24221504-1	2014	Mucopolysaccharidosis type VI (Maroteaux-Lamy syndrome, MPS VI, OMIM 253200) is caused by mutations in the gene coding for N-acetylgalactosamine-4-sulfatase (4-sulfatase, arylsulfatase B, ARSB, EC 3.1.6.12), a lysosomal enzyme involved in the degradation of dermatan sulfate (DS).	Dermatan Sulfate	276-278	arylsulfatase B	Homo sapiens	123-156
24221504-1	2014	Mucopolysaccharidosis type VI (Maroteaux-Lamy syndrome, MPS VI, OMIM 253200) is caused by mutations in the gene coding for N-acetylgalactosamine-4-sulfatase (4-sulfatase, arylsulfatase B, ARSB, EC 3.1.6.12), a lysosomal enzyme involved in the degradation of dermatan sulfate (DS).	Dermatan Sulfate	276-278	arylsulfatase B	Homo sapiens	145-156
24483599-1	2014	Hurler syndrome type 1 (MPS-1) is an autosomal recessive lysosomal disorder due to the deficiency of the enzyme alpha-L-iduronidase which is necessary for the degradation of dermatan and heparan sulfate.	Dermatan Sulfate	174-182	alpha-L-iduronidase	Homo sapiens	24-29
24483599-1	2014	Hurler syndrome type 1 (MPS-1) is an autosomal recessive lysosomal disorder due to the deficiency of the enzyme alpha-L-iduronidase which is necessary for the degradation of dermatan and heparan sulfate.	Dermatan Sulfate	174-182	alpha-L-iduronidase	Homo sapiens	112-131
24447999-11	2014	Surprisingly, wild-type CS/DS significantly reduced the binding of Fgf7 to keratinocytes in a concentration dependent manner unlike the Dcn(-/-) CS/DS that only affected the binding at higher concentrations.	Dermatan Sulfate	27-29	fibroblast growth factor 7	Mus musculus	67-71
24243352-1	2014	Mucopolysaccharidosis type VI (MPS VI, Maroteaux-Lamy syndrome) is an autosomal recessive disorder caused by the deficit of the arylsulfatase B (ARSB) enzyme, which leads to dermatan sulfate pathological storage, resulting in a wide spectrum of clinical phenotypes.	Dermatan Sulfate	174-190	arylsulfatase B	Homo sapiens	128-143
24247245-0	2014	Hyaluronic acid receptor for endocytosis (HARE)-mediated endocytosis of hyaluronan, heparin, dermatan sulfate, and acetylated low density lipoprotein (AcLDL), but not chondroitin sulfate types A, C, D, or E, activates NF-kappaB-regulated gene expression.	Dermatan Sulfate	93-109	stabilin 2	Homo sapiens	0-40
24247245-0	2014	Hyaluronic acid receptor for endocytosis (HARE)-mediated endocytosis of hyaluronan, heparin, dermatan sulfate, and acetylated low density lipoprotein (AcLDL), but not chondroitin sulfate types A, C, D, or E, activates NF-kappaB-regulated gene expression.	Dermatan Sulfate	93-109	stabilin 2	Homo sapiens	42-46
24247245-3	2014	Unique intermediate size Select-HA(TM), heparin, dermatan sulfate, and acetylated LDL stimulated dose-dependent HARE-mediated NF-kappaB activation of luciferase expression, with half-maximal values of 10-25 nM.	Dermatan Sulfate	49-65	stabilin 2	Homo sapiens	112-116
24326668-10	2014	Overexpression of Hs3st1 in MST-10H cells resulted in a change in the composition of heparan sulfate (HS)/HP and CS/dermatan sulfate (DS) glycosaminoglycans.	Dermatan Sulfate	116-132	heparan sulfate (glucosamine) 3-O-sulfotransferase 1	Mus musculus	18-24
24368159-1	2014	UNLABELLED: The lysosomal enzyme alpha-L-iduronidase hydrolyzes terminal iduronic acid from heparan sulfate and dermatan sulfate, and is an essential step in GAG degradation.	Dermatan Sulfate	112-128	alpha-L-iduronidase	Homo sapiens	33-52
24407717-2	2014	Deficient ARSB activity leads to lysosomal accumulation of dermatan sulfate in a wide range of tissues and organs.	Dermatan Sulfate	59-75	arylsulfatase B	Rattus norvegicus	10-14
24243352-1	2014	Mucopolysaccharidosis type VI (MPS VI, Maroteaux-Lamy syndrome) is an autosomal recessive disorder caused by the deficit of the arylsulfatase B (ARSB) enzyme, which leads to dermatan sulfate pathological storage, resulting in a wide spectrum of clinical phenotypes.	Dermatan Sulfate	174-190	arylsulfatase B	Homo sapiens	145-149
24167632-3	2013	To lower its effective dose, we precomplexed BMP-2 with the glycosaminoglycans (GAGs) dermatan sulfate (DS) or heparin (HP), prior to loading it into a hyaluronic acid (HA) hydrogel.	Dermatan Sulfate	86-102	bone morphogenetic protein 2	Rattus norvegicus	45-50
24167632-3	2013	To lower its effective dose, we precomplexed BMP-2 with the glycosaminoglycans (GAGs) dermatan sulfate (DS) or heparin (HP), prior to loading it into a hyaluronic acid (HA) hydrogel.	Dermatan Sulfate	104-106	bone morphogenetic protein 2	Rattus norvegicus	45-50
24167632-6	2013	Analysis of the kinetic interaction between BMP-2 and DS or HP showed that HP had approximately 10 times higher affinity for BMP-2 than DS, yet it equally stabilized the protein, as determined by alkaline phosphatase activity.	Dermatan Sulfate	54-56	bone morphogenetic protein 2	Rattus norvegicus	125-130
23385884-1	2013	N-acetylgalactosamine-4-sulfatase (Arylsulfatase B; ARSB) is the enzyme that removes sulfate groups from the N-acetylgalactosamine-4-sulfate residue at the non-reducing end of chondroitin-4-sulfate (C4S) and dermatan sulfate (DS).	Dermatan Sulfate	208-224	arylsulfatase B	Rattus norvegicus	0-33
23385884-1	2013	N-acetylgalactosamine-4-sulfatase (Arylsulfatase B; ARSB) is the enzyme that removes sulfate groups from the N-acetylgalactosamine-4-sulfate residue at the non-reducing end of chondroitin-4-sulfate (C4S) and dermatan sulfate (DS).	Dermatan Sulfate	208-224	arylsulfatase B	Rattus norvegicus	35-50
23385884-1	2013	N-acetylgalactosamine-4-sulfatase (Arylsulfatase B; ARSB) is the enzyme that removes sulfate groups from the N-acetylgalactosamine-4-sulfate residue at the non-reducing end of chondroitin-4-sulfate (C4S) and dermatan sulfate (DS).	Dermatan Sulfate	226-228	arylsulfatase B	Rattus norvegicus	35-50
23385884-1	2013	N-acetylgalactosamine-4-sulfatase (Arylsulfatase B; ARSB) is the enzyme that removes sulfate groups from the N-acetylgalactosamine-4-sulfate residue at the non-reducing end of chondroitin-4-sulfate (C4S) and dermatan sulfate (DS).	Dermatan Sulfate	208-224	arylsulfatase B	Rattus norvegicus	52-56
23385884-1	2013	N-acetylgalactosamine-4-sulfatase (Arylsulfatase B; ARSB) is the enzyme that removes sulfate groups from the N-acetylgalactosamine-4-sulfate residue at the non-reducing end of chondroitin-4-sulfate (C4S) and dermatan sulfate (DS).	Dermatan Sulfate	226-228	arylsulfatase B	Rattus norvegicus	52-56
23385884-1	2013	N-acetylgalactosamine-4-sulfatase (Arylsulfatase B; ARSB) is the enzyme that removes sulfate groups from the N-acetylgalactosamine-4-sulfate residue at the non-reducing end of chondroitin-4-sulfate (C4S) and dermatan sulfate (DS).	Dermatan Sulfate	226-228	arylsulfatase B	Rattus norvegicus	0-33
23707223-1	2013	Hunter disease or mucopolysaccharidosis type II (MPS II) is an X-linked recessive lysosomal disorder caused by the deficit of the enzyme iduronate-2-sulfatase (IDS), involved in the catabolism of the glycosaminoglycans heparan and dermatan sulfate.	Dermatan Sulfate	231-247	iduronate 2-sulfatase	Homo sapiens	137-158
23512580-0	2013	Plasmatic kinetics of dermatan sulfate during enzyme replacement therapy with iduronate-2-sulfatase in a mucopolysaccharidosis II patient.	Dermatan Sulfate	22-38	iduronate 2-sulfatase	Homo sapiens	78-99
23512580-2	2013	We report a kinetic study of plasmatic dermatan sulfate (DS) in a 3-year-old subject affected by a severe form of MPS II during the first 10 months of ERT with Idursulfase.	Dermatan Sulfate	39-55	iduronate 2-sulfatase	Homo sapiens	160-171
23512580-2	2013	We report a kinetic study of plasmatic dermatan sulfate (DS) in a 3-year-old subject affected by a severe form of MPS II during the first 10 months of ERT with Idursulfase.	Dermatan Sulfate	57-59	iduronate 2-sulfatase	Homo sapiens	160-171
23904514-2	2013	While IL-15 exhibits a chemotactic activity for PB CD16(-) NK cells, IL-15 attenuates their binding capacity to dermatan sulfate, the major CD62L ligand expressed on human uterine microvascular endothelial cells (HUtMVECs).	Dermatan Sulfate	112-128	interleukin 15	Homo sapiens	69-74
23904514-2	2013	While IL-15 exhibits a chemotactic activity for PB CD16(-) NK cells, IL-15 attenuates their binding capacity to dermatan sulfate, the major CD62L ligand expressed on human uterine microvascular endothelial cells (HUtMVECs).	Dermatan Sulfate	112-128	selectin L	Homo sapiens	140-145
23904514-7	2013	Binding to immobilized dermatan sulfate increased surface IL-15 receptor-alpha chain expression on CD16(-) NK cells.	Dermatan Sulfate	23-39	interleukin 15	Homo sapiens	58-63
23904514-7	2013	Binding to immobilized dermatan sulfate increased surface IL-15 receptor-alpha chain expression on CD16(-) NK cells.	Dermatan Sulfate	23-39	Fc gamma receptor IIIa	Homo sapiens	99-103
23707223-1	2013	Hunter disease or mucopolysaccharidosis type II (MPS II) is an X-linked recessive lysosomal disorder caused by the deficit of the enzyme iduronate-2-sulfatase (IDS), involved in the catabolism of the glycosaminoglycans heparan and dermatan sulfate.	Dermatan Sulfate	231-247	iduronate 2-sulfatase	Homo sapiens	160-163
23460644-14	2013	Furthermore, only dermatan sulfate influenced IFN-gamma signaling by significantly increasing CXCL-10 expression in contrast to decorin protein core alone.	Dermatan Sulfate	18-34	interferon gamma	Mus musculus	46-55
23360803-3	2013	To enable a novel approach in studies on DS versus CS roles during development and regeneration, we generated a mouse deficient in the dermatan 4-O-sulfotransferase1 (Chst14(-/-)), a key enzyme in the synthesis of iduronic acid-containing modules found in DS but not CS.	Dermatan Sulfate	256-258	carbohydrate sulfotransferase 14	Mus musculus	167-173
23460644-14	2013	Furthermore, only dermatan sulfate influenced IFN-gamma signaling by significantly increasing CXCL-10 expression in contrast to decorin protein core alone.	Dermatan Sulfate	18-34	chemokine (C-X-C motif) ligand 10	Mus musculus	94-101
23494731-0	2013	Identification of an unusually sulfated tetrasaccharide chondroitin/dermatan motif in mouse brain by combining chip-nanoelectrospray multistage MS2 -MS4 and high resolution MS. Chondroitin sulfate (CS)/dermatan sulfate (DS) are often found in nature as hybrid glycosaminoglycan chains in various proteoglycans.	Dermatan Sulfate	68-76	minisatellites detected by probe MMS2	Mus musculus	144-147
23494731-0	2013	Identification of an unusually sulfated tetrasaccharide chondroitin/dermatan motif in mouse brain by combining chip-nanoelectrospray multistage MS2 -MS4 and high resolution MS. Chondroitin sulfate (CS)/dermatan sulfate (DS) are often found in nature as hybrid glycosaminoglycan chains in various proteoglycans.	Dermatan Sulfate	68-76	minisatellites detected by probe MMS4	Mus musculus	149-152
23519970-3	2013	Through negatively-charged chondroitin and dermatan sulfate side chains or interactions of the G1 and G3 domains, versican is able to regulate many cellular processes including cell adhesion, proliferation, apoptosis, migration, angiogenesis, invasion and metastasis.	Dermatan Sulfate	43-59	versican	Homo sapiens	114-122
22773246-1	2013	BACKGROUND: Mucopolysaccharidosis I (MPS I) is a metabolic disorder caused by alpha-L-Iduronidase (IDUA) deficiency, resulting in lysosomal accumulation of heparan (HS) and dermatan sulphate (DS).	Dermatan Sulfate	173-190	iduronidase, alpha-L	Mus musculus	78-97
23593225-5	2013	Idua encodes alpha-L-iduronidase, an enzyme required for degradation of the glycosaminoglycans (GAGs) heparan sulfate and dermatan sulfate.	Dermatan Sulfate	122-138	iduronidase, alpha-L	Mus musculus	0-4
23593225-5	2013	Idua encodes alpha-L-iduronidase, an enzyme required for degradation of the glycosaminoglycans (GAGs) heparan sulfate and dermatan sulfate.	Dermatan Sulfate	122-138	iduronidase, alpha-L	Mus musculus	13-32
22886070-1	2013	Recently, we demonstrated that the human xylosyltransferase II (XT-II) has enzymatic activity and is able to catalyze the initial and rate-limiting step in the biosynthesis of glycosaminoglycans (GAGs) like chondroitin and dermatan sulfate, as well as heparan sulfate and heparin.	Dermatan Sulfate	223-239	xylosyltransferase 2	Homo sapiens	41-62
22886070-1	2013	Recently, we demonstrated that the human xylosyltransferase II (XT-II) has enzymatic activity and is able to catalyze the initial and rate-limiting step in the biosynthesis of glycosaminoglycans (GAGs) like chondroitin and dermatan sulfate, as well as heparan sulfate and heparin.	Dermatan Sulfate	223-239	xylosyltransferase 2	Homo sapiens	64-69
23801937-1	2013	Mucopolysaccharidosis type II (MPS II), also known as Hunter syndrome, is a rare, X-linked disease caused by a deficiency of the lysosomal enzyme iduronate-2-sulfatase, which catalyses a step in the catabolism of glycosaminoglycans resulting in accumulation of heparan and dermatan sulfate in many organs and tissues.	Dermatan Sulfate	273-289	iduronate 2-sulfatase	Homo sapiens	146-167
23100275-3	2013	Thrombin generation was determined by calibrated automated thrombinography in platelet-poor plasma from 44 apparently healthy subjects which was spiked with fixed concentrations of otamixaban, melagatran, unfractionated heparin, dermatan sulfate and pentasaccharide.	Dermatan Sulfate	229-245	coagulation factor II, thrombin	Homo sapiens	0-8
22773246-1	2013	BACKGROUND: Mucopolysaccharidosis I (MPS I) is a metabolic disorder caused by alpha-L-Iduronidase (IDUA) deficiency, resulting in lysosomal accumulation of heparan (HS) and dermatan sulphate (DS).	Dermatan Sulfate	173-190	iduronidase, alpha-L	Mus musculus	99-103
22773246-1	2013	BACKGROUND: Mucopolysaccharidosis I (MPS I) is a metabolic disorder caused by alpha-L-Iduronidase (IDUA) deficiency, resulting in lysosomal accumulation of heparan (HS) and dermatan sulphate (DS).	Dermatan Sulfate	192-194	iduronidase, alpha-L	Mus musculus	78-97
22773246-1	2013	BACKGROUND: Mucopolysaccharidosis I (MPS I) is a metabolic disorder caused by alpha-L-Iduronidase (IDUA) deficiency, resulting in lysosomal accumulation of heparan (HS) and dermatan sulphate (DS).	Dermatan Sulfate	192-194	iduronidase, alpha-L	Mus musculus	99-103
22550062-1	2013	The enzyme Arylsulfatase B (ARSB; N-acetylgalactosamine-4-sulfatase) removes 4-sulfate groups from chondroitin-4-sulfate and dermatan sulfate and is required for the degradation of these sulfated glycosaminoglycans (sGAGs).	Dermatan Sulfate	125-141	arylsulfatase B	Homo sapiens	28-32
22550062-1	2013	The enzyme Arylsulfatase B (ARSB; N-acetylgalactosamine-4-sulfatase) removes 4-sulfate groups from chondroitin-4-sulfate and dermatan sulfate and is required for the degradation of these sulfated glycosaminoglycans (sGAGs).	Dermatan Sulfate	125-141	arylsulfatase B	Homo sapiens	34-67
22550062-1	2013	The enzyme Arylsulfatase B (ARSB; N-acetylgalactosamine-4-sulfatase) removes 4-sulfate groups from chondroitin-4-sulfate and dermatan sulfate and is required for the degradation of these sulfated glycosaminoglycans (sGAGs).	Dermatan Sulfate	125-141	arylsulfatase B	Homo sapiens	11-26
22879413-8	2012	SPR data demonstrated the ability of FIB to bind noncovalently to corneal stroma molecules, Coll-I, decorin, dermatan sulfate, and corneal basement membrane molecules, laminin and heparan sulfate--only in the presence of Zn(2+).	Dermatan Sulfate	109-125	fibrinogen beta chain	Homo sapiens	37-40
23924722-3	2013	Here, PEDF was purified from human plasma by use of a dermatan sulfate affinity column, and then hydroxyapatite, gel filtration and ion exchange columns.	Dermatan Sulfate	54-70	serpin family F member 1	Homo sapiens	6-10
22987196-1	2013	Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II (HCII) to enhance thrombin inhibition.	Dermatan Sulfate	0-16	serpin family D member 1	Homo sapiens	86-105
22987196-1	2013	Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II (HCII) to enhance thrombin inhibition.	Dermatan Sulfate	0-16	serpin family D member 1	Homo sapiens	107-111
22987196-1	2013	Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II (HCII) to enhance thrombin inhibition.	Dermatan Sulfate	0-16	coagulation factor II, thrombin	Homo sapiens	124-132
22987196-1	2013	Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II (HCII) to enhance thrombin inhibition.	Dermatan Sulfate	18-20	serpin family D member 1	Homo sapiens	86-105
22987196-1	2013	Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II (HCII) to enhance thrombin inhibition.	Dermatan Sulfate	18-20	serpin family D member 1	Homo sapiens	107-111
22987196-1	2013	Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II (HCII) to enhance thrombin inhibition.	Dermatan Sulfate	18-20	coagulation factor II, thrombin	Homo sapiens	124-132
22419236-2	2013	Dermatan sulfate (DS) selectively inhibits thrombin, does not inhibit F-Xa and does not interfere with platelets (PLTS).	Dermatan Sulfate	0-16	coagulation factor II, thrombin	Homo sapiens	43-51
22419236-2	2013	Dermatan sulfate (DS) selectively inhibits thrombin, does not inhibit F-Xa and does not interfere with platelets (PLTS).	Dermatan Sulfate	18-20	coagulation factor II, thrombin	Homo sapiens	43-51
22877511-6	2012	This shows that the decorin protein and the dermatan sulfate chain of decorin have both a structural function and a signaling function.	Dermatan Sulfate	44-60	decorin	Homo sapiens	70-77
22206708-1	2012	Protein C inhibitor was purified from human plasma by use of a dermatan sulfate or heparin column, followed by hydroxyapatite, gel filtration and ion exchange columns.	Dermatan Sulfate	63-79	serpin family A member 5	Homo sapiens	0-19
22179554-1	2012	Deficiency of IDUA leads to lysosomal accumulation of glycosaminoglycans (GAG) heparan and dermatan sulfate and associated multi-systemic disease, the most severe form of which is known as Hurler syndrome.	Dermatan Sulfate	91-107	iduronidase, alpha-L	Mus musculus	14-18
22079206-3	2012	The enzyme arylsulfatase B (ARSB; N-acetylgalactosamine-4-sulfate) is the highly selective enzyme that removes the four-sulfate group from the nonreducing terminus of C4S and DS, thereby regulating subsequent degradation.	Dermatan Sulfate	175-177	arylsulfatase B	Homo sapiens	11-26
22079206-3	2012	The enzyme arylsulfatase B (ARSB; N-acetylgalactosamine-4-sulfate) is the highly selective enzyme that removes the four-sulfate group from the nonreducing terminus of C4S and DS, thereby regulating subsequent degradation.	Dermatan Sulfate	175-177	arylsulfatase B	Homo sapiens	28-32
22079206-7	2012	The ROS production from kappa-CGN was reduced by exposure to rhARSB, but increased by competition from C4S or DS, but not from chondroitin-6-sulfate.	Dermatan Sulfate	110-112	cingulin	Homo sapiens	30-33
22079206-0	2012	Molecular signature of kappa-carrageenan mimics chondroitin-4-sulfate and dermatan sulfate and enables interaction with arylsulfatase B.	Dermatan Sulfate	74-90	arylsulfatase B	Homo sapiens	120-135
22079206-9	2012	By mimicry of C4S and DS and by interaction with ARSB, kappa-CGN can directly interfere with the normal cellular functions of C4S, DS and ARSB.	Dermatan Sulfate	22-24	cingulin	Homo sapiens	61-64
22079206-1	2012	The common food additive kappa-carrageenan (kappa-CGN) is a sulfated polysaccharide that resembles chondroitin-4-sulfate (C4S) and dermatan sulfate (DS).	Dermatan Sulfate	131-147	cingulin	Homo sapiens	50-53
22079206-9	2012	By mimicry of C4S and DS and by interaction with ARSB, kappa-CGN can directly interfere with the normal cellular functions of C4S, DS and ARSB.	Dermatan Sulfate	22-24	arylsulfatase B	Homo sapiens	138-142
22079206-1	2012	The common food additive kappa-carrageenan (kappa-CGN) is a sulfated polysaccharide that resembles chondroitin-4-sulfate (C4S) and dermatan sulfate (DS).	Dermatan Sulfate	149-151	cingulin	Homo sapiens	50-53
22079206-9	2012	By mimicry of C4S and DS and by interaction with ARSB, kappa-CGN can directly interfere with the normal cellular functions of C4S, DS and ARSB.	Dermatan Sulfate	131-133	arylsulfatase B	Homo sapiens	49-53
22079206-9	2012	By mimicry of C4S and DS and by interaction with ARSB, kappa-CGN can directly interfere with the normal cellular functions of C4S, DS and ARSB.	Dermatan Sulfate	131-133	cingulin	Homo sapiens	61-64
22079206-10	2012	Since C4S and DS are present in high concentration in tissues, the impact of kappa-CGN exposure may be due to some extent to interference with the normal biological functions of ARSB, C4S and DS.	Dermatan Sulfate	14-16	cingulin	Homo sapiens	83-86
22947857-8	2012	In contrast to CD44-HA binding, the molecular interaction between CD44 and fibrin(ogen) is predominantly mediated by the chondroitin sulfate and dermatan sulfate on CD44.	Dermatan Sulfate	145-161	CD44 molecule (Indian blood group)	Homo sapiens	66-70
22947857-8	2012	In contrast to CD44-HA binding, the molecular interaction between CD44 and fibrin(ogen) is predominantly mediated by the chondroitin sulfate and dermatan sulfate on CD44.	Dermatan Sulfate	145-161	CD44 molecule (Indian blood group)	Homo sapiens	66-70
22001376-1	2012	Biglycan (BGN) is a small proteoglycan that consists of a protein core containing leucine-rich repeat regions and two glycosaminoglycan (GAG) chains of either chondroitin sulfate (CS) or dermatan sulfate (DS) type.	Dermatan Sulfate	187-203	biglycan	Homo sapiens	0-8
22533918-1	2012	Low molecular mass dermatan sulfate, obtained by depolymerization, induced the entrance in S phase of mitosis, enhanced the activity of matrix metalloproteinase-2, and could modulate cell migration of endothelial cells, through mechanisms independent of TNF-alpha autocrine regulation.	Dermatan Sulfate	19-35	matrix metallopeptidase 2	Homo sapiens	136-162
22533918-1	2012	Low molecular mass dermatan sulfate, obtained by depolymerization, induced the entrance in S phase of mitosis, enhanced the activity of matrix metalloproteinase-2, and could modulate cell migration of endothelial cells, through mechanisms independent of TNF-alpha autocrine regulation.	Dermatan Sulfate	19-35	tumor necrosis factor	Homo sapiens	254-263
22561305-7	2012	Based on these preliminary studies, DS may serve as a cofactor for FGF-10, and together they are likely to expedite the healing process by stimulating keratinocyte activity.	Dermatan Sulfate	36-38	fibroblast growth factor 10	Homo sapiens	67-73
21732093-2	2012	Recent studies have indicated that serum heparin-cofactor II-thrombin complex (HCII-T) may serve as an important biomarker in the group of MPSs where dermatan sulphate is stored.	Dermatan Sulfate	150-167	coagulation factor II, thrombin	Homo sapiens	61-69
22001376-1	2012	Biglycan (BGN) is a small proteoglycan that consists of a protein core containing leucine-rich repeat regions and two glycosaminoglycan (GAG) chains of either chondroitin sulfate (CS) or dermatan sulfate (DS) type.	Dermatan Sulfate	187-203	biglycan	Homo sapiens	10-13
22001376-1	2012	Biglycan (BGN) is a small proteoglycan that consists of a protein core containing leucine-rich repeat regions and two glycosaminoglycan (GAG) chains of either chondroitin sulfate (CS) or dermatan sulfate (DS) type.	Dermatan Sulfate	205-207	biglycan	Homo sapiens	0-8
22001376-1	2012	Biglycan (BGN) is a small proteoglycan that consists of a protein core containing leucine-rich repeat regions and two glycosaminoglycan (GAG) chains of either chondroitin sulfate (CS) or dermatan sulfate (DS) type.	Dermatan Sulfate	205-207	biglycan	Homo sapiens	10-13
22001376-2	2012	The development of novel, highly efficient analytical methods for structural identification of BGN-derived CS/DS motifs, possibly implicated in biological events, is currently the focus of research.	Dermatan Sulfate	110-112	biglycan	Homo sapiens	95-98
22001376-4	2012	The CS/DS chains were released from transfected 293 BGN by beta-elimination.	Dermatan Sulfate	7-9	biglycan	Homo sapiens	52-55
22506762-10	2012	The decorin protein was found in the tissue, the DS glycosaminoglycan chain was removed with thrombin digestion, and there was no change in the mechanical properties of the tissue due to the thrombin digestion relative to controls.	Dermatan Sulfate	49-51	coagulation factor II, thrombin	Homo sapiens	93-101
22085638-6	2012	These results further demonstrate that while IL-7 is principally a heparin/heparan sulfate binding protein, it also interacts with dermatan sulfate, chondroitin sulfates C, D, and E, indicating that this cytokine preferentially interacts with GAGs having a higher degree of sulfation.	Dermatan Sulfate	131-147	interleukin 7	Mus musculus	45-49
22428001-2	2012	ARSB removes 4-sulfate groups from the non-reducing end of chondroitin-4-sulfate and dermatan sulfate and is required for their degradation.	Dermatan Sulfate	85-101	arylsulfatase B	Homo sapiens	0-4
23023219-1	2012	BACKGROUND: Mucopolysaccharidosis type-VI (MPS-VI), which is inherited as an autosomal recessive trait, results from the deficiency of N-acetylgalactosamine 4-sulfatase (arylsulfatase B) activity and the lysosomal accumulation of dermatan sulfate.	Dermatan Sulfate	230-246	arylsulfatase B	Homo sapiens	135-168
23023219-1	2012	BACKGROUND: Mucopolysaccharidosis type-VI (MPS-VI), which is inherited as an autosomal recessive trait, results from the deficiency of N-acetylgalactosamine 4-sulfatase (arylsulfatase B) activity and the lysosomal accumulation of dermatan sulfate.	Dermatan Sulfate	230-246	arylsulfatase B	Homo sapiens	170-185
23056168-6	2012	Enzymatic inhibition studies coupled with flow-based adhesion assays and autoradiography reveal that PDGF augments the binding of CD44v to fibrin by significantly attenuating the extent of CD44 sulfation primarily on chondroitin and dermatan sulfate chains.	Dermatan Sulfate	233-249	CD44 molecule (Indian blood group)	Homo sapiens	130-134
23226541-0	2012	The dermatan sulfate proteoglycan decorin modulates alpha2beta1 integrin and the vimentin intermediate filament system during collagen synthesis.	Dermatan Sulfate	4-20	decorin	Mus musculus	34-41
23226541-0	2012	The dermatan sulfate proteoglycan decorin modulates alpha2beta1 integrin and the vimentin intermediate filament system during collagen synthesis.	Dermatan Sulfate	4-20	vimentin	Mus musculus	81-89
23226541-1	2012	Decorin, a small leucine-rich proteoglycan harboring a dermatan sulfate chain at its N-terminus, is involved in regulating matrix organization and cell signaling.	Dermatan Sulfate	55-71	decorin	Mus musculus	0-7
23226541-2	2012	Loss of the dermatan sulfate of decorin leads to an Ehlers-Danlos syndrome characterized by delayed wound healing.	Dermatan Sulfate	12-28	decorin	Mus musculus	32-39
21964831-0	2011	A response to: loss of dermatan-4-sulfotransferase 1 (D4ST1/CHST14) function represents the first dermatan sulfate biosynthesis defect, "dermatan sulfate-deficient Adducted Thumb-Clubfoot Syndrome".	Dermatan Sulfate	98-114	carbohydrate sulfotransferase 14	Homo sapiens	23-52
21964831-0	2011	A response to: loss of dermatan-4-sulfotransferase 1 (D4ST1/CHST14) function represents the first dermatan sulfate biosynthesis defect, "dermatan sulfate-deficient Adducted Thumb-Clubfoot Syndrome".	Dermatan Sulfate	98-114	carbohydrate sulfotransferase 14	Homo sapiens	54-59
21964831-0	2011	A response to: loss of dermatan-4-sulfotransferase 1 (D4ST1/CHST14) function represents the first dermatan sulfate biosynthesis defect, "dermatan sulfate-deficient Adducted Thumb-Clubfoot Syndrome".	Dermatan Sulfate	98-114	carbohydrate sulfotransferase 14	Homo sapiens	60-66
21805439-10	2011	Additionally, pharmaceuticals are being developed that use the dermatan sulfate activation of HCII for anticoagulation.	Dermatan Sulfate	63-79	serpin family D member 1	Homo sapiens	94-98
21792394-2	2011	As a consequence of the conversion of chondroitin sulfate (CS) to dermatan sulfate (DS), the glycosaminoglycans become more flexible and enable DS to perform more sophisticated signaling functions.	Dermatan Sulfate	66-82	colony stimulating factor 1	Homo sapiens	59-61
21792394-2	2011	As a consequence of the conversion of chondroitin sulfate (CS) to dermatan sulfate (DS), the glycosaminoglycans become more flexible and enable DS to perform more sophisticated signaling functions.	Dermatan Sulfate	144-146	colony stimulating factor 1	Homo sapiens	59-61
21792394-4	2011	C-terminal truncation constructs from S222A enabled us to identify an amino acid segment that lies within the CSF-1 part which prevents DS synthesis.	Dermatan Sulfate	136-138	colony stimulating factor 1	Homo sapiens	110-115
21708995-0	2011	Allelic variation of the Lyme disease spirochete adhesin DbpA influences spirochetal binding to decorin, dermatan sulfate, and mammalian cells.	Dermatan Sulfate	105-121	Y box protein 3	Mus musculus	57-61
21708995-6	2011	Each DbpA allele conferred upon B. burgdorferi strain B314 the ability to bind to cultured kidney epithelial (but not glial or endothelial) cells, as well as to purified decorin and dermatan sulfate.	Dermatan Sulfate	182-198	Y box protein 3	Mus musculus	5-9
21708995-8	2011	In most cases, decorin and dermatan sulfate binding correlated well, but DbpA of B. afzelii strain VS461 promoted differential binding to decorin and dermatan sulfate, indicating that the two activities are separable.	Dermatan Sulfate	150-166	Y box protein 3	Mus musculus	73-77
21833458-0	2011	Dermatan sulfate reduces monocyte chemoattractant protein 1 and TGF-beta production, as well as macrophage recruitment and myofibroblast accumulation in mice with unilateral ureteral obstruction.	Dermatan Sulfate	0-16	chemokine (C-C motif) ligand 2	Mus musculus	25-59
21833458-0	2011	Dermatan sulfate reduces monocyte chemoattractant protein 1 and TGF-beta production, as well as macrophage recruitment and myofibroblast accumulation in mice with unilateral ureteral obstruction.	Dermatan Sulfate	0-16	transforming growth factor, beta 1	Mus musculus	64-72
21833458-2	2011	Heparin and dermatan sulfate (DS) bind and block P- and L-selectin function in vitro.	Dermatan Sulfate	12-28	selectin, lymphocyte	Mus musculus	56-66
21833458-2	2011	Heparin and dermatan sulfate (DS) bind and block P- and L-selectin function in vitro.	Dermatan Sulfate	30-32	selectin, lymphocyte	Mus musculus	56-66
21833458-8	2011	DS treatment significantly (P < 0.05) reduced the content of collagen (stained area ~700 microm(2)), MCP-1 (stained area ~160 microm(2)) and TGF-beta (stained area ~5% of total area), in addition to myofibroblast (stained area ~190 microm(2)) and macrophage (number of cells ~32) accumulation in the obstructed kidney.	Dermatan Sulfate	0-2	chemokine (C-C motif) ligand 2	Mus musculus	104-109
21833458-8	2011	DS treatment significantly (P < 0.05) reduced the content of collagen (stained area ~700 microm(2)), MCP-1 (stained area ~160 microm(2)) and TGF-beta (stained area ~5% of total area), in addition to myofibroblast (stained area ~190 microm(2)) and macrophage (number of cells ~32) accumulation in the obstructed kidney.	Dermatan Sulfate	0-2	transforming growth factor, beta 1	Mus musculus	144-152
21676168-4	2011	OBJECTIVES AND METHODS: The aim of the present study was to determine the capacity of dermatan sulfates to inhibit P-selectin and to test their potential to affect thrombosis, inflammation and metastasis in respective experimental mouse models.	Dermatan Sulfate	86-103	selectin, platelet	Mus musculus	115-125
21676168-5	2011	RESULTS: Two dermatan sulfates isolated from the ascidians Styela plicata and Phallusia nigra, composed of the same disaccharide core structure (IdoA2-GalNAc)(n) , but sulfated at carbon 4 or 6 of the GalNAc, respectively, have opposed heparin cofactor II (HCII) activities and are potent inhibitors of P-selectin.	Dermatan Sulfate	13-30	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	257-261
21676168-5	2011	RESULTS: Two dermatan sulfates isolated from the ascidians Styela plicata and Phallusia nigra, composed of the same disaccharide core structure (IdoA2-GalNAc)(n) , but sulfated at carbon 4 or 6 of the GalNAc, respectively, have opposed heparin cofactor II (HCII) activities and are potent inhibitors of P-selectin.	Dermatan Sulfate	13-30	selectin, platelet	Mus musculus	303-313
21676168-8	2011	The analysis of arterial thrombi demonstrated markedly reduced platelet deposition after dermatan sulfate treatment, suggesting that the glycosaminoglycan inhibited P-selectin and thereby the binding of activated platelets during thrombus formation.	Dermatan Sulfate	89-105	selectin, platelet	Mus musculus	165-175
21250866-1	2011	BACKGROUND AIMS: Previously, we have demonstrated that administration of dermatan sulfate (DS) suppresses neointima formation in the mouse carotid artery by activating heparin co-factor II.	Dermatan Sulfate	73-89	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	168-188
21250866-1	2011	BACKGROUND AIMS: Previously, we have demonstrated that administration of dermatan sulfate (DS) suppresses neointima formation in the mouse carotid artery by activating heparin co-factor II.	Dermatan Sulfate	91-93	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	168-188
21250866-8	2011	Treatment with DS inhibited thrombosis, decreased CD45(+) cell accumulation and P-selectin expression at the site of injury, and reduced the neointimal area by 56%.	Dermatan Sulfate	15-17	protein tyrosine phosphatase, receptor type, C	Mus musculus	50-54
21250866-8	2011	Treatment with DS inhibited thrombosis, decreased CD45(+) cell accumulation and P-selectin expression at the site of injury, and reduced the neointimal area by 56%.	Dermatan Sulfate	15-17	selectin, platelet	Mus musculus	80-90
21406563-8	2011	The changes in CS/DS had implications on ligand-binding properties when tested in vitro for binding to major extracellular matrix (ECM) components such as type IV collagen, laminin and fibronectin.	Dermatan Sulfate	18-20	fibronectin 1	Rattus norvegicus	185-196
21647927-0	2011	Combining size-exclusion chromatography and fully automated chip-based nanoelectrospray quadrupole time-of-flight tandem mass spectrometry for structural analysis of chondroitin/dermatan sulfate in human decorin.	Dermatan Sulfate	178-194	decorin	Homo sapiens	204-211
21256835-6	2011	RESULTS: Glycosaminoglycans extracted from aneurysms have a more potent anticoagulant activity than those from normal arteries of young adults, mostly due to a relative enrichment of dermatan sulfate, which potentiates heparin cofactor II inhibition of thrombin.	Dermatan Sulfate	183-199	coagulation factor II, thrombin	Homo sapiens	253-261
20821239-1	2011	Endothelial cell-specific molecule-1 (ESM-1) is a secretory proteoglycan comprising a mature polypeptide of 165 amino acids and a single dermatan sulfate.	Dermatan Sulfate	137-153	endothelial cell specific molecule 1	Homo sapiens	0-36
21177331-4	2011	In this study, to clarify the distribution of the DS-type structure in the brain during development, the expression patterns of DS epimerase 1 (DS-epi1) and DS-epi2, both of which convert d-glucuronic acid into IdoA, were investigated by in situ hybridization.	Dermatan Sulfate	50-52	dermatan sulfate epimerase-like	Mus musculus	157-164
21177331-6	2011	Quantitative real-time polymerase chain reaction revealed the expression of DS-epi2 to be higher than that of DS-epi1 throughout development, suggesting that DS-epi2 but not DS-epi1 is mostly expressed in the brain and plays key roles in the epimerization of CS/DS during its biosynthesis.	Dermatan Sulfate	76-78	dermatan sulfate epimerase-like	Mus musculus	158-165
21177331-7	2011	Moreover, an analysis of the disaccharides of CS/DS demonstrated significant amounts of IdoA-containing iD units [IdoA(2S)-GalNAc(6S)] and iB units [IdoA(2S)-GalNAc(4S)], where 2S, 4S and 6S stand for 2-O-, 4-O- and 6-O-sulfate, respectively, in every region of the brain examined.	Dermatan Sulfate	49-51	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Mus musculus	123-132
21521498-1	2011	UNLABELLED: Mucopolysaccharidosis type I (MPS I) is an autosomal recessive lysosomal storage disorder caused by a genetic defect in alpha-L-iduronidase (IDUA) which is involved in the degradation of dermatan and heparan sulfates.	Dermatan Sulfate	199-207	alpha-L-iduronidase	Homo sapiens	132-151
21521498-1	2011	UNLABELLED: Mucopolysaccharidosis type I (MPS I) is an autosomal recessive lysosomal storage disorder caused by a genetic defect in alpha-L-iduronidase (IDUA) which is involved in the degradation of dermatan and heparan sulfates.	Dermatan Sulfate	199-207	alpha-L-iduronidase	Homo sapiens	153-157
21514431-0	2011	Dermatan sulfate interacts with dead cells and regulates CD5(+) B-cell fate: implications for a key role in autoimmunity.	Dermatan Sulfate	0-16	CD5 molecule	Homo sapiens	57-60
21309034-0	2011	Loss of dermatan-4-sulfotransferase 1 (D4ST1/CHST14) function represents the first dermatan sulfate biosynthesis defect, "dermatan sulfate-deficient adducted thumb-clubfoot syndrome".	Dermatan Sulfate	83-99	carbohydrate sulfotransferase 14	Homo sapiens	8-37
21309034-0	2011	Loss of dermatan-4-sulfotransferase 1 (D4ST1/CHST14) function represents the first dermatan sulfate biosynthesis defect, "dermatan sulfate-deficient adducted thumb-clubfoot syndrome".	Dermatan Sulfate	83-99	carbohydrate sulfotransferase 14	Homo sapiens	39-44
21309034-0	2011	Loss of dermatan-4-sulfotransferase 1 (D4ST1/CHST14) function represents the first dermatan sulfate biosynthesis defect, "dermatan sulfate-deficient adducted thumb-clubfoot syndrome".	Dermatan Sulfate	83-99	carbohydrate sulfotransferase 14	Homo sapiens	45-51
21624210-2	2011	IDUA is one of the enzymes involved in degradation of glycosaminoglycans heparan sulphate and dermatan sulphate.	Dermatan Sulfate	94-111	alpha-L-iduronidase	Homo sapiens	0-4
21193389-8	2011	Examination of chondroitin/dermatan sulfate catabolic enzymes showed that heparan sulfate and heparin can inhibit iduronate 2-sulfatase.	Dermatan Sulfate	27-43	iduronate 2-sulfatase	Homo sapiens	114-135
21193389-9	2011	Analysis of the chondroitin/dermatan sulfate fraction by chondroitinase ACII digestion showed dermatan sulfate storage, consistent with inhibition of iduronate 2-sulfatase.	Dermatan Sulfate	28-44	iduronate 2-sulfatase	Homo sapiens	150-171
20821239-1	2011	Endothelial cell-specific molecule-1 (ESM-1) is a secretory proteoglycan comprising a mature polypeptide of 165 amino acids and a single dermatan sulfate.	Dermatan Sulfate	137-153	endothelial cell specific molecule 1	Homo sapiens	38-43
21378286-1	2011	The enzyme arylsulfatase B (N-acetylgalactosamine-4-sulfatase; ARSB; ASB) removes 4-sulfate groups from the sulfated glycosaminoglycans (sGAG) chondroitin-4-sulfate (C4S) and dermatan sulfate (DS).	Dermatan Sulfate	175-191	arylsulfatase B	Homo sapiens	28-61
21378286-1	2011	The enzyme arylsulfatase B (N-acetylgalactosamine-4-sulfatase; ARSB; ASB) removes 4-sulfate groups from the sulfated glycosaminoglycans (sGAG) chondroitin-4-sulfate (C4S) and dermatan sulfate (DS).	Dermatan Sulfate	175-191	arylsulfatase B	Homo sapiens	63-67
21378286-1	2011	The enzyme arylsulfatase B (N-acetylgalactosamine-4-sulfatase; ARSB; ASB) removes 4-sulfate groups from the sulfated glycosaminoglycans (sGAG) chondroitin-4-sulfate (C4S) and dermatan sulfate (DS).	Dermatan Sulfate	175-191	arylsulfatase B	Homo sapiens	69-72
21378286-1	2011	The enzyme arylsulfatase B (N-acetylgalactosamine-4-sulfatase; ARSB; ASB) removes 4-sulfate groups from the sulfated glycosaminoglycans (sGAG) chondroitin-4-sulfate (C4S) and dermatan sulfate (DS).	Dermatan Sulfate	193-195	arylsulfatase B	Homo sapiens	28-61
21378286-1	2011	The enzyme arylsulfatase B (N-acetylgalactosamine-4-sulfatase; ARSB; ASB) removes 4-sulfate groups from the sulfated glycosaminoglycans (sGAG) chondroitin-4-sulfate (C4S) and dermatan sulfate (DS).	Dermatan Sulfate	193-195	arylsulfatase B	Homo sapiens	63-67
21378286-1	2011	The enzyme arylsulfatase B (N-acetylgalactosamine-4-sulfatase; ARSB; ASB) removes 4-sulfate groups from the sulfated glycosaminoglycans (sGAG) chondroitin-4-sulfate (C4S) and dermatan sulfate (DS).	Dermatan Sulfate	193-195	arylsulfatase B	Homo sapiens	69-72
20670608-1	2010	Irreversible inactivation of alpha-thrombin (T) by the serpin, heparin cofactor II (HCII), is accelerated by ternary complex formation with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (DS).	Dermatan Sulfate	182-198	coagulation factor II, thrombin	Homo sapiens	35-43
20980181-2	2011	MPS VI is characterized by an absence or deficiency of N-acetylgalactosamine 4-sulfatase (arylsulfatase B) resulting in accumulation of dermatan sulfate.	Dermatan Sulfate	136-152	arylsulfatase B	Homo sapiens	55-88
20980181-2	2011	MPS VI is characterized by an absence or deficiency of N-acetylgalactosamine 4-sulfatase (arylsulfatase B) resulting in accumulation of dermatan sulfate.	Dermatan Sulfate	136-152	arylsulfatase B	Homo sapiens	90-105
22303797-8	2011	MPS I is a progressive disease, in which tissue accummulation of heparan and dermatan sulphate result from defective activity or lack of alpha-L-iduronidase.	Dermatan Sulfate	77-94	alpha-L-iduronidase	Homo sapiens	137-156
21062008-4	2010	Using a gel mobility shift assay, we found that HBD2 bound to a range of GAGs including heparin/heparan sulfate (HS), dermatan sulfate (DS), and chondroitin sulfate.	Dermatan Sulfate	118-134	defensin beta 4A	Homo sapiens	48-52
21062008-4	2010	Using a gel mobility shift assay, we found that HBD2 bound to a range of GAGs including heparin/heparan sulfate (HS), dermatan sulfate (DS), and chondroitin sulfate.	Dermatan Sulfate	136-138	defensin beta 4A	Homo sapiens	48-52
21123810-0	2010	Replacing the enzyme alpha-L-iduronidase at birth ameliorates symptoms in the brain and periphery of dogs with mucopolysaccharidosis type I. Mucopolysaccharidosis type I (MPS I) is a lysosomal storage disease caused by loss of activity of alpha-l-iduronidase and attendant accumulation of the glycosaminoglycans dermatan sulfate and heparan sulfate.	Dermatan Sulfate	312-328	alpha-L-iduronidase	Canis lupus familiaris	21-40
20670608-1	2010	Irreversible inactivation of alpha-thrombin (T) by the serpin, heparin cofactor II (HCII), is accelerated by ternary complex formation with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (DS).	Dermatan Sulfate	182-198	serpin family D member 1	Homo sapiens	63-82
20670608-1	2010	Irreversible inactivation of alpha-thrombin (T) by the serpin, heparin cofactor II (HCII), is accelerated by ternary complex formation with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (DS).	Dermatan Sulfate	182-198	serpin family D member 1	Homo sapiens	84-88
20670608-1	2010	Irreversible inactivation of alpha-thrombin (T) by the serpin, heparin cofactor II (HCII), is accelerated by ternary complex formation with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (DS).	Dermatan Sulfate	200-202	coagulation factor II, thrombin	Homo sapiens	35-43
20670608-1	2010	Irreversible inactivation of alpha-thrombin (T) by the serpin, heparin cofactor II (HCII), is accelerated by ternary complex formation with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (DS).	Dermatan Sulfate	200-202	serpin family D member 1	Homo sapiens	63-82
20670608-1	2010	Irreversible inactivation of alpha-thrombin (T) by the serpin, heparin cofactor II (HCII), is accelerated by ternary complex formation with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (DS).	Dermatan Sulfate	200-202	serpin family D member 1	Homo sapiens	84-88
20581009-0	2010	Characterization and binding activity of the chondroitin/dermatan sulfate chain from Endocan, a soluble endothelial proteoglycan.	Dermatan Sulfate	57-73	endothelial cell specific molecule 1	Homo sapiens	85-92
20581009-1	2010	Endocan is a recently identified soluble chondroitin/dermatan sulfate (CS/DS) proteoglycan.	Dermatan Sulfate	53-69	endothelial cell specific molecule 1	Homo sapiens	0-7
20584902-1	2010	Endogenous pleiotrophin and hepatocyte growth factor (HGF) mediate the neurite outgrowth-promoting activity of chondroitin sulfate (CS)/dermatan sulfate (DS) hybrid chains isolated from embryonic pig brain.	Dermatan Sulfate	136-152	pleiotrophin	Sus scrofa	11-23
20842734-9	2010	Our findings confirm that the EDS-variant associated with CHST14 mutations forms a clinical spectrum, which we propose to coin as "musculocontractural EDS" and which results from a defect in dermatan sulfate biosynthesis, perturbing collagen assembly.	Dermatan Sulfate	191-207	carbohydrate sulfotransferase 14	Homo sapiens	58-64
20584902-9	2010	Computational chemistry using molecular modeling and calculations of the electrostatic potential of the hexasaccharide and two pleiotrophin-binding octasaccharides previously isolated from CS/DS hybrid chains of embryonic pig brain identified an electronegative zone potentially involved in the molecular recognition of the oligosaccharides by pleiotrophin.	Dermatan Sulfate	192-194	pleiotrophin	Sus scrofa	127-139
20584902-1	2010	Endogenous pleiotrophin and hepatocyte growth factor (HGF) mediate the neurite outgrowth-promoting activity of chondroitin sulfate (CS)/dermatan sulfate (DS) hybrid chains isolated from embryonic pig brain.	Dermatan Sulfate	136-152	hepatocyte growth factor	Sus scrofa	28-52
20584902-1	2010	Endogenous pleiotrophin and hepatocyte growth factor (HGF) mediate the neurite outgrowth-promoting activity of chondroitin sulfate (CS)/dermatan sulfate (DS) hybrid chains isolated from embryonic pig brain.	Dermatan Sulfate	136-152	hepatocyte growth factor	Sus scrofa	54-57
20584902-1	2010	Endogenous pleiotrophin and hepatocyte growth factor (HGF) mediate the neurite outgrowth-promoting activity of chondroitin sulfate (CS)/dermatan sulfate (DS) hybrid chains isolated from embryonic pig brain.	Dermatan Sulfate	154-156	pleiotrophin	Sus scrofa	11-23
20584902-1	2010	Endogenous pleiotrophin and hepatocyte growth factor (HGF) mediate the neurite outgrowth-promoting activity of chondroitin sulfate (CS)/dermatan sulfate (DS) hybrid chains isolated from embryonic pig brain.	Dermatan Sulfate	154-156	hepatocyte growth factor	Sus scrofa	28-52
20584902-1	2010	Endogenous pleiotrophin and hepatocyte growth factor (HGF) mediate the neurite outgrowth-promoting activity of chondroitin sulfate (CS)/dermatan sulfate (DS) hybrid chains isolated from embryonic pig brain.	Dermatan Sulfate	154-156	hepatocyte growth factor	Sus scrofa	54-57
20584902-3	2010	In this study, pleiotrophin- and HGF-binding domains in shark skin CS/DS were investigated.	Dermatan Sulfate	70-72	pleiotrophin	Sus scrofa	15-27
20584902-3	2010	In this study, pleiotrophin- and HGF-binding domains in shark skin CS/DS were investigated.	Dermatan Sulfate	70-72	hepatocyte growth factor	Sus scrofa	33-36
20584902-4	2010	A high affinity CS/DS fraction was isolated using a pleiotrophin-immobilized column.	Dermatan Sulfate	19-21	pleiotrophin	Sus scrofa	52-64
20584902-5	2010	It showed marked neurite outgrowth-promoting activity and strong inhibitory activity against the binding of pleiotrophin to immobilized CS/DS chains from embryonic pig brain.	Dermatan Sulfate	139-141	pleiotrophin	Sus scrofa	108-120
20584902-8	2010	It displayed a potent inhibitory effect on the binding of HGF to immobilized shark skin CS/DS chains, suggesting that the pleiotrophin- and HGF-binding domains at least partially overlap in the CS/DS chains involved in the neuritogenic activity.	Dermatan Sulfate	91-93	hepatocyte growth factor	Sus scrofa	58-61
20584902-8	2010	It displayed a potent inhibitory effect on the binding of HGF to immobilized shark skin CS/DS chains, suggesting that the pleiotrophin- and HGF-binding domains at least partially overlap in the CS/DS chains involved in the neuritogenic activity.	Dermatan Sulfate	197-199	hepatocyte growth factor	Sus scrofa	58-61
20584902-8	2010	It displayed a potent inhibitory effect on the binding of HGF to immobilized shark skin CS/DS chains, suggesting that the pleiotrophin- and HGF-binding domains at least partially overlap in the CS/DS chains involved in the neuritogenic activity.	Dermatan Sulfate	197-199	pleiotrophin	Sus scrofa	122-134
20584902-8	2010	It displayed a potent inhibitory effect on the binding of HGF to immobilized shark skin CS/DS chains, suggesting that the pleiotrophin- and HGF-binding domains at least partially overlap in the CS/DS chains involved in the neuritogenic activity.	Dermatan Sulfate	197-199	hepatocyte growth factor	Sus scrofa	140-143
20439988-5	2010	In GalNAc4S-6ST-null mice, GalNAc(4,6-SO(4)) residues in CS and DS disappeared completely, indicating that GalNAc4S-6ST should be a sole enzyme responsible for the synthesis of GalNAc(4,6-SO(4)) residues in both CS and DS.	Dermatan Sulfate	64-66	carbohydrate sulfotransferase 15	Mus musculus	3-15
20043808-4	2010	Pretreatment of the 42-residue Abeta fragment (Abeta1-42) with the ubiquitous brain carbohydrates, glucose, fructose, and the GAG chondroitin sulfate B (CSB) inhibits Abeta1-42-induced apoptosis and reduces the peptide neurotoxicity on neuroblastoma cells, a cytoprotective effect that is partially reverted by AGE inhibitors such as pyridoxamine and L-carnosine.	Dermatan Sulfate	130-151	amyloid beta precursor protein	Homo sapiens	31-36
20043808-4	2010	Pretreatment of the 42-residue Abeta fragment (Abeta1-42) with the ubiquitous brain carbohydrates, glucose, fructose, and the GAG chondroitin sulfate B (CSB) inhibits Abeta1-42-induced apoptosis and reduces the peptide neurotoxicity on neuroblastoma cells, a cytoprotective effect that is partially reverted by AGE inhibitors such as pyridoxamine and L-carnosine.	Dermatan Sulfate	153-156	amyloid beta precursor protein	Homo sapiens	31-36
20439988-0	2010	Mice deficient in N-acetylgalactosamine 4-sulfate 6-o-sulfotransferase are unable to synthesize chondroitin/dermatan sulfate containing N-acetylgalactosamine 4,6-bissulfate residues and exhibit decreased protease activity in bone marrow-derived mast cells.	Dermatan Sulfate	108-124	carbohydrate sulfotransferase 15	Mus musculus	18-70
20439988-2	2010	N-Acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) transfers sulfate from 3"-phosphoadenosine 5"-phosphosulfate to position 6 of N-acetylgalactosamine 4-sulfate in CS or DS to yield GalNAc(4,6-SO(4)) residues.	Dermatan Sulfate	187-189	carbohydrate sulfotransferase 15	Mus musculus	0-52
20439988-2	2010	N-Acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) transfers sulfate from 3"-phosphoadenosine 5"-phosphosulfate to position 6 of N-acetylgalactosamine 4-sulfate in CS or DS to yield GalNAc(4,6-SO(4)) residues.	Dermatan Sulfate	187-189	carbohydrate sulfotransferase 15	Mus musculus	54-66
20533528-4	2010	CHST14 encodes dermatan 4-O-sulfotransferase 1 (D4ST1), which transfers active sulfate from 3"-phosphoadenosine 5"-phosphosulfate to position 4 of the N-acetyl-D-galactosamine (GalNAc) residues of dermatan sulfate (DS).	Dermatan Sulfate	197-213	carbohydrate sulfotransferase 14	Homo sapiens	0-6
20533528-4	2010	CHST14 encodes dermatan 4-O-sulfotransferase 1 (D4ST1), which transfers active sulfate from 3"-phosphoadenosine 5"-phosphosulfate to position 4 of the N-acetyl-D-galactosamine (GalNAc) residues of dermatan sulfate (DS).	Dermatan Sulfate	197-213	carbohydrate sulfotransferase 14	Homo sapiens	48-53
20533528-4	2010	CHST14 encodes dermatan 4-O-sulfotransferase 1 (D4ST1), which transfers active sulfate from 3"-phosphoadenosine 5"-phosphosulfate to position 4 of the N-acetyl-D-galactosamine (GalNAc) residues of dermatan sulfate (DS).	Dermatan Sulfate	215-217	carbohydrate sulfotransferase 14	Homo sapiens	0-6
20533528-4	2010	CHST14 encodes dermatan 4-O-sulfotransferase 1 (D4ST1), which transfers active sulfate from 3"-phosphoadenosine 5"-phosphosulfate to position 4 of the N-acetyl-D-galactosamine (GalNAc) residues of dermatan sulfate (DS).	Dermatan Sulfate	215-217	carbohydrate sulfotransferase 14	Homo sapiens	48-53
20439988-5	2010	In GalNAc4S-6ST-null mice, GalNAc(4,6-SO(4)) residues in CS and DS disappeared completely, indicating that GalNAc4S-6ST should be a sole enzyme responsible for the synthesis of GalNAc(4,6-SO(4)) residues in both CS and DS.	Dermatan Sulfate	64-66	carbohydrate sulfotransferase 15	Mus musculus	107-119
20439988-5	2010	In GalNAc4S-6ST-null mice, GalNAc(4,6-SO(4)) residues in CS and DS disappeared completely, indicating that GalNAc4S-6ST should be a sole enzyme responsible for the synthesis of GalNAc(4,6-SO(4)) residues in both CS and DS.	Dermatan Sulfate	219-221	carbohydrate sulfotransferase 15	Mus musculus	3-15
20439988-5	2010	In GalNAc4S-6ST-null mice, GalNAc(4,6-SO(4)) residues in CS and DS disappeared completely, indicating that GalNAc4S-6ST should be a sole enzyme responsible for the synthesis of GalNAc(4,6-SO(4)) residues in both CS and DS.	Dermatan Sulfate	219-221	carbohydrate sulfotransferase 15	Mus musculus	107-119
20439988-6	2010	IdoA-GalNAc(4,6-SO(4)) units that account for approximately 40% of total disaccharide units of DS in the liver of the wild-type mice disappeared in the liver DS of GalNAc4S-6ST-null mice without reduction of IdoA content.	Dermatan Sulfate	95-97	carbohydrate sulfotransferase 15	Mus musculus	164-176
20439988-6	2010	IdoA-GalNAc(4,6-SO(4)) units that account for approximately 40% of total disaccharide units of DS in the liver of the wild-type mice disappeared in the liver DS of GalNAc4S-6ST-null mice without reduction of IdoA content.	Dermatan Sulfate	158-160	carbohydrate sulfotransferase 15	Mus musculus	164-176
20807649-3	2010	ATCS is caused by homozygous nonsense and missense mutations in CHST14 which encodes an N-acetylgalactosamine 4-O-sulfotransferase 1 (D4ST1) that catalyzes the 4-O-sulfation of N-acetylgalactosamine in the repeating iduronic acid-alpha-1,3-N-acetylgalactosamine disaccharide sequence to form dermatan sulfate (DS).	Dermatan Sulfate	292-308	carbohydrate sulfotransferase 14	Homo sapiens	64-70
20652491-1	2010	Mucopolysaccharidosis type II (MPS II; Hunter syndrome) is an X-linked inherited disorder caused by a deficiency of the enzyme iduronate-2-sulfatase (IDS), which results in the lysosomal accumulation of glycosaminoglycans (GAG) such as dermatan and heparan sulfate.	Dermatan Sulfate	236-244	iduronate 2-sulfatase	Homo sapiens	127-148
20652491-1	2010	Mucopolysaccharidosis type II (MPS II; Hunter syndrome) is an X-linked inherited disorder caused by a deficiency of the enzyme iduronate-2-sulfatase (IDS), which results in the lysosomal accumulation of glycosaminoglycans (GAG) such as dermatan and heparan sulfate.	Dermatan Sulfate	236-244	iduronate 2-sulfatase	Homo sapiens	150-153
20152898-1	2010	The enzyme arylsulfatase B (N-acetylgalactosamine 4-sulfatase; ASB; ARSB), which removes 4-sulfate groups from the nonreducing end of chondroitin-4-sulfate (C4S;CSA) and dermatan sulfate, has cellular effects, beyond those associated with the lysosomal storage disease mucopolysaccharidosis VI.	Dermatan Sulfate	170-186	arylsulfatase B	Homo sapiens	11-26
20152898-1	2010	The enzyme arylsulfatase B (N-acetylgalactosamine 4-sulfatase; ASB; ARSB), which removes 4-sulfate groups from the nonreducing end of chondroitin-4-sulfate (C4S;CSA) and dermatan sulfate, has cellular effects, beyond those associated with the lysosomal storage disease mucopolysaccharidosis VI.	Dermatan Sulfate	170-186	arylsulfatase B	Homo sapiens	28-61
20152898-1	2010	The enzyme arylsulfatase B (N-acetylgalactosamine 4-sulfatase; ASB; ARSB), which removes 4-sulfate groups from the nonreducing end of chondroitin-4-sulfate (C4S;CSA) and dermatan sulfate, has cellular effects, beyond those associated with the lysosomal storage disease mucopolysaccharidosis VI.	Dermatan Sulfate	170-186	arylsulfatase B	Homo sapiens	63-66
20152898-1	2010	The enzyme arylsulfatase B (N-acetylgalactosamine 4-sulfatase; ASB; ARSB), which removes 4-sulfate groups from the nonreducing end of chondroitin-4-sulfate (C4S;CSA) and dermatan sulfate, has cellular effects, beyond those associated with the lysosomal storage disease mucopolysaccharidosis VI.	Dermatan Sulfate	170-186	arylsulfatase B	Homo sapiens	68-72
20152898-1	2010	The enzyme arylsulfatase B (N-acetylgalactosamine 4-sulfatase; ASB; ARSB), which removes 4-sulfate groups from the nonreducing end of chondroitin-4-sulfate (C4S;CSA) and dermatan sulfate, has cellular effects, beyond those associated with the lysosomal storage disease mucopolysaccharidosis VI.	Dermatan Sulfate	170-186	complement C4A (Rodgers blood group)	Homo sapiens	157-160
20001848-9	2010	However, contrasts in the mechanical properties of the MDCN tissue suggest that the dermatan sulfate chains on decorin influences the organization/maturation and resultant mechanical properties of the matrix by as an yet-unidentified regulatory mechanism.	Dermatan Sulfate	84-100	decorin	Mus musculus	111-118
20162367-0	2010	Dermatan sulfate and heparan sulfate as a biomarker for mucopolysaccharidosis I. Mucopolysaccharidosis I (MPS I) is an autosomal recessive disorder caused by deficiency of alpha-L-iduronidase leading to accumulation of its catabolic substrates, dermatan sulfate (DS) and heparan sulfate (HS), in lysosomes.	Dermatan Sulfate	0-16	alpha-L-iduronidase	Homo sapiens	172-191
19751987-3	2010	alpha-l-iduronidase (encoded by the IDUA gene) is a lysosomal enzyme that participates in the degradation of dermatan sulfate and heparan sulfate.	Dermatan Sulfate	109-125	iduronidase, alpha-L	Mus musculus	0-19
19751987-3	2010	alpha-l-iduronidase (encoded by the IDUA gene) is a lysosomal enzyme that participates in the degradation of dermatan sulfate and heparan sulfate.	Dermatan Sulfate	109-125	iduronidase, alpha-L	Mus musculus	36-40
20385007-10	2010	Over 130 ARSB mutations have been reported, causing absent or reduced arylsulfatase B (N-acetylgalactosamine 4-sulfatase) activity and interrupted dermatan sulfate and chondroitin sulfate degradation.	Dermatan Sulfate	147-163	arylsulfatase B	Homo sapiens	9-13
20807649-3	2010	ATCS is caused by homozygous nonsense and missense mutations in CHST14 which encodes an N-acetylgalactosamine 4-O-sulfotransferase 1 (D4ST1) that catalyzes the 4-O-sulfation of N-acetylgalactosamine in the repeating iduronic acid-alpha-1,3-N-acetylgalactosamine disaccharide sequence to form dermatan sulfate (DS).	Dermatan Sulfate	292-308	carbohydrate sulfotransferase 8	Homo sapiens	88-132
20807649-3	2010	ATCS is caused by homozygous nonsense and missense mutations in CHST14 which encodes an N-acetylgalactosamine 4-O-sulfotransferase 1 (D4ST1) that catalyzes the 4-O-sulfation of N-acetylgalactosamine in the repeating iduronic acid-alpha-1,3-N-acetylgalactosamine disaccharide sequence to form dermatan sulfate (DS).	Dermatan Sulfate	292-308	carbohydrate sulfotransferase 14	Homo sapiens	134-139
20807649-3	2010	ATCS is caused by homozygous nonsense and missense mutations in CHST14 which encodes an N-acetylgalactosamine 4-O-sulfotransferase 1 (D4ST1) that catalyzes the 4-O-sulfation of N-acetylgalactosamine in the repeating iduronic acid-alpha-1,3-N-acetylgalactosamine disaccharide sequence to form dermatan sulfate (DS).	Dermatan Sulfate	310-312	carbohydrate sulfotransferase 14	Homo sapiens	64-70
20807649-3	2010	ATCS is caused by homozygous nonsense and missense mutations in CHST14 which encodes an N-acetylgalactosamine 4-O-sulfotransferase 1 (D4ST1) that catalyzes the 4-O-sulfation of N-acetylgalactosamine in the repeating iduronic acid-alpha-1,3-N-acetylgalactosamine disaccharide sequence to form dermatan sulfate (DS).	Dermatan Sulfate	310-312	carbohydrate sulfotransferase 8	Homo sapiens	88-132
20807649-3	2010	ATCS is caused by homozygous nonsense and missense mutations in CHST14 which encodes an N-acetylgalactosamine 4-O-sulfotransferase 1 (D4ST1) that catalyzes the 4-O-sulfation of N-acetylgalactosamine in the repeating iduronic acid-alpha-1,3-N-acetylgalactosamine disaccharide sequence to form dermatan sulfate (DS).	Dermatan Sulfate	310-312	carbohydrate sulfotransferase 14	Homo sapiens	134-139
20807652-3	2010	Endothelial injury allows circulating HCII to enter the vessel wall, where it binds to DS and presumably becomes activated.	Dermatan Sulfate	87-89	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	38-42
20807652-7	2010	These observations suggest that a major function of the HCII-DS system is to regulate the physiologic response to arterial injury.	Dermatan Sulfate	61-63	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	56-60
20004762-3	2009	The CHST14 gene encodes N-acetylgalactosamine 4-O-sulfotransferase 1 (D4ST1), which catalyzes 4-O sulfation of N-acetylgalactosamine in the repeating iduronic acid-alpha1,3-N-acetylgalactosamine disaccharide sequence to form dermatan sulfate.	Dermatan Sulfate	225-241	carbohydrate sulfotransferase 14	Homo sapiens	4-10
19682969-1	2009	A functional bioassay has been developed for measuring the intracellular activity of recombinant human arylsulfatase B (rhASB) on its natural glycosaminoglycan (GAG) substrates, dermatan sulfate (DS), and chondroitin sulfate (CS) when the enzyme is taken up into cultured ASB-deficient human fibroblasts (GM00519).	Dermatan Sulfate	196-198	arylsulfatase B	Homo sapiens	103-118
19682969-1	2009	A functional bioassay has been developed for measuring the intracellular activity of recombinant human arylsulfatase B (rhASB) on its natural glycosaminoglycan (GAG) substrates, dermatan sulfate (DS), and chondroitin sulfate (CS) when the enzyme is taken up into cultured ASB-deficient human fibroblasts (GM00519).	Dermatan Sulfate	196-198	arylsulfatase B	Homo sapiens	122-125
19682969-3	2009	ASB-deficient cells accumulate DS and CS, which may be partially hydrolyzed by other lysosomal hydrolases, with the reactions stopping if a GalNAc-4S residue is reached on the nonreducing end of the oligosaccharide.	Dermatan Sulfate	31-33	arylsulfatase B	Homo sapiens	0-3
19682969-7	2009	The assay measures depletion of DS/CS independently of their molecular size or processing state; in this approach, all DS- and CS-like substances accumulating in the absence of ASB activity are considered to be natural substrates of the enzyme.	Dermatan Sulfate	32-34	arylsulfatase B	Homo sapiens	177-180
19682969-1	2009	A functional bioassay has been developed for measuring the intracellular activity of recombinant human arylsulfatase B (rhASB) on its natural glycosaminoglycan (GAG) substrates, dermatan sulfate (DS), and chondroitin sulfate (CS) when the enzyme is taken up into cultured ASB-deficient human fibroblasts (GM00519).	Dermatan Sulfate	178-194	arylsulfatase B	Homo sapiens	103-118
19682969-1	2009	A functional bioassay has been developed for measuring the intracellular activity of recombinant human arylsulfatase B (rhASB) on its natural glycosaminoglycan (GAG) substrates, dermatan sulfate (DS), and chondroitin sulfate (CS) when the enzyme is taken up into cultured ASB-deficient human fibroblasts (GM00519).	Dermatan Sulfate	178-194	arylsulfatase B	Homo sapiens	122-125
20004762-3	2009	The CHST14 gene encodes N-acetylgalactosamine 4-O-sulfotransferase 1 (D4ST1), which catalyzes 4-O sulfation of N-acetylgalactosamine in the repeating iduronic acid-alpha1,3-N-acetylgalactosamine disaccharide sequence to form dermatan sulfate.	Dermatan Sulfate	225-241	carbohydrate sulfotransferase 8	Homo sapiens	24-68
20004762-3	2009	The CHST14 gene encodes N-acetylgalactosamine 4-O-sulfotransferase 1 (D4ST1), which catalyzes 4-O sulfation of N-acetylgalactosamine in the repeating iduronic acid-alpha1,3-N-acetylgalactosamine disaccharide sequence to form dermatan sulfate.	Dermatan Sulfate	225-241	carbohydrate sulfotransferase 14	Homo sapiens	70-75
20004762-4	2009	Mass spectrometry of glycosaminoglycans from a patient"s fibroblasts revealed absence of dermatan sulfate and excess of chondroitin sulfate, showing that 4-O sulfation by CHST14 is essential for dermatan sulfate formation in vivo.	Dermatan Sulfate	195-211	carbohydrate sulfotransferase 14	Homo sapiens	171-177
19631712-10	2009	In fibrosis affected palmar fascia DS/CS proteoglycans are able to form with PDGF-BB supramolecular complexes also including other matrix components such as type III collagen and fibronectin which bind the growth factor covalently.	Dermatan Sulfate	35-37	fibronectin 1	Homo sapiens	179-190
19337786-6	2009	Decorin, a member of the small leucine-rich proteoglycan gene family, is composed of a core protein and a dermatan/chondroitin sulfate chain.	Dermatan Sulfate	106-114	decorin	Mus musculus	0-7
19602578-1	2009	Iduronate-2-sulfatase (IDS) is a lysosomal enzyme expressed in pancreatic islets responsible for the degradation of proteoglycans such as perlecan and dermatan sulfate.	Dermatan Sulfate	151-167	iduronate 2-sulfatase	Homo sapiens	0-21
19834056-5	2009	As excess heparan and dermatan sulfates inhibit type II collagen degradation by cathepsin K and the spatial overlap between cathepsin K and heparan sulfate strongly increased in MPS I mice, the build up of subepiphyseal cartilage is speculated to be a direct consequence of cathepsin K inhibition by MPS I-associated GAGs.	Dermatan Sulfate	22-39	cathepsin K	Mus musculus	80-91
19661164-4	2009	In this study, dermatan sulfate structure was evaluated after downregulating or increasing dermatan 4-O-sulfotransferase 1 (D4ST-1) expression.	Dermatan Sulfate	15-31	carbohydrate sulfotransferase 14	Homo sapiens	124-130
19661164-7	2009	Analysis of the dermatan sulfate chains showed that D4ST-1 is essential for the biosynthesis of the disulfated structure iduronic acid-2-O-sulfate-N-acetylgalactosamine-4-O-sulfate, thus confirmed to be strictly connected with the iduronic acid blocks.	Dermatan Sulfate	16-32	carbohydrate sulfotransferase 14	Homo sapiens	52-58
19661164-9	2009	In conclusion, D4ST-1 is a key enzyme and is indispensable in the formation of important functional domains in dermatan sulfate and cannot be compensated by other 4-O-sulfotransferases.	Dermatan Sulfate	111-127	carbohydrate sulfotransferase 14	Homo sapiens	15-21
19516009-13	2009	Increased expression of chondroitin sulfate in retina and dermatan sulfate in choroid reflects the effects of injury and fibrosis using high doses of anti-TNF-alpha.	Dermatan Sulfate	58-74	tumor necrosis factor	Homo sapiens	155-164
19687302-0	2009	Dermatan sulfate epimerase 1-deficient mice have reduced content and changed distribution of iduronic acids in dermatan sulfate and an altered collagen structure in skin.	Dermatan Sulfate	111-127	dermatan sulfate epimerase	Mus musculus	0-28
19687302-1	2009	Dermatan sulfate epimerase 1 (DS-epi1) and DS-epi2 convert glucuronic acid to iduronic acid in chondroitin/dermatan sulfate biosynthesis.	Dermatan Sulfate	107-123	dermatan sulfate epimerase	Mus musculus	0-28
19687302-1	2009	Dermatan sulfate epimerase 1 (DS-epi1) and DS-epi2 convert glucuronic acid to iduronic acid in chondroitin/dermatan sulfate biosynthesis.	Dermatan Sulfate	107-123	dermatan sulfate epimerase	Mus musculus	30-37
19687302-1	2009	Dermatan sulfate epimerase 1 (DS-epi1) and DS-epi2 convert glucuronic acid to iduronic acid in chondroitin/dermatan sulfate biosynthesis.	Dermatan Sulfate	107-123	dermatan sulfate epimerase-like	Mus musculus	43-50
19687302-3	2009	The numbers of long blocks of adjacent iduronic acids are greatly decreased in skin decorin and biglycan chondroitin/dermatan sulfate, along with a parallel decrease in iduronic-2-O-sulfated-galactosamine-4-O-sulfated structures.	Dermatan Sulfate	117-133	biglycan	Mus musculus	96-104
19687302-6	2009	The lack of DS-epi1 affects the chondroitin/dermatan sulfate in many proteoglycans, and the consequences for skin collagen structure were initially analyzed.	Dermatan Sulfate	44-60	dermatan sulfate epimerase	Mus musculus	12-19
19687302-8	2009	The altered chondroitin/dermatan sulfate chains carried by decorin in skin are likely to affect collagen fibril formation and reduce the tensile strength of DS-epi1-null skin.	Dermatan Sulfate	24-40	dermatan sulfate epimerase	Mus musculus	157-164
19602578-1	2009	Iduronate-2-sulfatase (IDS) is a lysosomal enzyme expressed in pancreatic islets responsible for the degradation of proteoglycans such as perlecan and dermatan sulfate.	Dermatan Sulfate	151-167	iduronate 2-sulfatase	Homo sapiens	23-26
19542224-4	2009	New partners of endostatin include glycosaminoglycans (chondroitin and dermatan sulfate), matricellular proteins (thrombospondin-1 and SPARC), collagens (I, IV, and VI), the amyloid peptide Abeta-(1-42), and transglutaminase-2.	Dermatan Sulfate	71-87	collagen type XVIII alpha 1 chain	Homo sapiens	16-26
19088176-6	2009	CD16(-) NK cells bound maximally to dermatan sulfate (DS), which was diminished by enzymatic pretreatment with dermatanase and chondroitinase ABC, but not with chondroitinase ACII.	Dermatan Sulfate	36-52	Fc gamma receptor IIIa	Homo sapiens	0-4
19019854-7	2009	The CCD, like the full-length ANGPTL4, binds to heparan and dermatan sulfates in surface plasmon resonance assays and inhibits endothelial cell adhesion, motility, and tubule-like formation.	Dermatan Sulfate	60-77	angiopoietin like 4	Homo sapiens	30-37
19088176-6	2009	CD16(-) NK cells bound maximally to dermatan sulfate (DS), which was diminished by enzymatic pretreatment with dermatanase and chondroitinase ABC, but not with chondroitinase ACII.	Dermatan Sulfate	54-56	Fc gamma receptor IIIa	Homo sapiens	0-4
18971786-2	2008	BACKGROUND: HCII inhibits thrombin activity by binding to dermatan sulfate and has been shown to be a novel and independent risk factor for atherosclerosis.	Dermatan Sulfate	58-74	serpin family D member 1	Homo sapiens	12-16
19004834-7	2009	The presence of chondroitin and dermatan sulfate on CD44 standard and variant isoforms facilitates fibrin recognition.	Dermatan Sulfate	32-48	CD44 molecule (Indian blood group)	Homo sapiens	52-56
19152659-0	2009	FGF-10 and specific structural elements of dermatan sulfate size and sulfation promote maximal keratinocyte migration and cellular proliferation.	Dermatan Sulfate	43-59	fibroblast growth factor 10	Homo sapiens	0-6
19152659-5	2009	Structural variants of DS between 10 and 20 disaccharides containing iduronic acid showed maximal capacity to enable FGF-10 receptor stimulation.	Dermatan Sulfate	23-25	fibroblast growth factor 10	Homo sapiens	117-123
18971786-2	2008	BACKGROUND: HCII inhibits thrombin activity by binding to dermatan sulfate and has been shown to be a novel and independent risk factor for atherosclerosis.	Dermatan Sulfate	58-74	coagulation factor II, thrombin	Homo sapiens	26-34
19707363-1	2008	Mucopolysaccharidosis type II (MPS II, Hunter syndrome) is a heterogeneous, progressive X-linked recessively inherited lysosomal storage disease that is caused by a deficiency of the enzyme iduronate-2-sulfatase, resulting in abnormal tissue accumulation of the glycosaminoglycans, dermatan sulfate and heparan sulfate.	Dermatan Sulfate	282-298	iduronate 2-sulfatase	Homo sapiens	190-211
18406185-1	2008	Mucopolysaccharidosis VI (MPS VI; Maroteaux-Lamy syndrome) is an autosomal recessive lysosomal disorder caused by deficiency of N-acetylgalactosamine-4-sulfatase (ARSB), which is required for the degradation of dermatan sulfate.	Dermatan Sulfate	211-227	arylsulfatase B	Homo sapiens	128-161
18406185-1	2008	Mucopolysaccharidosis VI (MPS VI; Maroteaux-Lamy syndrome) is an autosomal recessive lysosomal disorder caused by deficiency of N-acetylgalactosamine-4-sulfatase (ARSB), which is required for the degradation of dermatan sulfate.	Dermatan Sulfate	211-227	arylsulfatase B	Homo sapiens	163-167
18413232-0	2008	Plasma kallikrein is activated on dermatan sulfate and cleaves factor H.	Dermatan Sulfate	34-50	kallikrein B1	Homo sapiens	0-17
18413232-1	2008	When human plasma is applied to a dermatan sulfate column, amidase activity is detected in the bound fraction and complement factor H is cleaved [A. Saito, H. Munakata, Factor H is a dermatan sulfate-binding protein: identification of a dermatan sulfate-mediated protease that cleaves factor H, J. Biochem.	Dermatan Sulfate	34-50	complement factor H	Homo sapiens	125-133
18413232-1	2008	When human plasma is applied to a dermatan sulfate column, amidase activity is detected in the bound fraction and complement factor H is cleaved [A. Saito, H. Munakata, Factor H is a dermatan sulfate-binding protein: identification of a dermatan sulfate-mediated protease that cleaves factor H, J. Biochem.	Dermatan Sulfate	34-50	complement factor H	Homo sapiens	169-177
18413232-1	2008	When human plasma is applied to a dermatan sulfate column, amidase activity is detected in the bound fraction and complement factor H is cleaved [A. Saito, H. Munakata, Factor H is a dermatan sulfate-binding protein: identification of a dermatan sulfate-mediated protease that cleaves factor H, J. Biochem.	Dermatan Sulfate	183-199	complement factor H	Homo sapiens	125-133
18413232-1	2008	When human plasma is applied to a dermatan sulfate column, amidase activity is detected in the bound fraction and complement factor H is cleaved [A. Saito, H. Munakata, Factor H is a dermatan sulfate-binding protein: identification of a dermatan sulfate-mediated protease that cleaves factor H, J. Biochem.	Dermatan Sulfate	183-199	complement factor H	Homo sapiens	169-177
18413232-1	2008	When human plasma is applied to a dermatan sulfate column, amidase activity is detected in the bound fraction and complement factor H is cleaved [A. Saito, H. Munakata, Factor H is a dermatan sulfate-binding protein: identification of a dermatan sulfate-mediated protease that cleaves factor H, J. Biochem.	Dermatan Sulfate	183-199	complement factor H	Homo sapiens	125-133
18413232-1	2008	When human plasma is applied to a dermatan sulfate column, amidase activity is detected in the bound fraction and complement factor H is cleaved [A. Saito, H. Munakata, Factor H is a dermatan sulfate-binding protein: identification of a dermatan sulfate-mediated protease that cleaves factor H, J. Biochem.	Dermatan Sulfate	183-199	complement factor H	Homo sapiens	169-177
18486607-2	2008	The deficiency of ARSB leads to an accumulation of dermatan sulfate (DS) in lysosomes and gross excretion in the urine.	Dermatan Sulfate	51-67	arylsulfatase B	Homo sapiens	18-22
18486607-2	2008	The deficiency of ARSB leads to an accumulation of dermatan sulfate (DS) in lysosomes and gross excretion in the urine.	Dermatan Sulfate	69-71	arylsulfatase B	Homo sapiens	18-22
18499864-0	2008	The ligand-binding profile of HARE: hyaluronan and chondroitin sulfates A, C, and D bind to overlapping sites distinct from the sites for heparin, acetylated low-density lipoprotein, dermatan sulfate, and CS-E.	Dermatan Sulfate	183-199	stabilin 2	Homo sapiens	30-34
18499864-1	2008	The hyaluronic acid receptor for endocytosis (HARE)/ Stabilin-2 is the primary systemic scavenger receptor for hyaluronan (HA), the chondroitin sulfates (CS), dermatan sulfate (DS), and nonglycosaminoglycan (GAG) ligands such as acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides, and advanced glycation end products.	Dermatan Sulfate	159-175	stabilin 2	Homo sapiens	46-50
18499864-1	2008	The hyaluronic acid receptor for endocytosis (HARE)/ Stabilin-2 is the primary systemic scavenger receptor for hyaluronan (HA), the chondroitin sulfates (CS), dermatan sulfate (DS), and nonglycosaminoglycan (GAG) ligands such as acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides, and advanced glycation end products.	Dermatan Sulfate	159-175	stabilin 2	Homo sapiens	53-63
18499864-1	2008	The hyaluronic acid receptor for endocytosis (HARE)/ Stabilin-2 is the primary systemic scavenger receptor for hyaluronan (HA), the chondroitin sulfates (CS), dermatan sulfate (DS), and nonglycosaminoglycan (GAG) ligands such as acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides, and advanced glycation end products.	Dermatan Sulfate	177-179	stabilin 2	Homo sapiens	46-50
18499864-1	2008	The hyaluronic acid receptor for endocytosis (HARE)/ Stabilin-2 is the primary systemic scavenger receptor for hyaluronan (HA), the chondroitin sulfates (CS), dermatan sulfate (DS), and nonglycosaminoglycan (GAG) ligands such as acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides, and advanced glycation end products.	Dermatan Sulfate	177-179	stabilin 2	Homo sapiens	53-63
18499864-9	2008	For example, Hep binding to HARE was competed by DS, CS-E, AcLDL, and dextran sulfate, but not by other CS types, HA, dextran, or heparosan.	Dermatan Sulfate	49-51	stabilin 2	Homo sapiens	28-32
18281504-0	2008	Vascular dermatan sulfate regulates the antithrombotic activity of heparin cofactor II.	Dermatan Sulfate	9-25	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	67-86
18281504-2	2008	Dermatan sulfate (DS) and heparan sulfate (HS) increase the rate of inhibition of thrombin by HCII in vitro, but it is unknown whether vascular glycosaminoglycans play a role in the antithrombotic effect of HCII in vivo.	Dermatan Sulfate	0-16	coagulation factor II	Mus musculus	82-90
18281504-2	2008	Dermatan sulfate (DS) and heparan sulfate (HS) increase the rate of inhibition of thrombin by HCII in vitro, but it is unknown whether vascular glycosaminoglycans play a role in the antithrombotic effect of HCII in vivo.	Dermatan Sulfate	0-16	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	94-98
18281504-2	2008	Dermatan sulfate (DS) and heparan sulfate (HS) increase the rate of inhibition of thrombin by HCII in vitro, but it is unknown whether vascular glycosaminoglycans play a role in the antithrombotic effect of HCII in vivo.	Dermatan Sulfate	0-16	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	207-211
18281504-2	2008	Dermatan sulfate (DS) and heparan sulfate (HS) increase the rate of inhibition of thrombin by HCII in vitro, but it is unknown whether vascular glycosaminoglycans play a role in the antithrombotic effect of HCII in vivo.	Dermatan Sulfate	18-20	coagulation factor II	Mus musculus	82-90
18281504-2	2008	Dermatan sulfate (DS) and heparan sulfate (HS) increase the rate of inhibition of thrombin by HCII in vitro, but it is unknown whether vascular glycosaminoglycans play a role in the antithrombotic effect of HCII in vivo.	Dermatan Sulfate	18-20	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	94-98
18281504-4	2008	When HCII was incubated with frozen sections of the mouse carotid artery, it bound specifically to DS in the adventitia.	Dermatan Sulfate	99-101	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	5-9
18281504-6	2008	These results support the hypothesis that HCII interacts with DS in the vessel wall after disruption of the endothelium and that this interaction regulates thrombus formation in vivo.	Dermatan Sulfate	62-64	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	42-46
17672828-1	2008	MPS VI (mucopolysaccharidosis type VI) is a lysosomal storage disease in which deficient activity of the enzyme N-acetylgalactosamine 4-sulfatase [ASB (arylsulfatase B)] impairs the stepwise degradation of the GAG (glycosaminoglycan) dermatan sulfate.	Dermatan Sulfate	234-250	arylsulfatase B	Homo sapiens	112-145
17672828-1	2008	MPS VI (mucopolysaccharidosis type VI) is a lysosomal storage disease in which deficient activity of the enzyme N-acetylgalactosamine 4-sulfatase [ASB (arylsulfatase B)] impairs the stepwise degradation of the GAG (glycosaminoglycan) dermatan sulfate.	Dermatan Sulfate	234-250	arylsulfatase B	Homo sapiens	147-150
17672828-1	2008	MPS VI (mucopolysaccharidosis type VI) is a lysosomal storage disease in which deficient activity of the enzyme N-acetylgalactosamine 4-sulfatase [ASB (arylsulfatase B)] impairs the stepwise degradation of the GAG (glycosaminoglycan) dermatan sulfate.	Dermatan Sulfate	234-250	arylsulfatase B	Homo sapiens	152-167
17955027-1	2008	Mucopolysaccharidosis VI (MPS VI) is caused by deficient activity of arylsulfatase B (ARSB), resulting in intralysosomal storage of dermatan sulfate (DS) and multisystem disease without central nervous system involvement.	Dermatan Sulfate	132-148	arylsulfatase B	Rattus norvegicus	69-84
18156656-1	2008	Dermatan sulfate is a glycosaminoglycan that selectively inhibits the action of thrombin through interaction with heparin cofactor II.	Dermatan Sulfate	0-16	coagulation factor II, thrombin	Bos taurus	80-88
18156656-1	2008	Dermatan sulfate is a glycosaminoglycan that selectively inhibits the action of thrombin through interaction with heparin cofactor II.	Dermatan Sulfate	0-16	serpin family D member 1	Bos taurus	114-133
18156656-4	2008	Previous studies have showed that dermatan sulfate derived from porcine/bovine intestinal mucosa/skin or marine invertebrates is capable of stimulating heparin cofactor II-mediated thrombin inhibition in vitro.	Dermatan Sulfate	34-50	serpin family D member 1	Bos taurus	152-171
18156656-4	2008	Previous studies have showed that dermatan sulfate derived from porcine/bovine intestinal mucosa/skin or marine invertebrates is capable of stimulating heparin cofactor II-mediated thrombin inhibition in vitro.	Dermatan Sulfate	34-50	coagulation factor II, thrombin	Bos taurus	181-189
18156656-7	2008	Heparin cofactor II/dermatan sulfate-mediated thrombin inhibition measured in vitro revealed activity comparable to or higher than the commercial standard with 2-fold differences observed between some tissues.	Dermatan Sulfate	20-36	serpin family D member 1	Bos taurus	0-19
18156656-7	2008	Heparin cofactor II/dermatan sulfate-mediated thrombin inhibition measured in vitro revealed activity comparable to or higher than the commercial standard with 2-fold differences observed between some tissues.	Dermatan Sulfate	20-36	coagulation factor II, thrombin	Bos taurus	46-54
17706452-5	2008	Heparin capably restored their growth, and unexpectedly exogenous chondroitin sulfate to WM9 and both chondroitin sulfate and dermatan sulfate to M5 cells allowed FGF-2 mitogenic stimulation.	Dermatan Sulfate	126-142	fibroblast growth factor 2	Homo sapiens	163-168
17706452-6	2008	Furthermore, in WM9 cells the degradation of membrane-bound chondroitin/dermatan sulfate stimulates basal growth and even enhances FGF-2 stimulation.	Dermatan Sulfate	72-88	fibroblast growth factor 2	Homo sapiens	131-136
17706452-8	2008	Both the amounts of chondroitin/dermatan/heparan sulfate and their sulfation levels differed between the cell lines and were distinctly modulated by FGF-2.	Dermatan Sulfate	32-40	fibroblast growth factor 2	Homo sapiens	149-154
17706452-9	2008	In this study, we show that chondroitin/dermatan sulfate-containing proteoglycans, likely in cooperation with heparan sulfate, participate in metastatic melanoma cell FGF-2-induced mitogenic response, which represents a novel finding and establishes the central role of sulfated glycosaminoglycans on melanoma growth.	Dermatan Sulfate	40-56	fibroblast growth factor 2	Homo sapiens	167-172
18446715-2	2008	Unlike unfractionated heparin (UFH), DS selectively inhibits thrombin, does not inhibit factor Xa, is effective on both free and fibrin-bound thrombin and does not interfere with platelets.	Dermatan Sulfate	37-39	coagulation factor II, thrombin	Homo sapiens	61-69
18446715-2	2008	Unlike unfractionated heparin (UFH), DS selectively inhibits thrombin, does not inhibit factor Xa, is effective on both free and fibrin-bound thrombin and does not interfere with platelets.	Dermatan Sulfate	37-39	coagulation factor II, thrombin	Homo sapiens	142-150
17955027-1	2008	Mucopolysaccharidosis VI (MPS VI) is caused by deficient activity of arylsulfatase B (ARSB), resulting in intralysosomal storage of dermatan sulfate (DS) and multisystem disease without central nervous system involvement.	Dermatan Sulfate	132-148	arylsulfatase B	Rattus norvegicus	86-90
17955027-1	2008	Mucopolysaccharidosis VI (MPS VI) is caused by deficient activity of arylsulfatase B (ARSB), resulting in intralysosomal storage of dermatan sulfate (DS) and multisystem disease without central nervous system involvement.	Dermatan Sulfate	150-152	arylsulfatase B	Rattus norvegicus	69-84
17955027-1	2008	Mucopolysaccharidosis VI (MPS VI) is caused by deficient activity of arylsulfatase B (ARSB), resulting in intralysosomal storage of dermatan sulfate (DS) and multisystem disease without central nervous system involvement.	Dermatan Sulfate	150-152	arylsulfatase B	Rattus norvegicus	86-90
17876721-2	2007	I2S catalyses a step in the catabolism of glycosaminoglycans (GAGs) dermatan sulfate and heparan sulfate, and when it is deficient or absent GAGs accumulate in tissues and organs.	Dermatan Sulfate	68-84	iduronate 2-sulfatase	Homo sapiens	0-3
17936880-1	2008	INTRODUCTION: Dermatan sulfate, a sulfated glycosaminoglycan, acts as an anticoagulant by accelerating the inhibition of thrombin by heparin cofactor II.	Dermatan Sulfate	14-30	coagulation factor II	Rattus norvegicus	121-129
17936880-1	2008	INTRODUCTION: Dermatan sulfate, a sulfated glycosaminoglycan, acts as an anticoagulant by accelerating the inhibition of thrombin by heparin cofactor II.	Dermatan Sulfate	14-30	serpin family D member 1	Rattus norvegicus	133-152
17936880-4	2008	RESULTS: After a single intravenous administration of low molecular dermatan sulfate in rats, fibrinolytic activity increased simultaneously with thrombin clotting time prolongation.	Dermatan Sulfate	68-84	coagulation factor II	Rattus norvegicus	146-154
17616540-1	2007	Hunter syndrome (or Mucopolysaccharidosis type II, MPS II) is an X-linked recessive disorder due to the deficiency of the iduronate-2-sulfatase (IDS) enzyme, resulting in the accumulation of heparan and dermatan sulfates in the lysosomes.	Dermatan Sulfate	203-220	iduronate 2-sulfatase	Homo sapiens	122-143
17616540-1	2007	Hunter syndrome (or Mucopolysaccharidosis type II, MPS II) is an X-linked recessive disorder due to the deficiency of the iduronate-2-sulfatase (IDS) enzyme, resulting in the accumulation of heparan and dermatan sulfates in the lysosomes.	Dermatan Sulfate	203-220	iduronate 2-sulfatase	Homo sapiens	145-148
18174963-1	2007	Hunter syndrome (mucopolysaccharidosis II, MPS II) is a rare X-linked lysosomal storage disorder caused by the deficiency of enzyme iduronate-2-sulfatase (I2S), which results in accumulation of undegraded dermatan and heparan sulfate in various tissues and organs.	Dermatan Sulfate	205-213	iduronate 2-sulfatase	Homo sapiens	132-153
18174963-1	2007	Hunter syndrome (mucopolysaccharidosis II, MPS II) is a rare X-linked lysosomal storage disorder caused by the deficiency of enzyme iduronate-2-sulfatase (I2S), which results in accumulation of undegraded dermatan and heparan sulfate in various tissues and organs.	Dermatan Sulfate	205-213	iduronate 2-sulfatase	Homo sapiens	155-158
17878401-1	2007	Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin when bound to dermatan sulfate or heparin.	Dermatan Sulfate	84-100	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	0-19
17878401-1	2007	Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin when bound to dermatan sulfate or heparin.	Dermatan Sulfate	84-100	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	21-25
17878401-1	2007	Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin when bound to dermatan sulfate or heparin.	Dermatan Sulfate	84-100	coagulation factor II	Mus musculus	61-69
17239341-2	2007	In the present study, DS demonstrated a high level of binding activity to receptor activator of NF-kappaB ligand (RANKL) and obstructed the binding of RANK to RANKL, determined using a quartz-crystal microbalance (QCM) technique.	Dermatan Sulfate	22-24	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	114-119
17928217-3	2007	Hybrid chondroitin/dermatan sulfate chains are also involved in formation of the neural network by capturing and presenting heparin-binding growth factors like basic fibroblast growth factor, pleiotrophin, and hepatocyte growth factor to stem cells or neuronal cells.	Dermatan Sulfate	19-35	pleiotrophin	Homo sapiens	192-204
17928217-3	2007	Hybrid chondroitin/dermatan sulfate chains are also involved in formation of the neural network by capturing and presenting heparin-binding growth factors like basic fibroblast growth factor, pleiotrophin, and hepatocyte growth factor to stem cells or neuronal cells.	Dermatan Sulfate	19-35	hepatocyte growth factor	Homo sapiens	210-234
17500059-4	2007	Evaluation of the specificity of GD3G7 toward various glycosaminoglycan preparations showed that this antibody specifically reacted with squid CS-E (rich in the GlcUAbeta1-3GalNAc(4,6-O-sulfate) disaccharide unit E), hagfish CS-H (rich in the IdoUAalpha1-3GalNAc(4,6-O-sulfate) unit iE), and shark skin DS (rich in both E and iE units).	Dermatan Sulfate	303-305	cystathionase (cystathionine gamma-lyase)	Mus musculus	143-147
17324393-4	2007	Since the enzyme arylsulfatase B (ASB) catalyzes hydrolysis of the sulfate ester of N-acetylgalactosamine 4-sulfate, a component of dermatan sulfate and chondroitin A sulfate, determination of ASB activity in human airway epithelial cells, corrected and uncorrected for CFTR, was undertaken.	Dermatan Sulfate	132-148	arylsulfatase B	Homo sapiens	17-32
17324393-4	2007	Since the enzyme arylsulfatase B (ASB) catalyzes hydrolysis of the sulfate ester of N-acetylgalactosamine 4-sulfate, a component of dermatan sulfate and chondroitin A sulfate, determination of ASB activity in human airway epithelial cells, corrected and uncorrected for CFTR, was undertaken.	Dermatan Sulfate	132-148	arylsulfatase B	Homo sapiens	34-37
17324393-4	2007	Since the enzyme arylsulfatase B (ASB) catalyzes hydrolysis of the sulfate ester of N-acetylgalactosamine 4-sulfate, a component of dermatan sulfate and chondroitin A sulfate, determination of ASB activity in human airway epithelial cells, corrected and uncorrected for CFTR, was undertaken.	Dermatan Sulfate	132-148	arylsulfatase B	Homo sapiens	193-196
17324393-4	2007	Since the enzyme arylsulfatase B (ASB) catalyzes hydrolysis of the sulfate ester of N-acetylgalactosamine 4-sulfate, a component of dermatan sulfate and chondroitin A sulfate, determination of ASB activity in human airway epithelial cells, corrected and uncorrected for CFTR, was undertaken.	Dermatan Sulfate	132-148	CF transmembrane conductance regulator	Homo sapiens	270-274
17239341-0	2007	Dermatan sulfate inhibits osteoclast formation by binding to receptor activator of NF-kappa B ligand.	Dermatan Sulfate	0-16	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	61-100
17239341-2	2007	In the present study, DS demonstrated a high level of binding activity to receptor activator of NF-kappaB ligand (RANKL) and obstructed the binding of RANK to RANKL, determined using a quartz-crystal microbalance (QCM) technique.	Dermatan Sulfate	22-24	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	74-112
17474085-9	2007	We also showed for the first time that AS-A had a specific affinity for chondroitin sulfate B, a component of cumulus matrix proteoglycan networks; this might provide a mechanism of cumulus matrix destabilization induced by sperm surface AS-A.	Dermatan Sulfate	72-93	arylsulfatase A	Mus musculus	39-43
17474085-9	2007	We also showed for the first time that AS-A had a specific affinity for chondroitin sulfate B, a component of cumulus matrix proteoglycan networks; this might provide a mechanism of cumulus matrix destabilization induced by sperm surface AS-A.	Dermatan Sulfate	72-93	arylsulfatase A	Mus musculus	238-242
17459751-1	2007	Mucopolysaccharidosis II (MPS II; Hunter syndrome) is an X-linked metabolic disorder caused by a deficiency of the lysosomal enzyme iduronate-2-sulfatase (I2S), which catalyzes the catabolism of glycosaminoglycans (GAG) by cleaving the O-linked sulfate from dermatan sulfate and heparan sulfate.	Dermatan Sulfate	258-274	iduronate 2-sulfatase	Mus musculus	132-153
17459751-1	2007	Mucopolysaccharidosis II (MPS II; Hunter syndrome) is an X-linked metabolic disorder caused by a deficiency of the lysosomal enzyme iduronate-2-sulfatase (I2S), which catalyzes the catabolism of glycosaminoglycans (GAG) by cleaving the O-linked sulfate from dermatan sulfate and heparan sulfate.	Dermatan Sulfate	258-274	iduronate 2-sulfatase	Mus musculus	155-158
17239341-2	2007	In the present study, DS demonstrated a high level of binding activity to receptor activator of NF-kappaB ligand (RANKL) and obstructed the binding of RANK to RANKL, determined using a quartz-crystal microbalance (QCM) technique.	Dermatan Sulfate	22-24	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	159-164
17239341-4	2007	In addition, immunoblot analyses revealed that DS reduced the levels of phosphorylation of p38 mitogen-activated protein kinase and extracellular signal-regulated kinase protein in mouse osteoclast progenitor cells stimulated with RANKL.	Dermatan Sulfate	47-49	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	231-236
17239341-5	2007	Together, these results indicate that DS regulates osteoclast formation through binding to RANKL and inhibition of signal transduction in osteoclast progenitor cells, suggesting that it has an important role in bone metabolism in pathological conditions.	Dermatan Sulfate	38-40	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	91-96
16650906-1	2007	BACKGROUND: Heparin cofactor II (HCII) could inactivate thrombin after binding to dermatan sulfate at injured arterial walls, and has been shown to be a novel and independent antiatherosclerotic factor.	Dermatan Sulfate	82-98	serpin family D member 1	Homo sapiens	12-31
17194895-1	2007	Heparin cofactor II (HCII) has several biochemical properties that distinguish it from other serpins: (1) it specifically inhibits thrombin; (2) the mechanism of inhibition involves binding of an acidic domain in HCII to thrombin exosite I; and (3) the rate of inhibition increases dramatically in the presence of dermatan sulfate molecules having specific structures.	Dermatan Sulfate	314-330	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	0-19
17194895-1	2007	Heparin cofactor II (HCII) has several biochemical properties that distinguish it from other serpins: (1) it specifically inhibits thrombin; (2) the mechanism of inhibition involves binding of an acidic domain in HCII to thrombin exosite I; and (3) the rate of inhibition increases dramatically in the presence of dermatan sulfate molecules having specific structures.	Dermatan Sulfate	314-330	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	21-25
17194895-1	2007	Heparin cofactor II (HCII) has several biochemical properties that distinguish it from other serpins: (1) it specifically inhibits thrombin; (2) the mechanism of inhibition involves binding of an acidic domain in HCII to thrombin exosite I; and (3) the rate of inhibition increases dramatically in the presence of dermatan sulfate molecules having specific structures.	Dermatan Sulfate	314-330	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	213-217
17194895-1	2007	Heparin cofactor II (HCII) has several biochemical properties that distinguish it from other serpins: (1) it specifically inhibits thrombin; (2) the mechanism of inhibition involves binding of an acidic domain in HCII to thrombin exosite I; and (3) the rate of inhibition increases dramatically in the presence of dermatan sulfate molecules having specific structures.	Dermatan Sulfate	314-330	coagulation factor II	Mus musculus	221-229
17194895-3	2007	Studies with HCII knockout mice directly support the hypothesis that HCII interacts with dermatan sulfate in the arterial wall after endothelial injury and thereby exerts an antithrombotic effect.	Dermatan Sulfate	89-105	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	13-17
17194895-3	2007	Studies with HCII knockout mice directly support the hypothesis that HCII interacts with dermatan sulfate in the arterial wall after endothelial injury and thereby exerts an antithrombotic effect.	Dermatan Sulfate	89-105	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	69-73
17158902-2	2007	Alternatively spliced forms of CD97 bind integrins alpha5beta1 and alphavbeta3, decay accelerating factor, or dermatan sulfate.	Dermatan Sulfate	110-126	adhesion G protein-coupled receptor E5	Mus musculus	31-35
16650906-1	2007	BACKGROUND: Heparin cofactor II (HCII) could inactivate thrombin after binding to dermatan sulfate at injured arterial walls, and has been shown to be a novel and independent antiatherosclerotic factor.	Dermatan Sulfate	82-98	serpin family D member 1	Homo sapiens	33-37
16650906-1	2007	BACKGROUND: Heparin cofactor II (HCII) could inactivate thrombin after binding to dermatan sulfate at injured arterial walls, and has been shown to be a novel and independent antiatherosclerotic factor.	Dermatan Sulfate	82-98	coagulation factor II, thrombin	Homo sapiens	56-64
16828054-5	2006	GAGs from different structure/origin (heparan sulfate, dermatan sulfate, and chondroitin sulfate) exert similar activity on OPG binding.	Dermatan Sulfate	55-71	TNF receptor superfamily member 11b	Homo sapiens	124-127
17222891-6	2007	In the presence of HCII, DSb, a slightly oversulfated DS, had the highest inhibitory effect, whereas heparin and DSd, the most oversulfated derivative, had lower potencies in this case.	Dermatan Sulfate	25-27	serpin family D member 1	Homo sapiens	19-23
17222891-7	2007	These data suggest that the inhibition of thrombin-induced platelet aggregation by the oversulfated DS derivatives is related to their ability to potentiate thrombin inactivation by AT or HCII.	Dermatan Sulfate	100-102	coagulation factor II, thrombin	Homo sapiens	42-50
17222891-7	2007	These data suggest that the inhibition of thrombin-induced platelet aggregation by the oversulfated DS derivatives is related to their ability to potentiate thrombin inactivation by AT or HCII.	Dermatan Sulfate	100-102	coagulation factor II, thrombin	Homo sapiens	157-165
17222891-7	2007	These data suggest that the inhibition of thrombin-induced platelet aggregation by the oversulfated DS derivatives is related to their ability to potentiate thrombin inactivation by AT or HCII.	Dermatan Sulfate	100-102	serpin family D member 1	Homo sapiens	188-192
17270255-1	2007	INTRODUCTION: Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II to enhance antithrombin action.	Dermatan Sulfate	14-30	serpin family C member 1	Homo sapiens	131-143
17270255-1	2007	INTRODUCTION: Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II to enhance antithrombin action.	Dermatan Sulfate	32-34	serpin family C member 1	Homo sapiens	131-143
17270255-8	2007	The facilitation of the conversion of Glu-plasminogen to plasmin in the presence of DS was confirmed by SDS-PAGE; high molecular weight-DS effect was greater than low molecular weight-DS in accordance with the chromogenic assays.	Dermatan Sulfate	84-86	plasminogen	Homo sapiens	42-49
16690200-6	2006	Tumor-associated glycanated decorin was found to contain significant amounts of dermatan sulfate (DS) sequences.	Dermatan Sulfate	80-96	decorin	Homo sapiens	28-35
16690200-6	2006	Tumor-associated glycanated decorin was found to contain significant amounts of dermatan sulfate (DS) sequences.	Dermatan Sulfate	98-100	decorin	Homo sapiens	28-35
16961606-10	2006	Additionally, odiparcil-induced heparin cofactor II (HCII)-dependent antithrombin activity was shown to be a function of dermatan sulfate-like GAG production.	Dermatan Sulfate	121-137	serpin family D member 1	Rattus norvegicus	32-51
16961606-10	2006	Additionally, odiparcil-induced heparin cofactor II (HCII)-dependent antithrombin activity was shown to be a function of dermatan sulfate-like GAG production.	Dermatan Sulfate	121-137	serpin family D member 1	Rattus norvegicus	53-57
16624894-0	2006	N-Acetylgalactosamine 4,6-O-sulfate residues mediate binding and activation of heparin cofactor II by porcine mucosal dermatan sulfate.	Dermatan Sulfate	118-134	serpin family D member 1	Homo sapiens	79-98
16624894-1	2006	Dermatan sulfate (DS) accelerates the inhibition of thrombin by heparin cofactor II (HCII).	Dermatan Sulfate	0-16	coagulation factor II, thrombin	Homo sapiens	52-60
16624894-1	2006	Dermatan sulfate (DS) accelerates the inhibition of thrombin by heparin cofactor II (HCII).	Dermatan Sulfate	0-16	serpin family D member 1	Homo sapiens	64-83
16624894-1	2006	Dermatan sulfate (DS) accelerates the inhibition of thrombin by heparin cofactor II (HCII).	Dermatan Sulfate	0-16	serpin family D member 1	Homo sapiens	85-89
16624894-1	2006	Dermatan sulfate (DS) accelerates the inhibition of thrombin by heparin cofactor II (HCII).	Dermatan Sulfate	18-20	coagulation factor II, thrombin	Homo sapiens	52-60
16624894-1	2006	Dermatan sulfate (DS) accelerates the inhibition of thrombin by heparin cofactor II (HCII).	Dermatan Sulfate	18-20	serpin family D member 1	Homo sapiens	64-83
16624894-1	2006	Dermatan sulfate (DS) accelerates the inhibition of thrombin by heparin cofactor II (HCII).	Dermatan Sulfate	18-20	serpin family D member 1	Homo sapiens	85-89
16624894-3	2006	DS from porcine intestinal mucosa has a much lower content of this disaccharide but activates HCII with potency similar to that of porcine skin DS.	Dermatan Sulfate	0-2	serpin family D member 1	Homo sapiens	94-98
16899604-1	2006	PURPOSE: We evaluated the expression of endocan, a soluble lung- and kidney-selective endothelial cell-specific dermatan sulfate proteoglycan, in non-small cell lung tumors compared with normal lung and studied the significance of high levels of circulating endocan in patients with non-small cell lung cancer.	Dermatan Sulfate	112-128	endothelial cell specific molecule 1	Homo sapiens	40-47
16624894-4	2006	Therefore, we sought to characterize oligosaccharides from porcine mucosal DS that interact with HCII.	Dermatan Sulfate	75-77	serpin family D member 1	Homo sapiens	97-101
16624894-11	2006	These data support the hypothesis that modification of IdoA-->GalNAc4SO3 subunits in the DS polymer by either 2-O-sulfation of IdoA or 6-O-sulfation of GalNAc can generate molecules with HCII-binding sites and anticoagulant activity.	Dermatan Sulfate	92-94	serpin family D member 1	Homo sapiens	190-194
16583246-3	2006	Compound heterozygous mutations in the B4GALT7 gene, resulting in aberrant glycosylation of the dermatan sulfate proteoglycan decorin, had been described in a single patient affected with the progeroid form of EDS.	Dermatan Sulfate	96-112	beta-1,4-galactosyltransferase 7	Homo sapiens	39-46
16583246-8	2006	Glycosaminoglycan chains were of the dermatan/chondroitin sulfate type both in beta4GalT-7(Arg270Cys) and control cells, and epimerization was reduced for decorin and biglycan.	Dermatan Sulfate	37-45	beta-1,4-galactosyltransferase 7	Homo sapiens	79-90
16489125-3	2006	The biological activities of DS have been attributed to its high content of IdoA(alpha1-3)GalNAc4S(beta1-4) disaccharide units.	Dermatan Sulfate	29-31	adrenoceptor alpha 1D	Homo sapiens	81-89
16489125-3	2006	The biological activities of DS have been attributed to its high content of IdoA(alpha1-3)GalNAc4S(beta1-4) disaccharide units.	Dermatan Sulfate	29-31	UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2	Homo sapiens	99-106
16339402-0	2006	Placental dermatan sulfate: isolation, anticoagulant activity, and association with heparin cofactor II.	Dermatan Sulfate	10-26	serpin family D member 1	Homo sapiens	84-103
16505484-0	2006	Biosynthesis of dermatan sulfate: chondroitin-glucuronate C5-epimerase is identical to SART2.	Dermatan Sulfate	16-32	dermatan sulfate epimerase	Homo sapiens	87-92
16505484-11	2006	NCAG1 also contains a putative chondroitin sulfate sulfotransferase domain and thus may be involved in dermatan sulfate biosynthesis.	Dermatan Sulfate	103-119	dermatan sulfate epimerase like	Homo sapiens	0-5
16442510-0	2006	Thrombin inhibition by antithrombin in the presence of oversulfated dermatan sulfates.	Dermatan Sulfate	68-85	coagulation factor II, thrombin	Homo sapiens	0-8
16442510-0	2006	Thrombin inhibition by antithrombin in the presence of oversulfated dermatan sulfates.	Dermatan Sulfate	68-85	serpin family C member 1	Homo sapiens	23-35
16442510-1	2006	DSS1 and DSS2 are two oversulfated dermatan sulfate derivatives with sulfur contents of 7.8% and 11.5%, respectively.	Dermatan Sulfate	35-51	SEM1 26S proteasome subunit	Homo sapiens	0-4
16339402-4	2006	Dermatan sulfate (DS) specifically activates HCII and is abundant in the placenta, but the locations of DS and HCII in the placenta have not been determined.	Dermatan Sulfate	0-16	serpin family D member 1	Homo sapiens	45-49
16339402-4	2006	Dermatan sulfate (DS) specifically activates HCII and is abundant in the placenta, but the locations of DS and HCII in the placenta have not been determined.	Dermatan Sulfate	18-20	serpin family D member 1	Homo sapiens	45-49
16339402-6	2006	DS isolated from human placenta contains disaccharides implicated in activation of HCII and has anticoagulant activity similar to that of mucosal DS.	Dermatan Sulfate	0-2	serpin family D member 1	Homo sapiens	83-87
16339402-8	2006	HCII colocalizes with DS in the walls of fetal blood vessels and is also present in syncytiotrophoblast cells.	Dermatan Sulfate	22-24	serpin family D member 1	Homo sapiens	0-4
16339402-9	2006	Our data suggest that DS is in a position to activate HCII in the fetal blood vessels or in the stroma of placental villi after injury to the syncytiotrophoblast layer and thereby inhibit fibrin generation in the placenta.	Dermatan Sulfate	22-24	serpin family D member 1	Homo sapiens	54-58
16533727-7	2006	In particular, the addition of DS resulted in increases of about 1.3-fold, 1.6-fold and 2.0-fold in the numbers of total cells, megakaryocytes and CFU-Meg, respectively, compared with the control culture stimulated by thrombopoietin alone after 9-12 days of serum-free liquid culture.	Dermatan Sulfate	31-33	protein tyrosine phosphatase non-receptor type 4	Homo sapiens	151-154
16533727-7	2006	In particular, the addition of DS resulted in increases of about 1.3-fold, 1.6-fold and 2.0-fold in the numbers of total cells, megakaryocytes and CFU-Meg, respectively, compared with the control culture stimulated by thrombopoietin alone after 9-12 days of serum-free liquid culture.	Dermatan Sulfate	31-33	thrombopoietin	Homo sapiens	218-232
16168566-1	2006	Endocan, previously called endothelial cell specific molecule-1, is a soluble proteoglycan of 50 kDa, constituted of a mature polypeptide of 165 amino acids and a single dermatan sulphate chain covalently linked to the serine residue at position 137.	Dermatan Sulfate	170-187	endothelial cell specific molecule 1	Homo sapiens	0-7
16674280-7	2006	Keratinocytes stained positive for PCNA (proliferation), K10 (suprabasal differentiation), and K16 (hyperproliferation) markers although cell morphology was poor for organotypical cultures on dermatan- loaded polypyrrole compared with de-epidermalized dermis.	Dermatan Sulfate	192-200	keratin 16	Homo sapiens	95-98
16168566-1	2006	Endocan, previously called endothelial cell specific molecule-1, is a soluble proteoglycan of 50 kDa, constituted of a mature polypeptide of 165 amino acids and a single dermatan sulphate chain covalently linked to the serine residue at position 137.	Dermatan Sulfate	170-187	endothelial cell specific molecule 1	Homo sapiens	27-63
16394262-6	2006	In addition, dermatan sulfate induces ICAM-1 expression on endothelial cells and also recruits leukocytes via selectin interactions.	Dermatan Sulfate	13-29	intercellular adhesion molecule 1	Homo sapiens	38-44
16303928-9	2005	CONCLUSIONS: Opticin binds to heparin, HS, chondroitin 4-sulfate, and dermatan sulfate, the binding affinity being dependent on sulfation pattern and oligosaccharide chain length.	Dermatan Sulfate	70-86	opticin	Homo sapiens	13-20
16283671-3	2005	MPS type I (MPS I) is caused by low or undetectable activity of alpha-L-iduronidase, an enzyme involved in removing the terminal iduronic acid residues from heparan and dermatan sulfate.	Dermatan Sulfate	169-185	alpha-L-iduronidase	Homo sapiens	64-83
15854029-3	2005	Integrins alpha4beta1, alpha5beta1, and alphavbeta3 and dermatan sulfate CD44 were required for this invasive migration.	Dermatan Sulfate	56-72	CD44 molecule (Indian blood group)	Homo sapiens	73-77
16120610-0	2005	Demonstration of the pleiotrophin-binding oligosaccharide sequences isolated from chondroitin sulfate/dermatan sulfate hybrid chains of embryonic pig brains.	Dermatan Sulfate	102-118	pleiotrophin	Mus musculus	21-33
16120610-2	2005	CS/DS chains isolated from embryonic pig brains (E-CS/DS) promote the outgrowth of neurites in embryonic mouse hippocampal neurons in culture by interacting with pleiotrophin (PTN), a heparin-binding growth factor.	Dermatan Sulfate	3-5	pleiotrophin	Mus musculus	162-174
16120610-2	2005	CS/DS chains isolated from embryonic pig brains (E-CS/DS) promote the outgrowth of neurites in embryonic mouse hippocampal neurons in culture by interacting with pleiotrophin (PTN), a heparin-binding growth factor.	Dermatan Sulfate	3-5	pleiotrophin	Mus musculus	176-179
16120610-2	2005	CS/DS chains isolated from embryonic pig brains (E-CS/DS) promote the outgrowth of neurites in embryonic mouse hippocampal neurons in culture by interacting with pleiotrophin (PTN), a heparin-binding growth factor.	Dermatan Sulfate	54-56	pleiotrophin	Mus musculus	162-174
16120610-2	2005	CS/DS chains isolated from embryonic pig brains (E-CS/DS) promote the outgrowth of neurites in embryonic mouse hippocampal neurons in culture by interacting with pleiotrophin (PTN), a heparin-binding growth factor.	Dermatan Sulfate	54-56	pleiotrophin	Mus musculus	176-179
16120610-3	2005	Here, we analyzed oligosaccharides isolated from E-CS/DS, which showed that octasaccharides were the minimal size capable of interacting with PTN at a physiological salt concentration.	Dermatan Sulfate	54-56	pleiotrophin	Sus scrofa	142-145
16120610-8	2005	Thus, chain size and composition are crucial to the interaction with PTN, and PTN binds to multiple sequences in E-CS/DS chains with distinct affinity.	Dermatan Sulfate	118-120	pleiotrophin	Sus scrofa	78-81
16120610-9	2005	Notably, not only heparan sulfate but also CS/DS hybrid chain structures of mammalian brains contain a high degree of microheterogeneity with a cluster of oversulfated disaccharides and appear to play roles in regulating the functions of PTN.	Dermatan Sulfate	46-48	pleiotrophin	Homo sapiens	238-241
15947088-1	2005	In mucopolysaccharidosis-I (MPS-I), alpha-L-iduronidase deficiency leads to progressive heparan sulfate (HS) and dermatan sulfate (DS) glycosaminoglycan (GAG) accumulation.	Dermatan Sulfate	113-129	alpha-L-iduronidase	Homo sapiens	36-55
15947088-1	2005	In mucopolysaccharidosis-I (MPS-I), alpha-L-iduronidase deficiency leads to progressive heparan sulfate (HS) and dermatan sulfate (DS) glycosaminoglycan (GAG) accumulation.	Dermatan Sulfate	131-133	alpha-L-iduronidase	Homo sapiens	36-55
15500445-2	2005	IDS (iduronate-2-sulphatase; EC 3.1.6.13) is a lysosomal exo-sulphatase that belongs to this protein family and is involved in the degradation of the glycosaminoglycans heparan sulphate and dermatan sulphate.	Dermatan Sulfate	190-207	iduronate 2-sulfatase	Homo sapiens	0-3
15632143-0	2005	Heparin-binding growth factor, pleiotrophin, mediates neuritogenic activity of embryonic pig brain-derived chondroitin sulfate/dermatan sulfate hybrid chains.	Dermatan Sulfate	127-143	pleiotrophin	Sus scrofa	31-43
15632143-4	2005	Here we showed that pleiotrophin (PTN), a heparin-binding growth factor, produced mainly by glia cells, was the predominant binding partner for E-CS/DS in the membrane-associated protein fraction of neonatal rat brain.	Dermatan Sulfate	149-151	pleiotrophin	Rattus norvegicus	20-32
15632143-4	2005	Here we showed that pleiotrophin (PTN), a heparin-binding growth factor, produced mainly by glia cells, was the predominant binding partner for E-CS/DS in the membrane-associated protein fraction of neonatal rat brain.	Dermatan Sulfate	149-151	pleiotrophin	Rattus norvegicus	34-37
15632143-11	2005	Interaction analysis indicated that the 473HD epitope and PTN-binding domains in the E-CS/DS chains largely overlap.	Dermatan Sulfate	90-92	pleiotrophin	Sus scrofa	58-61
15632143-13	2005	Oversulfated disaccharides and nonconsecutive iduronic acid-containing units were the requirements for the E-CS/DS chains to bind PTN and to exhibit the neuritogenic activities.	Dermatan Sulfate	112-114	pleiotrophin	Sus scrofa	130-133
15500445-2	2005	IDS (iduronate-2-sulphatase; EC 3.1.6.13) is a lysosomal exo-sulphatase that belongs to this protein family and is involved in the degradation of the glycosaminoglycans heparan sulphate and dermatan sulphate.	Dermatan Sulfate	190-207	iduronate 2-sulfatase	Homo sapiens	5-27
15563459-0	2005	Structural and sequence motifs in dermatan sulfate for promoting fibroblast growth factor-2 (FGF-2) and FGF-7 activity.	Dermatan Sulfate	34-50	fibroblast growth factor 2	Homo sapiens	65-91
15563459-0	2005	Structural and sequence motifs in dermatan sulfate for promoting fibroblast growth factor-2 (FGF-2) and FGF-7 activity.	Dermatan Sulfate	34-50	fibroblast growth factor 2	Homo sapiens	93-98
15563459-0	2005	Structural and sequence motifs in dermatan sulfate for promoting fibroblast growth factor-2 (FGF-2) and FGF-7 activity.	Dermatan Sulfate	34-50	fibroblast growth factor 7	Homo sapiens	104-109
15563459-5	2005	Dermatan sulfate is abundant in the wound environment and binds and activates growth factors such as fibroblast growth factor-2 (FGF-2) and FGF-7, which are present during the wound repair process.	Dermatan Sulfate	0-16	fibroblast growth factor 2	Homo sapiens	101-127
15563459-5	2005	Dermatan sulfate is abundant in the wound environment and binds and activates growth factors such as fibroblast growth factor-2 (FGF-2) and FGF-7, which are present during the wound repair process.	Dermatan Sulfate	0-16	fibroblast growth factor 2	Homo sapiens	129-134
15563459-5	2005	Dermatan sulfate is abundant in the wound environment and binds and activates growth factors such as fibroblast growth factor-2 (FGF-2) and FGF-7, which are present during the wound repair process.	Dermatan Sulfate	0-16	fibroblast growth factor 7	Homo sapiens	140-145
15635159-7	2005	On the other hand, SDS-polyacrylamide gel electrophoresis and Western blot analysis of the PG core proteins indicated that the Na-SP-releasable PGs are both a large heparan sulfate PG, perlecan, and a small chondroitin/dermatan sulfate PG, biglycan, without change in the size of the core proteins.	Dermatan Sulfate	219-235	nuclear autoantigenic sperm protein	Bos taurus	127-132
15693006-11	2005	Dermatan sulfate was shown to be the ligand of the largest isoforms of EMR2 and CD97 in rheumatoid synovium.	Dermatan Sulfate	0-16	adhesion G protein-coupled receptor E2	Homo sapiens	71-75
15693006-11	2005	Dermatan sulfate was shown to be the ligand of the largest isoforms of EMR2 and CD97 in rheumatoid synovium.	Dermatan Sulfate	0-16	adhesion G protein-coupled receptor E5	Homo sapiens	80-84
15693006-13	2005	CONCLUSION: The EGF-TM7 receptors EMR2 and CD97 are abundantly expressed on myeloid cells in ST of RA patients where their cognate ligands dermatan sulfate and CD55 are detected.	Dermatan Sulfate	139-155	adhesion G protein-coupled receptor E2	Homo sapiens	34-38
15693006-13	2005	CONCLUSION: The EGF-TM7 receptors EMR2 and CD97 are abundantly expressed on myeloid cells in ST of RA patients where their cognate ligands dermatan sulfate and CD55 are detected.	Dermatan Sulfate	139-155	adhesion G protein-coupled receptor E5	Homo sapiens	43-47
15749837-0	2005	Factor H is a dermatan sulfate-binding protein: identification of a dermatan sulfate-mediated protease that cleaves factor H.	Dermatan Sulfate	14-30	complement factor H	Homo sapiens	0-8
15749837-0	2005	Factor H is a dermatan sulfate-binding protein: identification of a dermatan sulfate-mediated protease that cleaves factor H.	Dermatan Sulfate	14-30	complement factor H	Homo sapiens	116-124
15749837-1	2005	Dermatan sulfate mediates the blood coagulation cascade by binding to heparin cofactor II and potentiating the antithrombin activity.	Dermatan Sulfate	0-16	serpin family C member 1	Homo sapiens	111-123
15749837-3	2005	When human plasma was applied on the dermatan sulfate column, factor H was bound and cleaved.	Dermatan Sulfate	37-53	complement factor H	Homo sapiens	62-70
15749837-7	2005	The finding that dermatan sulfate-mediated cleavage of factor H was inhibited by (p-amidinophenyl) methanesulfonyl fluoride, but not N-ethylmaleimide or EDTA, indicates that a serine protease in the plasma was activated on the dermatan sulfate column and factor H was cleaved without intervention of the plasma protease inhibitors.	Dermatan Sulfate	17-33	complement factor H	Homo sapiens	55-63
15749837-7	2005	The finding that dermatan sulfate-mediated cleavage of factor H was inhibited by (p-amidinophenyl) methanesulfonyl fluoride, but not N-ethylmaleimide or EDTA, indicates that a serine protease in the plasma was activated on the dermatan sulfate column and factor H was cleaved without intervention of the plasma protease inhibitors.	Dermatan Sulfate	17-33	complement factor H	Homo sapiens	255-263
15749837-7	2005	The finding that dermatan sulfate-mediated cleavage of factor H was inhibited by (p-amidinophenyl) methanesulfonyl fluoride, but not N-ethylmaleimide or EDTA, indicates that a serine protease in the plasma was activated on the dermatan sulfate column and factor H was cleaved without intervention of the plasma protease inhibitors.	Dermatan Sulfate	227-243	complement factor H	Homo sapiens	55-63
16038721-2	2005	The rate of inactivation of thrombin by heparin cofactor II is increased in the presence of dermatan sulfate, which is produced by fibroblasts or smooth muscle cells.	Dermatan Sulfate	92-108	coagulation factor II, thrombin	Homo sapiens	28-36
16435196-1	2005	Mucopolysaccharidosis type VI (Maroteaux-Lamy syndrome, MPS VI) is an autosomal recessive disorder caused by deficiency of N-acetylgalactosamine-4-sulphatase (ARSB),which leads to the lysosomal accumulation and excretion of dermatan sulphate (DS).	Dermatan Sulfate	224-241	arylsulfatase B	Homo sapiens	159-163
16435196-1	2005	Mucopolysaccharidosis type VI (Maroteaux-Lamy syndrome, MPS VI) is an autosomal recessive disorder caused by deficiency of N-acetylgalactosamine-4-sulphatase (ARSB),which leads to the lysosomal accumulation and excretion of dermatan sulphate (DS).	Dermatan Sulfate	243-245	arylsulfatase B	Homo sapiens	159-163
16435198-2	2005	The deficiency of alpha-L-iduronidase (EC 1.2.3.76), one of the enzymes responsible for the degradation of glycosaminoglycans, results in accumulation of heparan and dermatan sulphate in these patients.	Dermatan Sulfate	166-183	alpha-L-iduronidase	Homo sapiens	18-37
15639191-1	2005	Mucopolysaccharidosis I is a lysosomal storage disorder caused by a deficiency of the lysosomal hydrolase alpha-l-iduronidase, which is required for the degradation of heparan sulphate and dermatan sulphate.	Dermatan Sulfate	189-206	alpha-L-iduronidase	Homo sapiens	106-125
15526370-0	2004	Effects of dermatan sulfate derivatives on platelet surface P-selectin expression and protein C activity in blood of inflammatory bowel disease patients.	Dermatan Sulfate	11-27	selectin P	Homo sapiens	60-70
15324304-2	2004	We showed previously that C4ST-1 purified from rat chondrosarcoma and recombinant C4ST-1 both transfer sulphate efficiently to position 4 of the GalNAc residues of DSDS (desulphated dermatan sulphate).	Dermatan Sulfate	182-199	carbohydrate sulfotransferase 11	Rattus norvegicus	26-32
15324304-2	2004	We showed previously that C4ST-1 purified from rat chondrosarcoma and recombinant C4ST-1 both transfer sulphate efficiently to position 4 of the GalNAc residues of DSDS (desulphated dermatan sulphate).	Dermatan Sulfate	182-199	carbohydrate sulfotransferase 11	Rattus norvegicus	82-88
15315969-1	2004	Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Dermatan Sulfate	97-113	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	0-19
15315969-1	2004	Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Dermatan Sulfate	97-113	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	21-25
15315969-1	2004	Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Dermatan Sulfate	97-113	coagulation factor II	Mus musculus	61-69
15315969-4	2004	Intravenous administration of porcine skin dermatan sulfate induced a dose-dependent prolongation of the carotid artery occlusion time in HCII(+/+) mice that was not observed in HCII(-/-) animals.	Dermatan Sulfate	43-59	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	138-142
15315969-4	2004	Intravenous administration of porcine skin dermatan sulfate induced a dose-dependent prolongation of the carotid artery occlusion time in HCII(+/+) mice that was not observed in HCII(-/-) animals.	Dermatan Sulfate	43-59	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	178-182
15315969-6	2004	Using invertebrate dermatan sulfate preparations, we showed that N-acetylgalactosamine-4-O-sulfate residues are required for the HCII-dependent antithrombotic effect.	Dermatan Sulfate	19-35	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	129-133
15315969-7	2004	Furthermore, the invertebrate dermatan sulfates, which have higher charge densities than mammalian dermatan sulfate, slightly prolonged the thrombotic occlusion time of HCII(-/-) mice.	Dermatan Sulfate	30-47	serpin family D member 1	Homo sapiens	169-173
15315969-7	2004	Furthermore, the invertebrate dermatan sulfates, which have higher charge densities than mammalian dermatan sulfate, slightly prolonged the thrombotic occlusion time of HCII(-/-) mice.	Dermatan Sulfate	30-46	serpin family D member 1	Homo sapiens	169-173
15315969-8	2004	These results indicate that HCII mediates the antithrombotic effect of porcine skin dermatan sulfate after injury to the carotid arterial endothelium in mice, whereas more highly charged dermatan sulfates possess weak antithrombotic activity independent of HCII.	Dermatan Sulfate	84-100	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	28-32
15526370-1	2004	AIM: To investigate the effect of dermatan sulfate (DS) derivatives on platelet surface P-selectin expression and blood activated protein C (APC) activity in patients with inflammatory bowel disease (IBD), and to clarity the anti-inflammatory mechanism of DS derivatives.	Dermatan Sulfate	34-50	selectin P	Homo sapiens	88-98
15526370-1	2004	AIM: To investigate the effect of dermatan sulfate (DS) derivatives on platelet surface P-selectin expression and blood activated protein C (APC) activity in patients with inflammatory bowel disease (IBD), and to clarity the anti-inflammatory mechanism of DS derivatives.	Dermatan Sulfate	52-54	selectin P	Homo sapiens	88-98
15526370-6	2004	The effects of DS derivatives on P-selectin expression were assayed by ELISA method, and blood APC activity was assayed by the synthetic chromogenic substrate method.	Dermatan Sulfate	15-17	selectin P	Homo sapiens	33-43
15148272-2	2004	Because heparin cofactor II (HCII) inhibits thrombin actions after binding to dermatan sulfate at injured arterial walls, HCII may negatively regulate thrombin actions in vascular walls.	Dermatan Sulfate	78-94	serpin family D member 1	Homo sapiens	8-27
15149955-1	2004	The lysosomal enzyme iduronate-2-sulfatase (IDS) is expressed in pancreatic islets and is responsible for degradation of proteoglycans, such as perlecan and dermatan sulfate.	Dermatan Sulfate	157-173	iduronate 2-sulfatase	Mus musculus	21-42
15203110-5	2004	Heparin, heparan sulfate and dermatan sulfate, at various HARP to glycosaminoglycan ratios, partially protect HARP from plasmin degradation.	Dermatan Sulfate	29-45	pleiotrophin	Homo sapiens	58-62
15203110-5	2004	Heparin, heparan sulfate and dermatan sulfate, at various HARP to glycosaminoglycan ratios, partially protect HARP from plasmin degradation.	Dermatan Sulfate	29-45	pleiotrophin	Homo sapiens	110-114
15203110-5	2004	Heparin, heparan sulfate and dermatan sulfate, at various HARP to glycosaminoglycan ratios, partially protect HARP from plasmin degradation.	Dermatan Sulfate	29-45	plasminogen	Homo sapiens	120-127
15347686-9	2004	Syndecan-1 extracted from wounded mouse skin also displayed an increase in dermatan sulfate synthesis compared with unwounded skin.	Dermatan Sulfate	75-91	syndecan 1	Mus musculus	0-10
15358546-4	2004	Both chondroitin sulfate and dermatan sulfate, in addition to heparin, were found to bind VWF equally well.	Dermatan Sulfate	29-45	von Willebrand factor	Homo sapiens	90-93
15236403-1	2004	A defect of the lysosomal enzyme alpha-L-iduronidase (IDUA) interrupts heparan and dermatan sulfate degradation and causes neuropathology in children with severe forms of mucopolysaccharidosis type I (MPSI, Hurler syndrome).	Dermatan Sulfate	83-99	alpha-L-iduronidase	Homo sapiens	33-52
15236403-1	2004	A defect of the lysosomal enzyme alpha-L-iduronidase (IDUA) interrupts heparan and dermatan sulfate degradation and causes neuropathology in children with severe forms of mucopolysaccharidosis type I (MPSI, Hurler syndrome).	Dermatan Sulfate	83-99	alpha-L-iduronidase	Homo sapiens	54-58
15148272-2	2004	Because heparin cofactor II (HCII) inhibits thrombin actions after binding to dermatan sulfate at injured arterial walls, HCII may negatively regulate thrombin actions in vascular walls.	Dermatan Sulfate	78-94	serpin family D member 1	Homo sapiens	29-33
15148272-2	2004	Because heparin cofactor II (HCII) inhibits thrombin actions after binding to dermatan sulfate at injured arterial walls, HCII may negatively regulate thrombin actions in vascular walls.	Dermatan Sulfate	78-94	coagulation factor II, thrombin	Homo sapiens	44-52
15148272-2	2004	Because heparin cofactor II (HCII) inhibits thrombin actions after binding to dermatan sulfate at injured arterial walls, HCII may negatively regulate thrombin actions in vascular walls.	Dermatan Sulfate	78-94	serpin family D member 1	Homo sapiens	122-126
15148272-2	2004	Because heparin cofactor II (HCII) inhibits thrombin actions after binding to dermatan sulfate at injured arterial walls, HCII may negatively regulate thrombin actions in vascular walls.	Dermatan Sulfate	78-94	coagulation factor II, thrombin	Homo sapiens	151-159
15078125-1	2004	Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin).	Dermatan Sulfate	76-92	serpin family C member 1	Homo sapiens	214-230
15081804-1	2004	alpha-L-Iduronidase is a glycosyl hydrolase involved in the sequential degradation of the glycosaminoglycans heparan sulphate and dermatan sulphate.	Dermatan Sulfate	130-147	alpha-L-iduronidase	Homo sapiens	0-19
15009704-0	2004	Fibroblast invasive migration into fibronectin/fibrin gels requires a previously uncharacterized dermatan sulfate-CD44 proteoglycan.	Dermatan Sulfate	97-113	fibronectin 1	Homo sapiens	35-46
15009704-0	2004	Fibroblast invasive migration into fibronectin/fibrin gels requires a previously uncharacterized dermatan sulfate-CD44 proteoglycan.	Dermatan Sulfate	97-113	CD44 molecule (Indian blood group)	Homo sapiens	114-118
15009704-5	2004	We found that dermatan sulfate was required for fibroblast migration into a fibronectin/fibrin gel.	Dermatan Sulfate	14-30	fibronectin 1	Homo sapiens	76-87
14704908-6	2004	RESULTS: Degradation of the samples with chondroitinases ABC, AC and B revealed that, in the aqueous humour from PEX eyes, collagen type IX and biglycan had a more dermatan sulphate than did normal eyes.	Dermatan Sulfate	164-181	biglycan	Homo sapiens	144-152
14718373-2	2004	In a lysosomal storage disorder known as mucopolysaccharidosis I, caused by a deficiency of the exohydrolase alpha-l-iduronidase, fragments of two different glycosaminoglycans, dermatan sulfate and heparan sulfate, have been shown to accumulate.	Dermatan Sulfate	177-193	alpha-L-iduronidase	Homo sapiens	109-128
14744972-2	2004	Because heparin cofactor II (HCII) inhibits thrombin action in the presence of dermatan sulfate, which is abundantly present in arterial wall, HCII may affect vascular remodeling by modulating thrombin action.	Dermatan Sulfate	79-95	serpin family D member 1	Homo sapiens	8-27
14744972-2	2004	Because heparin cofactor II (HCII) inhibits thrombin action in the presence of dermatan sulfate, which is abundantly present in arterial wall, HCII may affect vascular remodeling by modulating thrombin action.	Dermatan Sulfate	79-95	serpin family D member 1	Homo sapiens	29-33
14744972-2	2004	Because heparin cofactor II (HCII) inhibits thrombin action in the presence of dermatan sulfate, which is abundantly present in arterial wall, HCII may affect vascular remodeling by modulating thrombin action.	Dermatan Sulfate	79-95	coagulation factor II, thrombin	Homo sapiens	44-52
14744972-2	2004	Because heparin cofactor II (HCII) inhibits thrombin action in the presence of dermatan sulfate, which is abundantly present in arterial wall, HCII may affect vascular remodeling by modulating thrombin action.	Dermatan Sulfate	79-95	serpin family D member 1	Homo sapiens	143-147
14744972-2	2004	Because heparin cofactor II (HCII) inhibits thrombin action in the presence of dermatan sulfate, which is abundantly present in arterial wall, HCII may affect vascular remodeling by modulating thrombin action.	Dermatan Sulfate	79-95	coagulation factor II, thrombin	Homo sapiens	193-201
14707087-3	2004	EGF-TM7 receptors bind cellular ligands as demonstrated by the interaction of CD97 with decay accelerating factor (CD55) and dermatan sulfate.	Dermatan Sulfate	125-141	adhesion G protein-coupled receptor E1	Mus musculus	0-7
15078125-1	2004	Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin).	Dermatan Sulfate	76-92	coagulation factor II, thrombin	Homo sapiens	218-226
15078125-1	2004	Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin).	Dermatan Sulfate	76-92	serpin family D member 1	Homo sapiens	284-303
15078125-1	2004	Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin).	Dermatan Sulfate	76-92	serpin family D member 1	Homo sapiens	305-309
15078125-1	2004	Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin).	Dermatan Sulfate	76-92	coagulation factor II, thrombin	Homo sapiens	270-278
15078125-2	2004	Although AT and HCII are structural homologs, only heparin binds to AT, and HCII has different binding sites for heparin and dermatan sulfate.	Dermatan Sulfate	125-141	serpin family D member 1	Homo sapiens	76-80
15078125-3	2004	Whereas the binding site of heparin for AT is a unique pentasaccharide sequence contained in only about one third of the chains of this GAG, HCII-binding sequences of heparin and dermatan sulfate are less specific and contained in practically all the GAG chains.	Dermatan Sulfate	179-195	serpin family D member 1	Homo sapiens	141-145
15078125-6	2004	Whereas it inactivates the binding site for AT causing a drop of the anticoagulant activity, it enhances the HCII-associated activity of both heparin and dermatan sulfate.	Dermatan Sulfate	154-170	serpin family D member 1	Homo sapiens	109-113
14653390-4	2003	RESULTS: The results showed that IL-6 elicited an inhibitory effect on collagen and GAG levels in CLP fibroblasts by lowering hyaluronan and dermatan sulfate secretion.	Dermatan Sulfate	141-157	interleukin 6	Homo sapiens	33-37
14634134-6	2003	The FAK-deficient mast cells had a reduction in the content of chondroitin/dermatan sulfate, the major glycosaminoglycan component of the granular matrix.	Dermatan Sulfate	75-91	PTK2 protein tyrosine kinase 2	Mus musculus	4-7
12799343-1	2003	Hybrid chondroitin/dermatan sulfate (CS/DS) glycosaminoglycan chains, derived from decorin secreted by human skin fibroblasts, were shown to interact with FGF-2, as did oligosaccharides derived therefrom by chondroitin B lyase digestion.	Dermatan Sulfate	19-35	fibroblast growth factor 2	Homo sapiens	155-160
12933790-9	2003	The 175-kDa rHARE binds HA, dermatan sulfate, and chondroitin sulfates A, C, D, and E, but not chondroitin, heparin, heparan sulfate, or keratan sulfate.	Dermatan Sulfate	28-44	stabilin 2	Rattus norvegicus	12-17
12847091-1	2003	4-O-Sulfation of GalNAc is a high frequency modification of chondroitin sulfate and dermatan sulfate (DS), and three major GalNAc 4-O-sulfotransferases including dermatan 4-O-sulfotransferase-1 (D4ST-1) and chondroitin 4-O-sulfotransferases-1 and -2 (C4ST-1 and -2) have been identified.	Dermatan Sulfate	102-104	carbohydrate sulfotransferase 14	Homo sapiens	195-201
12847091-1	2003	4-O-Sulfation of GalNAc is a high frequency modification of chondroitin sulfate and dermatan sulfate (DS), and three major GalNAc 4-O-sulfotransferases including dermatan 4-O-sulfotransferase-1 (D4ST-1) and chondroitin 4-O-sulfotransferases-1 and -2 (C4ST-1 and -2) have been identified.	Dermatan Sulfate	102-104	carbohydrate sulfotransferase 11	Homo sapiens	207-249
12847091-1	2003	4-O-Sulfation of GalNAc is a high frequency modification of chondroitin sulfate and dermatan sulfate (DS), and three major GalNAc 4-O-sulfotransferases including dermatan 4-O-sulfotransferase-1 (D4ST-1) and chondroitin 4-O-sulfotransferases-1 and -2 (C4ST-1 and -2) have been identified.	Dermatan Sulfate	102-104	carbohydrate sulfotransferase 11	Homo sapiens	251-264
12886459-5	2003	On the other hand, heparin, heparan sulfate, and bovine and tuna dermatan sulfate improved (1.2 to 3.4 times) kallikrein inhibition by antithrombin (1.4 microM), while chondroitin 4- and 6-sulfates reduced it (1.3 times).	Dermatan Sulfate	65-81	kallikrein related peptidase 4	Homo sapiens	110-120
12886459-4	2003	Almost all available glycosaminoglycans (heparin, heparan sulfate, bovine and tuna dermatan sulfate, chondroitin 4- and 6-sulfates) reduced (1.2 to 3.0 times) the catalytic efficiency of kallikrein (in a nanomolar range) on the hydrolysis of plasminogen (0.3 to 1.8 microM) and increased (1.9 to 7.7 times) the enzyme efficiency in factor XII (0.1 to 10 microM) activation.	Dermatan Sulfate	83-99	kallikrein related peptidase 4	Homo sapiens	187-197
12886459-5	2003	On the other hand, heparin, heparan sulfate, and bovine and tuna dermatan sulfate improved (1.2 to 3.4 times) kallikrein inhibition by antithrombin (1.4 microM), while chondroitin 4- and 6-sulfates reduced it (1.3 times).	Dermatan Sulfate	65-81	serpin family C member 1	Homo sapiens	135-147
12730206-13	2003	Collectively, our results show that carbohydrate recognition domains of SP-D interact with the dermatan sulfate moiety of decorin via lectin activity and that the core protein of decorin binds the collagen-like region of SP-D in vitro, and these interactions may be operative in vivo.	Dermatan Sulfate	95-111	surfactant protein D	Homo sapiens	72-76
12731055-7	2003	Heparan sulfate and dermatan sulfate, but not chondroitin sulfate, also inhibited the actions of CCL11 and CCL13 in assays of cellular shape change and chemotaxis.	Dermatan Sulfate	20-36	C-C motif chemokine ligand 11	Homo sapiens	97-102
12798179-9	2003	The high sensitivity of the new method allows the determination of dermatan sulfate contaminations in a heparin raw sample down to 0.04% (w/w) and broadens the practical applicability of CE-LIF for the quantitation of the endogenous levels of glycosaminoglycans in animal samples and for pharmacokinetic control after therapeutical heparin administration.	Dermatan Sulfate	67-83	LIF interleukin 6 family cytokine	Homo sapiens	190-193
12730206-4	2003	The human decorin that co-purified with SP-D is a 130-150-kDa proteoglycan, which has a 46-kDa protein core and approximately 90-kDa dermatan sulfate chain.	Dermatan Sulfate	133-149	surfactant protein D	Homo sapiens	40-44
12796199-4	2003	Arylsulfatase B, also known as N-acetyl galactosamine 4-sulfatase, can degrade DS and chondroitin-4 sulfate.	Dermatan Sulfate	79-81	arylsulfatase B	Homo sapiens	0-15
12796199-4	2003	Arylsulfatase B, also known as N-acetyl galactosamine 4-sulfatase, can degrade DS and chondroitin-4 sulfate.	Dermatan Sulfate	79-81	arylsulfatase B	Homo sapiens	31-65
12731055-7	2003	Heparan sulfate and dermatan sulfate, but not chondroitin sulfate, also inhibited the actions of CCL11 and CCL13 in assays of cellular shape change and chemotaxis.	Dermatan Sulfate	20-36	C-C motif chemokine ligand 13	Homo sapiens	107-112
12531251-6	2003	Of particular, interest were the quite different sulphation profiles of CS and DS chains in HGC in which, non-sulphated and 6-sulphated disaccharide units were increased 10 and 4 times, respectively, in comparison to HNG.	Dermatan Sulfate	79-81	neurogranin	Homo sapiens	217-220
12716937-2	2003	MPS VII mice lack lysosomal beta-glucuronidase (GUSB) activity, leading to the accumulation of partially degraded chondroitin, dermatan, and heparan sulfates in most tissues.	Dermatan Sulfate	127-135	glucuronidase, beta	Mus musculus	28-46
12716937-2	2003	MPS VII mice lack lysosomal beta-glucuronidase (GUSB) activity, leading to the accumulation of partially degraded chondroitin, dermatan, and heparan sulfates in most tissues.	Dermatan Sulfate	127-135	glucuronidase, beta	Mus musculus	48-52
12653636-1	2003	Hepatocyte growth factor (HGF)/scatter factor (SF) is a unique growth factor, in that it binds both heparan sulphate (HS) and dermatan sulphate (DS).	Dermatan Sulfate	126-143	hepatocyte growth factor	Homo sapiens	26-29
12653636-1	2003	Hepatocyte growth factor (HGF)/scatter factor (SF) is a unique growth factor, in that it binds both heparan sulphate (HS) and dermatan sulphate (DS).	Dermatan Sulfate	145-147	hepatocyte growth factor	Homo sapiens	26-29
12818259-0	2003	Additive thrombin inhibition by fast moving heparin and dermatan sulfate explains the anticoagulant effect of sulodexide, a natural mixture of glycosaminoglycans.	Dermatan Sulfate	56-72	coagulation factor II, thrombin	Homo sapiens	9-17
12818259-10	2003	CONCLUSIONS: Thrombin inhibition produced by sulodexide is due to the additive effect of its components, namely, HCII catalysis by DS and AT catalysis by FMH.	Dermatan Sulfate	131-133	coagulation factor II, thrombin	Homo sapiens	13-21
12818259-10	2003	CONCLUSIONS: Thrombin inhibition produced by sulodexide is due to the additive effect of its components, namely, HCII catalysis by DS and AT catalysis by FMH.	Dermatan Sulfate	131-133	serpin family D member 1	Homo sapiens	113-117
12752450-3	2003	Hence, S. pyogenes strains expressing a large number of different types of M proteins bound to dermatan sulfate (DS), highly sulfated fractions of heparan sulfate (HS) and heparin, whereas strains deficient in M protein surface expression failed to interact with these GAGs.	Dermatan Sulfate	95-111	myomesin 2	Homo sapiens	75-84
12752450-3	2003	Hence, S. pyogenes strains expressing a large number of different types of M proteins bound to dermatan sulfate (DS), highly sulfated fractions of heparan sulfate (HS) and heparin, whereas strains deficient in M protein surface expression failed to interact with these GAGs.	Dermatan Sulfate	113-115	myomesin 2	Homo sapiens	75-84
12752450-7	2003	Together with the finding that exogenous DS and HS could inhibit streptococcal adhesion, these data suggest that GAGs function as receptors in M protein-mediated adhesion of S. pyogenes.	Dermatan Sulfate	41-43	myomesin 2	Homo sapiens	143-152
12505197-0	2003	A role for chondroitin sulphate B in the activity of interleukin 12 in stimulating gamma-interferon secretion.	Dermatan Sulfate	11-33	interferon gamma	Mus musculus	83-99
12522561-1	2003	Mucopolysaccharidosis VII (MPS VII) is an autosomal recessive disorder caused by the deficiency of beta-glucuronidase leading to the intralysosomal storage of heparan, dermatan, and chondroitin sulfate.	Dermatan Sulfate	168-176	glucuronidase beta	Homo sapiens	99-117
12527107-0	2003	Galectin 1 inhibits incorporation of vitronectin and chondroitin sulfate B into the extracellular matrix of human vascular smooth muscle cells.	Dermatan Sulfate	53-74	galectin 1	Homo sapiens	0-10
12603746-5	2003	Three B. burgdorferi surface proteins, Bgp, DbpA and DbpB, have been demonstrated previously to bind to GAGs or to GAG-containing molecules, and we show here that recombinant derivatives of each of these proteins were able to bind to purified heparin and dermatan sulphate.	Dermatan Sulfate	255-272	Y-box binding protein 3	Homo sapiens	44-48
12603746-5	2003	Three B. burgdorferi surface proteins, Bgp, DbpA and DbpB, have been demonstrated previously to bind to GAGs or to GAG-containing molecules, and we show here that recombinant derivatives of each of these proteins were able to bind to purified heparin and dermatan sulphate.	Dermatan Sulfate	255-272	Y-box binding protein 1	Homo sapiens	53-57
12215437-5	2002	FGF-7 did not support cell proliferation in the absence of glycosaminoglycan or with addition of heparan sulfate or chondroitin sulfate A/C but did stimulate BaF/KGFR division in the presence of dermatan sulfate or highly sulfated low molecular weight fractions of dermatan.	Dermatan Sulfate	195-211	fibroblast growth factor 7	Homo sapiens	0-5
12529676-5	2003	Competition experiments showed that 125I-SDF-1 alpha binding to the BMEC cell line 4LHBMEC was inhibited by heparins, heparan sulfate (HS) intestinal mucosa, chondroitin and dermatan sulfate (CS/DS), but not by HS bovine kidney.	Dermatan Sulfate	174-190	C-X-C motif chemokine ligand 12	Homo sapiens	41-46
12186633-2	2002	We found that recombinant human PrP (rPrP) binds GAGs including chondroitin sulphate A, chondroitin sulphate B, hyaluronic acid, and heparin.	Dermatan Sulfate	88-110	prion protein	Homo sapiens	32-35
12186633-2	2002	We found that recombinant human PrP (rPrP) binds GAGs including chondroitin sulphate A, chondroitin sulphate B, hyaluronic acid, and heparin.	Dermatan Sulfate	88-110	prion protein	Rattus norvegicus	37-41
15000815-1	2003	Mucopolysaccharidosis type VI, or Maroteaux-Lamy syndrome, is an autosomal recessive disease caused by the deficiency of arylsulfatase B (ARSB; N-acetyl-galactosamine-4-sulfatase, E.C.3.1.6.12), which is involved in the stepwise degradation of dermatan sulfate and chondroitin sulfate.	Dermatan Sulfate	244-260	arylsulfatase B	Homo sapiens	138-142
15000815-1	2003	Mucopolysaccharidosis type VI, or Maroteaux-Lamy syndrome, is an autosomal recessive disease caused by the deficiency of arylsulfatase B (ARSB; N-acetyl-galactosamine-4-sulfatase, E.C.3.1.6.12), which is involved in the stepwise degradation of dermatan sulfate and chondroitin sulfate.	Dermatan Sulfate	244-260	arylsulfatase B	Homo sapiens	144-178
12423630-3	2002	We report here the in vitro synthesis of CS-E from chondrotin sulfate A (CS-A) by the purified squid N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) which catalyzed transfer of sulfate from 3(")-phosphoadenosine-5(")-phosphosulfate to position 6 of GalNAc(4SO(4)) residues of CS-A and dermatan sulfate (DS).	Dermatan Sulfate	305-321	chorionic somatomammotropin hormone 1	Homo sapiens	73-77
12423630-3	2002	We report here the in vitro synthesis of CS-E from chondrotin sulfate A (CS-A) by the purified squid N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) which catalyzed transfer of sulfate from 3(")-phosphoadenosine-5(")-phosphosulfate to position 6 of GalNAc(4SO(4)) residues of CS-A and dermatan sulfate (DS).	Dermatan Sulfate	305-321	carbohydrate sulfotransferase 15	Homo sapiens	155-167
12423630-3	2002	We report here the in vitro synthesis of CS-E from chondrotin sulfate A (CS-A) by the purified squid N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) which catalyzed transfer of sulfate from 3(")-phosphoadenosine-5(")-phosphosulfate to position 6 of GalNAc(4SO(4)) residues of CS-A and dermatan sulfate (DS).	Dermatan Sulfate	323-325	chorionic somatomammotropin hormone 1	Homo sapiens	73-77
12423630-3	2002	We report here the in vitro synthesis of CS-E from chondrotin sulfate A (CS-A) by the purified squid N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) which catalyzed transfer of sulfate from 3(")-phosphoadenosine-5(")-phosphosulfate to position 6 of GalNAc(4SO(4)) residues of CS-A and dermatan sulfate (DS).	Dermatan Sulfate	323-325	carbohydrate sulfotransferase 15	Homo sapiens	155-167
12423630-6	2002	GalNAc4S-6ST also catalyzed the synthesis of oversulfated DS with GalNAc(4,6-SO(4)) residues from DS.	Dermatan Sulfate	58-60	carbohydrate sulfotransferase 15	Homo sapiens	0-12
12423630-6	2002	GalNAc4S-6ST also catalyzed the synthesis of oversulfated DS with GalNAc(4,6-SO(4)) residues from DS.	Dermatan Sulfate	98-100	carbohydrate sulfotransferase 15	Homo sapiens	0-12
12423630-7	2002	Squid GalNAc4S-6ST thus should provide a useful tool for preparing CS-E and oversulfated DS with a defined proportion of GalNAc(4,6-SO(4)) residues.	Dermatan Sulfate	89-91	carbohydrate sulfotransferase 15	Homo sapiens	6-18
12215437-0	2002	Dermatan sulfate binds and potentiates activity of keratinocyte growth factor (FGF-7).	Dermatan Sulfate	0-16	fibroblast growth factor 7	Homo sapiens	51-77
12215437-0	2002	Dermatan sulfate binds and potentiates activity of keratinocyte growth factor (FGF-7).	Dermatan Sulfate	0-16	fibroblast growth factor 7	Homo sapiens	79-84
12215437-6	2002	Dermatan sulfate also enabled FGF-7-dependent phosphorylation of mitogen-activated protein kinase and promoted binding of radiolabeled FGF-7 to FGFR2 IIIb.	Dermatan Sulfate	0-16	fibroblast growth factor 7	Homo sapiens	30-35
12215437-6	2002	Dermatan sulfate also enabled FGF-7-dependent phosphorylation of mitogen-activated protein kinase and promoted binding of radiolabeled FGF-7 to FGFR2 IIIb.	Dermatan Sulfate	0-16	fibroblast growth factor 7	Homo sapiens	135-140
12215437-8	2002	Thus, dermatan sulfate, the predominant glycosaminoglycan in skin, is the principle cofactor for FGF-7.	Dermatan Sulfate	6-22	fibroblast growth factor 7	Homo sapiens	97-102
12423248-4	2002	The heparin-resistant binding of [125I]bFGF to TM-BBB4 was significantly inhibited by a cationic polypeptide poly-L-lysine (300 micro m), and compounds which contain a sulfate moiety, e.g. heparin and chondroitin sulfate-B (each 10 micro g/mL).	Dermatan Sulfate	201-222	fibroblast growth factor 2	Mus musculus	39-43
13679662-1	2002	Dermatan sulphate (DS) is a glycosaminoglycan which selectively catalyzes the inactivation of thrombin by Heparin Cofactor II without interacting with Antithrombin III.	Dermatan Sulfate	0-17	coagulation factor II, thrombin	Homo sapiens	94-102
13679662-1	2002	Dermatan sulphate (DS) is a glycosaminoglycan which selectively catalyzes the inactivation of thrombin by Heparin Cofactor II without interacting with Antithrombin III.	Dermatan Sulfate	0-17	serpin family C member 1	Homo sapiens	151-167
13679662-1	2002	Dermatan sulphate (DS) is a glycosaminoglycan which selectively catalyzes the inactivation of thrombin by Heparin Cofactor II without interacting with Antithrombin III.	Dermatan Sulfate	19-21	coagulation factor II, thrombin	Homo sapiens	94-102
13679662-1	2002	Dermatan sulphate (DS) is a glycosaminoglycan which selectively catalyzes the inactivation of thrombin by Heparin Cofactor II without interacting with Antithrombin III.	Dermatan Sulfate	19-21	serpin family C member 1	Homo sapiens	151-167
13679662-2	2002	DS does not interact with other coagulation factors and, unlike heparin, is able to inactivate thrombin bound to fibrin or to the surface of an injured vessel.	Dermatan Sulfate	0-2	coagulation factor II, thrombin	Homo sapiens	95-103
12095635-0	2002	Contribution of basic residues of the A helix of heparin cofactor II to heparin- or dermatan sulfate-mediated thrombin inhibition.	Dermatan Sulfate	84-100	serpin family D member 1	Homo sapiens	49-68
12413592-6	2002	Dermatan sulfate (DSO4)-catalyzed HCII thrombin inhibition was unchanged in R93A/R97A/R101A thrombin compared to wild-type recombinant thrombin.	Dermatan Sulfate	0-16	serpin family D member 1	Homo sapiens	34-38
12413592-6	2002	Dermatan sulfate (DSO4)-catalyzed HCII thrombin inhibition was unchanged in R93A/R97A/R101A thrombin compared to wild-type recombinant thrombin.	Dermatan Sulfate	0-16	coagulation factor II, thrombin	Homo sapiens	39-47
12149217-8	2002	A drastic decrease (up to 500-fold) of the second-order rate constant pertaining to heparin cofactor II (HCII) interaction, especially in the presence of dermatan sulfate, was found for the FIIa-MT67 compared with FIIa-WT, suggesting a severe impairment of thrombin inhibition by HCII in vivo.	Dermatan Sulfate	154-170	serpin family D member 1	Homo sapiens	84-103
12149217-8	2002	A drastic decrease (up to 500-fold) of the second-order rate constant pertaining to heparin cofactor II (HCII) interaction, especially in the presence of dermatan sulfate, was found for the FIIa-MT67 compared with FIIa-WT, suggesting a severe impairment of thrombin inhibition by HCII in vivo.	Dermatan Sulfate	154-170	serpin family D member 1	Homo sapiens	105-109
12095635-0	2002	Contribution of basic residues of the A helix of heparin cofactor II to heparin- or dermatan sulfate-mediated thrombin inhibition.	Dermatan Sulfate	84-100	coagulation factor II, thrombin	Homo sapiens	110-118
12095635-1	2002	Inhibition of thrombin by heparin cofactor II (HCII) is accelerated 1000-fold by heparin or dermatan sulfate.	Dermatan Sulfate	92-108	coagulation factor II, thrombin	Homo sapiens	14-22
12095635-1	2002	Inhibition of thrombin by heparin cofactor II (HCII) is accelerated 1000-fold by heparin or dermatan sulfate.	Dermatan Sulfate	92-108	serpin family D member 1	Homo sapiens	26-45
12095635-1	2002	Inhibition of thrombin by heparin cofactor II (HCII) is accelerated 1000-fold by heparin or dermatan sulfate.	Dermatan Sulfate	92-108	serpin family D member 1	Homo sapiens	47-51
12095635-3	2002	K101Q greatly reduced heparin cofactor activity and required a more than 10-fold higher concentration of dermatan sulfate to accelerate thrombin inhibition compared with wild-type recombinant HCII.	Dermatan Sulfate	105-121	coagulation factor II, thrombin	Homo sapiens	136-144
12095635-5	2002	These results provide evidence that basic residues of the A helix of HCII (Lys(101) and Arg(106)) are necessary for heparin- or dermatan sulfate-accelerated thrombin inhibition.	Dermatan Sulfate	128-144	serpin family D member 1	Homo sapiens	69-73
12095635-5	2002	These results provide evidence that basic residues of the A helix of HCII (Lys(101) and Arg(106)) are necessary for heparin- or dermatan sulfate-accelerated thrombin inhibition.	Dermatan Sulfate	128-144	coagulation factor II, thrombin	Homo sapiens	157-165
12023510-8	2002	Hypoxia enhanced the effect of all TGF-beta isoforms, particularly that of TGF-beta3, on the secretion of hyaluronic acid and chondroitin and dermatan sulfates.	Dermatan Sulfate	142-159	transforming growth factor beta 1	Homo sapiens	35-43
12060613-8	2002	The decorin component of tumor stroma was previously shown to contain high levels of chondroitin sulfate as opposed to dermatan sulfate side chains, and those molecules contained unusually high levels of O- and 6-sulfate linkages.	Dermatan Sulfate	119-135	decorin	Homo sapiens	4-11
12094292-5	2002	The inhibitory activity of Na-SP was the strongest when compared to that of heparan sulfate, heparin, dextran sulfate, dermatan sulfate, chondroitin sulfate A/C and hyaluronan.	Dermatan Sulfate	119-135	nuclear autoantigenic sperm protein	Bos taurus	27-32
11855549-1	2002	Decorin, a small proteoglycan containing a dermatan sulfate (DS) chain, is expressed abnormally in human colon cancer stroma.	Dermatan Sulfate	43-59	decorin	Homo sapiens	0-7
11991744-3	2002	Cell attachment of the VLP is efficiently inhibited by soluble heparin and dextran sulfate and less efficiently abrogated by several other glycosaminoglycans (GAGs) including chondroitin sulfate A and chondroitin sulfate B (dermatan sulfate), as determined by deconvolution microscopic immunodetection of the viral gag protein and by quantitative binding studies of metabolically labeled (35)S-VLP.	Dermatan Sulfate	201-222	VHL like	Homo sapiens	23-26
11991744-3	2002	Cell attachment of the VLP is efficiently inhibited by soluble heparin and dextran sulfate and less efficiently abrogated by several other glycosaminoglycans (GAGs) including chondroitin sulfate A and chondroitin sulfate B (dermatan sulfate), as determined by deconvolution microscopic immunodetection of the viral gag protein and by quantitative binding studies of metabolically labeled (35)S-VLP.	Dermatan Sulfate	224-240	VHL like	Homo sapiens	23-26
11821431-0	2002	Oversulfated chondroitin/dermatan sulfates containing GlcAbeta1/IdoAalpha1-3GalNAc(4,6-O-disulfate) interact with L- and P-selectin and chemokines.	Dermatan Sulfate	25-42	selectin P	Homo sapiens	121-131
11821431-1	2002	We previously reported that versican, a large chondroitin/dermatan sulfate (CS/DS) proteoglycan, interacts through its CS/DS chains with adhesion molecules L- and P-selectin and CD44, as well as chemokines.	Dermatan Sulfate	58-74	versican	Homo sapiens	28-36
11861306-6	2002	Exogenous IDUA expression led to a normalization of glycosaminoglycan storage in MPS-IH cells, as evidenced by a dramatic decrease in the amount of (35)SO(4) sequestered within the heparan sulfate and dermatan sulfate compartments of these cells.	Dermatan Sulfate	201-217	alpha-L-iduronidase	Homo sapiens	10-14
11855549-1	2002	Decorin, a small proteoglycan containing a dermatan sulfate (DS) chain, is expressed abnormally in human colon cancer stroma.	Dermatan Sulfate	61-63	decorin	Homo sapiens	0-7
11668612-2	2001	Mutations in the 4S gene are responsible for 4S deficiency, which leads to the intralysosomal storage of partially degraded glycosaminoglycans, dermatan sulfate, and chondroitin 4-sulfate.	Dermatan Sulfate	144-160	arylsulfatase B	Homo sapiens	17-19
11788461-2	2002	Transforming growth factor (TGF)-beta1 has been identified in atherosclerotic vessels and has been shown to stimulate the synthesis of chondroitin sulfate- and dermatan sulfate-containing proteoglycans by arterial smooth muscle cells (ASMCs), but whether it promotes lipid retention has not been addressed.	Dermatan Sulfate	160-176	transforming growth factor beta 1	Homo sapiens	0-38
11572857-6	2001	The recombinant protein expressed from the human GalNAc4S-6ST cDNA transferred sulfate from 3"-phosphoadenosine 5"-phosphosulfate to position 6 of the nonreducing terminal and internal GalNAc(4SO(4)) residues contained in chondroitin sulfate A and dermatan sulfate.	Dermatan Sulfate	248-264	carbohydrate sulfotransferase 15	Homo sapiens	49-61
11816710-3	2001	It inhibits thrombin due to the formation of a covalent complex with heparin cofactor II, as in the case of mammalian dermatan sulfate, but the effect occurs at lower concentrations for the invertebrate polysaccharide.	Dermatan Sulfate	118-134	coagulation factor II, thrombin	Homo sapiens	12-20
11853965-8	2002	Dermatan sulfate (DS) was the predominant glycosaminoglycan (GAG) present on biglycan and decorin in both tissues.	Dermatan Sulfate	0-16	biglycan	Homo sapiens	77-85
11853965-8	2002	Dermatan sulfate (DS) was the predominant glycosaminoglycan (GAG) present on biglycan and decorin in both tissues.	Dermatan Sulfate	18-20	biglycan	Homo sapiens	77-85
11805133-1	2002	Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin rapidly in the presence of dermatan sulfate, heparan sulfate, or heparin.	Dermatan Sulfate	97-113	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	0-19
11805133-1	2002	Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin rapidly in the presence of dermatan sulfate, heparan sulfate, or heparin.	Dermatan Sulfate	97-113	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	21-25
11805133-1	2002	Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin rapidly in the presence of dermatan sulfate, heparan sulfate, or heparin.	Dermatan Sulfate	97-113	coagulation factor II	Mus musculus	61-69
11590178-10	2001	The glycosaminoglycan component of endocan consists of a single DS chain covalently attached to serine 137.	Dermatan Sulfate	64-66	endothelial cell specific molecule 1	Homo sapiens	35-42
11590178-12	2001	Moreover, DS chains purified from endocan mimicked the endocan-mediated increase of cell proliferation in the presence of HGF/SF.	Dermatan Sulfate	10-12	endothelial cell specific molecule 1	Homo sapiens	34-41
11590178-12	2001	Moreover, DS chains purified from endocan mimicked the endocan-mediated increase of cell proliferation in the presence of HGF/SF.	Dermatan Sulfate	10-12	endothelial cell specific molecule 1	Homo sapiens	55-62
11590178-12	2001	Moreover, DS chains purified from endocan mimicked the endocan-mediated increase of cell proliferation in the presence of HGF/SF.	Dermatan Sulfate	10-12	hepatocyte growth factor	Homo sapiens	122-128
11598131-9	2001	Similarly, WISP-1 interaction with human skin fibroblasts was inhibited by dermatan sulfate, decorin, and biglycan or by treatment of the cell surface with dermatan sulfate-specific lyases.	Dermatan Sulfate	75-91	cellular communication network factor 4	Homo sapiens	11-17
11598131-9	2001	Similarly, WISP-1 interaction with human skin fibroblasts was inhibited by dermatan sulfate, decorin, and biglycan or by treatment of the cell surface with dermatan sulfate-specific lyases.	Dermatan Sulfate	156-172	cellular communication network factor 4	Homo sapiens	11-17
11572857-1	2001	N-Acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) transfers sulfate from 3"-phosphoadenosine 5"-phosphosulfate to position 6 of N-acetylgalactosamine 4-sulfate (GalNAc(4SO(4))) in chondroitin sulfate and dermatan sulfate.	Dermatan Sulfate	222-238	carbohydrate sulfotransferase 15	Homo sapiens	54-66
11668612-2	2001	Mutations in the 4S gene are responsible for 4S deficiency, which leads to the intralysosomal storage of partially degraded glycosaminoglycans, dermatan sulfate, and chondroitin 4-sulfate.	Dermatan Sulfate	144-160	arylsulfatase B	Homo sapiens	45-47
11405343-1	2001	Mucopolysaccharidosis type I is due to a deficiency of the lysosomal enzyme alpha-L-iduronidase (EC 3.2.1.76) and is associated with a defect in the catabolism of the glycosaminoglycans heparan and dermatan sulphate.	Dermatan Sulfate	198-215	alpha-L-iduronidase	Homo sapiens	76-95
12940068-6	2001	Chondroitin sulfate A and chondroitin sulfate B reduced cell surface apoE by 23.6% and 15.3% respectively while incubations with chondrointin sulfate C not effective.	Dermatan Sulfate	26-47	apolipoprotein E	Homo sapiens	69-73
11414686-0	2001	The glucuronyl C5-epimerase activity is the limiting factor in the dermatan sulfate biosynthesis.	Dermatan Sulfate	67-83	glucuronic acid epimerase	Homo sapiens	4-27
11414686-1	2001	An early step in the biosynthesis of dermatan sulfate is polymerization to chondroitin, which then is modified by the D-glucuronyl C5-epimerase and mainly 4-O-sulfotransferase.	Dermatan Sulfate	37-53	glucuronic acid epimerase	Homo sapiens	120-143
11414686-9	2001	The data indicate that the activity of the d-glucuronyl C5-epimerase is the main factor for formation of dermatan sulfate in tissues.	Dermatan Sulfate	105-121	glucuronic acid epimerase	Homo sapiens	45-68
11294849-0	2001	Molecular basis for the susceptibility of fibrin-bound thrombin to inactivation by heparin cofactor ii in the presence of dermatan sulfate but not heparin.	Dermatan Sulfate	122-138	coagulation factor II, thrombin	Homo sapiens	55-63
11294849-1	2001	Although fibrin-bound thrombin is resistant to inactivation by heparin.antithrombin and heparin.heparin cofactor II complexes, indirect studies in plasma systems suggest that the dermatan sulfate.heparin cofactor II complex can inhibit fibrin-bound thrombin.	Dermatan Sulfate	179-195	coagulation factor II, thrombin	Homo sapiens	22-30
11294849-5	2001	In contrast, dermatan sulfate binds to thrombin but does not bind to fibrin.	Dermatan Sulfate	13-29	coagulation factor II, thrombin	Homo sapiens	39-47
11294849-7	2001	thrombin.fibrin complex forms, without dermatan sulfate-mediated bridging of thrombin to fibrin, only two binary interactions exist (thrombin.fibrin and thrombin.	Dermatan Sulfate	39-55	coagulation factor II, thrombin	Homo sapiens	0-8
11294849-10	2001	This study explains why fibrin-bound thrombin is susceptible to inactivation by heparin cofactor II in the presence of dermatan sulfate but not heparin.	Dermatan Sulfate	119-135	coagulation factor II, thrombin	Homo sapiens	37-45
11925507-0	2001	Requirement of chondroitin sulfate/dermatan sulfate recognition in midkine-dependent migration of macrophages.	Dermatan Sulfate	35-51	midkine	Homo sapiens	67-74
11925507-3	2001	MK-induced migration of peritoneal exudate macrophages was inhibited by heparin, chondroitin sulfate E and dermatan sulfate, but not by chondroitin sulfate D or chondroitin 6-sulfate.	Dermatan Sulfate	107-123	midkine	Homo sapiens	0-2
11925507-6	2001	These results indicated that a chondroitin sulfate, i.e. an E-type oversulfated structure with dermatan sulfate domain, is involved in MK-induced migration of macrophages.	Dermatan Sulfate	95-111	midkine	Homo sapiens	135-137
11322944-4	2001	By solid-phase assays, we showed that dermatan sulfate chains of decorin bind to the heparin-binding site included within the fibronectin-type III domains 10 and 11 of TN-X.	Dermatan Sulfate	38-54	tenascin XB	Homo sapiens	168-172
11139592-4	2001	GalNAc-4-ST2 transfers sulfate to the C-4 hydroxyl of terminal beta1,4-linked GalNAc in the sequence GalNAc-beta1,4GlcNAcbeta-R found on N-linked oligosaccharides and nonterminal beta1,4-linked GalNAc in chondroitin and dermatan.	Dermatan Sulfate	220-228	carbohydrate sulfotransferase 9	Homo sapiens	0-12
11322427-1	2001	PURPOSE: Maroteaux-Lamy syndrome is one of the mucopolysaccharidoses caused by enzyme deficiency (arylsulfatase B) that leads to incomplete degradation and storage of dermatan sulfate.	Dermatan Sulfate	167-183	arylsulfatase B	Homo sapiens	98-113
11692908-8	2001	To reduce thrombin generation, i.e., the mechanism by which heparin-induced thrombocytopenia induces thrombotic events, intravenous treatment with dermatan sulphate and low-dose urokinase was initiated.	Dermatan Sulfate	147-164	coagulation factor II, thrombin	Homo sapiens	10-18
11050699-0	2000	Pharmacodynamic study of low molecular weight dermatan sulphate (Desmin) after a single subcutaneous administration in patients with renal insufficiency.	Dermatan Sulfate	46-63	desmin	Homo sapiens	65-71
11290371-1	2001	In the current study, two specific glycosaminoglycan lyases, chondroitinase AC and chondroitinase B, were utilized to examine the roles of chondroitin sulfates and dermatan sulfate in tumor metastasis and angiogenesis.	Dermatan Sulfate	164-180	galactosamine (N-acetyl)-6-sulfatase	Homo sapiens	83-97
11732625-3	2001	Insulin and WGA stimulated [3H]glucosamine incorporation into hyaluronic acid (HA) and heparan sulphate (HS) without any alteration of chondroitin sulphate (CS) and dermatan sulphate (DS) contents.	Dermatan Sulfate	184-186	insulin	Homo sapiens	0-7
10871629-1	2000	N-Acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST), which transfers sulfate from 3"-phosphoadenosine 5"-phosphosulfate (PAPS) to position 6 of N-acetylgalactosamine 4-sulfate in chondroitin sulfate and dermatan sulfate, was purified 19,600-fold to apparent homogeneity from the squid cartilage.	Dermatan Sulfate	219-235	carbohydrate sulfotransferase 15	Homo sapiens	54-66
10974347-2	2000	In contrast, surface-bound thrombin is not resistant to inhibition by heparin cofactor II (HCII) and its acceleration of its inhibitory effect by dermatan sulfate.	Dermatan Sulfate	146-162	prothrombin	Oryctolagus cuniculus	27-35
10974347-4	2000	Recently, a novel HCII agonist, Intimatan, has been synthesized by site-specific sulphation of highly purified dermatan sulfate comprising primarily of L-iduronic acid-4-O-sulphated N-acetyl-D-galactosamine, yielding a 4, 6-O-disulphate compound on the galactopyranose ring with a lower molecular weight, higher solubility, and specific activity than its parent, dermatan sulfate.	Dermatan Sulfate	111-127	heparin cofactor 2	Oryctolagus cuniculus	18-22
10974347-4	2000	Recently, a novel HCII agonist, Intimatan, has been synthesized by site-specific sulphation of highly purified dermatan sulfate comprising primarily of L-iduronic acid-4-O-sulphated N-acetyl-D-galactosamine, yielding a 4, 6-O-disulphate compound on the galactopyranose ring with a lower molecular weight, higher solubility, and specific activity than its parent, dermatan sulfate.	Dermatan Sulfate	363-379	heparin cofactor 2	Oryctolagus cuniculus	18-22
10963998-1	2000	Decorin and glypican are two examples of exclusively chondroitin/dermatan sulfate and heparan sulfate-substituted proteoglycans, respectively.	Dermatan Sulfate	65-81	glypican 1	Homo sapiens	12-20
10961890-6	2000	Soluble heparin, heparan sulfate, chondroitin sulfate, and dermatan sulfate were shown to inhibit the hIL-10-induced expression of CD16 and CD64 in a concentration-dependent manner.	Dermatan Sulfate	59-75	interleukin 10	Homo sapiens	102-108
10961890-6	2000	Soluble heparin, heparan sulfate, chondroitin sulfate, and dermatan sulfate were shown to inhibit the hIL-10-induced expression of CD16 and CD64 in a concentration-dependent manner.	Dermatan Sulfate	59-75	Fc gamma receptor IIIa	Homo sapiens	131-135
10961890-6	2000	Soluble heparin, heparan sulfate, chondroitin sulfate, and dermatan sulfate were shown to inhibit the hIL-10-induced expression of CD16 and CD64 in a concentration-dependent manner.	Dermatan Sulfate	59-75	Fc gamma receptor Ia	Homo sapiens	140-144
11776053-16	2000	GAG was similar to dermatan sulfate both in the efficiency and in the mechanism of antithrombin.	Dermatan Sulfate	19-35	serpin family C member 1	Homo sapiens	83-95
10866805-9	2000	These results suggest that midkine binds to a polysulfated domain in the chondroitin sulfate chain with a region of dermatan sulfate structure.	Dermatan Sulfate	116-132	midkine	Mus musculus	27-34
10781601-7	2000	Surprisingly, proteins expressed by these cDNAs transferred sulfate to the C-4 position of N-acetylgalactosamine in chondroitin and desulfated dermatan sulfate, thus we named these two enzymes, chondroitin 4-O-sulfotransferase 1 and -2 (C4ST-1 and C4ST-2).	Dermatan Sulfate	143-159	carbohydrate sulfotransferase 11	Homo sapiens	194-235
10781601-11	2000	These results indicate C4ST-1 and C4ST-2 play complementary roles in chondroitin and dermatan sulfate synthesis in different tissues.	Dermatan Sulfate	85-101	carbohydrate sulfotransferase 11	Homo sapiens	23-29
10781601-7	2000	Surprisingly, proteins expressed by these cDNAs transferred sulfate to the C-4 position of N-acetylgalactosamine in chondroitin and desulfated dermatan sulfate, thus we named these two enzymes, chondroitin 4-O-sulfotransferase 1 and -2 (C4ST-1 and C4ST-2).	Dermatan Sulfate	143-159	carbohydrate sulfotransferase 11	Homo sapiens	237-243
10781601-11	2000	These results indicate C4ST-1 and C4ST-2 play complementary roles in chondroitin and dermatan sulfate synthesis in different tissues.	Dermatan Sulfate	85-101	carbohydrate sulfotransferase 12	Homo sapiens	34-40
10781601-7	2000	Surprisingly, proteins expressed by these cDNAs transferred sulfate to the C-4 position of N-acetylgalactosamine in chondroitin and desulfated dermatan sulfate, thus we named these two enzymes, chondroitin 4-O-sulfotransferase 1 and -2 (C4ST-1 and C4ST-2).	Dermatan Sulfate	143-159	carbohydrate sulfotransferase 12	Homo sapiens	248-254
10781601-9	2000	Moreover, analysis of (35)S-labeled dermatan sulfate formed by C4ST-1 indicate that sulfation preferentially took place in GlcA-->GalNAc unit than in IdoA-->GalNAc unit, suggesting that 4-O-sulfation at N-acetylgalactosamine may precede epimerization of glucuronic acid to iduronic acid during dermatan sulfate biosynthesis.	Dermatan Sulfate	36-52	carbohydrate sulfotransferase 11	Homo sapiens	63-69
10773191-2	2000	Here we provide evidence that TN-R derived from adult mouse brain expresses chondroitin sulfate (CS) glycosaminoglycans (GAGs), i.e. C-6S and C-4S, that are recognized by the CS/dermatan sulfate-specific monoclonal antibodies 473 HD and CS-56.	Dermatan Sulfate	178-194	tenascin R	Mus musculus	30-34
10747885-1	2000	Hepatocyte growth factor/scatter factor (HGF/SF) is a heparan/dermatan sulfate-binding growth factor produced by stromal cells that acts as a paracrine effector on neighboring epithelia.	Dermatan Sulfate	62-78	hepatocyte growth factor	Homo sapiens	41-47
10749870-0	2000	Altered dermatan sulfate structure and reduced heparin cofactor II-stimulating activity of biglycan and decorin from human atherosclerotic plaque.	Dermatan Sulfate	8-24	biglycan	Homo sapiens	91-99
10749870-1	2000	Biglycan and decorin are small dermatan sulfate-containing proteoglycans in the extracellular matrix of the artery wall.	Dermatan Sulfate	31-47	biglycan	Homo sapiens	0-8
10749870-2	2000	The dermatan sulfate chains are known to stimulate thrombin inhibition by heparin cofactor II (HCII), a plasma proteinase inhibitor that has been detected within the artery wall.	Dermatan Sulfate	4-20	coagulation factor II, thrombin	Homo sapiens	51-59
10749870-2	2000	The dermatan sulfate chains are known to stimulate thrombin inhibition by heparin cofactor II (HCII), a plasma proteinase inhibitor that has been detected within the artery wall.	Dermatan Sulfate	4-20	serpin family D member 1	Homo sapiens	74-93
10749870-2	2000	The dermatan sulfate chains are known to stimulate thrombin inhibition by heparin cofactor II (HCII), a plasma proteinase inhibitor that has been detected within the artery wall.	Dermatan Sulfate	4-20	serpin family D member 1	Homo sapiens	95-99
10753952-1	2000	Heparin cofactor II (HCII) is a plasma serine protease inhibitor whose ability to inhibit alpha-thrombin is accelerated by a variety of sulfated polysaccharides in addition to heparin and dermatan sulfate.	Dermatan Sulfate	188-204	serpin family D member 1	Homo sapiens	0-19
10753952-1	2000	Heparin cofactor II (HCII) is a plasma serine protease inhibitor whose ability to inhibit alpha-thrombin is accelerated by a variety of sulfated polysaccharides in addition to heparin and dermatan sulfate.	Dermatan Sulfate	188-204	serpin family D member 1	Homo sapiens	21-25
10625699-8	2000	Specifically, TGF-beta(1) induced an accumulation of small chondroitin/dermatan sulfate PGs (CS/DSPGs) with core proteins of approximately 50 kDa in the medium of both dense and sparse cultures, but a cell layer-associated heparan sulfate PG with a core protein size of approximately 400 kDa accumulated only in dense cultures.	Dermatan Sulfate	71-87	transforming growth factor beta 1	Bos taurus	14-25
10706937-1	2000	Heparin cofactor II is postulated to be an extravascular thrombin inhibitor that is physiologically stimulated by dermatan sulfate.	Dermatan Sulfate	114-130	serpin family D member 1	Rattus norvegicus	0-19
10706937-1	2000	Heparin cofactor II is postulated to be an extravascular thrombin inhibitor that is physiologically stimulated by dermatan sulfate.	Dermatan Sulfate	114-130	coagulation factor II	Rattus norvegicus	57-65
10702409-0	2000	Impaired elastogenesis in Hurler disease: dermatan sulfate accumulation linked to deficiency in elastin-binding protein and elastic fiber assembly.	Dermatan Sulfate	42-58	elastin	Homo sapiens	96-103
10702409-1	2000	Hurler disease resulting from a deficiency in alpha-L-iduronidase, which causes an accumulation of dermatan sulfate and heparan sulfate glycosaminoglycans, is characterized by connective tissue and skeletal deformations, cardiomyopathy, cardiac valve defects, and progressive coronary artery stenosis.	Dermatan Sulfate	99-115	alpha-L-iduronidase	Homo sapiens	46-65
10702409-3	2000	Our data suggest that dermatan sulfate-bearing moieties bind to and cause functional inactivation of the 67-kd elastin-binding protein, a molecular chaperone for tropoelastin, which normally facilitates its secretion and assembly into elastic fibers.	Dermatan Sulfate	22-38	elastin	Homo sapiens	111-118
10702409-3	2000	Our data suggest that dermatan sulfate-bearing moieties bind to and cause functional inactivation of the 67-kd elastin-binding protein, a molecular chaperone for tropoelastin, which normally facilitates its secretion and assembly into elastic fibers.	Dermatan Sulfate	22-38	elastin	Homo sapiens	162-174
10723065-4	2000	Here we provide first evidence that TN-R derived from whole rat brain or cultured oligodendrocytes expresses chondroitin sulfate (CS) glycosaminoglycans (GAGs), i.e., C-4S and C-6S, that are recognized by CS-56, a CS/dermatan sulfate-specific monoclonal antibody.	Dermatan Sulfate	217-233	tenascin R	Rattus norvegicus	36-40
10640393-7	2000	The slower migrating species is absent in normal ligaments and may represent a different glycoform (containing either a single or two short chondroitin/dermatan sulfate chains) of biglycan.	Dermatan Sulfate	152-168	biglycan	Oryctolagus cuniculus	180-188
10623797-6	2000	Enzyme treatment of mouse mast cells revealed that binding of IFN-gamma was predominantly to chondroitin sulfate B (dermatan sulfate).	Dermatan Sulfate	93-114	interferon gamma	Mus musculus	62-71
10623797-6	2000	Enzyme treatment of mouse mast cells revealed that binding of IFN-gamma was predominantly to chondroitin sulfate B (dermatan sulfate).	Dermatan Sulfate	116-132	interferon gamma	Mus musculus	62-71
10623797-7	2000	Binding of IFN-gamma to dermatan sulfate was confirmed by inhibition ELISA.	Dermatan Sulfate	24-40	interferon gamma	Mus musculus	11-20
10536375-11	1999	Overall, these results show that the inhibitory action of DCN is dependent of substratum binding, is differentially mediated by its glycosaminoglycan side chains (chondroitin-sulfate vs. dermatan-sulfate chains), and is independent of a steric hindrance effect exerted by its glycosaminoglycan side chains.	Dermatan Sulfate	187-203	decorin	Homo sapiens	58-61
10600521-5	1999	In vitro, different glycosaminoglycans, such as dermatan sulfate and chondroitin sulfate-C, also induce a dimer assembly of HARP.	Dermatan Sulfate	48-64	pleiotrophin	Homo sapiens	124-128
10632469-2	1999	In an in vitro test, bovine intestine dermatan sulfate exhibited stronger effects on stimulation of heparin cofactor II and activation of Glu-plasminogen by tissue plasminogen activator.	Dermatan Sulfate	38-54	serpin family D member 1	Bos taurus	100-119
10661319-8	1999	This coordinated distribution suggests that stromelysin-1 may have a functional role, being implicated in predentine in the degradation of chondroitin-4-sulphate/dermatan sulphate-containing proteoglycans, and consequently allowing keratan sulphate proteoglycan concentration to increase near the border where mineralization is initiated.	Dermatan Sulfate	162-179	matrix metallopeptidase 3	Rattus norvegicus	44-57
11008173-1	2000	We have shown previously in the rat that biglycan, a recently discovered chondroitin sulfate proteoglycan, has neurotrophic effects which are mediated by its chondroitin/dermatan sulfate chains.	Dermatan Sulfate	170-186	biglycan	Rattus norvegicus	41-49
10536375-7	1999	DCN bearing dermatan-sulfate chains (i.e., skin and cartilage DCN) was about 20-fold more effective in inhibiting cell migration than DCN bearing chondroitin-sulfate chains (i.e., bone DCN).	Dermatan Sulfate	12-28	decorin	Homo sapiens	0-3
10536375-7	1999	DCN bearing dermatan-sulfate chains (i.e., skin and cartilage DCN) was about 20-fold more effective in inhibiting cell migration than DCN bearing chondroitin-sulfate chains (i.e., bone DCN).	Dermatan Sulfate	12-28	decorin	Homo sapiens	62-65
10536375-7	1999	DCN bearing dermatan-sulfate chains (i.e., skin and cartilage DCN) was about 20-fold more effective in inhibiting cell migration than DCN bearing chondroitin-sulfate chains (i.e., bone DCN).	Dermatan Sulfate	12-28	decorin	Homo sapiens	62-65
10907447-3	1999	Included among these compounds are indirect thrombin inhibitors such as dermatan sulfate, heparanoids and low-molecular weight heparin.	Dermatan Sulfate	72-88	coagulation factor II, thrombin	Homo sapiens	44-52
10536375-9	1999	These data assert that the dermatan-sulfate chains of DCN are responsible for a negative influence on cell migration.	Dermatan Sulfate	27-43	decorin	Homo sapiens	54-57
10496984-0	1999	Matrix localization of tissue factor pathway inhibitor-2/matrix-associated serine protease inhibitor (TFPI-2/MSPI) involves arginine-mediated ionic interactions with heparin and dermatan sulfate: heparin accelerates the activity of TFPI-2/MSPI toward plasmin.	Dermatan Sulfate	178-194	tissue factor pathway inhibitor 2	Homo sapiens	23-56
10496984-0	1999	Matrix localization of tissue factor pathway inhibitor-2/matrix-associated serine protease inhibitor (TFPI-2/MSPI) involves arginine-mediated ionic interactions with heparin and dermatan sulfate: heparin accelerates the activity of TFPI-2/MSPI toward plasmin.	Dermatan Sulfate	178-194	tissue factor pathway inhibitor 2	Homo sapiens	102-108
10496984-12	1999	Collectively, our results demonstrate that conformation-dependent arginine-mediated ionic interactions are responsible for the TFPI-2/MSPI triplet binding to fibroblast ECM, heparin, and dermatan sulfate and that heparin augmented the rate of inhibition of plasmin by TFPI-2/MSPI.	Dermatan Sulfate	187-203	tissue factor pathway inhibitor 2	Homo sapiens	127-133
10496984-0	1999	Matrix localization of tissue factor pathway inhibitor-2/matrix-associated serine protease inhibitor (TFPI-2/MSPI) involves arginine-mediated ionic interactions with heparin and dermatan sulfate: heparin accelerates the activity of TFPI-2/MSPI toward plasmin.	Dermatan Sulfate	178-194	tissue factor pathway inhibitor 2	Homo sapiens	232-238
10496984-0	1999	Matrix localization of tissue factor pathway inhibitor-2/matrix-associated serine protease inhibitor (TFPI-2/MSPI) involves arginine-mediated ionic interactions with heparin and dermatan sulfate: heparin accelerates the activity of TFPI-2/MSPI toward plasmin.	Dermatan Sulfate	178-194	plasminogen	Homo sapiens	251-258
10496984-5	1999	We found that TFPI-2/MSPI bound specifically to heparin and dermatan sulfate.	Dermatan Sulfate	60-76	tissue factor pathway inhibitor 2	Homo sapiens	14-20
10496984-7	1999	However, binding affinity for TFPI-2/MSPI with heparin was 250-300 times greater than that for TFPI-2/MSPI with dermatan sulfate.	Dermatan Sulfate	112-128	tissue factor pathway inhibitor 2	Homo sapiens	95-101
10488098-0	1999	Comparison of heparin- and dermatan sulfate-mediated catalysis of thrombin inactivation by heparin cofactor II.	Dermatan Sulfate	27-43	coagulation factor II, thrombin	Homo sapiens	66-74
10488098-0	1999	Comparison of heparin- and dermatan sulfate-mediated catalysis of thrombin inactivation by heparin cofactor II.	Dermatan Sulfate	27-43	serpin family D member 1	Homo sapiens	91-110
10488098-1	1999	Heparin and dermatan sulfate activate heparin cofactor II (HCII) comparably, presumably by liberating the amino terminus of HCII to bind to exosite I of thrombin.	Dermatan Sulfate	12-28	serpin family D member 1	Homo sapiens	38-57
10488098-1	1999	Heparin and dermatan sulfate activate heparin cofactor II (HCII) comparably, presumably by liberating the amino terminus of HCII to bind to exosite I of thrombin.	Dermatan Sulfate	12-28	serpin family D member 1	Homo sapiens	59-63
10488098-1	1999	Heparin and dermatan sulfate activate heparin cofactor II (HCII) comparably, presumably by liberating the amino terminus of HCII to bind to exosite I of thrombin.	Dermatan Sulfate	12-28	serpin family D member 1	Homo sapiens	124-128
10488098-1	1999	Heparin and dermatan sulfate activate heparin cofactor II (HCII) comparably, presumably by liberating the amino terminus of HCII to bind to exosite I of thrombin.	Dermatan Sulfate	12-28	coagulation factor II, thrombin	Homo sapiens	153-161
10488098-7	1999	Fluorescence spectroscopy revealed that dermatan sulfate evokes greater conformational changes in HCII than heparin, suggesting that dermatan sulfate stimulates HCII by producing more effective displacement of the amino terminus.	Dermatan Sulfate	40-56	serpin family D member 1	Homo sapiens	98-102
10488098-7	1999	Fluorescence spectroscopy revealed that dermatan sulfate evokes greater conformational changes in HCII than heparin, suggesting that dermatan sulfate stimulates HCII by producing more effective displacement of the amino terminus.	Dermatan Sulfate	133-149	serpin family D member 1	Homo sapiens	98-102
10488098-7	1999	Fluorescence spectroscopy revealed that dermatan sulfate evokes greater conformational changes in HCII than heparin, suggesting that dermatan sulfate stimulates HCII by producing more effective displacement of the amino terminus.	Dermatan Sulfate	133-149	serpin family D member 1	Homo sapiens	161-165
10494755-1	1999	Heparin cofactor II (HCII) is a specific inhibitor of thrombin in the presence of heparin or dermatan sulphate.	Dermatan Sulfate	93-110	serpin family D member 1	Homo sapiens	0-19
10596456-1	1999	BACKGROUND: The MPS-I is an autosomal recessive disorder caused by mutations in the IDUA gene that induce to a deficiency of glycosidase alpha-L-iduronidase that is required for degradation of heparan and dermatan sulfate.	Dermatan Sulfate	205-221	alpha-L-iduronidase	Homo sapiens	84-88
10596456-1	1999	BACKGROUND: The MPS-I is an autosomal recessive disorder caused by mutations in the IDUA gene that induce to a deficiency of glycosidase alpha-L-iduronidase that is required for degradation of heparan and dermatan sulfate.	Dermatan Sulfate	205-221	alpha-L-iduronidase	Homo sapiens	137-156
10494755-1	1999	Heparin cofactor II (HCII) is a specific inhibitor of thrombin in the presence of heparin or dermatan sulphate.	Dermatan Sulfate	93-110	serpin family D member 1	Homo sapiens	21-25
10494755-1	1999	Heparin cofactor II (HCII) is a specific inhibitor of thrombin in the presence of heparin or dermatan sulphate.	Dermatan Sulfate	93-110	coagulation factor II, thrombin	Homo sapiens	54-62
10187838-0	1999	Molecular cloning and characterization of a human uronyl 2-sulfotransferase that sulfates iduronyl and glucuronyl residues in dermatan/chondroitin sulfate.	Dermatan Sulfate	126-134	uronyl 2-sulfotransferase	Homo sapiens	50-75
10456450-3	1999	Agents that selectively inhibit thrombin, such as dermatan sulphate, have potential for a favourable benefit-risk ratio in the prevention of this complication.	Dermatan Sulfate	50-67	coagulation factor II, thrombin	Homo sapiens	32-40
10341217-1	1999	Hepatocyte growth factor interacts with both heparan and dermatan sulphates, in addition to its specific signalling receptor, Met.	Dermatan Sulfate	57-75	hepatocyte growth factor	Canis lupus familiaris	0-24
10318803-8	1999	These results altogether indicate that EXTL2/EXTR2 encodes the alpha1,4-N-acetylhexosaminyltransferase that transfers GalNAc/GlcNAc to the tetrasaccharide representing the common glycosaminoglycan-protein linkage region and that is most likely the critical enzyme that determines and initiates the heparin/heparan sulfate synthesis, separating it from the chondroitin sulfate/dermatan sulfate synthesis.	Dermatan Sulfate	376-392	exostosin like glycosyltransferase 2	Homo sapiens	39-44
10318803-8	1999	These results altogether indicate that EXTL2/EXTR2 encodes the alpha1,4-N-acetylhexosaminyltransferase that transfers GalNAc/GlcNAc to the tetrasaccharide representing the common glycosaminoglycan-protein linkage region and that is most likely the critical enzyme that determines and initiates the heparin/heparan sulfate synthesis, separating it from the chondroitin sulfate/dermatan sulfate synthesis.	Dermatan Sulfate	376-392	exostosin like glycosyltransferase 2	Homo sapiens	45-50
10225976-0	1999	Dermatan sulfate activates nuclear factor-kappab and induces endothelial and circulating intercellular adhesion molecule-1.	Dermatan Sulfate	0-16	intercellular adhesion molecule 1	Homo sapiens	89-122
10225976-3	1999	Cultured human dermal microvascular endothelial cells exposed to DS responded with rapid nuclear translocation of nuclear factor-kappaB (NF-kappaB), increased expression of intercellular adhesion molecule-1 (ICAM-1) mRNA, and increased ICAM-1 cell surface protein.	Dermatan Sulfate	65-67	intercellular adhesion molecule 1	Homo sapiens	173-206
10225976-3	1999	Cultured human dermal microvascular endothelial cells exposed to DS responded with rapid nuclear translocation of nuclear factor-kappaB (NF-kappaB), increased expression of intercellular adhesion molecule-1 (ICAM-1) mRNA, and increased ICAM-1 cell surface protein.	Dermatan Sulfate	65-67	intercellular adhesion molecule 1	Homo sapiens	208-214
10225976-3	1999	Cultured human dermal microvascular endothelial cells exposed to DS responded with rapid nuclear translocation of nuclear factor-kappaB (NF-kappaB), increased expression of intercellular adhesion molecule-1 (ICAM-1) mRNA, and increased ICAM-1 cell surface protein.	Dermatan Sulfate	65-67	intercellular adhesion molecule 1	Homo sapiens	236-242
10225976-7	1999	The ICAM-1-inductive activity of DS was confirmed in vivo.	Dermatan Sulfate	33-35	intercellular adhesion molecule 1	Homo sapiens	4-10
10075664-5	1999	We report that heparan sulfate, dermatan sulfate, and to a lesser extent, chondroitin sulfate A, displaced HARP bound to the extracellular compartment.	Dermatan Sulfate	32-48	pleiotrophin	Mus musculus	107-111
10209287-8	1999	These results suggest that, like dermatan sulphate and heparin, other polyanions stimulate HCII primarily by an allosteric mechanism requiring the N-terminal acidic domain.	Dermatan Sulfate	33-50	serpin family D member 1	Homo sapiens	91-95
10209287-1	1999	A variety of sulphated polyanions in addition to heparin and dermatan sulphate stimulate the inhibition of thrombin by heparin cofactor II (HCII).	Dermatan Sulfate	61-78	coagulation factor II, thrombin	Homo sapiens	107-115
10209287-1	1999	A variety of sulphated polyanions in addition to heparin and dermatan sulphate stimulate the inhibition of thrombin by heparin cofactor II (HCII).	Dermatan Sulfate	61-78	serpin family D member 1	Homo sapiens	119-138
10209287-1	1999	A variety of sulphated polyanions in addition to heparin and dermatan sulphate stimulate the inhibition of thrombin by heparin cofactor II (HCII).	Dermatan Sulfate	61-78	serpin family D member 1	Homo sapiens	140-144
10209287-2	1999	Previous investigations indicated that the binding sites on HCII for heparin and dermatan sulphate overlap but are not identical.	Dermatan Sulfate	81-98	serpin family D member 1	Homo sapiens	60-64
10075664-6	1999	Binding analyses with a biosensor showed that HARP bound heparin with fast association and dissociation kinetics (kass = 1.6 x 10(6) M-1 s-1; kdiss = 0.02 s-1), yielding a Kd value of 13 nM; the interaction between HARP and dermatan sulfate was characterized by slower association kinetics (kass = 0.68 x 10(6) M-1 s-1) and a lower affinity (Kd = 51 nM).	Dermatan Sulfate	224-240	pleiotrophin	Mus musculus	46-50
10075664-7	1999	Exogenous heparin, heparan sulfate, and dermatan sulfate potentiated the growth-stimulatory activity of HARP, suggesting that corresponding proteoglycans could be involved in the regulation of the mitogenic activity of HARP.	Dermatan Sulfate	40-56	pleiotrophin	Mus musculus	104-108
10075664-7	1999	Exogenous heparin, heparan sulfate, and dermatan sulfate potentiated the growth-stimulatory activity of HARP, suggesting that corresponding proteoglycans could be involved in the regulation of the mitogenic activity of HARP.	Dermatan Sulfate	40-56	pleiotrophin	Mus musculus	219-223
10914239-1	1999	Danaparoid sodium is an antithrombin composed of 3 glycosaminoglycans: heparan sulfate, dermatan sulfate and chondroitin sulfate.	Dermatan Sulfate	88-104	serpin family C member 1	Homo sapiens	24-36
10384999-5	1999	Dermatan sulphate was rich in iduronic acid (62% of total uronic acid) and composed of non-sulphated (44%), and mono-sulphated disaccharides bearing esterified sulphate groups at positions C-4 (53%) or C-6 (3%) of the N-acetyl galactosamine.	Dermatan Sulfate	0-17	complement C4A (Rodgers blood group)	Homo sapiens	189-192
10384999-5	1999	Dermatan sulphate was rich in iduronic acid (62% of total uronic acid) and composed of non-sulphated (44%), and mono-sulphated disaccharides bearing esterified sulphate groups at positions C-4 (53%) or C-6 (3%) of the N-acetyl galactosamine.	Dermatan Sulfate	0-17	complement C6	Homo sapiens	202-205
10447264-5	1999	The disease is caused by the inability to degrade dermatan sulphate and heparan sulphate due to mutations in the iduronate-2-sulphatase gene (IDS).	Dermatan Sulfate	50-67	iduronate 2-sulfatase	Homo sapiens	142-145
10093889-5	1999	For example, we suggest that the heparin cofactor II (HCII) catalysts, dermatan sulfate and Intimatan, inhibit surface-bound thrombin more effectively than heparin/ATIII, thereby inhibiting intimal hyperplasia effectively.	Dermatan Sulfate	71-87	serpin family D member 1	Homo sapiens	33-52
10093889-5	1999	For example, we suggest that the heparin cofactor II (HCII) catalysts, dermatan sulfate and Intimatan, inhibit surface-bound thrombin more effectively than heparin/ATIII, thereby inhibiting intimal hyperplasia effectively.	Dermatan Sulfate	71-87	serpin family D member 1	Homo sapiens	54-58
10093889-5	1999	For example, we suggest that the heparin cofactor II (HCII) catalysts, dermatan sulfate and Intimatan, inhibit surface-bound thrombin more effectively than heparin/ATIII, thereby inhibiting intimal hyperplasia effectively.	Dermatan Sulfate	71-87	coagulation factor II, thrombin	Homo sapiens	125-133
10349131-1	1999	Heparin Cofactor II (HCII) is a glycoprotein in human plasma which inactivates thrombin rapidly in the presence of dermatan sulfate.	Dermatan Sulfate	115-131	serpin family D member 1	Homo sapiens	0-19
10349131-1	1999	Heparin Cofactor II (HCII) is a glycoprotein in human plasma which inactivates thrombin rapidly in the presence of dermatan sulfate.	Dermatan Sulfate	115-131	serpin family D member 1	Homo sapiens	21-25
10349131-1	1999	Heparin Cofactor II (HCII) is a glycoprotein in human plasma which inactivates thrombin rapidly in the presence of dermatan sulfate.	Dermatan Sulfate	115-131	coagulation factor II, thrombin	Homo sapiens	79-87
10349131-7	1999	HCII thrombin inhibition possibly takes place in extravascular sites where dermatan sulfate is present.	Dermatan Sulfate	75-91	serpin family D member 1	Homo sapiens	0-4
10349131-7	1999	HCII thrombin inhibition possibly takes place in extravascular sites where dermatan sulfate is present.	Dermatan Sulfate	75-91	coagulation factor II, thrombin	Homo sapiens	5-13
9837939-0	1998	Covalent heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate complexes.	Dermatan Sulfate	61-77	heparin cofactor 2	Oryctolagus cuniculus	9-28
9837939-0	1998	Covalent heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate complexes.	Dermatan Sulfate	61-77	heparin cofactor 2	Oryctolagus cuniculus	41-60
9837939-5	1998	Covalent heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate complexes had catalytic antithrombin activities similar to those of the corresponding starting heparin and dermatan sulfate (86% and 110% of standard heparin and dermatan sulfate activity, respectively).	Dermatan Sulfate	185-201	heparin cofactor 2	Oryctolagus cuniculus	41-60
9837939-2	1998	Heparin cofactor II is a naturally occurring anticoagulant that acts by specifically inhibiting thrombin and is facilitated by the binding of glycosaminoglycans such as heparin and dermatan sulfate.	Dermatan Sulfate	181-197	heparin cofactor 2	Oryctolagus cuniculus	0-19
9837939-5	1998	Covalent heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate complexes had catalytic antithrombin activities similar to those of the corresponding starting heparin and dermatan sulfate (86% and 110% of standard heparin and dermatan sulfate activity, respectively).	Dermatan Sulfate	185-201	heparin cofactor 2	Oryctolagus cuniculus	9-28
9837939-4	1998	We have produced permanently activated heparin cofactor II molecules by covalent linkage to either heparin or dermatan sulfate.	Dermatan Sulfate	110-126	heparin cofactor 2	Oryctolagus cuniculus	39-58
9837939-5	1998	Covalent heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate complexes had catalytic antithrombin activities similar to those of the corresponding starting heparin and dermatan sulfate (86% and 110% of standard heparin and dermatan sulfate activity, respectively).	Dermatan Sulfate	185-201	heparin cofactor 2	Oryctolagus cuniculus	41-60
9837939-6	1998	Both heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate had fast bimolecular rate constants of 1.4 x 10(7) M-1 s-1 and 1.3 x 10(7) M-1 s-1, respectively, for reaction with thrombin.	Dermatan Sulfate	57-73	heparin cofactor 2	Oryctolagus cuniculus	5-24
9837939-5	1998	Covalent heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate complexes had catalytic antithrombin activities similar to those of the corresponding starting heparin and dermatan sulfate (86% and 110% of standard heparin and dermatan sulfate activity, respectively).	Dermatan Sulfate	61-77	heparin cofactor 2	Oryctolagus cuniculus	41-60
9837939-6	1998	Both heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate had fast bimolecular rate constants of 1.4 x 10(7) M-1 s-1 and 1.3 x 10(7) M-1 s-1, respectively, for reaction with thrombin.	Dermatan Sulfate	57-73	heparin cofactor 2	Oryctolagus cuniculus	37-56
9837939-5	1998	Covalent heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate complexes had catalytic antithrombin activities similar to those of the corresponding starting heparin and dermatan sulfate (86% and 110% of standard heparin and dermatan sulfate activity, respectively).	Dermatan Sulfate	185-201	heparin cofactor 2	Oryctolagus cuniculus	9-28
9837939-6	1998	Both heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate had fast bimolecular rate constants of 1.4 x 10(7) M-1 s-1 and 1.3 x 10(7) M-1 s-1, respectively, for reaction with thrombin.	Dermatan Sulfate	57-73	prothrombin	Oryctolagus cuniculus	190-198
9813026-10	1998	The larger effects of the thrombin exosite-I mutants for HCII inhibition with heparin and dermatan sulfate indicate its need for exosite-I, presumably through contact of the "hirudin-like" domain of HCII with exosite-I of thrombin.	Dermatan Sulfate	90-106	coagulation factor II, thrombin	Homo sapiens	26-34
9837939-7	1998	The intravenous half-life of the covalent complexes in rabbits was significantly longer than that of free heparin or dermatan sulfate (4.4, 3.4, 0.33, and 0.50 h for heparin cofactor II-heparin, heparin cofactor II-dermatan sulfate, heparin, and dermatan sulfate, respectively).	Dermatan Sulfate	117-133	heparin cofactor 2	Oryctolagus cuniculus	166-185
9813026-10	1998	The larger effects of the thrombin exosite-I mutants for HCII inhibition with heparin and dermatan sulfate indicate its need for exosite-I, presumably through contact of the "hirudin-like" domain of HCII with exosite-I of thrombin.	Dermatan Sulfate	90-106	serpin family D member 1	Homo sapiens	199-203
9843172-1	1998	Heparin cofactor II (HCII) is a serpin that inhibits thrombin rapidly in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	100-116	serpin family D member 1	Homo sapiens	0-19
9774395-7	1998	In contrast dermatan sulfates from S. plicata and H. pyriformis are potent anticoagulants due to potentiation of thrombin inhibition by heparin cofactor II.	Dermatan Sulfate	12-29	coagulation factor II, thrombin	Homo sapiens	113-121
9774430-0	1998	Dermatan sulfate released after injury is a potent promoter of fibroblast growth factor-2 function.	Dermatan Sulfate	0-16	fibroblast growth factor 2	Homo sapiens	63-89
9774430-6	1998	Dermatan sulfate, and not heparan sulfate, was the major contributor to this activity, and dermatan sulfate bound FGF-2 with Kd = 2.48 microM.	Dermatan Sulfate	91-107	fibroblast growth factor 2	Homo sapiens	114-119
9774430-7	1998	These data demonstrate that proteoglycans released during wound repair are functionally active and provide the first evidence that dermatan sulfate is a potent mediator of fibroblast growth factor-2 responsiveness.	Dermatan Sulfate	131-147	fibroblast growth factor 2	Homo sapiens	172-198
9843172-1	1998	Heparin cofactor II (HCII) is a serpin that inhibits thrombin rapidly in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	100-116	serpin family D member 1	Homo sapiens	21-25
9843172-1	1998	Heparin cofactor II (HCII) is a serpin that inhibits thrombin rapidly in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	100-116	coagulation factor II, thrombin	Homo sapiens	53-61
9843172-3	1998	In this report, we show that both frog and chicken plasma contain a dermatan sulfate-dependent inhibitor that forms a 118-kDa complex with human 125I-thrombin.	Dermatan Sulfate	68-84	coagulation factor II, thrombin	Homo sapiens	150-158
9727420-7	1998	The increases were associated with highly charged molecular forms of decorin and biglycan, indicating modification of the proteins with dermatan sulfate chains of increased sulfation.	Dermatan Sulfate	136-152	decorin	Homo sapiens	69-76
9727420-9	1998	CONCLUSIONS: The increased dermatan sulfate associated with chronic corneal pathologic conditions results from stromal accumulation of decorin and particularly of biglycan in the affected corneas.	Dermatan Sulfate	27-43	decorin	Homo sapiens	135-142
9727420-9	1998	CONCLUSIONS: The increased dermatan sulfate associated with chronic corneal pathologic conditions results from stromal accumulation of decorin and particularly of biglycan in the affected corneas.	Dermatan Sulfate	27-43	biglycan	Homo sapiens	163-171
9727420-7	1998	The increases were associated with highly charged molecular forms of decorin and biglycan, indicating modification of the proteins with dermatan sulfate chains of increased sulfation.	Dermatan Sulfate	136-152	biglycan	Homo sapiens	81-89
9725536-3	1998	Scheie syndrome (MPS I S) is due to the deficient activity of alpha-L-iduronidase leading to the intralysosomal accumulation of dermatan sulfate and heparan sulfate.	Dermatan Sulfate	128-144	alpha-L-iduronidase	Homo sapiens	62-81
9694594-1	1998	Collagen XIV is known to bind to the dermatan sulfate chain of decorin and to the heparan sulfate chain of perlecan.	Dermatan Sulfate	37-53	collagen type XIV alpha 1 chain	Gallus gallus	0-12
9692613-3	1998	The increase in thrombin-heparin cofactor II complexes suggests that the site of the additional thrombin generation is relatively rich in dermatan sulfate.	Dermatan Sulfate	138-154	coagulation factor II, thrombin	Homo sapiens	16-24
9692613-3	1998	The increase in thrombin-heparin cofactor II complexes suggests that the site of the additional thrombin generation is relatively rich in dermatan sulfate.	Dermatan Sulfate	138-154	coagulation factor II, thrombin	Homo sapiens	96-104
9692613-11	1998	The role of this placental dermatan sulfate in local regulation of thrombin in the placenta warrants further study.	Dermatan Sulfate	27-43	coagulation factor II, thrombin	Homo sapiens	67-75
9268591-7	1997	A significant decrease of dermatan sulfate levels with aging correlates well with the observed increase in the level of beta-glucuronidase activity.	Dermatan Sulfate	26-42	glucuronidase beta	Homo sapiens	120-138
9684733-0	1998	Pharmacokinetics of low molecular weight dermatan sulphate (desmin) in different cohorts of patients.	Dermatan Sulfate	41-58	desmin	Homo sapiens	60-66
9568695-7	1998	Other sulfated GAGs and related macromolecules were also effective in the enhancement of amylin fibril formation in the order of heparin > heparan sulfate > chondroitin-4-sulfate = dermatan sulfate = dextran sulfate > pentosan polysulfate, implicating the importance of the specific GAG/carbohydrate backbone.	Dermatan Sulfate	187-203	islet amyloid polypeptide	Homo sapiens	89-95
9485475-1	1998	Heparin cofactor II (HCII) inhibits thrombin rapidly in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	83-99	serpin family D member 1	Homo sapiens	0-19
9485475-1	1998	Heparin cofactor II (HCII) inhibits thrombin rapidly in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	83-99	serpin family D member 1	Homo sapiens	21-25
9485475-1	1998	Heparin cofactor II (HCII) inhibits thrombin rapidly in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	83-99	coagulation factor II, thrombin	Homo sapiens	36-44
9417075-1	1998	We have demonstrated by affinity chromatography that hepatocyte growth factor/scatter factor (HGF/SF) binds strongly to dermatan sulfate (DS), with a similar ionic strength dependence to that previously seen with heparan sulfate (HS).	Dermatan Sulfate	120-136	hepatocyte growth factor	Homo sapiens	94-100
9417075-1	1998	We have demonstrated by affinity chromatography that hepatocyte growth factor/scatter factor (HGF/SF) binds strongly to dermatan sulfate (DS), with a similar ionic strength dependence to that previously seen with heparan sulfate (HS).	Dermatan Sulfate	138-140	hepatocyte growth factor	Homo sapiens	94-100
9353333-5	1997	Purified recombinant meizothrombin and meizothrombin(desF1) were inhibited by HCII in the presence of dermatan sulfate with maximal second-order rate constants of 8 x 10(6) M-1.min-1 and 1.8 x 10(7) M-1.min-1, respectively, but were inhibited less than one-tenth as fast by AT in the presence of heparin.	Dermatan Sulfate	102-118	serpin family D member 1	Homo sapiens	78-82
9353333-7	1997	When HCII and dermatan sulfate were present continuously during the prothrombinase reaction, meizothrombin was trapped as a sodium dodecyl sulfate-stable complex with HCII and no amidolytic activity could be detected with a thrombin substrate.	Dermatan Sulfate	14-30	serpin family D member 1	Homo sapiens	167-171
9353333-7	1997	When HCII and dermatan sulfate were present continuously during the prothrombinase reaction, meizothrombin was trapped as a sodium dodecyl sulfate-stable complex with HCII and no amidolytic activity could be detected with a thrombin substrate.	Dermatan Sulfate	14-30	coagulation factor II, thrombin	Homo sapiens	71-79
9425437-1	1997	Hurler syndrome (mucopolysaccharidosis IH or MPS IH) is a congenital mucopolysaccharide storage disorder resulting from a genetic deficiency of alpha-L-iduronidase (IDUA), which is required for lysosomal degradation of glycosaminoglycans heparan sulfate and dermatan sulfate.	Dermatan Sulfate	258-274	alpha-L-iduronidase	Homo sapiens	144-163
9425437-1	1997	Hurler syndrome (mucopolysaccharidosis IH or MPS IH) is a congenital mucopolysaccharide storage disorder resulting from a genetic deficiency of alpha-L-iduronidase (IDUA), which is required for lysosomal degradation of glycosaminoglycans heparan sulfate and dermatan sulfate.	Dermatan Sulfate	258-274	alpha-L-iduronidase	Homo sapiens	165-169
9394322-1	1997	BACKGROUND: Dermatan sulphate (DS) is a selective thrombin inhibitor with antithrombotic properties and low bleeding potential.	Dermatan Sulfate	12-29	coagulation factor II, thrombin	Homo sapiens	50-58
9394322-1	1997	BACKGROUND: Dermatan sulphate (DS) is a selective thrombin inhibitor with antithrombotic properties and low bleeding potential.	Dermatan Sulfate	31-33	coagulation factor II, thrombin	Homo sapiens	50-58
9305797-8	1997	The glycosaminoglycan chains on both decorin and biglycan were identified as dermatan sulphate by their susceptibility to chondroitinase-B.	Dermatan Sulfate	77-94	decorin	Bos taurus	37-44
9305797-8	1997	The glycosaminoglycan chains on both decorin and biglycan were identified as dermatan sulphate by their susceptibility to chondroitinase-B.	Dermatan Sulfate	77-94	biglycan	Bos taurus	49-57
9682679-11	1998	An increase in the length of the dermatan sulphate chain on decorin, a previously reported characteristic of this glycosaminoglycan in hypertrophic scar, was seen in all but two of the strains treated with transforming growth factor-beta 1.	Dermatan Sulfate	33-50	transforming growth factor beta 1	Homo sapiens	206-239
9626917-0	1998	Desmin (a low molecular weight dermatan sulphate) versus heparin in the treatment of patients with deep venous thrombosis.	Dermatan Sulfate	31-48	desmin	Homo sapiens	0-6
9626917-1	1998	OBJECTIVE: There is theoretical and experimental evidence which indicates that Desmin, a low molecular weight dermatan sulphate, could be an attractive alternative to heparin in the treatment of deep venous thrombosis (DVT).	Dermatan Sulfate	110-127	desmin	Homo sapiens	79-85
9488672-7	1998	The affinity of HPRG for various GAGs measured in a competition assay decreased in the following order: heparin > dermatan sulfate > heparan sulfate > chondroitin sulfate A.	Dermatan Sulfate	117-133	histidine rich glycoprotein	Homo sapiens	16-20
9488672-8	1998	Binding of HPRG to immobilized dermatan sulfate had a midpoint at pH 6.5, was less influenced by zinc, and exhibited cooperativity.	Dermatan Sulfate	31-47	histidine rich glycoprotein	Homo sapiens	11-15
9255408-3	1997	The results of these studies on 12 sliced layers (average thickness of 250 microns) of skin show that the content of glucuronic acid in DS decreases when moving from the outer surface of the skin to the inside, while the degree of sulfation of the C-2 hydroxy group of iduronate and the C-4 and C-6 hydroxy groups of N-acetylgalactosamine increases with depth.	Dermatan Sulfate	136-138	complement C4A (Rodgers blood group)	Homo sapiens	287-298
9266027-6	1997	These results suggest that the increased amount of dermatan/chondroitin sulphate in SSc fibroblasts reflects an enhanced expression of decorin core protein.	Dermatan Sulfate	51-60	decorin	Homo sapiens	135-142
9153251-11	1997	The known inhibitors of the interaction of alpha-dystroglycan with laminin-1, including EDTA, sulfatide, fucoidan, dextran sulfate, heparin, and sialic acid, also perturbed the adhesion of RT4 cells to laminin-1, whereas the reagents which do not inhibit the interaction, including dextran, chondroitin sulfate, dermatan sulfate, and GlcNAc, did not.	Dermatan Sulfate	312-328	dystroglycan 1	Homo sapiens	49-61
9240182-6	1997	HPLC showed that CSBS contained a small amount of dermatan sulphate and abundant heparan sulphate, both of which inhibited crystal growth.	Dermatan Sulfate	50-67	filamin A	Homo sapiens	17-21
9240182-7	1997	CONCLUSION: Both heparan sulphate and dermatan sulphate may inhibit calcium oxalate crystallization, the former being the predominant GAG in CSBS.	Dermatan Sulfate	38-55	filamin A	Homo sapiens	141-145
9165101-4	1997	Furthermore, a lower, but significant Ca2(+)-independent binding of SAP to heparan sulfate, dermatan sulfate, AA protein and the amyloid precursor protein beta2M was observed.	Dermatan Sulfate	92-108	amyloid P component, serum	Homo sapiens	68-71
15622771-4	1997	CONCLUSION: Sjamp was similar to dermatan sulfate both in the efficiency and in the mechanism of antithrombin.	Dermatan Sulfate	33-49	serpin family C member 1	Homo sapiens	97-109
9124611-4	1997	The diminished activity of oxidized SLPI could be almost completely restored when an iduronate-containing glycosaminoglycan, such as heparin, heparan sulfate, or dermatan sulfate, was added to the reaction medium.	Dermatan Sulfate	162-178	secretory leukocyte peptidase inhibitor	Homo sapiens	36-40
9100165-2	1997	Ten patients affected by proximal deep venous thrombosis were treated in an open study with a low-molecular-weight dermatan sulphate (Desmin), administered at doses of 400 mg (intravenous bolus) followed by 1200 mg/day infused intravenously for 10 days, without activated partial thromboplastin adjustment.	Dermatan Sulfate	115-132	desmin	Homo sapiens	134-140
8995662-8	1997	Our biosensor analyses showed that both heparan sulfate and dermatan sulfate inhibited gB2 binding (ED50 = 1 to 5 microg/ml), indicating that gB2 interacts with both heparin-like and dermatan sulfate glycosaminoglycans.	Dermatan Sulfate	60-76	gamma-aminobutyric acid type B receptor subunit 2	Homo sapiens	87-90
9068899-0	1997	Mechanism of thrombin inhibition by heparin cofactor II in the presence of dermatan sulphates, native or oversulphated, and a heparin-like dextran derivative.	Dermatan Sulfate	75-93	coagulation factor II, thrombin	Homo sapiens	13-21
9068899-0	1997	Mechanism of thrombin inhibition by heparin cofactor II in the presence of dermatan sulphates, native or oversulphated, and a heparin-like dextran derivative.	Dermatan Sulfate	75-93	serpin family D member 1	Homo sapiens	36-55
9068899-1	1997	The kinetics of thrombin inhibition by heparin cofactor II (HC II) in the presence of dermatan sulphates, native (DS), or oversulphated (DSS 1 and DSS 2) and a biospecific dextran derivative substituted with carboxymethyl, carboxymethyl-benzylamide and carboxymethyl benzylamide-sulphonate functional groups (CMDBS), has been studied as a function of the sulphated polysaccharide concentration.	Dermatan Sulfate	86-104	coagulation factor II, thrombin	Homo sapiens	16-24
9013976-6	1997	Binding of C1q to CSPG was competitively inhibited by free glycosaminoglycans (GAG) in the order dextran sulfate > heparin > heparan sulfate > chondroitin-6-sulfate (CS-C) > dermatan sulfate (CS-B) > chondroitin-4-sulfate (CS-A).	Dermatan Sulfate	186-202	complement C1q A chain	Homo sapiens	11-14
8995662-8	1997	Our biosensor analyses showed that both heparan sulfate and dermatan sulfate inhibited gB2 binding (ED50 = 1 to 5 microg/ml), indicating that gB2 interacts with both heparin-like and dermatan sulfate glycosaminoglycans.	Dermatan Sulfate	60-76	gamma-aminobutyric acid type B receptor subunit 2	Homo sapiens	142-145
9352383-0	1997	Bioavailability of Desmin, a low molecular weight dermatan sulfate, after subcutaneous administration to healthy volunteers.	Dermatan Sulfate	50-66	desmin	Homo sapiens	19-25
8994426-0	1997	Effect of nonspecific binding to plasma proteins on the antithrombin activities of unfractionated heparin, low-molecular-weight heparin, and dermatan sulfate.	Dermatan Sulfate	141-157	serpin family C member 1	Homo sapiens	56-68
8994426-10	1997	In contrast, with UFH or DS, the rate of thrombin inhibition is twofold slower in plasma than in buffer.	Dermatan Sulfate	25-27	coagulation factor II, thrombin	Homo sapiens	41-49
9352383-1	1997	The bioavailability of two different s.c. doses of Desmin (a new low molecular weight dermatan sulfate) was evaluated in 12 healthy volunteers (6 men, 6 women aged 22-45 years) who were injected, on 3 separate days and with a wash-out period of at least 21 days between each administration, with 200 and 300 mg of Desmin by the s.c. route and 200 mg by the i.v.	Dermatan Sulfate	86-102	desmin	Homo sapiens	51-57
9200333-1	1997	Dermatan sulfate (DS) is a component of connective tissue and catalyzes the heparin cofactor II-mediated inhibition of thrombin.	Dermatan Sulfate	0-16	coagulation factor II, thrombin	Homo sapiens	119-127
9200333-1	1997	Dermatan sulfate (DS) is a component of connective tissue and catalyzes the heparin cofactor II-mediated inhibition of thrombin.	Dermatan Sulfate	18-20	coagulation factor II, thrombin	Homo sapiens	119-127
9067256-7	1996	Glycosaminoglycans such as chondroitin sulfate, dermatan sulfate and a chondroitin polysulfate, interacted with myeloblastin as non-essential activators in the presence of peptide substrates (activation up to a 6.7-fold factor) and as partial inhibitors (about 50% inhibition at saturation) in the presence of elastin.	Dermatan Sulfate	48-64	proteinase 3	Homo sapiens	112-124
8885144-0	1996	Active site for heparin cofactor II in low molecular mass dermatan sulfate.	Dermatan Sulfate	58-74	serpin family D member 1	Homo sapiens	16-35
8885144-3	1996	Unlike heparin, DS does not act through Antithrombin III (ATIII) but primarily through thrombin on Heparin Cofactor II (HCII).	Dermatan Sulfate	16-18	serpin family C member 1	Homo sapiens	58-63
8885144-3	1996	Unlike heparin, DS does not act through Antithrombin III (ATIII) but primarily through thrombin on Heparin Cofactor II (HCII).	Dermatan Sulfate	16-18	serpin family D member 1	Homo sapiens	99-118
8885144-3	1996	Unlike heparin, DS does not act through Antithrombin III (ATIII) but primarily through thrombin on Heparin Cofactor II (HCII).	Dermatan Sulfate	16-18	serpin family D member 1	Homo sapiens	120-124
8885144-10	1996	The important influence on the HCII activity of natural IdoA-GalNAc-4,6SO3 disaccharide was confirmed by investigation on oversulfated DS obtained by a limited and selective chemical 6-O-sulfation in GalNAc4SO3 units of DS.	Dermatan Sulfate	135-137	serpin family D member 1	Homo sapiens	31-35
8885144-10	1996	The important influence on the HCII activity of natural IdoA-GalNAc-4,6SO3 disaccharide was confirmed by investigation on oversulfated DS obtained by a limited and selective chemical 6-O-sulfation in GalNAc4SO3 units of DS.	Dermatan Sulfate	220-222	serpin family D member 1	Homo sapiens	31-35
8792767-1	1996	Heparin cofactor II (HCII) is a potent thrombin inhibitor in the presence of heparin and dermatan sulfate, glycosaminoglycans that accelerate the inhibition reaction.	Dermatan Sulfate	89-105	serpin family D member 1	Homo sapiens	0-19
8792767-1	1996	Heparin cofactor II (HCII) is a potent thrombin inhibitor in the presence of heparin and dermatan sulfate, glycosaminoglycans that accelerate the inhibition reaction.	Dermatan Sulfate	89-105	serpin family D member 1	Homo sapiens	21-25
8792767-1	1996	Heparin cofactor II (HCII) is a potent thrombin inhibitor in the presence of heparin and dermatan sulfate, glycosaminoglycans that accelerate the inhibition reaction.	Dermatan Sulfate	89-105	coagulation factor II, thrombin	Homo sapiens	39-47
8939995-0	1996	Distinct isoforms of chicken decorin contain either one or two dermatan sulfate chains.	Dermatan Sulfate	63-79	decorin	Gallus gallus	29-36
8939995-2	1996	In mammals, decorin carries one chondroitin/dermatan sulfate chain as a distinction from its homologue, biglycan, which contains two glycosaminoglycan chains.	Dermatan Sulfate	44-60	decorin	Gallus gallus	12-19
8910299-2	1996	Mucopolysaccharidosis type VI (MPS VI) is an autosomal recessive disease caused by a deficiency of N-acetylgalactosamine 4-sulfatase (4S) leading to the lysosomal accumulation and urinary excretion of dermatan sulfate.	Dermatan Sulfate	201-217	arylsulfatase B	Felis catus	99-132
8810655-2	1996	Patients were randomly allocated to three treatment groups to receive a new low-molecular-weight dermatan sulfate (Desmin) at the dose, respectively, of 100 mg once daily by subcutaneous (SC) route, 100 mg twice a day SC, and 200 mg once daily by intramuscular (IM) route.	Dermatan Sulfate	97-113	desmin	Homo sapiens	115-121
8710849-1	1996	Mucopolysaccharidosis VI (MPS VI) is a lysosomal storage disease with autosomal recessive inheritance caused by a deficiency of the enzyme arylsulfatase B (ASB), which is involved in degradation of dermatan sulfate and chondroitin 4-sulfate.	Dermatan Sulfate	198-214	arylsulfatase B	Mus musculus	156-159
8755662-2	1996	Mucopolysacchariodosis type VI (MPS VI) is the lysosomal storage disorder caused by the deficient activity of arylsulfatase B (ASB; N-acetylgalactosamine 4-sulfatase) and the subsequent accumulation of the glycosaminoglycan (GAG), dermatan sulfate.	Dermatan Sulfate	231-247	arylsulfatase B	Homo sapiens	110-125
8755662-2	1996	Mucopolysacchariodosis type VI (MPS VI) is the lysosomal storage disorder caused by the deficient activity of arylsulfatase B (ASB; N-acetylgalactosamine 4-sulfatase) and the subsequent accumulation of the glycosaminoglycan (GAG), dermatan sulfate.	Dermatan Sulfate	231-247	arylsulfatase B	Homo sapiens	127-130
8755662-2	1996	Mucopolysacchariodosis type VI (MPS VI) is the lysosomal storage disorder caused by the deficient activity of arylsulfatase B (ASB; N-acetylgalactosamine 4-sulfatase) and the subsequent accumulation of the glycosaminoglycan (GAG), dermatan sulfate.	Dermatan Sulfate	231-247	arylsulfatase B	Homo sapiens	132-165
8668693-2	1996	Mucin is a gelatinous substance composed of glycosaminoglycanes, especially hyaluronic acid and dermatan sulfate bound to small quantities of chondoitin sulfate and heparin sulfate.	Dermatan Sulfate	96-112	LOC100508689	Homo sapiens	0-5
8837309-0	1996	Pharmacology of a new low molecular weight dermatan sulphate (Desmin) in healthy volunteers: repeated daily intramuscular administration of 400 mg for a week.	Dermatan Sulfate	43-60	desmin	Homo sapiens	62-68
8651289-1	1996	Maroteaux-Lamy syndrome, or mucopolysaccharidosis type VI (MPS-VI), is a lysosomal storage disorder characterized by the defective degradation of dermatan sulfate due to the deficiency of N-acetylgalactosamine-4-sulfatase (4S).	Dermatan Sulfate	146-162	arylsulfatase B	Homo sapiens	188-221
8663298-8	1996	Examination of several well characterized glycosaminoglycans to inhibit the binding of heparin to both heparin-binding IGFBP-3 peptides revealed that the most potent inhibitors were heparin, heparan sulfate, and dermatan sulfate; chondroitin sulfate A and hyaluronic acid were intermediate in their inhibitory activities; and chondroitin sulfate C caused no inhibition.	Dermatan Sulfate	212-228	insulin like growth factor binding protein 3	Homo sapiens	119-126
8674529-2	1996	Considering 3H incorporation, we found that IFNgamma increased the production of glycosaminoglycan synthesis, including hyaluronic acid, heparan and chondroitin/dermatan sulfate.	Dermatan Sulfate	161-177	interferon gamma	Homo sapiens	44-52
8791281-6	1996	H suppressed the stimulation of the synthesis of HA, CS and DS by TGF-beta.	Dermatan Sulfate	60-62	transforming growth factor, beta 1	Rattus norvegicus	66-74
8725717-0	1996	The effects of dermatan sulfate at submicrogram/ml concentrations on in vitro thrombin generation.	Dermatan Sulfate	15-31	coagulation factor II, thrombin	Homo sapiens	78-86
8725717-3	1996	We investigated the ability of dermatan sulfate added to plasma at 0.2, 0.5 and 1.0 microgram/ml to inhibit thrombin generation initiated by low concentrations of recombinant human tissue factor in defibrinated plasma.	Dermatan Sulfate	31-47	coagulation factor II, thrombin	Homo sapiens	108-116
8725717-4	1996	A dose dependent decrease in thrombin potential was demonstrated at therapeutically relevant concentrations of dermatan sulfate (0.5 and 1.0 microgram/ml) but there was no induction of a lag phase in thrombin generation.	Dermatan Sulfate	111-127	coagulation factor II, thrombin	Homo sapiens	29-37
8725717-7	1996	The effect on the thrombin potential was somewhat greater at the lowest concentration of tissue factor and amounted to a maximum inhibition of approximately 50% at 1 microgram/ml dermatan sulfate.	Dermatan Sulfate	179-195	coagulation factor II, thrombin	Homo sapiens	18-26
8725717-8	1996	A dose dependent increase in formation of thrombin-heparin cofactor II complexes and a decrease in thrombin-antithrombin complex formation with increasing dermatan sulfate concentration were observed at all dermatan sulfate concentrations.	Dermatan Sulfate	155-171	coagulation factor II, thrombin	Homo sapiens	99-107
8725717-10	1996	We conclude that dermatan sulfate, at the concentrations tested, catalyses inhibition of free thrombin by heparin cofactor II but not efficiently enough to inhibit prothrombinase formation.	Dermatan Sulfate	17-33	coagulation factor II, thrombin	Homo sapiens	94-102
8701414-3	1996	DS extracted and purified from pig mucosa has a relative molecular mass (Mr) of about 23,100 and is composed of about 10% nonsulfated disaccharide, 80% monosulfated disaccharides and about 10% disulfated disaccharides, with a sulfate to carboxyl ratio of 1.00 and a heparin cofactor II (HCII) activity of about 160 units/mg.	Dermatan Sulfate	0-2	serpin family D member 1	Sus scrofa	266-285
8656041-3	1996	We found that binding of iodine 125-labeled PF4 to HEL cells was inhibited by heparin, heparan sulfate, and dermatan sulfate and to a smaller extent by chondroitin sulfate.	Dermatan Sulfate	108-124	platelet factor 4	Homo sapiens	44-47
8701414-3	1996	DS extracted and purified from pig mucosa has a relative molecular mass (Mr) of about 23,100 and is composed of about 10% nonsulfated disaccharide, 80% monosulfated disaccharides and about 10% disulfated disaccharides, with a sulfate to carboxyl ratio of 1.00 and a heparin cofactor II (HCII) activity of about 160 units/mg.	Dermatan Sulfate	0-2	serpin family D member 1	Sus scrofa	287-291
8603018-4	1996	Using recently developed sensitive assays for FXIa-inhibitor complexes we found thrombin-mediated and FXII-dependent activation of endogenous FXI in plasma in the presence of heparan sulphate, heparin, dermatan sulphate or dextran sulphate.	Dermatan Sulfate	202-219	coagulation factor II, thrombin	Homo sapiens	80-88
8562924-1	1996	Heparin cofactor II (HCII) is a serine proteinase inhibitor in human plasma that rapidly inhibits thrombin in the presence of dermatan sulfate or heparin.	Dermatan Sulfate	126-142	serpin family D member 1	Homo sapiens	0-19
8562924-1	1996	Heparin cofactor II (HCII) is a serine proteinase inhibitor in human plasma that rapidly inhibits thrombin in the presence of dermatan sulfate or heparin.	Dermatan Sulfate	126-142	serpin family D member 1	Homo sapiens	21-25
8603018-4	1996	Using recently developed sensitive assays for FXIa-inhibitor complexes we found thrombin-mediated and FXII-dependent activation of endogenous FXI in plasma in the presence of heparan sulphate, heparin, dermatan sulphate or dextran sulphate.	Dermatan Sulfate	202-219	coagulation factor XI	Homo sapiens	46-49
8562924-1	1996	Heparin cofactor II (HCII) is a serine proteinase inhibitor in human plasma that rapidly inhibits thrombin in the presence of dermatan sulfate or heparin.	Dermatan Sulfate	126-142	coagulation factor II, thrombin	Homo sapiens	98-106
8603018-6	1996	We conclude that endogenous FXI in plasma can be activated by thrombin in the presence of various glycosaminoglycans, including the physiological compounds heparan sulphate and dermatan sulphate, but only at very high concentrations of thrombin, corresponding to 100% prothrombin activation in undiluted plasma.	Dermatan Sulfate	177-194	coagulation factor XI	Homo sapiens	28-31
8603018-6	1996	We conclude that endogenous FXI in plasma can be activated by thrombin in the presence of various glycosaminoglycans, including the physiological compounds heparan sulphate and dermatan sulphate, but only at very high concentrations of thrombin, corresponding to 100% prothrombin activation in undiluted plasma.	Dermatan Sulfate	177-194	coagulation factor II, thrombin	Homo sapiens	62-70
8845462-1	1996	Low-molecular-weight (LMW)-dermatan sulfate (Desmin) with the mean molecular weight of 5600 Da has been obtained by limited depolymerization of natural dermatan sulfate.	Dermatan Sulfate	27-43	desmin	Homo sapiens	45-51
8815578-2	1996	However, the low molecular weight (LMW) dermatan sulphate Desmin 370 has been shown to generate circulating anti-Xa activity following administration to humans.	Dermatan Sulfate	40-57	desmin	Homo sapiens	58-64
8815580-3	1996	In conditioned medium, HuH-7 cells constantly produced HC II that was functionally active and formed a complex with thrombin in the presence of dermatan sulfate.	Dermatan Sulfate	144-160	MIR7-3 host gene	Homo sapiens	23-28
8815580-3	1996	In conditioned medium, HuH-7 cells constantly produced HC II that was functionally active and formed a complex with thrombin in the presence of dermatan sulfate.	Dermatan Sulfate	144-160	serpin family D member 1	Homo sapiens	55-60
8815580-3	1996	In conditioned medium, HuH-7 cells constantly produced HC II that was functionally active and formed a complex with thrombin in the presence of dermatan sulfate.	Dermatan Sulfate	144-160	coagulation factor II, thrombin	Homo sapiens	116-124
8838671-9	1996	Fibroblasts responded to the addition of dermatan sulfate, heparan sulfate and heparin with a decrease in fibronectin, collagenase and interleukin-6 mRNA.	Dermatan Sulfate	41-57	fibronectin 1	Homo sapiens	106-117
8838671-9	1996	Fibroblasts responded to the addition of dermatan sulfate, heparan sulfate and heparin with a decrease in fibronectin, collagenase and interleukin-6 mRNA.	Dermatan Sulfate	41-57	interleukin 6	Homo sapiens	135-148
8845462-1	1996	Low-molecular-weight (LMW)-dermatan sulfate (Desmin) with the mean molecular weight of 5600 Da has been obtained by limited depolymerization of natural dermatan sulfate.	Dermatan Sulfate	152-168	desmin	Homo sapiens	45-51
8836009-9	1996	In addition it was found that dermatan sulfate levels, expressed as antithrombin activity by heparin cofactor II, were significantly increased over control values.	Dermatan Sulfate	30-46	serpin family D member 1	Rattus norvegicus	93-112
8944417-7	1996	They induced a dermatan sulfate-like activity in the plasma of treated rats, as measured by heparin cofactor II-mediated thrombin inhibition assay.	Dermatan Sulfate	15-31	serpin family D member 1	Rattus norvegicus	92-111
8944417-7	1996	They induced a dermatan sulfate-like activity in the plasma of treated rats, as measured by heparin cofactor II-mediated thrombin inhibition assay.	Dermatan Sulfate	15-31	coagulation factor II	Rattus norvegicus	121-129
8665399-0	1996	Release of interleukin-1 beta by dermatan sulfate suppresses hepatocyte growth.	Dermatan Sulfate	33-49	interleukin 1 beta	Rattus norvegicus	11-29
8665399-6	1996	Similarly, more than 10 hr was required after the addition of DS before IL-1 beta mRNA was detected.	Dermatan Sulfate	62-64	interleukin 1 beta	Rattus norvegicus	72-81
8665399-7	1996	These findings suggest that DS in the medium induced the production of IL-1 beta which, in turn, reduced DNA synthesis in hepatocytes.	Dermatan Sulfate	28-30	interleukin 1 beta	Rattus norvegicus	71-80
8747085-4	1995	TGF beta 1 induced a more marked increase in collagen and fibronectin release and greater production of sulphated GAGs as DS and heparan sulphate (HS) in the otosclerotic cells.	Dermatan Sulfate	122-124	transforming growth factor beta 1	Homo sapiens	0-10
8746633-9	1995	In the presence of glycosaminoglycans, the maximal thrombin inhibition rate (k2 x 10(-3) M-1 min-1) for rHCII was 10.4 +/- 2.5 at 100 micrograms/ml heparin and 16.0 +/- 4.3 at 1000 micrograms/ml dermatan sulfate compared to 9.0 +/- 0.7 at 200 micrograms/ml heparin and 18.5 +/- 5.3 at 1000 micrograms/ml dermatan sulfate for pHCII.	Dermatan Sulfate	195-211	coagulation factor II, thrombin	Homo sapiens	51-59
8746633-9	1995	In the presence of glycosaminoglycans, the maximal thrombin inhibition rate (k2 x 10(-3) M-1 min-1) for rHCII was 10.4 +/- 2.5 at 100 micrograms/ml heparin and 16.0 +/- 4.3 at 1000 micrograms/ml dermatan sulfate compared to 9.0 +/- 0.7 at 200 micrograms/ml heparin and 18.5 +/- 5.3 at 1000 micrograms/ml dermatan sulfate for pHCII.	Dermatan Sulfate	195-211	CD59 molecule (CD59 blood group)	Homo sapiens	93-98
8746633-9	1995	In the presence of glycosaminoglycans, the maximal thrombin inhibition rate (k2 x 10(-3) M-1 min-1) for rHCII was 10.4 +/- 2.5 at 100 micrograms/ml heparin and 16.0 +/- 4.3 at 1000 micrograms/ml dermatan sulfate compared to 9.0 +/- 0.7 at 200 micrograms/ml heparin and 18.5 +/- 5.3 at 1000 micrograms/ml dermatan sulfate for pHCII.	Dermatan Sulfate	195-211	serpin family D member 1	Rattus norvegicus	104-109
8746633-9	1995	In the presence of glycosaminoglycans, the maximal thrombin inhibition rate (k2 x 10(-3) M-1 min-1) for rHCII was 10.4 +/- 2.5 at 100 micrograms/ml heparin and 16.0 +/- 4.3 at 1000 micrograms/ml dermatan sulfate compared to 9.0 +/- 0.7 at 200 micrograms/ml heparin and 18.5 +/- 5.3 at 1000 micrograms/ml dermatan sulfate for pHCII.	Dermatan Sulfate	304-320	coagulation factor II, thrombin	Homo sapiens	51-59
8746633-9	1995	In the presence of glycosaminoglycans, the maximal thrombin inhibition rate (k2 x 10(-3) M-1 min-1) for rHCII was 10.4 +/- 2.5 at 100 micrograms/ml heparin and 16.0 +/- 4.3 at 1000 micrograms/ml dermatan sulfate compared to 9.0 +/- 0.7 at 200 micrograms/ml heparin and 18.5 +/- 5.3 at 1000 micrograms/ml dermatan sulfate for pHCII.	Dermatan Sulfate	304-320	CD59 molecule (CD59 blood group)	Homo sapiens	93-98
8746633-9	1995	In the presence of glycosaminoglycans, the maximal thrombin inhibition rate (k2 x 10(-3) M-1 min-1) for rHCII was 10.4 +/- 2.5 at 100 micrograms/ml heparin and 16.0 +/- 4.3 at 1000 micrograms/ml dermatan sulfate compared to 9.0 +/- 0.7 at 200 micrograms/ml heparin and 18.5 +/- 5.3 at 1000 micrograms/ml dermatan sulfate for pHCII.	Dermatan Sulfate	304-320	serpin family D member 1	Rattus norvegicus	104-109
7487873-5	1995	Although bFGF and/or TGF-beta 1 induced a similar stimulation in cell-surface chondroitin sulphate/dermatan sulphate and heparan sulphate (HS) proteoglycan synthesis, only the turnover of HS proteoglycans was increased.	Dermatan Sulfate	99-116	transforming growth factor beta 1	Sus scrofa	21-31
8530090-1	1995	Iduronate-2-sulfatase (IDS) is involved in the degradation of heparan sulfate and dermatan sulfate in the lysosomes, and a deficiency in this enzyme results in Hunter syndrome.	Dermatan Sulfate	82-98	iduronate 2-sulfatase	Homo sapiens	0-21
8530090-1	1995	Iduronate-2-sulfatase (IDS) is involved in the degradation of heparan sulfate and dermatan sulfate in the lysosomes, and a deficiency in this enzyme results in Hunter syndrome.	Dermatan Sulfate	82-98	iduronate 2-sulfatase	Homo sapiens	23-26
7626005-1	1995	Iduronate 2-sulphatase (IDS) is a lysosomal enzyme involved in degradation of dermatan sulphate and heparan sulphate.	Dermatan Sulfate	78-95	iduronate 2-sulfatase	Homo sapiens	0-22
8533121-0	1995	Pharmacology of desmin (low molecular weight dermatan sulphate) in healthy volunteers following intravenous bolus administration of different dosages (200, 400, 800 mg).	Dermatan Sulfate	45-62	desmin	Homo sapiens	16-22
8533121-1	1995	Eight healthy volunteers (6 males, 2 females, mean age 31.6 yrs), were administered--on three separate days--200, 400 and 800 mg of a new low molecular weight Dermatan sulphate (Desmin), given as a single i.v.	Dermatan Sulfate	159-176	desmin	Homo sapiens	178-184
7626005-1	1995	Iduronate 2-sulphatase (IDS) is a lysosomal enzyme involved in degradation of dermatan sulphate and heparan sulphate.	Dermatan Sulfate	78-95	iduronate 2-sulfatase	Homo sapiens	24-27
7721830-8	1995	The novel aspect of this molecule is the presence of a terminal alpha-Gal-NAc residue at a position that is normally occupied by beta-GalNAc in chondroitin/dermatan sulfate or by alpha-Glc-NAc in heparin or heparan sulfate chains.	Dermatan Sulfate	156-172	synuclein alpha	Homo sapiens	74-77
7647222-3	1995	A low-molecular-weight dermatan sulphate releases only very small amounts of TFPI after intravenous injection without a clear dose-dependent effect.	Dermatan Sulfate	23-40	tissue factor pathway inhibitor	Homo sapiens	77-81
7781777-3	1995	HCII inhibits thrombin in both a progressive reaction, and in an accelerated reaction catalyzed by a glycosaminoglycan, dermatan sulphate (DS).	Dermatan Sulfate	139-141	heparin cofactor 2	Oryctolagus cuniculus	0-4
7781777-3	1995	HCII inhibits thrombin in both a progressive reaction, and in an accelerated reaction catalyzed by a glycosaminoglycan, dermatan sulphate (DS).	Dermatan Sulfate	139-141	prothrombin	Oryctolagus cuniculus	14-22
7676405-0	1995	Structural heterogeneity of dermatan sulfate chains: correlation with heparin cofactor II activating properties.	Dermatan Sulfate	28-44	serpin family D member 1	Bos taurus	70-89
7676405-5	1995	The ability of DS crude preparation to activate the heparin cofactor II (HCII) mediated inhibition of thrombin depends on the relative amount of highly active DS chains; this activity is related to the overall charge of DS chains and particularly with the content of IdoUA-2-SO4-->GalNAc-4-SO4 and UA-->GalNAc-4,6-di-SO4 disaccharides.	Dermatan Sulfate	15-17	serpin family D member 1	Bos taurus	52-71
7676405-5	1995	The ability of DS crude preparation to activate the heparin cofactor II (HCII) mediated inhibition of thrombin depends on the relative amount of highly active DS chains; this activity is related to the overall charge of DS chains and particularly with the content of IdoUA-2-SO4-->GalNAc-4-SO4 and UA-->GalNAc-4,6-di-SO4 disaccharides.	Dermatan Sulfate	15-17	serpin family D member 1	Bos taurus	73-77
7676405-5	1995	The ability of DS crude preparation to activate the heparin cofactor II (HCII) mediated inhibition of thrombin depends on the relative amount of highly active DS chains; this activity is related to the overall charge of DS chains and particularly with the content of IdoUA-2-SO4-->GalNAc-4-SO4 and UA-->GalNAc-4,6-di-SO4 disaccharides.	Dermatan Sulfate	15-17	coagulation factor II, thrombin	Bos taurus	102-110
7676405-5	1995	The ability of DS crude preparation to activate the heparin cofactor II (HCII) mediated inhibition of thrombin depends on the relative amount of highly active DS chains; this activity is related to the overall charge of DS chains and particularly with the content of IdoUA-2-SO4-->GalNAc-4-SO4 and UA-->GalNAc-4,6-di-SO4 disaccharides.	Dermatan Sulfate	159-161	serpin family D member 1	Bos taurus	52-71
7676405-5	1995	The ability of DS crude preparation to activate the heparin cofactor II (HCII) mediated inhibition of thrombin depends on the relative amount of highly active DS chains; this activity is related to the overall charge of DS chains and particularly with the content of IdoUA-2-SO4-->GalNAc-4-SO4 and UA-->GalNAc-4,6-di-SO4 disaccharides.	Dermatan Sulfate	159-161	serpin family D member 1	Bos taurus	73-77
7676405-5	1995	The ability of DS crude preparation to activate the heparin cofactor II (HCII) mediated inhibition of thrombin depends on the relative amount of highly active DS chains; this activity is related to the overall charge of DS chains and particularly with the content of IdoUA-2-SO4-->GalNAc-4-SO4 and UA-->GalNAc-4,6-di-SO4 disaccharides.	Dermatan Sulfate	159-161	coagulation factor II, thrombin	Bos taurus	102-110
7676405-5	1995	The ability of DS crude preparation to activate the heparin cofactor II (HCII) mediated inhibition of thrombin depends on the relative amount of highly active DS chains; this activity is related to the overall charge of DS chains and particularly with the content of IdoUA-2-SO4-->GalNAc-4-SO4 and UA-->GalNAc-4,6-di-SO4 disaccharides.	Dermatan Sulfate	159-161	serpin family D member 1	Bos taurus	52-71
7676405-5	1995	The ability of DS crude preparation to activate the heparin cofactor II (HCII) mediated inhibition of thrombin depends on the relative amount of highly active DS chains; this activity is related to the overall charge of DS chains and particularly with the content of IdoUA-2-SO4-->GalNAc-4-SO4 and UA-->GalNAc-4,6-di-SO4 disaccharides.	Dermatan Sulfate	159-161	serpin family D member 1	Bos taurus	73-77
7676405-5	1995	The ability of DS crude preparation to activate the heparin cofactor II (HCII) mediated inhibition of thrombin depends on the relative amount of highly active DS chains; this activity is related to the overall charge of DS chains and particularly with the content of IdoUA-2-SO4-->GalNAc-4-SO4 and UA-->GalNAc-4,6-di-SO4 disaccharides.	Dermatan Sulfate	159-161	coagulation factor II, thrombin	Bos taurus	102-110
7779094-0	1995	Formation of heparan sulfate or chondroitin/dermatan sulfate on recombinant domain I of mouse perlecan expressed in Chinese hamster ovary cells.	Dermatan Sulfate	44-60	LOW QUALITY PROTEIN: basement membrane-specific heparan sulfate proteoglycan core protein	Cricetulus griseus	94-102
7663435-1	1995	The iduronate-2-sulfatase (IDS) is a lysosomal enzyme that acts on sulphate groups on C-2 positions of the iduronic acid residues of the mucopolysaccharides heparan sulphate and dermatan sulphate.	Dermatan Sulfate	178-195	iduronate 2-sulfatase	Homo sapiens	4-25
8589262-2	1995	IL-7 binds to heparin and heparan sulfate, to a lesser extent to dermatan sulfate and does not bind to chondroitin sulfate.	Dermatan Sulfate	65-81	interleukin 7	Mus musculus	0-4
7721830-8	1995	The novel aspect of this molecule is the presence of a terminal alpha-Gal-NAc residue at a position that is normally occupied by beta-GalNAc in chondroitin/dermatan sulfate or by alpha-Glc-NAc in heparin or heparan sulfate chains.	Dermatan Sulfate	156-172	synuclein alpha	Homo sapiens	137-140
7545318-4	1995	Dermatan sulfate catalyses the inhibition of thrombin by heparin cofactor II.	Dermatan Sulfate	0-16	coagulation factor II, thrombin	Homo sapiens	45-53
7592530-14	1995	Analysis of proteoglycans of the culture medium has shown that most of the medium proteoglycans were keratan sulfate proteoglycan and free keratan sulfate chain (or keratan sulfate chain with a short peptide) during all ages after Day 7, although the major proteoglycan of Day 5 medium was chondroitin sulfate/dermatan sulfate proteoglycan.	Dermatan Sulfate	310-326	versican	Gallus gallus	82-94
7592530-14	1995	Analysis of proteoglycans of the culture medium has shown that most of the medium proteoglycans were keratan sulfate proteoglycan and free keratan sulfate chain (or keratan sulfate chain with a short peptide) during all ages after Day 7, although the major proteoglycan of Day 5 medium was chondroitin sulfate/dermatan sulfate proteoglycan.	Dermatan Sulfate	310-326	versican	Gallus gallus	82-94
7592529-3	1995	Two predominant proteoglycans were identified in the stromal fraction: keratan sulfate proteoglycan and chondroitin sulfate/dermatan sulfate proteoglycan.	Dermatan Sulfate	124-140	versican	Gallus gallus	16-28
7545318-10	1995	In addition, the concentrations of thrombin-heparin cofactor II decreased 3 to 5 days after delivery, reflecting the disappearance of the catalytically active dermatan sulfate elaborated by the placenta.	Dermatan Sulfate	159-175	coagulation factor II, thrombin	Homo sapiens	35-43
7545318-11	1995	Thus, heparin cofactor II normally inactivates thrombin in vivo, with its role increasing in conditions associated with high levels of heparin cofactor II and/or dermatan sulfate.	Dermatan Sulfate	162-178	coagulation factor II, thrombin	Homo sapiens	47-55
8680403-2	1995	These mutations lead to a deficiency of the glycosidase alpha-L-iduronidase (IDUA), which is required for the degradation of heparan sulphate and dermatan sulphate and thus the storage of these glycosaminoglycans in the lysosome.	Dermatan Sulfate	146-163	alpha-L-iduronidase	Homo sapiens	56-75
7833476-0	1995	Fibrinogen inhibits the heparin cofactor II-mediated antithrombin activity of dermatan sulfate.	Dermatan Sulfate	78-94	fibrinogen beta chain	Homo sapiens	0-10
7833476-0	1995	Fibrinogen inhibits the heparin cofactor II-mediated antithrombin activity of dermatan sulfate.	Dermatan Sulfate	78-94	serpin family C member 1	Homo sapiens	53-65
7833476-2	1995	The antithrombin activity of several dermatan sulfate preparations has been measured in whole human plasma and found to be -55% of that in purified systems.	Dermatan Sulfate	37-53	serpin family C member 1	Homo sapiens	4-16
7833476-3	1995	Kinetic studies under pseudo-first-order conditions indicated that the reduction in antithrombin activity of dermatan sulfate in plasma compared with that in buffer was due to noncompetitive inhibition with respect to dermatan sulfate.	Dermatan Sulfate	109-125	serpin family C member 1	Homo sapiens	84-96
7833476-3	1995	Kinetic studies under pseudo-first-order conditions indicated that the reduction in antithrombin activity of dermatan sulfate in plasma compared with that in buffer was due to noncompetitive inhibition with respect to dermatan sulfate.	Dermatan Sulfate	218-234	serpin family C member 1	Homo sapiens	84-96
7833476-4	1995	Analysis of the protein profile bound to immobilized dermatan sulphate showed that on a molar basis, histidine-rich glycoprotein and apolipoprotein E were the most abundant proteins specifically bound, together with significant amounts of fibrinogen and vitronectin.	Dermatan Sulfate	53-70	apolipoprotein E	Homo sapiens	133-149
7833476-4	1995	Analysis of the protein profile bound to immobilized dermatan sulphate showed that on a molar basis, histidine-rich glycoprotein and apolipoprotein E were the most abundant proteins specifically bound, together with significant amounts of fibrinogen and vitronectin.	Dermatan Sulfate	53-70	fibrinogen beta chain	Homo sapiens	239-249
7833476-4	1995	Analysis of the protein profile bound to immobilized dermatan sulphate showed that on a molar basis, histidine-rich glycoprotein and apolipoprotein E were the most abundant proteins specifically bound, together with significant amounts of fibrinogen and vitronectin.	Dermatan Sulfate	53-70	vitronectin	Homo sapiens	254-265
7833476-5	1995	Addition of these proteins to the purified system showed that only fibrinogen inhibited the antithrombin activity of dermatan sulfate and that it did so in a concentration-dependent manner over the physiologic range of plasma fibrinogen levels.	Dermatan Sulfate	117-133	fibrinogen beta chain	Homo sapiens	67-77
7833476-5	1995	Addition of these proteins to the purified system showed that only fibrinogen inhibited the antithrombin activity of dermatan sulfate and that it did so in a concentration-dependent manner over the physiologic range of plasma fibrinogen levels.	Dermatan Sulfate	117-133	serpin family C member 1	Homo sapiens	92-104
7833476-6	1995	These results indicate that the anticoagulant activity of dermatan sulfate may be modulated in human plasma by fibrinogen.	Dermatan Sulfate	58-74	fibrinogen beta chain	Homo sapiens	111-121
7588997-1	1995	[125I]-Labeled thrombin was incubated with human plasma and its interactions with the two plasma protease inhibitors antithrombin III (AT-III) or heparin cofactor II (HC-II) were investigated in the presence of oat spelts xylan sulfate (OSXS), sodium pentosan polysulfate (SP-54), and the results were compared with heparin and dermatan sulfate.	Dermatan Sulfate	328-344	coagulation factor II, thrombin	Homo sapiens	15-23
8680403-2	1995	These mutations lead to a deficiency of the glycosidase alpha-L-iduronidase (IDUA), which is required for the degradation of heparan sulphate and dermatan sulphate and thus the storage of these glycosaminoglycans in the lysosome.	Dermatan Sulfate	146-163	alpha-L-iduronidase	Homo sapiens	77-81
7740443-1	1994	Dermatan sulphate catalyses thrombin inhibition by heparin cofactor II; it has a lower haemorrhagic to antithrombotic ratio than that of heparin in animal models.	Dermatan Sulfate	0-17	coagulation factor II, thrombin	Homo sapiens	28-36
7527332-4	1994	The addition of heparin, heparan sulfate, and dermatan sulfate (100 micrograms/ml) to the medium of fibroblast monolayer cultures inhibited IGFBP-5 degradation, as determined by the conversion of intact IGFBP-5 to a 23-kilodalton fragment.	Dermatan Sulfate	46-62	insulin like growth factor binding protein 5	Homo sapiens	140-147
7527332-4	1994	The addition of heparin, heparan sulfate, and dermatan sulfate (100 micrograms/ml) to the medium of fibroblast monolayer cultures inhibited IGFBP-5 degradation, as determined by the conversion of intact IGFBP-5 to a 23-kilodalton fragment.	Dermatan Sulfate	46-62	insulin like growth factor binding protein 5	Homo sapiens	203-210
7798630-5	1995	Oncostatin M treatment increased both types I and III procollagens and their mRNA transcripts, as well as levels of hyaluronic acid, chondroitin-4/6 sulfates, and dermatan sulfate, but not fibronectin or general noncollagenous protein synthesis.	Dermatan Sulfate	163-179	oncostatin M	Homo sapiens	0-12
7806495-8	1994	Specific mutations in exosite II (R89E, R245E, K248E, and K252E) disrupted thrombin binding to both dermatan sulfate and heparin, indicating that both glycosaminoglycans bind to a common site in exosite II.	Dermatan Sulfate	100-116	coagulation factor II, thrombin	Homo sapiens	75-83
7806495-10	1994	These results are incompatible with a template model for thrombin inhibition by HCII and dermatan sulfate.	Dermatan Sulfate	89-105	coagulation factor II, thrombin	Homo sapiens	57-65
7881183-9	1994	For example, some dermatan sulphates contained D-glucuronate-rich domains that were always 6-sulphated (scleral decorin), others were always 4-sulphated (decorin from bovine dermis, cartilage and bone; biglycan from aorta) or 6-sulphated near the linkage region, but 4-sulphated in more distal domains (decorin from porcine dermis and bovine tendon).	Dermatan Sulfate	18-36	decorin	Bos taurus	112-119
7998955-1	1994	Mucopolysaccharidosis type I (MPS I, Hurler and Scheie syndromes) is an autosomal recessive lysosomal storage disorder that results from a deficiency of the hydrolase alpha-L-iduronidase (IDUA) which is involved in the lysosomal degradation of both heparan sulphate (HS) and dermatan sulphate (DS).	Dermatan Sulfate	275-292	alpha-L-iduronidase	Homo sapiens	167-186
7998955-1	1994	Mucopolysaccharidosis type I (MPS I, Hurler and Scheie syndromes) is an autosomal recessive lysosomal storage disorder that results from a deficiency of the hydrolase alpha-L-iduronidase (IDUA) which is involved in the lysosomal degradation of both heparan sulphate (HS) and dermatan sulphate (DS).	Dermatan Sulfate	275-292	alpha-L-iduronidase	Homo sapiens	188-192
7998955-1	1994	Mucopolysaccharidosis type I (MPS I, Hurler and Scheie syndromes) is an autosomal recessive lysosomal storage disorder that results from a deficiency of the hydrolase alpha-L-iduronidase (IDUA) which is involved in the lysosomal degradation of both heparan sulphate (HS) and dermatan sulphate (DS).	Dermatan Sulfate	294-296	alpha-L-iduronidase	Homo sapiens	167-186
7998955-1	1994	Mucopolysaccharidosis type I (MPS I, Hurler and Scheie syndromes) is an autosomal recessive lysosomal storage disorder that results from a deficiency of the hydrolase alpha-L-iduronidase (IDUA) which is involved in the lysosomal degradation of both heparan sulphate (HS) and dermatan sulphate (DS).	Dermatan Sulfate	294-296	alpha-L-iduronidase	Homo sapiens	188-192
7695089-0	1994	Quantitation of dermatan sulfate active site for heparin cofactor II by 1H nuclear magnetic resonance spectroscopy.	Dermatan Sulfate	16-32	serpin family D member 1	Sus scrofa	49-68
7695089-1	1994	The sequence (IdoA2SO3-GalNAc4SO3)n contributes to the HCII-mediated inhibition of thrombin by dermatan sulfate (DS).	Dermatan Sulfate	95-111	coagulation factor II, thrombin	Sus scrofa	83-91
7695089-1	1994	The sequence (IdoA2SO3-GalNAc4SO3)n contributes to the HCII-mediated inhibition of thrombin by dermatan sulfate (DS).	Dermatan Sulfate	113-115	coagulation factor II, thrombin	Sus scrofa	83-91
7961776-8	1994	Dermatan sulfate chains prepared from biglycan, examined in both denaturing and physiologic solvents, show no significant difference in molecular weight (Mz approximately 22,000), whether or not the solvents contain Zn2+.	Dermatan Sulfate	0-16	biglycan	Bos taurus	38-46
7881183-9	1994	For example, some dermatan sulphates contained D-glucuronate-rich domains that were always 6-sulphated (scleral decorin), others were always 4-sulphated (decorin from bovine dermis, cartilage and bone; biglycan from aorta) or 6-sulphated near the linkage region, but 4-sulphated in more distal domains (decorin from porcine dermis and bovine tendon).	Dermatan Sulfate	18-36	biglycan	Bos taurus	202-210
7881183-10	1994	Decorin from bone and articular cartilage, as well as biglycan from articular and nasal cartilage, carried largely chondroitin sulphate chains, but also some dermatan sulphate, whereas galactosaminoglycan chains derived from aggrecan of nasal cartilage were free of L-iduronate.	Dermatan Sulfate	158-175	decorin	Bos taurus	0-7
7813515-3	1994	The major [35S]methionine-labeled proteoglycan present is identified as the small chondroitin/dermatan sulfate proteoglycan decorin (PG II.	Dermatan Sulfate	94-110	decorin	Bos taurus	124-131
7519608-0	1994	Heparin, heparan sulfate, and dermatan sulfate regulate formation of the insulin-like growth factor-I and insulin-like growth factor-binding protein complexes.	Dermatan Sulfate	30-46	insulin like growth factor 1	Homo sapiens	73-101
7919526-9	1994	Decorin and biglycan possess one and two dermatan sulfate chains, respectively, whereas fibromodulin bears several keratan sulfate chains.	Dermatan Sulfate	41-57	biglycan	Homo sapiens	12-20
7519189-3	1994	We report here that the monoclonal antibody 473HD, which binds to the surface of early differentiation stages of murine astrocytes and oligodendrocytes, reacts with the chondroitin sulfate/dermatan sulfate hybrid epitope DSD-1 expressed on a central nervous system chondroitin sulfate proteoglycan designated DSD-1-PG.	Dermatan Sulfate	189-205	protein tyrosine phosphatase, receptor type Z, polypeptide 1	Mus musculus	309-317
8018657-1	1994	An increase in dermatan sulfate-proteoglycan (DSPG) production occurs in cultured aortic smooth muscle cells exposed to macrophage-conditioned media, an effect that is abrogated by an antibody to interleukin-1 (IL-1).	Dermatan Sulfate	15-31	interleukin 1 alpha	Homo sapiens	196-209
7974391-10	1994	A number of different glycosaminoglycans were tested and the following order of TFPI affinity was found: heparin >> dermatan sulphate > heparan sulphate > chondroitin sulphate C.	Dermatan Sulfate	122-139	tissue factor pathway inhibitor	Homo sapiens	80-84
8018657-1	1994	An increase in dermatan sulfate-proteoglycan (DSPG) production occurs in cultured aortic smooth muscle cells exposed to macrophage-conditioned media, an effect that is abrogated by an antibody to interleukin-1 (IL-1).	Dermatan Sulfate	15-31	interleukin 1 beta	Homo sapiens	211-215
7974347-7	1994	Expression of an appropriately modified form of the rabbit HCII clone in an in vitro reticulocyte expression system yielded two major polypeptides, of 60 and 56 kD respectively, both of which were able to form SDS-stable complexes with human alpha-thrombin, in a reaction accelerated by dermatan sulphate.	Dermatan Sulfate	287-304	heparin cofactor 2	Oryctolagus cuniculus	59-63
8091403-0	1994	Relative influence of different disulphate disaccharide clusters on the HCII-mediated inhibition of thrombin by dermatan sulphates of different origins.	Dermatan Sulfate	112-130	serpin family D member 1	Homo sapiens	72-76
8091403-0	1994	Relative influence of different disulphate disaccharide clusters on the HCII-mediated inhibition of thrombin by dermatan sulphates of different origins.	Dermatan Sulfate	112-130	coagulation factor II, thrombin	Homo sapiens	100-108
8091403-1	1994	Besides the major monosulphated disaccharide sequences (IdoA-GalNAc4SO3), dermatan sulphates (DS) contain the oversulphated sequences (IdoA2SO3-GalNAc4SO3) and (IdoA-GalNAc4, 6SO3), the concentration of which is correlated with the HCII-mediated inhibition of thrombin by DS.	Dermatan Sulfate	74-92	serpin family D member 1	Homo sapiens	232-236
8091403-1	1994	Besides the major monosulphated disaccharide sequences (IdoA-GalNAc4SO3), dermatan sulphates (DS) contain the oversulphated sequences (IdoA2SO3-GalNAc4SO3) and (IdoA-GalNAc4, 6SO3), the concentration of which is correlated with the HCII-mediated inhibition of thrombin by DS.	Dermatan Sulfate	74-92	coagulation factor II, thrombin	Homo sapiens	260-268
8182050-8	1994	Heparan sulfate, chondroitin sulfate, and dermatan sulfate, three glycosaminoglycans structurally related to heparin, were > or = 80-fold less effective in binding to RMCP-1 than heparin.	Dermatan Sulfate	42-58	mast cell protease 1-like 1	Rattus norvegicus	170-176
8085247-2	1994	Recent studies suggest that dermatan sulphate which catalyzes thrombin inhibition by heparin cofactor II (HCII), can inhibit TF and TG as effectively as HEP.	Dermatan Sulfate	28-45	prothrombin	Oryctolagus cuniculus	62-70
8085247-2	1994	Recent studies suggest that dermatan sulphate which catalyzes thrombin inhibition by heparin cofactor II (HCII), can inhibit TF and TG as effectively as HEP.	Dermatan Sulfate	28-45	heparin cofactor 2	Oryctolagus cuniculus	85-104
8085247-2	1994	Recent studies suggest that dermatan sulphate which catalyzes thrombin inhibition by heparin cofactor II (HCII), can inhibit TF and TG as effectively as HEP.	Dermatan Sulfate	28-45	heparin cofactor 2	Oryctolagus cuniculus	106-110
8161203-5	1994	The binding of [125I]bFGF to rat growth plate ECM was inhibited by the addition of heparin, heparan sulfate, and dermatan sulfate.	Dermatan Sulfate	113-129	fibroblast growth factor 2	Rattus norvegicus	21-25
8197917-5	1994	Chondroitinase ABC treatment also eliminated the staining of filaments in the collagenous layers (chondroitin sulfate and dermatan sulfate).	Dermatan Sulfate	122-138	galactosamine (N-acetyl)-6-sulfate sulfatase	Mus musculus	0-14
21244893-3	1994	Both heparin cofactor II and thrombin interact with highly negatively charged glycosaminoglycans like heparin and dermatan sulfate, and they both are leukocyte chemoattractants.	Dermatan Sulfate	114-130	coagulation factor II, thrombin	Homo sapiens	29-37
8017769-4	1994	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic region of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Dermatan Sulfate	28-44	serpin family D member 1	Homo sapiens	89-93
8017769-4	1994	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic region of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Dermatan Sulfate	28-44	coagulation factor II, thrombin	Homo sapiens	140-148
8017769-4	1994	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic region of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Dermatan Sulfate	28-44	coagulation factor II, thrombin	Homo sapiens	187-195
8017769-4	1994	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic region of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Dermatan Sulfate	28-44	serpin family D member 1	Homo sapiens	196-200
8017769-1	1994	The binding sites for dermatan sulfate and heparin in HCII overlap but are not identical.	Dermatan Sulfate	22-38	serpin family D member 1	Homo sapiens	54-58
8017769-2	1994	This may explain the observation that HCII binds nonspecifically to heparin oligosaccharides, but preferentially binds to a minor hexasaccharide isolated from dermatan sulfate.	Dermatan Sulfate	159-175	serpin family D member 1	Homo sapiens	38-42
8017769-3	1994	The tissue distribution of dermatan sulfate molecules containing the high-affinity HCII binding site may regulate HCII activity in vivo.	Dermatan Sulfate	27-43	serpin family D member 1	Homo sapiens	83-87
8017769-3	1994	The tissue distribution of dermatan sulfate molecules containing the high-affinity HCII binding site may regulate HCII activity in vivo.	Dermatan Sulfate	27-43	serpin family D member 1	Homo sapiens	114-118
8181003-7	1994	The HCII activities were evaluated for different relative molecular mass of dermatan sulfate.	Dermatan Sulfate	76-92	serpin family D member 1	Homo sapiens	4-8
8070133-6	1994	The localised increases in HA and DS content in areas where collagen and elastin were increased suggests that these GAGs are functionally related to these fibrous proteins in aorta, whereas CS and HS are not.	Dermatan Sulfate	34-36	elastin	Homo sapiens	73-80
8029809-5	1994	DS appears to be as effective as H in controlling thrombin production during leukaemic cytolysis and may represent a safer alternative to H in the management of DIC in acute leukaemia.	Dermatan Sulfate	0-2	coagulation factor II, thrombin	Homo sapiens	50-58
7517179-7	1994	However, when binding of CD44 was tested in vitro to chondroitinase-sensitive purified glycosaminoglycans, such as chondroitin-4-sulfate, chondroitin-6-sulfate and dermatan sulfate, no binding was demonstrable, suggesting either that a novel type of chondroitinase-sensitive glycosaminoglycan is recognized by CD44 or that association of the glycosaminoglycan with a core protein is required for recognition by CD44.	Dermatan Sulfate	164-180	CD44 antigen	Mus musculus	25-29
7908224-1	1994	Heparin cofactor II (HCII) is a glycoprotein in human plasma that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Dermatan Sulfate	111-127	serpin family D member 1	Homo sapiens	0-19
7908224-1	1994	Heparin cofactor II (HCII) is a glycoprotein in human plasma that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Dermatan Sulfate	111-127	serpin family D member 1	Homo sapiens	21-25
7908224-1	1994	Heparin cofactor II (HCII) is a glycoprotein in human plasma that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Dermatan Sulfate	111-127	coagulation factor II, thrombin	Homo sapiens	75-83
7524808-3	1994	Both control and PXE elastin fibres were positive for heparan, dermatan and chondroitin 0-sulphates, decorin and biglycan.	Dermatan Sulfate	63-71	elastin	Homo sapiens	21-28
8057139-5	1994	Therefore, it may be either chondroitin sulfate B (CSB) (dermatan sulfate) or one of the "chondroitin sulfate isomers" (D-H).	Dermatan Sulfate	57-73	excision repair cross-complementing rodent repair deficiency, complementation group 6	Mus musculus	28-55
7824960-0	1994	Pharmacological activity of a low molecular weight dermatan sulfate (desmin) in healthy volunteers.	Dermatan Sulfate	51-67	desmin	Homo sapiens	69-75
8280062-0	1993	Structure and contribution to the heparin cofactor II-mediated inhibition of thrombin of naturally oversulphated sequences of dermatan sulphate.	Dermatan Sulfate	126-143	serpin family D member 1	Sus scrofa	34-53
8241508-6	1993	This was confirmed in a heparin cofactor II-dependent antithrombin assay for DS that showed anticoagulant equivalent to 2.2 +/- 0.3 micrograms/mL (mean +/- SD) of porcine mucosal DS.	Dermatan Sulfate	77-79	serpin family C member 1	Homo sapiens	54-66
8148486-0	1993	Evidence for thrombin binding to dermatan sulphate sites in the rabbit aorta subendothelium in vitro.	Dermatan Sulfate	33-50	prothrombin	Oryctolagus cuniculus	13-21
8148486-1	1993	The proposal that thrombin binds to dermatan sulphate chains of extracellular proteoglycans has been examined directly using the subendothelium of the rabbit aorta.	Dermatan Sulfate	36-53	prothrombin	Oryctolagus cuniculus	18-26
8148486-4	1993	The addition of dermatan sulphate inhibited, competitively, up to 50% of thrombin from binding to the subendothelium whereas chondroitin-4 or -6 sulphates had little or no effect.	Dermatan Sulfate	16-33	prothrombin	Oryctolagus cuniculus	73-81
8148486-7	1993	It is concluded that, when 125I-thrombin is bound in vitro at a concentration of < 30 fmol/cm2 of aorta intima-media, approximately 50% of subendothelial 125I-thrombin is bound to dermatan sulphate chains of proteoglycan in the extracellular matrix.	Dermatan Sulfate	183-200	prothrombin	Oryctolagus cuniculus	32-40
8148486-7	1993	It is concluded that, when 125I-thrombin is bound in vitro at a concentration of < 30 fmol/cm2 of aorta intima-media, approximately 50% of subendothelial 125I-thrombin is bound to dermatan sulphate chains of proteoglycan in the extracellular matrix.	Dermatan Sulfate	183-200	prothrombin	Oryctolagus cuniculus	162-170
8148486-8	1993	The possibility is discussed that dermatan sulphate chains may function as thrombin-binding loci to control or augment thrombin activity in the ECM of the injured vascular wall in vivo.	Dermatan Sulfate	34-51	prothrombin	Oryctolagus cuniculus	75-83
8148486-8	1993	The possibility is discussed that dermatan sulphate chains may function as thrombin-binding loci to control or augment thrombin activity in the ECM of the injured vascular wall in vivo.	Dermatan Sulfate	34-51	prothrombin	Oryctolagus cuniculus	119-127
8280062-0	1993	Structure and contribution to the heparin cofactor II-mediated inhibition of thrombin of naturally oversulphated sequences of dermatan sulphate.	Dermatan Sulfate	126-143	coagulation factor II, thrombin	Sus scrofa	77-85
8280062-10	1993	The heparin cofactor II activity of DS, RO-DS and SD-DS fragments decreases with decreasing M(r).	Dermatan Sulfate	36-38	serpin family D member 1	Sus scrofa	4-23
7691835-7	1993	Thus hyaluronic acid, dermatan sulphate, chondroitin-4-sulphate, chondroitin-6-sulphate, and even unchanged dextran all potentiated aFGF induced neuronal survival.	Dermatan Sulfate	22-39	fibroblast growth factor 1	Mus musculus	132-136
8245966-4	1993	A beta(1-28) associates with heparin, heparan sulfate, dermatan sulfate, and chondroitin sulfate.	Dermatan Sulfate	55-71	amyloid beta precursor protein	Homo sapiens	0-6
8404691-5	1993	Treatment of whole ovarian dispersates with IL-1 beta (10 ng/ml) produced substantial increments in the accumulation of extracellular macromolecular material [11.5-, 2.9- and 2.6-fold for hyaluronic acid (HA), heparan sulfate (HS) and dermatan sulfate (DS) proteoglycans, respectively].	Dermatan Sulfate	235-251	interleukin 1 beta	Rattus norvegicus	44-53
8404691-5	1993	Treatment of whole ovarian dispersates with IL-1 beta (10 ng/ml) produced substantial increments in the accumulation of extracellular macromolecular material [11.5-, 2.9- and 2.6-fold for hyaluronic acid (HA), heparan sulfate (HS) and dermatan sulfate (DS) proteoglycans, respectively].	Dermatan Sulfate	253-255	interleukin 1 beta	Rattus norvegicus	44-53
8244397-1	1993	Deficiency of the lysosomal enzyme iduronate-2-sulfatase (IDS; EC 3.1.6.13) results in the storage of the glycosaminoglycans heparan sulfate and dermatan sulfate, which leads to the lysosomal storage disorder mucopolysaccharidosis type II.	Dermatan Sulfate	145-161	iduronate 2-sulfatase	Homo sapiens	35-56
8244397-1	1993	Deficiency of the lysosomal enzyme iduronate-2-sulfatase (IDS; EC 3.1.6.13) results in the storage of the glycosaminoglycans heparan sulfate and dermatan sulfate, which leads to the lysosomal storage disorder mucopolysaccharidosis type II.	Dermatan Sulfate	145-161	iduronate 2-sulfatase	Homo sapiens	58-61
8317997-5	1993	Dermatan sulphate was the predominant glycosaminoglycan present on biglycan and decorin in annulus fibrosus extracts, whereas chondroitin 4-sulphate was present in both small proteoglycans isolated from cartilage end-plate.	Dermatan Sulfate	0-17	biglycan	Homo sapiens	67-75
8259546-0	1993	The additive effect of low molecular weight heparins on thrombin inhibition by dermatan sulfate.	Dermatan Sulfate	79-95	coagulation factor II, thrombin	Homo sapiens	56-64
8259546-2	1993	In platelet poor plasma, LMWH enhances the effect of DS on thrombin (IIa) inhibition as determined by thrombin clotting times and with a chromogenic substrate assay.	Dermatan Sulfate	53-55	coagulation factor II, thrombin	Homo sapiens	59-67
8259546-2	1993	In platelet poor plasma, LMWH enhances the effect of DS on thrombin (IIa) inhibition as determined by thrombin clotting times and with a chromogenic substrate assay.	Dermatan Sulfate	53-55	coagulation factor II, thrombin	Homo sapiens	102-110
8259546-6	1993	DS addition selectively increases the formation of heparin cofactor II (HCII)-IIa complexes, whereas LMWH enhances ATIII-IIa complex generation.	Dermatan Sulfate	0-2	serpin family D member 1	Homo sapiens	72-76
8259546-7	1993	Compared to plasma containing DS alone, the formation of ATIII-IIa complexes also is increased when the combination of DS and LMWH is added.	Dermatan Sulfate	119-121	serpin family C member 1	Homo sapiens	57-62
8335699-1	1993	Three sulphated polysaccharides, dermatan sulphate, fucan and heparin, were fractionated according to their affinity towards antithrombin III (ATIII) and heparin cofactor II (HCII), the two main physiological thrombin (IIa) inhibitors.	Dermatan Sulfate	33-50	serpin family C member 1	Homo sapiens	125-141
8335699-1	1993	Three sulphated polysaccharides, dermatan sulphate, fucan and heparin, were fractionated according to their affinity towards antithrombin III (ATIII) and heparin cofactor II (HCII), the two main physiological thrombin (IIa) inhibitors.	Dermatan Sulfate	33-50	serpin family C member 1	Homo sapiens	143-148
8335699-1	1993	Three sulphated polysaccharides, dermatan sulphate, fucan and heparin, were fractionated according to their affinity towards antithrombin III (ATIII) and heparin cofactor II (HCII), the two main physiological thrombin (IIa) inhibitors.	Dermatan Sulfate	33-50	serpin family D member 1	Homo sapiens	154-173
8335699-1	1993	Three sulphated polysaccharides, dermatan sulphate, fucan and heparin, were fractionated according to their affinity towards antithrombin III (ATIII) and heparin cofactor II (HCII), the two main physiological thrombin (IIa) inhibitors.	Dermatan Sulfate	33-50	serpin family D member 1	Homo sapiens	175-179
8508806-7	1993	The capacity of different GAGs to protect bFGF from proteolytic cleavage decreases in the following order: heparin > heparan sulfate > dermatan sulfate = chondroitin sulfates A and C > hyaluronic acid = K5 polysaccharide, indicating that both the degree of sulfation and the backbone structure of GAG modulate its interaction with bFGF.	Dermatan Sulfate	141-157	fibroblast growth factor 2	Homo sapiens	42-46
8461463-1	1993	The relationship between the antithrombotic activity of dermatan sulfate (DS) in vivo and its catalytic effect on the inhibition of thrombin by heparin cofactor II (HC II) in vitro was investigated.	Dermatan Sulfate	56-72	prothrombin	Oryctolagus cuniculus	132-140
8489237-7	1993	The galactosamine-containing glycosaminoglycans, chondroitin sulfate and dermatan sulfate, differ from heparin in that they increase the quantity of soluble elastin in the culture medium and decrease the deposition of insoluble elastin in the extracellular matrix.	Dermatan Sulfate	73-89	elastin	Rattus norvegicus	157-164
8489237-7	1993	The galactosamine-containing glycosaminoglycans, chondroitin sulfate and dermatan sulfate, differ from heparin in that they increase the quantity of soluble elastin in the culture medium and decrease the deposition of insoluble elastin in the extracellular matrix.	Dermatan Sulfate	73-89	elastin	Rattus norvegicus	228-235
8338783-1	1993	Transplacental passage of the low molecular weight dermatan sulphate Desmin 370 was investigated in pregnant sheep, using 125I-labelled Desmin 370 to optimize the sensitivity of the study.	Dermatan Sulfate	51-68	desmin	Ovis aries	69-75
8461463-1	1993	The relationship between the antithrombotic activity of dermatan sulfate (DS) in vivo and its catalytic effect on the inhibition of thrombin by heparin cofactor II (HC II) in vitro was investigated.	Dermatan Sulfate	56-72	heparin cofactor 2	Oryctolagus cuniculus	144-163
8461463-1	1993	The relationship between the antithrombotic activity of dermatan sulfate (DS) in vivo and its catalytic effect on the inhibition of thrombin by heparin cofactor II (HC II) in vitro was investigated.	Dermatan Sulfate	56-72	heparin cofactor 2	Oryctolagus cuniculus	165-170
8461463-1	1993	The relationship between the antithrombotic activity of dermatan sulfate (DS) in vivo and its catalytic effect on the inhibition of thrombin by heparin cofactor II (HC II) in vitro was investigated.	Dermatan Sulfate	74-76	prothrombin	Oryctolagus cuniculus	132-140
8461463-1	1993	The relationship between the antithrombotic activity of dermatan sulfate (DS) in vivo and its catalytic effect on the inhibition of thrombin by heparin cofactor II (HC II) in vitro was investigated.	Dermatan Sulfate	74-76	heparin cofactor 2	Oryctolagus cuniculus	144-163
8461463-1	1993	The relationship between the antithrombotic activity of dermatan sulfate (DS) in vivo and its catalytic effect on the inhibition of thrombin by heparin cofactor II (HC II) in vitro was investigated.	Dermatan Sulfate	74-76	heparin cofactor 2	Oryctolagus cuniculus	165-170
8497846-1	1993	An iodinated derivative of the low molecular weight dermatan sulphate Desmin 370 was administered to rats by intravenous, subcutaneous and intramuscular routes in conjunction with unlabelled Desmin 370.	Dermatan Sulfate	52-69	desmin	Rattus norvegicus	70-76
1493802-10	1992	Sulfated polysaccharides such as heparinsulfate and dermatansulfate modulate the interaction of 5"-nucleotidase and laminin/nidogen in a complex biphasic manner and might also regulate the binding reaction in vivo.	Dermatan Sulfate	52-67	5'-nucleotidase ecto	Gallus gallus	96-111
8440685-5	1993	Treatment of skin decorin and GAG chains with chondroitinase ABC totally eliminated the ability of these compounds to accelerate thrombin inhibition by heparin cofactor II suggesting that dermatan sulfate was responsible for this action.	Dermatan Sulfate	188-204	decorin	Homo sapiens	18-25
8440685-5	1993	Treatment of skin decorin and GAG chains with chondroitinase ABC totally eliminated the ability of these compounds to accelerate thrombin inhibition by heparin cofactor II suggesting that dermatan sulfate was responsible for this action.	Dermatan Sulfate	188-204	coagulation factor II, thrombin	Homo sapiens	129-137
8429040-9	1993	The rate constants for inhibition of wild-type thrombin by HCII in the presence of heparin or dermatan sulfate were 9.2 x 10(8) M-1 min-1 and 9.0 x 10(8) M-1 min-1, respectively.	Dermatan Sulfate	94-110	coagulation factor II, thrombin	Homo sapiens	47-55
8429040-9	1993	The rate constants for inhibition of wild-type thrombin by HCII in the presence of heparin or dermatan sulfate were 9.2 x 10(8) M-1 min-1 and 9.0 x 10(8) M-1 min-1, respectively.	Dermatan Sulfate	94-110	serpin family D member 1	Homo sapiens	59-63
8429040-9	1993	The rate constants for inhibition of wild-type thrombin by HCII in the presence of heparin or dermatan sulfate were 9.2 x 10(8) M-1 min-1 and 9.0 x 10(8) M-1 min-1, respectively.	Dermatan Sulfate	94-110	CD59 molecule (CD59 blood group)	Homo sapiens	132-137
8429040-9	1993	The rate constants for inhibition of wild-type thrombin by HCII in the presence of heparin or dermatan sulfate were 9.2 x 10(8) M-1 min-1 and 9.0 x 10(8) M-1 min-1, respectively.	Dermatan Sulfate	94-110	CD59 molecule (CD59 blood group)	Homo sapiens	158-163
8440685-1	1993	Two small interstitial dermatan sulfate-containing proteoglycans, biglycan and decorin, are present in extracellular matrices of skin, tendon, ligament, and cartilage.	Dermatan Sulfate	23-39	biglycan	Homo sapiens	66-74
8440685-1	1993	Two small interstitial dermatan sulfate-containing proteoglycans, biglycan and decorin, are present in extracellular matrices of skin, tendon, ligament, and cartilage.	Dermatan Sulfate	23-39	decorin	Homo sapiens	79-86
8440685-3	1993	In solution, heparin cofactor II inhibition of thrombin is accelerated by intact biglycan or decorin and by the dermatan sulfate-containing glycosaminoglycan (GAG) chains prepared from the proteoglycans, while core protein from cartilage biglycan had no effect.	Dermatan Sulfate	112-128	coagulation factor II, thrombin	Homo sapiens	47-55
8431448-4	1993	Inhibition of thrombin by PAI-1 was quantitatively analyzed in the presence of a wide range of concentrations of heparin, heparan sulfate, dermatan sulfate, chondroitin 4-sulfate, chondroitin 6-sulfate, keratan sulfate, and hyaluronic acid by measuring residual amidolytic activity.	Dermatan Sulfate	139-155	serpin family E member 1	Homo sapiens	26-31
8457895-3	1993	On a poly-D-lysine substrate, the rank ordering of specific neurite growth activity based on protein concentration was 330 kDa HSPG >> 100 kDa HSPG/chondroitin sulphate (CS) PG mixture or hybrid > 330 kDa CSPG > 50 kDa CSPG/dermatan sulphate (DS) PG mixture or hybrid and the 31 kDa sulphoprotein.	Dermatan Sulfate	236-253	glypican 3	Homo sapiens	127-131
8477906-4	1993	Any compound that inactivates thrombin, or can potentiate thrombin inactivation by an inhibitor, can be measured with this assay, including standard heparin, low molecular weight heparins, hirudin, alpha-NAPAP, pentosan polysulphate and dermatan sulphate.	Dermatan Sulfate	237-254	coagulation factor II, thrombin	Homo sapiens	58-66
1493802-10	1992	Sulfated polysaccharides such as heparinsulfate and dermatansulfate modulate the interaction of 5"-nucleotidase and laminin/nidogen in a complex biphasic manner and might also regulate the binding reaction in vivo.	Dermatan Sulfate	52-67	laminin, beta 2 (laminin S)	Gallus gallus	116-123
1505961-1	1992	In humans, a deficiency of the lysosomal hydrolase alpha-L-iduronidase (IDUA;EC 3.2.1.76) results in the lysosomal storage of the glycosaminoglycans heparan sulfate and dermatan sulfate, thereby causing the lysosomal storage disorder mucopolysaccharidosis type I.	Dermatan Sulfate	169-185	alpha-L-iduronidase	Homo sapiens	51-70
1429568-6	1992	Internalization of bFGF in CHO cells not expressing FGF receptors was inhibited by heparin, heparan sulfate, and dermatan sulfate, the same glycosaminoglycans that block binding to cell-surface heparin sulfates.	Dermatan Sulfate	113-129	fibroblast growth factor 2	Bos taurus	19-23
1429568-6	1992	Internalization of bFGF in CHO cells not expressing FGF receptors was inhibited by heparin, heparan sulfate, and dermatan sulfate, the same glycosaminoglycans that block binding to cell-surface heparin sulfates.	Dermatan Sulfate	113-129	fibroblast growth factor 2	Bos taurus	20-23
1333106-3	1992	In the present study the inhibitory activity of HC II was investigated as function of various dermatan sulfate fractions and its stability was tested against oxidation reagents similar to thus secreted by activated leucocytes.	Dermatan Sulfate	94-110	serpin family D member 1	Homo sapiens	48-53
1333106-4	1992	High affinity dermatan sulfate (DS) increased the antithrombin inhibition activity of HC II about 1000-fold in contrast to about 100-fold in the case of low affinity DS.	Dermatan Sulfate	14-30	serpin family C member 1	Homo sapiens	50-62
1333106-4	1992	High affinity dermatan sulfate (DS) increased the antithrombin inhibition activity of HC II about 1000-fold in contrast to about 100-fold in the case of low affinity DS.	Dermatan Sulfate	14-30	serpin family D member 1	Homo sapiens	86-91
1333106-4	1992	High affinity dermatan sulfate (DS) increased the antithrombin inhibition activity of HC II about 1000-fold in contrast to about 100-fold in the case of low affinity DS.	Dermatan Sulfate	32-34	serpin family C member 1	Homo sapiens	50-62
1333106-4	1992	High affinity dermatan sulfate (DS) increased the antithrombin inhibition activity of HC II about 1000-fold in contrast to about 100-fold in the case of low affinity DS.	Dermatan Sulfate	32-34	serpin family D member 1	Homo sapiens	86-91
1427856-1	1992	Arylsulfatase B (ARSB) is the lysosomal enzyme that catalyzes the hydrolysis of 4-sulfate groups from N-acetylgalactosamine 4-sulfate moieties on the glycosaminoglycans, dermatan sulfate and chondroitin sulfate A.	Dermatan Sulfate	170-186	arylsulfatase B	Homo sapiens	0-15
1427856-1	1992	Arylsulfatase B (ARSB) is the lysosomal enzyme that catalyzes the hydrolysis of 4-sulfate groups from N-acetylgalactosamine 4-sulfate moieties on the glycosaminoglycans, dermatan sulfate and chondroitin sulfate A.	Dermatan Sulfate	170-186	arylsulfatase B	Homo sapiens	17-21
1505961-1	1992	In humans, a deficiency of the lysosomal hydrolase alpha-L-iduronidase (IDUA;EC 3.2.1.76) results in the lysosomal storage of the glycosaminoglycans heparan sulfate and dermatan sulfate, thereby causing the lysosomal storage disorder mucopolysaccharidosis type I.	Dermatan Sulfate	169-185	alpha-L-iduronidase	Homo sapiens	72-76
1442260-1	1992	The binding sites for dermatan sulfate and heparin in HCII overlap but are not identical.	Dermatan Sulfate	22-38	serpin family D member 1	Homo sapiens	54-58
1550122-1	1992	alpha-L-Iduronidase activity is deficient in mucopolysaccharidosis type I (MPS I; Hurler syndrome, Scheie syndrome) patients and results in the disruption of the sequential degradation of the glycosaminoglycans dermatan sulfate and heparan sulfate.	Dermatan Sulfate	211-227	alpha-L-iduronidase	Homo sapiens	0-19
1581235-2	1992	Suc-DS was on average 2-3 times more potent than DS in catalysing the inhibition of thrombin by heparin cofactor II and in prolonging the activated partial thromboplastin time and the thrombin clotting time.	Dermatan Sulfate	4-6	prothrombin	Oryctolagus cuniculus	84-92
1581235-2	1992	Suc-DS was on average 2-3 times more potent than DS in catalysing the inhibition of thrombin by heparin cofactor II and in prolonging the activated partial thromboplastin time and the thrombin clotting time.	Dermatan Sulfate	4-6	heparin cofactor 2	Oryctolagus cuniculus	96-115
1581235-2	1992	Suc-DS was on average 2-3 times more potent than DS in catalysing the inhibition of thrombin by heparin cofactor II and in prolonging the activated partial thromboplastin time and the thrombin clotting time.	Dermatan Sulfate	4-6	prothrombin	Oryctolagus cuniculus	184-192
1740413-4	1992	Interestingly, in the presence of glycosaminoglycans the maximal inhibition rate constants by HC with heparin and dermatan sulfate, respectively, were as follows: 30.0 x 10(7) and 60.5 x 10(7) for alpha-thrombin, 14.6 x 10(7) and 24.3 x 10(7) for epsilon-thrombin, and 0.017 x 10(7) and 0.034 x 10(7) M-1 min-1 for gamma T-thrombin.	Dermatan Sulfate	114-130	coagulation factor II, thrombin	Homo sapiens	203-211
1740413-4	1992	Interestingly, in the presence of glycosaminoglycans the maximal inhibition rate constants by HC with heparin and dermatan sulfate, respectively, were as follows: 30.0 x 10(7) and 60.5 x 10(7) for alpha-thrombin, 14.6 x 10(7) and 24.3 x 10(7) for epsilon-thrombin, and 0.017 x 10(7) and 0.034 x 10(7) M-1 min-1 for gamma T-thrombin.	Dermatan Sulfate	114-130	coagulation factor II, thrombin	Homo sapiens	255-263
1740413-4	1992	Interestingly, in the presence of glycosaminoglycans the maximal inhibition rate constants by HC with heparin and dermatan sulfate, respectively, were as follows: 30.0 x 10(7) and 60.5 x 10(7) for alpha-thrombin, 14.6 x 10(7) and 24.3 x 10(7) for epsilon-thrombin, and 0.017 x 10(7) and 0.034 x 10(7) M-1 min-1 for gamma T-thrombin.	Dermatan Sulfate	114-130	CD59 molecule (CD59 blood group)	Homo sapiens	305-310
1740413-4	1992	Interestingly, in the presence of glycosaminoglycans the maximal inhibition rate constants by HC with heparin and dermatan sulfate, respectively, were as follows: 30.0 x 10(7) and 60.5 x 10(7) for alpha-thrombin, 14.6 x 10(7) and 24.3 x 10(7) for epsilon-thrombin, and 0.017 x 10(7) and 0.034 x 10(7) M-1 min-1 for gamma T-thrombin.	Dermatan Sulfate	114-130	coagulation factor II, thrombin	Homo sapiens	255-263
1521342-2	1992	Heparin cofactor II (HCII) is a thrombin inhibitor in human plasma, the activity of which is enhanced by heparin and dermatan sulfate.	Dermatan Sulfate	117-133	serpin family D member 1	Homo sapiens	0-19
1521342-2	1992	Heparin cofactor II (HCII) is a thrombin inhibitor in human plasma, the activity of which is enhanced by heparin and dermatan sulfate.	Dermatan Sulfate	117-133	serpin family D member 1	Homo sapiens	21-25
1521342-2	1992	Heparin cofactor II (HCII) is a thrombin inhibitor in human plasma, the activity of which is enhanced by heparin and dermatan sulfate.	Dermatan Sulfate	117-133	coagulation factor II, thrombin	Homo sapiens	32-40
1730217-2	1992	Heparin and dermatan sulfate prolong the lag phases associated with the activation of the three proteins by catalyzing the inhibition of endogenously generated thrombin.	Dermatan Sulfate	12-28	coagulation factor II, thrombin	Homo sapiens	160-168
1579900-0	1992	Use of purified dermatan sulfate for heparin cofactor II (HC II) assay.	Dermatan Sulfate	16-32	serpin family D member 1	Homo sapiens	37-56
1579900-0	1992	Use of purified dermatan sulfate for heparin cofactor II (HC II) assay.	Dermatan Sulfate	16-32	serpin family D member 1	Homo sapiens	58-63
1377216-4	1992	SAP also blocked the effects of heparin and dermatan sulfate on the inhibition of thrombin by heparin cofactor II.	Dermatan Sulfate	44-60	amyloid P component, serum	Homo sapiens	0-3
1377216-4	1992	SAP also blocked the effects of heparin and dermatan sulfate on the inhibition of thrombin by heparin cofactor II.	Dermatan Sulfate	44-60	coagulation factor II, thrombin	Homo sapiens	82-90
1593214-3	1992	The absolute increment in the total amount of liver SGAG in the vitamin A--pretreated group was followed by a more important increase in the concentration of dermatan sulfate as compared with the CCl4 group (dermatan sulfate-to-heparan sulfate ratio: 1.15 for the CCl4 group vs 1.70 for the vitamin A--pretreated group).	Dermatan Sulfate	208-224	C-C motif chemokine ligand 4	Rattus norvegicus	264-268
1381850-1	1992	Heparin cofactor II (HCII) is a specific thrombin inhibitor; its inhibitory activity is stimulated by heparin (Hep) and dermatan sulfate (DS).	Dermatan Sulfate	120-136	serpin family D member 1	Homo sapiens	21-25
1381850-1	1992	Heparin cofactor II (HCII) is a specific thrombin inhibitor; its inhibitory activity is stimulated by heparin (Hep) and dermatan sulfate (DS).	Dermatan Sulfate	138-140	serpin family D member 1	Homo sapiens	21-25
1629944-6	1992	Antibodies against rat decorin, a chondroitin/dermatan sulfate PG synthesized by various cell types, specifically immunoprecipitated this PG from a mixture of PGs.	Dermatan Sulfate	46-62	decorin	Rattus norvegicus	23-30
1555588-0	1992	Transforming growth factor-beta induces selective increase of proteoglycan production and changes in the copolymeric structure of dermatan sulphate in human skin fibroblasts.	Dermatan Sulfate	130-147	transforming growth factor beta 1	Homo sapiens	0-31
1555588-5	1992	Only a small effect was observed on another dermatan sulphate proteoglycan, PG-S2 (also named decorin).	Dermatan Sulfate	44-61	decorin	Homo sapiens	76-81
1555588-10	1992	However, the dermatan sulphate chains on biglycan and decorin from TGF-beta treated cultures contained a larger proportion of D-glucuronosyl residues than those derived from untreated cultures.	Dermatan Sulfate	13-30	biglycan	Homo sapiens	41-49
1555588-10	1992	However, the dermatan sulphate chains on biglycan and decorin from TGF-beta treated cultures contained a larger proportion of D-glucuronosyl residues than those derived from untreated cultures.	Dermatan Sulfate	13-30	transforming growth factor beta 1	Homo sapiens	67-75
1555588-13	1992	Furthermore, the dermatan sulphate chains synthesized on the xyloside in TGF-beta-treated fibroblasts contained a larger proportion of D-glucuronosyl residues than those of the control.	Dermatan Sulfate	17-34	transforming growth factor beta 1	Homo sapiens	73-81
1386167-0	1992	Plasmin stimulates the release of dermatan sulfate from vascular smooth muscle cells in culture.	Dermatan Sulfate	34-50	plasminogen	Bos taurus	0-7
1386167-6	1992	A characterization of 35S-GAG revealed that plasmin increased both dermatan sulfate and the other 35S-GAG in the medium.	Dermatan Sulfate	67-83	plasminogen	Bos taurus	44-51
1386167-8	1992	From these results, it was suggested that a endogenous thrombin inhibitor heparin cofactor II may be activated in the liquid phase by dermatan sulfate released from plasmin-stimulated vascular smooth muscle cells when the vascular is disrupted and plasma is exposed to extravessel.	Dermatan Sulfate	134-150	coagulation factor II, thrombin	Bos taurus	55-63
1386167-8	1992	From these results, it was suggested that a endogenous thrombin inhibitor heparin cofactor II may be activated in the liquid phase by dermatan sulfate released from plasmin-stimulated vascular smooth muscle cells when the vascular is disrupted and plasma is exposed to extravessel.	Dermatan Sulfate	134-150	serpin family D member 1	Bos taurus	74-93
1386167-8	1992	From these results, it was suggested that a endogenous thrombin inhibitor heparin cofactor II may be activated in the liquid phase by dermatan sulfate released from plasmin-stimulated vascular smooth muscle cells when the vascular is disrupted and plasma is exposed to extravessel.	Dermatan Sulfate	134-150	plasminogen	Bos taurus	165-172
1621239-1	1992	Dermatan sulphate (MF 701) is a natural glycosaminoglycan that catalyses thrombin inhibition by heparin cofactor II.	Dermatan Sulfate	0-17	coagulation factor II, thrombin	Homo sapiens	73-81
1554154-0	1992	Interaction between histidine-rich glycoprotein and platelet factor 4 with dermatan sulfate and low-molecular-weight dermatan sulfate.	Dermatan Sulfate	75-91	histidine rich glycoprotein	Homo sapiens	20-47
1554154-0	1992	Interaction between histidine-rich glycoprotein and platelet factor 4 with dermatan sulfate and low-molecular-weight dermatan sulfate.	Dermatan Sulfate	117-133	histidine rich glycoprotein	Homo sapiens	20-47
1554154-5	1992	In fact, HRG is 10 times less effective than PF 4 in neutralizing the 50% antithrombin activity of HC II in the presence of DS.	Dermatan Sulfate	124-126	histidine rich glycoprotein	Homo sapiens	9-12
1554154-5	1992	In fact, HRG is 10 times less effective than PF 4 in neutralizing the 50% antithrombin activity of HC II in the presence of DS.	Dermatan Sulfate	124-126	serpin family D member 1	Homo sapiens	99-104
1442260-2	1992	This may explain the observation that HCII binds non-specifically to heparin oligosaccharides but preferentially binds to a minor hexasaccharide isolated from dermatan sulfate having the structure shown in Fig.	Dermatan Sulfate	159-175	serpin family D member 1	Homo sapiens	38-42
1442260-4	1992	The tissue distribution of dermatan sulfate molecules containing the high-affinity HCII binding site may regulate HCII activity in vivo.	Dermatan Sulfate	27-43	serpin family D member 1	Homo sapiens	83-87
1442260-4	1992	The tissue distribution of dermatan sulfate molecules containing the high-affinity HCII binding site may regulate HCII activity in vivo.	Dermatan Sulfate	27-43	serpin family D member 1	Homo sapiens	114-118
1442260-5	1992	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic domain of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Dermatan Sulfate	28-44	serpin family D member 1	Homo sapiens	89-93
1442260-5	1992	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic domain of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Dermatan Sulfate	28-44	coagulation factor II, thrombin	Homo sapiens	140-148
1442260-5	1992	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic domain of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Dermatan Sulfate	28-44	coagulation factor II, thrombin	Homo sapiens	187-195
1442260-5	1992	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic domain of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Dermatan Sulfate	28-44	serpin family D member 1	Homo sapiens	196-200
1370306-1	1992	We used a polyclonal antibody and a mixture of three monoclonal antibodies (MAb), all recognizing the protein core of the small dermatan sulfate proteoglycan (DSPG) (known as PG-II or decorin) derived from human skin fibroblasts, to immunolocalize this molecule in the characteristic lesions in Alzheimer"s brain.	Dermatan Sulfate	128-144	decorin	Homo sapiens	175-180
1301941-1	1992	Mucopolysaccharidosis type I (MPS-I) is an autosomal recessive genetic disease caused by a deficiency of the glycosidase alpha-L-iduronidase which is required for the lysosomal degradation of the glycosaminoglycans heparan sulfate and dermatan sulfate.	Dermatan Sulfate	235-251	alpha-L-iduronidase	Homo sapiens	121-140
1576824-3	1992	The dermatan sulfate proteoglycans (DS-PGI and DS-PGII) were detected in normal and osteoarthritic cartilage.	Dermatan Sulfate	4-20	biglycan	Homo sapiens	39-42
1301196-1	1992	Mucopolysaccharidosis type I (MPS-I) is an autosomal recessive genetic disease caused by a deficiency of the glycosidase alpha-L-iduronidase which is required for the lysosomal degradation of the glycosaminoglycans heparan sulfate and dermatan sulfate.	Dermatan Sulfate	235-251	alpha-L-iduronidase	Homo sapiens	121-140
1946389-1	1991	alpha-L-Iduronidase (IDUA; EC 3.2.1.76) is a lysosomal hydrolase in the metabolic pathway responsible for the degradation of the glycosaminoglycans heparan sulfate and dermatan sulfate.	Dermatan Sulfate	168-184	alpha-L-iduronidase	Homo sapiens	0-19
1661296-6	1991	We hypothesized that CS or dermatan sulfate (DS), both N-acetylgalactosamine glycosaminoglycans (GAGs), may be similar to free galactosugars in causing release of the 67-kD elastin binding protein (EBP) from the smooth muscle cell surfaces and impaired elastin fiber assembly.	Dermatan Sulfate	27-43	EBP, cholestenol delta-isomerase	Rattus norvegicus	198-201
1661296-6	1991	We hypothesized that CS or dermatan sulfate (DS), both N-acetylgalactosamine glycosaminoglycans (GAGs), may be similar to free galactosugars in causing release of the 67-kD elastin binding protein (EBP) from the smooth muscle cell surfaces and impaired elastin fiber assembly.	Dermatan Sulfate	45-47	EBP, cholestenol delta-isomerase	Rattus norvegicus	198-201
1661296-8	1991	Also, reduced EBP was observed in fetal lamb and neonatal rat Ao smooth muscle cells incubated with N-acetylgalactosamine GAGs, CS, and DS, but not with N-acetylglucosamine containing GAGs, heparan sulfate (HS), or hyaluronan.	Dermatan Sulfate	136-138	EBP, cholestenol delta-isomerase	Rattus norvegicus	14-17
1946389-1	1991	alpha-L-Iduronidase (IDUA; EC 3.2.1.76) is a lysosomal hydrolase in the metabolic pathway responsible for the degradation of the glycosaminoglycans heparan sulfate and dermatan sulfate.	Dermatan Sulfate	168-184	alpha-L-iduronidase	Homo sapiens	21-25
1805447-6	1991	On the other hand, A10 cells synthesized both dermatan sulfate and heparan sulfate which are capable of activating HCII.	Dermatan Sulfate	46-62	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	115-119
1646824-3	1991	However, heparin and protein-free dermatan sulfate were able to inhibit endocytosis of decorin in a concentration-dependent manner.	Dermatan Sulfate	34-50	decorin	Homo sapiens	87-94
1805447-7	1991	From these results, it was suggested that HCII would be activated by glycosaminoglycans (GAGs) such as dermatan sulfate of the cell layers and could inhibit thrombin-induced PGI2 production.	Dermatan Sulfate	103-119	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	42-46
1939083-3	1991	Dermatan sulfate and heparin increase the rate of inhibition of thrombin, but not of chymotrypsin, greater than 1000-fold.	Dermatan Sulfate	0-16	coagulation factor II, thrombin	Homo sapiens	64-72
1746001-3	1991	DS enhances the action of heparin cofactor II which inhibits thrombin only.	Dermatan Sulfate	0-2	coagulation factor II, thrombin	Homo sapiens	61-69
1746001-5	1991	The concentrations of DS and PS were chosen so as to obtain equal anti-thrombin and anti-factor Xa activities as in 0.05 U/ml heparin.	Dermatan Sulfate	22-24	coagulation factor II, thrombin	Homo sapiens	71-79
1935986-4	1991	Rat skeletal muscle ECM contains a chondrotin/dermatan sulfate PG which was immunoprecipitated by antibodies against rat decorin.	Dermatan Sulfate	46-62	decorin	Rattus norvegicus	121-128
1831893-8	1991	The relationship between these severe venous thrombotic episodes and the HCII deficiency is discussed in relation to the dermatan sulphate-HCII couple physiology.	Dermatan Sulfate	121-138	serpin family D member 1	Homo sapiens	73-77
1917344-2	1991	In MPS I (Hurler"s syndrome), reduced activity of alpha-L-iduronidase leads to intralysosomal storage of dermatan and heparan sulfate in various tissues.	Dermatan Sulfate	105-113	alpha-L-iduronidase	Homo sapiens	50-69
1794040-1	1991	In this report we describe a system capable of resolving all of the known unsaturated disaccharides derived from the chondroitin sulphates, dermatan sulphate and hyaluronic acid by chondroitinase digestion.	Dermatan Sulfate	140-157	galactosamine (N-acetyl)-6-sulfatase	Homo sapiens	181-195
1926059-4	1991	Thrombin generation was significantly inhibited by DS and heparin as compared to placebo.	Dermatan Sulfate	51-53	coagulation factor II, thrombin	Homo sapiens	0-8
1926059-10	1991	In conclusion, single s.c. doses of DS (200, or 400 mg) inhibit ex vivo thrombin generation equally or more than 5,000 IU heparin and for a longer time.	Dermatan Sulfate	36-38	coagulation factor II, thrombin	Homo sapiens	72-80
1646716-2	1991	The relationship between thrombomodulin-associated O-linked glycosammoglycans (GAGs) and the exogenous GAGs heparin or dermatan sulfate was studied in the inhibition of thrombin by antithrombin III (AT III) or heparin cofactor II (HC II).	Dermatan Sulfate	119-135	thrombomodulin	Oryctolagus cuniculus	25-39
1646716-4	1991	The rapid inactivation of thrombin by HC II in the presence of dermatan sulfate was prevented by both the high-Mr rec-TM and the rabbit TM.	Dermatan Sulfate	63-79	prothrombin	Oryctolagus cuniculus	26-34
1646716-4	1991	The rapid inactivation of thrombin by HC II in the presence of dermatan sulfate was prevented by both the high-Mr rec-TM and the rabbit TM.	Dermatan Sulfate	63-79	heparin cofactor 2	Oryctolagus cuniculus	38-43
1646210-5	1991	The DS bound to the silica matrix was also tested as a chromatographic support for the purification of HCII from human plasma; the optimum conditions for HCII adsorption and desorption were determined.	Dermatan Sulfate	4-6	serpin family D member 1	Homo sapiens	103-107
1905276-5	1991	By contrast, media from ASB-deficient cultures initiated from the inferior region of the eye contained much higher levels of radiolabeled dermatan/chondroitin sulfate than ASB-deficient cultures from the superior region or normal cultures.	Dermatan Sulfate	138-147	arylsulfatase B	Felis catus	24-27
2019790-3	1991	We have also reported that dermatan sulfate, which catalyzes thrombin inhibition by heparin cofactor II, inhibits thrombus growth in rabbits more effectively than heparin.	Dermatan Sulfate	27-43	prothrombin	Oryctolagus cuniculus	61-69
2019790-3	1991	We have also reported that dermatan sulfate, which catalyzes thrombin inhibition by heparin cofactor II, inhibits thrombus growth in rabbits more effectively than heparin.	Dermatan Sulfate	27-43	heparin cofactor 2	Oryctolagus cuniculus	84-103
2019790-8	1991	In contrast, the catalytic action of dermatan sulfate on thrombin inhibition by plasma heparin cofactor II was unimpaired by fibrinogen-fibrin.	Dermatan Sulfate	37-53	coagulation factor II, thrombin	Homo sapiens	57-65
2019790-8	1991	In contrast, the catalytic action of dermatan sulfate on thrombin inhibition by plasma heparin cofactor II was unimpaired by fibrinogen-fibrin.	Dermatan Sulfate	37-53	heparin cofactor 2	Oryctolagus cuniculus	87-106
1823614-4	1991	Dermatan sulfate chains built onto xyloside at concentrations of 50 microM and below have a copolymeric structure similar to that of chains from the two PG-S variants.	Dermatan Sulfate	0-16	adaptor related protein complex 1 subunit sigma 2	Homo sapiens	153-157
1646210-0	1991	Immobilization of dermatan sulphate on a silica matrix and its possible use as an affinity chromatography support for heparin cofactor II purification.	Dermatan Sulfate	18-35	serpin family D member 1	Homo sapiens	118-137
1646210-1	1991	Dermatan sulphate (DS) is a glycosaminoglycan which catalyses specifically thrombin inhibition by a plasmatic inhibitor, Heparin cofactor II (HCII).	Dermatan Sulfate	0-17	coagulation factor II, thrombin	Homo sapiens	75-83
1646210-1	1991	Dermatan sulphate (DS) is a glycosaminoglycan which catalyses specifically thrombin inhibition by a plasmatic inhibitor, Heparin cofactor II (HCII).	Dermatan Sulfate	0-17	serpin family D member 1	Homo sapiens	121-140
1646210-1	1991	Dermatan sulphate (DS) is a glycosaminoglycan which catalyses specifically thrombin inhibition by a plasmatic inhibitor, Heparin cofactor II (HCII).	Dermatan Sulfate	0-17	serpin family D member 1	Homo sapiens	142-146
1646210-1	1991	Dermatan sulphate (DS) is a glycosaminoglycan which catalyses specifically thrombin inhibition by a plasmatic inhibitor, Heparin cofactor II (HCII).	Dermatan Sulfate	19-21	coagulation factor II, thrombin	Homo sapiens	75-83
1646210-5	1991	The DS bound to the silica matrix was also tested as a chromatographic support for the purification of HCII from human plasma; the optimum conditions for HCII adsorption and desorption were determined.	Dermatan Sulfate	4-6	serpin family D member 1	Homo sapiens	154-158
1646210-1	1991	Dermatan sulphate (DS) is a glycosaminoglycan which catalyses specifically thrombin inhibition by a plasmatic inhibitor, Heparin cofactor II (HCII).	Dermatan Sulfate	19-21	serpin family D member 1	Homo sapiens	121-140
1646210-1	1991	Dermatan sulphate (DS) is a glycosaminoglycan which catalyses specifically thrombin inhibition by a plasmatic inhibitor, Heparin cofactor II (HCII).	Dermatan Sulfate	19-21	serpin family D member 1	Homo sapiens	142-146
2028443-2	1991	Also when dermatan sulfate which does not enhance the action of AT III is used for the activation of HC II there is a considerable influence on the remaining thrombin activity which alters the test results.	Dermatan Sulfate	10-26	serpin family D member 1	Homo sapiens	101-106
1646210-2	1991	DS was insolubilized on a silica matrix to study its interaction with HCII.	Dermatan Sulfate	0-2	serpin family D member 1	Homo sapiens	70-74
1671335-1	1991	Heparin cofactor II (HCII) is a 66-kDa plasma glycoprotein that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Dermatan Sulfate	109-125	serpin family D member 1	Homo sapiens	0-19
1671335-1	1991	Heparin cofactor II (HCII) is a 66-kDa plasma glycoprotein that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Dermatan Sulfate	109-125	serpin family D member 1	Homo sapiens	21-25
1671335-1	1991	Heparin cofactor II (HCII) is a 66-kDa plasma glycoprotein that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Dermatan Sulfate	109-125	coagulation factor II, thrombin	Homo sapiens	73-81
2045458-1	1991	Heparin cofactor II (HCII) is an inhibitor of thrombin in human plasma whose activity is enhanced by heparin and dermatan sulphate.	Dermatan Sulfate	113-130	serpin family D member 1	Homo sapiens	0-19
2045458-1	1991	Heparin cofactor II (HCII) is an inhibitor of thrombin in human plasma whose activity is enhanced by heparin and dermatan sulphate.	Dermatan Sulfate	113-130	serpin family D member 1	Homo sapiens	21-25
2045458-1	1991	Heparin cofactor II (HCII) is an inhibitor of thrombin in human plasma whose activity is enhanced by heparin and dermatan sulphate.	Dermatan Sulfate	113-130	coagulation factor II, thrombin	Homo sapiens	46-54
2045458-7	1991	The HCII activity was evaluated as antithrombin dermatan sulphate cofactor activity.	Dermatan Sulfate	48-65	serpin family D member 1	Homo sapiens	4-8
2028443-2	1991	Also when dermatan sulfate which does not enhance the action of AT III is used for the activation of HC II there is a considerable influence on the remaining thrombin activity which alters the test results.	Dermatan Sulfate	10-26	coagulation factor II, thrombin	Homo sapiens	158-166
1832659-1	1991	Quantitative biosynthetic studies with cultures highly enriched for glial fibrillary acidic protein (GFAP+) cells of neonatal mammalian brain demonstrated production of four proteoglycans: hyaluronate (HA), heparan sulphate (HS), chondroitin sulphate (CS), and dermatan sulphate (DS).	Dermatan Sulfate	261-278	glial fibrillary acidic protein	Homo sapiens	68-99
1832659-1	1991	Quantitative biosynthetic studies with cultures highly enriched for glial fibrillary acidic protein (GFAP+) cells of neonatal mammalian brain demonstrated production of four proteoglycans: hyaluronate (HA), heparan sulphate (HS), chondroitin sulphate (CS), and dermatan sulphate (DS).	Dermatan Sulfate	280-282	glial fibrillary acidic protein	Homo sapiens	68-99
1794749-1	1991	The polyanions heparin and dermatan sulfate catalyze alpha-thrombin inhibition and can delay the onset of factor VIII and factor V necessary for intrinsic prothrombin activation to begin in plasma.	Dermatan Sulfate	27-43	coagulation factor II, thrombin	Homo sapiens	59-67
2220820-1	1990	The lysosomal hydrolase alpha-L-iduronidase (IDUA) is one of the enzymes in the metabolic pathway responsible for the degradation of the glycosaminoglycans heparan sulfate and dermatan sulfate.	Dermatan Sulfate	176-192	alpha-L-iduronidase	Homo sapiens	24-43
2266131-3	1990	Highly specific requirements with respect to the nature of the involved amino acids as well as to their spatial arrangements were found to be crucial for efficient activation of hLS2 by dermatan sulfate.	Dermatan Sulfate	186-202	serpin family D member 1	Homo sapiens	178-182
2287949-3	1990	Carbohydrate substituants (one or two chondroitin sulfate/dermatan sulfate chains for decorin and biglycan respectively, chains of keratan sulfate for fibromodulin and oligosaccharides) present variations from tissue to tissue and with age and other factors.	Dermatan Sulfate	58-74	biglycan	Homo sapiens	98-106
2220820-1	1990	The lysosomal hydrolase alpha-L-iduronidase (IDUA) is one of the enzymes in the metabolic pathway responsible for the degradation of the glycosaminoglycans heparan sulfate and dermatan sulfate.	Dermatan Sulfate	176-192	alpha-L-iduronidase	Homo sapiens	45-49
2122463-1	1990	Iduronate 2-sulfatase (IDS, EC 3.1.6.13) is required for the lysosomal degradation of heparan sulfate and dermatan sulfate.	Dermatan Sulfate	106-122	iduronate 2-sulfatase	Homo sapiens	0-21
2122463-1	1990	Iduronate 2-sulfatase (IDS, EC 3.1.6.13) is required for the lysosomal degradation of heparan sulfate and dermatan sulfate.	Dermatan Sulfate	106-122	iduronate 2-sulfatase	Homo sapiens	23-26
2211700-1	1990	Dermatan sulfate increases the rate of inhibition of thrombin by heparin cofactor II (HCII) approximately 1000-fold by providing a catalytic template to which both the inhibitor and the protease bind.	Dermatan Sulfate	0-16	coagulation factor II, thrombin	Homo sapiens	53-61
2211700-1	1990	Dermatan sulfate increases the rate of inhibition of thrombin by heparin cofactor II (HCII) approximately 1000-fold by providing a catalytic template to which both the inhibitor and the protease bind.	Dermatan Sulfate	0-16	serpin family D member 1	Homo sapiens	65-84
2226466-5	1990	Heparin catalyses both thrombin and factor Xa inhibition; dermatan sulfate catalyses only thrombin inhibition, while the pentasaccharide only catalyses factor Xa inhibition.	Dermatan Sulfate	58-74	coagulation factor II, thrombin	Homo sapiens	90-98
2211700-1	1990	Dermatan sulfate increases the rate of inhibition of thrombin by heparin cofactor II (HCII) approximately 1000-fold by providing a catalytic template to which both the inhibitor and the protease bind.	Dermatan Sulfate	0-16	serpin family D member 1	Homo sapiens	86-90
2211700-4	1990	To characterize the HCII-binding site in dermatan sulfate, we isolated the smallest fragment of dermatan sulfate that bound to HCII with high affinity.	Dermatan Sulfate	41-57	serpin family D member 1	Homo sapiens	20-24
2211700-4	1990	To characterize the HCII-binding site in dermatan sulfate, we isolated the smallest fragment of dermatan sulfate that bound to HCII with high affinity.	Dermatan Sulfate	41-57	serpin family D member 1	Homo sapiens	127-131
2211700-4	1990	To characterize the HCII-binding site in dermatan sulfate, we isolated the smallest fragment of dermatan sulfate that bound to HCII with high affinity.	Dermatan Sulfate	96-112	serpin family D member 1	Homo sapiens	20-24
2211700-4	1990	To characterize the HCII-binding site in dermatan sulfate, we isolated the smallest fragment of dermatan sulfate that bound to HCII with high affinity.	Dermatan Sulfate	96-112	serpin family D member 1	Homo sapiens	127-131
2282507-5	1990	Here we show that dermatan sulfate as well as de-sulfated heparin, are also able to extract collagen-tailed AChE.	Dermatan Sulfate	18-34	acetylcholinesterase	Rattus norvegicus	108-112
2282507-6	1990	Taking into account that the solubilization of the asymmetric AChE is concomitant with the liberation of a dermatan sulfate proteoglycan from the rat neuromuscular junction, the present results open the possibility that the collagen-tailed AChE is also anchored to dermatan sulfate proteoglycans at the synaptic basal lamina.	Dermatan Sulfate	107-123	acetylcholinesterase	Rattus norvegicus	62-66
2282507-6	1990	Taking into account that the solubilization of the asymmetric AChE is concomitant with the liberation of a dermatan sulfate proteoglycan from the rat neuromuscular junction, the present results open the possibility that the collagen-tailed AChE is also anchored to dermatan sulfate proteoglycans at the synaptic basal lamina.	Dermatan Sulfate	107-123	acetylcholinesterase	Rattus norvegicus	240-244
2282507-6	1990	Taking into account that the solubilization of the asymmetric AChE is concomitant with the liberation of a dermatan sulfate proteoglycan from the rat neuromuscular junction, the present results open the possibility that the collagen-tailed AChE is also anchored to dermatan sulfate proteoglycans at the synaptic basal lamina.	Dermatan Sulfate	265-281	acetylcholinesterase	Rattus norvegicus	62-66
2282507-6	1990	Taking into account that the solubilization of the asymmetric AChE is concomitant with the liberation of a dermatan sulfate proteoglycan from the rat neuromuscular junction, the present results open the possibility that the collagen-tailed AChE is also anchored to dermatan sulfate proteoglycans at the synaptic basal lamina.	Dermatan Sulfate	265-281	acetylcholinesterase	Rattus norvegicus	240-244
2156859-4	1990	Likewise, a heparin- and dermatan sulfate-binding peptide which represents a portion of the glycosaminoglycan-binding domain of vitronectin (VN) selectively inhibited activities b and c, indicating the presence of clustered acidic domain(s) in TM responsible for these activities.	Dermatan Sulfate	25-41	vitronectin	Oryctolagus cuniculus	128-139
2196322-2	1990	A role for HCII as an inhibitor of thrombin in the presence of dermatan sulfate and heparin has been proposed.	Dermatan Sulfate	63-79	serpin family D member 1	Homo sapiens	11-15
2196322-2	1990	A role for HCII as an inhibitor of thrombin in the presence of dermatan sulfate and heparin has been proposed.	Dermatan Sulfate	63-79	coagulation factor II, thrombin	Homo sapiens	35-43
2201287-0	1990	Non-uniform influence of transforming growth factor-beta on the biosynthesis of different forms of small chondroitin sulphate/dermatan sulphate proteoglycan.	Dermatan Sulfate	126-143	transforming growth factor beta 1	Homo sapiens	25-56
1966669-5	1990	Chondroitin sulphate and heparan sulphate had no effect on tPA and PAI-1 levels but dermatan sulphate reduced PAI-1 significantly.	Dermatan Sulfate	84-101	serpin family E member 1	Homo sapiens	110-115
2347433-3	1990	The heparin cofactor heparin and dermatan sulfate-dependent inhibition of thrombin was significantly reduced, showing a remarkable decrease of the maximum second order rate constant.	Dermatan Sulfate	33-49	coagulation factor II, thrombin	Homo sapiens	74-82
2226352-9	1990	In the cell-matrix fraction, TGF-beta increased the proportion of heparan sulfate that was membrane bound as well as the proportion of dermatan sulfate in the intracellular compartment.	Dermatan Sulfate	135-151	transforming growth factor beta 1	Homo sapiens	29-37
2226352-10	1990	In the medium fraction, TGF-beta increased the proportion of hyaluronic acid, chondroitin sulfate and dermatan sulfate released.	Dermatan Sulfate	102-118	transforming growth factor beta 1	Homo sapiens	24-32
2122537-0	1990	Heparin cofactor II inhibits thrombin-stimulated release of tissue plasminogen activator from cultured human endothelial cells in the presence of dermatan sulfate.	Dermatan Sulfate	146-162	serpin family D member 1	Homo sapiens	0-19
2122537-0	1990	Heparin cofactor II inhibits thrombin-stimulated release of tissue plasminogen activator from cultured human endothelial cells in the presence of dermatan sulfate.	Dermatan Sulfate	146-162	coagulation factor II, thrombin	Homo sapiens	29-37
2122537-0	1990	Heparin cofactor II inhibits thrombin-stimulated release of tissue plasminogen activator from cultured human endothelial cells in the presence of dermatan sulfate.	Dermatan Sulfate	146-162	chromosome 20 open reading frame 181	Homo sapiens	60-88
2122537-3	1990	In contrast, in the presence of dermatan sulfate, HC II inhibited thrombin stimulation of t-PA:Ag release more strongly than AT III did.	Dermatan Sulfate	32-48	serpin family D member 1	Homo sapiens	50-55
2122537-3	1990	In contrast, in the presence of dermatan sulfate, HC II inhibited thrombin stimulation of t-PA:Ag release more strongly than AT III did.	Dermatan Sulfate	32-48	coagulation factor II, thrombin	Homo sapiens	66-74
2122537-3	1990	In contrast, in the presence of dermatan sulfate, HC II inhibited thrombin stimulation of t-PA:Ag release more strongly than AT III did.	Dermatan Sulfate	32-48	plasminogen activator, tissue type	Homo sapiens	90-94
2122537-4	1990	The release of plasminogen activator inhibitor-1 antigen (PAI-1:Ag) was also stimulated by thrombin; this stimulation was inhibited only by the combination of HC II and dermatan sulfate.	Dermatan Sulfate	169-185	serpin family E member 1	Homo sapiens	15-48
2122537-4	1990	The release of plasminogen activator inhibitor-1 antigen (PAI-1:Ag) was also stimulated by thrombin; this stimulation was inhibited only by the combination of HC II and dermatan sulfate.	Dermatan Sulfate	169-185	serpin family E member 1	Homo sapiens	58-63
2122537-4	1990	The release of plasminogen activator inhibitor-1 antigen (PAI-1:Ag) was also stimulated by thrombin; this stimulation was inhibited only by the combination of HC II and dermatan sulfate.	Dermatan Sulfate	169-185	coagulation factor II, thrombin	Homo sapiens	91-99
2122537-6	1990	Based on these results, it was suggested that HC II may inhibit an increase in fibrinolytic activity mediated by thrombin-stimulated endothelial cells in the liquid phase through a suppression of thrombin stimulation of t-PA:Ag release, when plasma is exposed to vascular smooth muscle cells or fibroblasts which synthesize a significant amount of dermatan sulfate.	Dermatan Sulfate	348-364	serpin family D member 1	Homo sapiens	46-51
2122537-6	1990	Based on these results, it was suggested that HC II may inhibit an increase in fibrinolytic activity mediated by thrombin-stimulated endothelial cells in the liquid phase through a suppression of thrombin stimulation of t-PA:Ag release, when plasma is exposed to vascular smooth muscle cells or fibroblasts which synthesize a significant amount of dermatan sulfate.	Dermatan Sulfate	348-364	coagulation factor II, thrombin	Homo sapiens	113-121
2138609-8	1990	Dermatan sulfate accelerated thrombin inhibition by both forms of rHCII, but the maximum rate constant in the presence of dermatan sulfate was only 2-fold higher for rHCII(Leu444----Arg) (k2 = 5.3 x 10(8) M-1 min-1) than for native rHCII (k2 = 2.2 x 10(8) M-1 min-1).	Dermatan Sulfate	0-16	serpin family D member 1	Rattus norvegicus	66-71
2138609-8	1990	Dermatan sulfate accelerated thrombin inhibition by both forms of rHCII, but the maximum rate constant in the presence of dermatan sulfate was only 2-fold higher for rHCII(Leu444----Arg) (k2 = 5.3 x 10(8) M-1 min-1) than for native rHCII (k2 = 2.2 x 10(8) M-1 min-1).	Dermatan Sulfate	122-138	serpin family D member 1	Rattus norvegicus	66-71
2138609-9	1990	Heparin was less effective than dermatan sulfate in stimulating both forms of rHCII.	Dermatan Sulfate	32-48	serpin family D member 1	Rattus norvegicus	78-83
2156859-4	1990	Likewise, a heparin- and dermatan sulfate-binding peptide which represents a portion of the glycosaminoglycan-binding domain of vitronectin (VN) selectively inhibited activities b and c, indicating the presence of clustered acidic domain(s) in TM responsible for these activities.	Dermatan Sulfate	25-41	vitronectin	Oryctolagus cuniculus	141-143
2156859-7	1990	These results suggest that at least two acidic thrombin binding domains are present in rabbit TM, whereby a dermatan sulfate-like glycosaminoglycan moiety constitutes the secondary binding domain for thrombin, eliciting both the direct as well as the AT III-dependent anticoagulant function of rabbit TM (activities b and c) but not protein C activation (activity a).	Dermatan Sulfate	108-124	prothrombin	Oryctolagus cuniculus	200-208
2407884-3	1990	In control experiments we found that mesangial cells produced two distinct proteoglycans identified as the small chondroitin/dermatan sulfate proteoglycans biglycan (PG I) and decorin (PG II) by showing that their mobility on SDS-PAGE changed upon digestion by chondroitinase ABC, and that they reacted with antibodies raised against synthetic peptides from the core protein sequence of human biglycan and decorin.	Dermatan Sulfate	125-141	biglycan	Homo sapiens	156-164
2407884-3	1990	In control experiments we found that mesangial cells produced two distinct proteoglycans identified as the small chondroitin/dermatan sulfate proteoglycans biglycan (PG I) and decorin (PG II) by showing that their mobility on SDS-PAGE changed upon digestion by chondroitinase ABC, and that they reacted with antibodies raised against synthetic peptides from the core protein sequence of human biglycan and decorin.	Dermatan Sulfate	125-141	biglycan	Homo sapiens	166-170
33815739-1	2021	Dermatan sulfate epimerase 1 (DS-epi1, EC 5.1.3.19) catalyzes the conversion of d-glucuronic acid to l-iduronic acid on the polymer level, a key step in the biosynthesis of the glycosaminoglycan dermatan sulfate.	Dermatan Sulfate	195-211	dermatan sulfate epimerase	Homo sapiens	0-28
2106134-3	1990	This abnormality is the consequence of a deficiency in galactosyltransferase I (xylosylprotein 4-beta-galactosyltransferase; EC 2.4.1.133), which catalyzes the second glycosyl transfer reaction in the assembly of the dermatan sulfate chain.	Dermatan Sulfate	217-233	beta-1,4-galactosyltransferase 7	Homo sapiens	55-123
2123768-7	1990	Observations made on chondroitinase ABC and chondroitinase AC digests of proteoglycans indicate that dermatan sulfate is linked to the core proteins through chondroitin sulfates.	Dermatan Sulfate	101-117	galactosamine (N-acetyl)-6-sulfatase	Homo sapiens	21-35
2123768-7	1990	Observations made on chondroitinase ABC and chondroitinase AC digests of proteoglycans indicate that dermatan sulfate is linked to the core proteins through chondroitin sulfates.	Dermatan Sulfate	101-117	galactosamine (N-acetyl)-6-sulfatase	Homo sapiens	44-58
2138364-1	1990	We evaluated the in vitro anticoagulant action of dermatan sulfate (DS) (aPTT, antiXa, anti-thrombin) and its effect on human platelet aggregation and beta TG/PF4 release induced by threshold doses of aggregating agents, compared with standard heparin (SH).	Dermatan Sulfate	50-66	pro-platelet basic protein	Homo sapiens	151-158
2138364-1	1990	We evaluated the in vitro anticoagulant action of dermatan sulfate (DS) (aPTT, antiXa, anti-thrombin) and its effect on human platelet aggregation and beta TG/PF4 release induced by threshold doses of aggregating agents, compared with standard heparin (SH).	Dermatan Sulfate	50-66	platelet factor 4	Homo sapiens	159-162
2138364-5	1990	These data in vitro confirm that thrombin inhibition induced by DS is accompanied by a far lesser aPTT prolongation compared to heparin, without any appreciable interference with platelet function.	Dermatan Sulfate	64-66	coagulation factor II, thrombin	Homo sapiens	33-41
33815739-1	2021	Dermatan sulfate epimerase 1 (DS-epi1, EC 5.1.3.19) catalyzes the conversion of d-glucuronic acid to l-iduronic acid on the polymer level, a key step in the biosynthesis of the glycosaminoglycan dermatan sulfate.	Dermatan Sulfate	195-211	dermatan sulfate epimerase	Homo sapiens	30-37
34360653-2	2021	In MPS II, the first step of degradation of heparan sulfate (HS) and dermatan sulfate (DS) is blocked by a deficiency in the lysosomal enzyme iduronate 2-sulfatase (IDS), while, in MPS I, blockage of the second step is caused by a deficiency in iduronidase (IDUA).	Dermatan Sulfate	69-85	iduronate 2-sulfatase	Homo sapiens	142-163
18418554-1	2009	MPS VI (mucopolysaccharidosis VI, known as Maroteaux-Lamy syndrome) is a multi-systemic inherited disease, resulting from a deficiency of N-acetylgalactosamine-4-sulfatase, causing accumulation of the glycosaminoglycan (GAG) dermatan sulfate in all tissues.	Dermatan Sulfate	225-241	arylsulfatase B	Homo sapiens	138-171
34270745-0	2021	Dermatan sulfate is an activating ligand of anaplastic lymphoma kinase.	Dermatan Sulfate	0-16	ALK receptor tyrosine kinase	Homo sapiens	44-70
34270745-4	2021	Here we show that dermatan sulfate (DS, chondroitin sulfate B) directly interacts with the extracellular N-terminal region of ALK as well as HS.	Dermatan Sulfate	18-34	ALK receptor tyrosine kinase	Homo sapiens	126-129
34953930-1	2022	Endocan is known to be a circulating dermatan sulfate proteoglycan that regulates endothelial cell function.	Dermatan Sulfate	37-53	endothelial cell specific molecule 1	Homo sapiens	0-7
34850861-1	2021	Musculocontractural Ehlers-Danlos syndrome (mcEDS) is caused by generalized depletion of dermatan sulfate (DS) due to biallelic pathogenic variants in CHST14 encoding dermatan 4-O-sulfotransferase 1 (D4ST1) (mcEDS-CHST14).	Dermatan Sulfate	89-105	carbohydrate sulfotransferase 14	Mus musculus	151-157
34850861-1	2021	Musculocontractural Ehlers-Danlos syndrome (mcEDS) is caused by generalized depletion of dermatan sulfate (DS) due to biallelic pathogenic variants in CHST14 encoding dermatan 4-O-sulfotransferase 1 (D4ST1) (mcEDS-CHST14).	Dermatan Sulfate	89-105	carbohydrate sulfotransferase 14	Mus musculus	167-198
34850861-1	2021	Musculocontractural Ehlers-Danlos syndrome (mcEDS) is caused by generalized depletion of dermatan sulfate (DS) due to biallelic pathogenic variants in CHST14 encoding dermatan 4-O-sulfotransferase 1 (D4ST1) (mcEDS-CHST14).	Dermatan Sulfate	89-105	carbohydrate sulfotransferase 14	Mus musculus	200-205
34850861-1	2021	Musculocontractural Ehlers-Danlos syndrome (mcEDS) is caused by generalized depletion of dermatan sulfate (DS) due to biallelic pathogenic variants in CHST14 encoding dermatan 4-O-sulfotransferase 1 (D4ST1) (mcEDS-CHST14).	Dermatan Sulfate	89-105	carbohydrate sulfotransferase 14	Mus musculus	214-220
34409033-12	2021	CS/DS thus has varied cell regulatory properties and structural ECM supportive roles in the CNS/PNS depending on the glycoform present and its location in tissue niches and specific cellular contexts.	Dermatan Sulfate	3-5	citrate synthase	Homo sapiens	0-2
34270745-4	2021	Here we show that dermatan sulfate (DS, chondroitin sulfate B) directly interacts with the extracellular N-terminal region of ALK as well as HS.	Dermatan Sulfate	36-38	ALK receptor tyrosine kinase	Homo sapiens	126-129
34270745-4	2021	Here we show that dermatan sulfate (DS, chondroitin sulfate B) directly interacts with the extracellular N-terminal region of ALK as well as HS.	Dermatan Sulfate	40-61	ALK receptor tyrosine kinase	Homo sapiens	126-129
34948256-3	2021	The enzyme deficit causes a pathological accumulation of the undegraded glycosaminoglycans dermatan-sulphate and chondroitin-sulphate, natural substrates of ASB activity.	Dermatan Sulfate	91-108	arylsulfatase B	Homo sapiens	157-160
34901009-7	2021	These observations suggest that CS/DS are essential for skeletal development as well as the assembly of collagen fibrils in the skin, and that their respective knockout mice can be utilized as models for human genetic disorders with mutations in chondroitin synthase 1 and DS-epimerase 1.	Dermatan Sulfate	35-37	chondroitin sulfate synthase 1	Homo sapiens	246-268
34441282-11	2021	Patients with MPS I, MPS II, and MPS IIIB had significantly elevated HS and DS levels in DBS.	Dermatan Sulfate	76-78	N-acetyl-alpha-glucosaminidase	Homo sapiens	33-41
34360653-2	2021	In MPS II, the first step of degradation of heparan sulfate (HS) and dermatan sulfate (DS) is blocked by a deficiency in the lysosomal enzyme iduronate 2-sulfatase (IDS), while, in MPS I, blockage of the second step is caused by a deficiency in iduronidase (IDUA).	Dermatan Sulfate	69-85	iduronate 2-sulfatase	Homo sapiens	165-168
34360653-2	2021	In MPS II, the first step of degradation of heparan sulfate (HS) and dermatan sulfate (DS) is blocked by a deficiency in the lysosomal enzyme iduronate 2-sulfatase (IDS), while, in MPS I, blockage of the second step is caused by a deficiency in iduronidase (IDUA).	Dermatan Sulfate	69-85	alpha-L-iduronidase	Homo sapiens	245-256
34360653-2	2021	In MPS II, the first step of degradation of heparan sulfate (HS) and dermatan sulfate (DS) is blocked by a deficiency in the lysosomal enzyme iduronate 2-sulfatase (IDS), while, in MPS I, blockage of the second step is caused by a deficiency in iduronidase (IDUA).	Dermatan Sulfate	69-85	alpha-L-iduronidase	Homo sapiens	258-262
34360653-2	2021	In MPS II, the first step of degradation of heparan sulfate (HS) and dermatan sulfate (DS) is blocked by a deficiency in the lysosomal enzyme iduronate 2-sulfatase (IDS), while, in MPS I, blockage of the second step is caused by a deficiency in iduronidase (IDUA).	Dermatan Sulfate	87-89	iduronate 2-sulfatase	Homo sapiens	142-163
34360653-2	2021	In MPS II, the first step of degradation of heparan sulfate (HS) and dermatan sulfate (DS) is blocked by a deficiency in the lysosomal enzyme iduronate 2-sulfatase (IDS), while, in MPS I, blockage of the second step is caused by a deficiency in iduronidase (IDUA).	Dermatan Sulfate	87-89	iduronate 2-sulfatase	Homo sapiens	165-168
34113352-0	2021	Dermatan Sulfate Is a Potential Regulator of IgH via Interactions With Pre-BCR, GTF2I, and BiP ER Complex in Pre-B Lymphoblasts.	Dermatan Sulfate	0-16	immunoglobulin heavy chain complex	Mus musculus	45-48
34200372-11	2021	The glycosaminoglycans heparan sulphate and dermatan sulphate, but not chondroitin sulphate, also inhibited the binding of spike protein, indicating that it might bind to one or both of these glycosaminoglycans on the surface of target cells.	Dermatan Sulfate	44-61	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	123-128
34113352-0	2021	Dermatan Sulfate Is a Potential Regulator of IgH via Interactions With Pre-BCR, GTF2I, and BiP ER Complex in Pre-B Lymphoblasts.	Dermatan Sulfate	0-16	general transcription factor II I	Mus musculus	80-85
34113352-0	2021	Dermatan Sulfate Is a Potential Regulator of IgH via Interactions With Pre-BCR, GTF2I, and BiP ER Complex in Pre-B Lymphoblasts.	Dermatan Sulfate	0-16	heat shock protein 5	Mus musculus	91-94
34113352-1	2021	Dermatan sulfate (DS) and autoantigen (autoAg) complexes are capable of stimulating autoreactive CD5+ B1 cells.	Dermatan Sulfate	0-16	CD5 antigen	Mus musculus	97-100
34113352-1	2021	Dermatan sulfate (DS) and autoantigen (autoAg) complexes are capable of stimulating autoreactive CD5+ B1 cells.	Dermatan Sulfate	18-20	CD5 antigen	Mus musculus	97-100
34113352-3	2021	CD19, CD5, CD72, PI3K, and Fas possess varying degrees of DS affinity.	Dermatan Sulfate	58-60	CD19 antigen	Mus musculus	0-4
34109132-2	2021	Endothelial cell-specific molecule 1 (ESM-1), a soluble dermatan sulfate proteoglycan, also known as endocan, serves as a diagnostic and prognostic indicator due to its aberrant expression under pathological conditions, including cancer, sepsis, kidney diseases, and cardiovascular disease.	Dermatan Sulfate	56-72	endothelial cell specific molecule 1	Homo sapiens	0-36
34109132-2	2021	Endothelial cell-specific molecule 1 (ESM-1), a soluble dermatan sulfate proteoglycan, also known as endocan, serves as a diagnostic and prognostic indicator due to its aberrant expression under pathological conditions, including cancer, sepsis, kidney diseases, and cardiovascular disease.	Dermatan Sulfate	56-72	endothelial cell specific molecule 1	Homo sapiens	38-43
34113352-3	2021	CD19, CD5, CD72, PI3K, and Fas possess varying degrees of DS affinity.	Dermatan Sulfate	58-60	CD5 antigen	Mus musculus	6-9
34113352-3	2021	CD19, CD5, CD72, PI3K, and Fas possess varying degrees of DS affinity.	Dermatan Sulfate	58-60	CD72 antigen	Mus musculus	11-15
35454082-1	2022	Endocan is a soluble dermatan sulfate proteoglycan expressed by endothelial cells and detected in serum/plasma.	Dermatan Sulfate	21-37	endothelial cell specific molecule 1	Homo sapiens	0-7
34807422-5	2021	Musculocontractural EDS is caused by mutations in CHST14 or DSE, both of which encode enzymes responsible for the post-translational biosynthesis of dermatan sulfate.	Dermatan Sulfate	149-165	carbohydrate sulfotransferase 14	Homo sapiens	50-56
34807422-5	2021	Musculocontractural EDS is caused by mutations in CHST14 or DSE, both of which encode enzymes responsible for the post-translational biosynthesis of dermatan sulfate.	Dermatan Sulfate	149-165	dermatan sulfate epimerase	Homo sapiens	60-63
35552694-3	2022	In the biosynthesis of CS/DS containing GalNAc4S6S, three groups of sulfotransferases are involved; chondroitin 4-sulfotransferases (C4STs), dermatan 4-sulfotransferase-1 (D4ST-1) and GalNAc 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST).	Dermatan Sulfate	26-28	carbohydrate sulfotransferase 14	Homo sapiens	141-170
35552694-3	2022	In the biosynthesis of CS/DS containing GalNAc4S6S, three groups of sulfotransferases are involved; chondroitin 4-sulfotransferases (C4STs), dermatan 4-sulfotransferase-1 (D4ST-1) and GalNAc 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST).	Dermatan Sulfate	26-28	carbohydrate sulfotransferase 14	Homo sapiens	172-178
35552694-3	2022	In the biosynthesis of CS/DS containing GalNAc4S6S, three groups of sulfotransferases are involved; chondroitin 4-sulfotransferases (C4STs), dermatan 4-sulfotransferase-1 (D4ST-1) and GalNAc 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST).	Dermatan Sulfate	26-28	carbohydrate sulfotransferase 15	Homo sapiens	184-221
35552694-3	2022	In the biosynthesis of CS/DS containing GalNAc4S6S, three groups of sulfotransferases are involved; chondroitin 4-sulfotransferases (C4STs), dermatan 4-sulfotransferase-1 (D4ST-1) and GalNAc 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST).	Dermatan Sulfate	26-28	carbohydrate sulfotransferase 15	Homo sapiens	223-235
35401574-15	2022	Summary Sentence: An autoantigen-ome by dermatan sulfate affinity from human lung HFL1 cells may explain neurological and autoimmune manifestations of COVID-19.	Dermatan Sulfate	40-56	complement factor H related 1	Homo sapiens	82-86
35284671-1	2022	Mucopolysaccharidosis type II (MPS II), also known as Hunter syndrome, is a rare X-linked recessive disease caused by a deficiency of the lysosomal enzyme iduronate-2-sulfatase (IDS), which activates intracellular accumulation of nonmetabolized glycosaminoglycans such as heparan sulfate and dermatan sulfate.	Dermatan Sulfate	292-308	iduronate 2-sulfatase	Mus musculus	155-176
35284671-1	2022	Mucopolysaccharidosis type II (MPS II), also known as Hunter syndrome, is a rare X-linked recessive disease caused by a deficiency of the lysosomal enzyme iduronate-2-sulfatase (IDS), which activates intracellular accumulation of nonmetabolized glycosaminoglycans such as heparan sulfate and dermatan sulfate.	Dermatan Sulfate	292-308	iduronate 2-sulfatase	Mus musculus	178-181
2512688-4	1989	However, HCII caused a marked decrease in the thrombin-stimulated prostacyclin prostacyclin production in the presence of 2 mg/ml dermatan sulfate (DS).	Dermatan Sulfate	130-146	serpin family D member 1	Homo sapiens	9-13
2512987-3	1989	In this study we assayed in rats the DAO-releasing capability of heparan sulphate, dermatan sulphate, chondroitin sulphate A and hyaluronic acid, all heparin related compounds.	Dermatan Sulfate	83-100	amine oxidase, copper containing 1	Rattus norvegicus	37-40
2794047-8	1989	Thrombin binds to dermatan sulfate in the ECM, as demonstrated by the inhibition of 125I-alpha-thrombin binding to ECM pretreated with chondroitinase ABC, but not with heparitinase or chondroitinase AC.	Dermatan Sulfate	18-34	coagulation factor II, thrombin	Homo sapiens	0-8
2794047-8	1989	Thrombin binds to dermatan sulfate in the ECM, as demonstrated by the inhibition of 125I-alpha-thrombin binding to ECM pretreated with chondroitinase ABC, but not with heparitinase or chondroitinase AC.	Dermatan Sulfate	18-34	coagulation factor II, thrombin	Homo sapiens	95-103
35176450-1	2022	Versican is a large chondroitin sulfate/dermatan sulfate proteoglycan that plays a key role in the formation of the provisional matrix.	Dermatan Sulfate	40-56	versican	Mus musculus	0-8
2790187-1	1989	Dermatan sulfate (DS), a catalyst of the thrombin-heparin cofactor II interaction, has antithrombotic activity and is devoid of significant hemorrhagic risk in several animal models.	Dermatan Sulfate	0-16	coagulation factor II, thrombin	Homo sapiens	41-49
2790187-1	1989	Dermatan sulfate (DS), a catalyst of the thrombin-heparin cofactor II interaction, has antithrombotic activity and is devoid of significant hemorrhagic risk in several animal models.	Dermatan Sulfate	18-20	coagulation factor II, thrombin	Homo sapiens	41-49
2512688-4	1989	However, HCII caused a marked decrease in the thrombin-stimulated prostacyclin prostacyclin production in the presence of 2 mg/ml dermatan sulfate (DS).	Dermatan Sulfate	130-146	coagulation factor II, thrombin	Homo sapiens	46-54
2512688-4	1989	However, HCII caused a marked decrease in the thrombin-stimulated prostacyclin prostacyclin production in the presence of 2 mg/ml dermatan sulfate (DS).	Dermatan Sulfate	148-150	serpin family D member 1	Homo sapiens	9-13
2512688-4	1989	However, HCII caused a marked decrease in the thrombin-stimulated prostacyclin prostacyclin production in the presence of 2 mg/ml dermatan sulfate (DS).	Dermatan Sulfate	148-150	coagulation factor II, thrombin	Homo sapiens	46-54
2512688-5	1989	The significant inhibition by HCII occurred when the DS concentrations were 0.2 microgram/ml and higher.	Dermatan Sulfate	53-55	serpin family D member 1	Homo sapiens	30-34
2512688-6	1989	From these results we suggest that HCII may prevent a prostacyclin-induced inhibition of platelet aggregation for hemostasis when plasma is exposed to vascular smooth muscle cells or fibroblasts which synthesize a significant amount of DS.	Dermatan Sulfate	236-238	serpin family D member 1	Homo sapiens	35-39
2590169-4	1989	Both dermatan sulphate proteoglycan I (DS-PGI) and dermatan sulphate proteoglycan II (DS-PGII) were identified and the former was present in greater abundance.	Dermatan Sulfate	5-22	biglycan	Homo sapiens	42-45
2590169-7	1989	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.	Dermatan Sulfate	131-148	biglycan	Homo sapiens	165-171
2621717-6	1989	The binding interaction between dermatan sulphate and fibronectin was significantly greater than between heparan sulphate and fibronectin (P less than 0.05); the binding interaction between GAGs from small follicles and fibronectin was significantly greater than between GAGs from large follicles (P less than 0.05).	Dermatan Sulfate	32-49	fibronectin 1	Bos taurus	54-65
2621717-8	1989	Dermatan sulphate from small follicles bound to fibronectin (42%), laminin (36%) and LDL (14%) and that from large follicles bound to fibronectin (14%), laminin (23%) and LDL (14%).	Dermatan Sulfate	0-17	fibronectin 1	Bos taurus	48-59
2735661-2	1989	Our results indicate that for equivalent anti-thrombin activities, dermatan sulfate is a more effective inhibitor of fibrin accretion onto existing thrombi than is heparin.	Dermatan Sulfate	67-83	coagulation factor II, thrombin	Homo sapiens	46-54
2763268-6	1989	PF4 affinity for GAGs is as follows: heparin greater than heparan sulphate much greater than dermatan sulphate.	Dermatan Sulfate	93-110	platelet factor 4	Homo sapiens	0-3
2470345-10	1989	(3) Forms I and II of liver alpha-L-iduronidase showed no difference in their activities towards disaccharide substrates derived from two glycosaminoglycan sources, heparan sulphate and dermatan sulphate.	Dermatan Sulfate	186-203	alpha-L-iduronidase	Homo sapiens	28-47
2914965-13	1989	The enhancement of thrombin inhibition by fucoidan, like heparin and dermatan sulfate, is eliminated by selective chemical modification of lysyl residues either of heparin cofactor II or of thrombin.	Dermatan Sulfate	69-85	coagulation factor II, thrombin	Homo sapiens	19-27
2914965-13	1989	The enhancement of thrombin inhibition by fucoidan, like heparin and dermatan sulfate, is eliminated by selective chemical modification of lysyl residues either of heparin cofactor II or of thrombin.	Dermatan Sulfate	69-85	coagulation factor II, thrombin	Homo sapiens	190-198
2786880-10	1989	Immunocytochemistry of extracellular matrix components revealed a decrease in staining intensity of chondroitin and dermatan sulfate in the 3-week matrix following IL-1 beta incubation.	Dermatan Sulfate	116-132	interleukin 1 beta	Homo sapiens	164-173
2713501-2	1989	An in vivo role for thrombin (IIa) inhibition by HCII in the presence of certain glycosaminoglycans (dermatan sulfate and heparin) can be proposed.	Dermatan Sulfate	101-117	coagulation factor II, thrombin	Homo sapiens	20-28
2713501-2	1989	An in vivo role for thrombin (IIa) inhibition by HCII in the presence of certain glycosaminoglycans (dermatan sulfate and heparin) can be proposed.	Dermatan Sulfate	101-117	serpin family D member 1	Homo sapiens	49-53
2735661-5	1989	It is more likely that dermatan sulfate mediates this beneficial effect by more effectively inhibiting thrombin within a thrombus than can heparin.	Dermatan Sulfate	23-39	coagulation factor II, thrombin	Homo sapiens	103-111
2735662-4	1989	Dermatan sulfate, which has no anti-factor Xa activity, partially impairs both thrombin generation and stasis thrombosis.	Dermatan Sulfate	0-16	coagulation factor II, thrombin	Homo sapiens	79-87
2735662-8	1989	Drugs which act primarily on factor Xa (oligosaccharides) or thrombin by non-ATIII pathways (dermatan sulfate) are less efficient than UFH as antithrombotic drugs.	Dermatan Sulfate	93-109	coagulation factor II, thrombin	Homo sapiens	61-69
2735662-8	1989	Drugs which act primarily on factor Xa (oligosaccharides) or thrombin by non-ATIII pathways (dermatan sulfate) are less efficient than UFH as antithrombotic drugs.	Dermatan Sulfate	93-109	serpin family C member 1	Homo sapiens	77-82
2708007-4	1989	3H-heparin binding to peptide F-9 was specific as determined by competition with excess unlabeled heparin, dextran sulfate, and dermatan sulfate.	Dermatan Sulfate	128-144	coagulation factor IX	Mus musculus	30-33
3217919-2	1988	DS accelerates thrombin inhibition by heparin cofactor II (HC II).	Dermatan Sulfate	0-2	coagulation factor II, thrombin	Homo sapiens	15-23
2976993-4	1988	In the presence of 0.3 micrograms/ml heparin, 0.5 micrograms/ml pentosan polysulfate, or 2 micrograms/ml dermatan sulfate, S protein induced a concentration-dependent reduction of the inhibition rate of thrombin by heparin cofactor II.	Dermatan Sulfate	105-121	vitronectin	Homo sapiens	123-132
2976993-4	1988	In the presence of 0.3 micrograms/ml heparin, 0.5 micrograms/ml pentosan polysulfate, or 2 micrograms/ml dermatan sulfate, S protein induced a concentration-dependent reduction of the inhibition rate of thrombin by heparin cofactor II.	Dermatan Sulfate	105-121	coagulation factor II, thrombin	Homo sapiens	203-211
2905842-10	1988	The fourth agent, dermatan sulfate, potentiates the activity of heparin cofactor II but fails to inhibit intrinsic prothrombin activation even at concentrations which exceed 60 micrograms/ml of plasma.	Dermatan Sulfate	18-34	heparin cofactor 2	Oryctolagus cuniculus	64-83
3217919-2	1988	DS accelerates thrombin inhibition by heparin cofactor II (HC II).	Dermatan Sulfate	0-2	serpin family D member 1	Homo sapiens	38-57
3217919-2	1988	DS accelerates thrombin inhibition by heparin cofactor II (HC II).	Dermatan Sulfate	0-2	serpin family D member 1	Homo sapiens	59-64
3217919-5	1988	Firstly, at fixed concentrations of DS and of HC II, the rate of thrombin inhibition increases when the ionic strength of the medium decreases.	Dermatan Sulfate	36-38	coagulation factor II, thrombin	Homo sapiens	65-73
3217919-7	1988	In the conditions described, there is a linear relationship between DS concentrations in plasma from 0 to 2 micrograms/ml and the log of residual thrombin activity.	Dermatan Sulfate	68-70	coagulation factor II, thrombin	Homo sapiens	146-154
2967302-8	1988	Increasing concentrations of heparan sulfate, dermatan sulfate, and chondroitin sulfate correlated with increasing aFGF potentiation.	Dermatan Sulfate	46-62	fibroblast growth factor 1	Rattus norvegicus	115-119
3417782-5	1988	The binding of [3H]heparin to peptide F-9 was dramatically reduced when heparin but not other glycosaminoglycans other than heparin (dextran sulfate, dermatan sulfate) were used in competition assays.	Dermatan Sulfate	150-166	coagulation factor IX	Homo sapiens	38-41
2902851-0	1988	Effect of oversulphated chondroitin and dermatan sulphate upon thrombin and factor Xa inactivation by antithrombin III or heparin cofactor II.	Dermatan Sulfate	40-57	coagulation factor II, thrombin	Homo sapiens	63-71
2902851-0	1988	Effect of oversulphated chondroitin and dermatan sulphate upon thrombin and factor Xa inactivation by antithrombin III or heparin cofactor II.	Dermatan Sulfate	40-57	coagulation factor X	Homo sapiens	76-85
2902851-0	1988	Effect of oversulphated chondroitin and dermatan sulphate upon thrombin and factor Xa inactivation by antithrombin III or heparin cofactor II.	Dermatan Sulfate	40-57	serpin family C member 1	Homo sapiens	102-118
2967302-17	1988	Heparan sulfate and chondroitin sulfate showed concentration-dependent potentiation of NGF; maximally active concentrations of heparan sulfate (100 micrograms/ml) and chondroitin sulfate (1 mg/ml) increased the potency of NGF 3-fold, whereas heparin, dermatan sulfate and hyaluronic acid had no effect.	Dermatan Sulfate	251-267	nerve growth factor	Rattus norvegicus	87-90
2967302-9	1988	The maximally active concentrations of heparan sulfate (100 micrograms/ml), dermatan sulfate (10 mg/ml), and chondroitin sulfate (1 mg/ml) increased the activity of aFGF 11-, 110-, and 11-fold, respectively.	Dermatan Sulfate	76-92	fibroblast growth factor 1	Rattus norvegicus	165-169
3388296-4	1988	The disappearance of DS from plasma was characterized by measuring both the circulating radioactivity and the biological activity using an original assay based upon the catalysis of heparin cofactor II - thrombin formation.	Dermatan Sulfate	21-23	heparin cofactor 2	Oryctolagus cuniculus	182-201
3388296-4	1988	The disappearance of DS from plasma was characterized by measuring both the circulating radioactivity and the biological activity using an original assay based upon the catalysis of heparin cofactor II - thrombin formation.	Dermatan Sulfate	21-23	prothrombin	Oryctolagus cuniculus	204-212
2894851-1	1988	Heparin cofactor II (HCII) is an inhibitor of thrombin in plasma that is activated by dermatan sulfate or heparin.	Dermatan Sulfate	86-102	serpin family D member 1	Homo sapiens	0-19
3348170-2	1988	Functional assays for heparin cofactor II (HC-II) are based on the inactivation of thrombin by HC-II in the presence of dermatan sulfate (DS).	Dermatan Sulfate	120-136	serpin family D member 1	Homo sapiens	22-41
3348170-2	1988	Functional assays for heparin cofactor II (HC-II) are based on the inactivation of thrombin by HC-II in the presence of dermatan sulfate (DS).	Dermatan Sulfate	120-136	serpin family D member 1	Homo sapiens	43-48
3348170-2	1988	Functional assays for heparin cofactor II (HC-II) are based on the inactivation of thrombin by HC-II in the presence of dermatan sulfate (DS).	Dermatan Sulfate	120-136	coagulation factor II, thrombin	Homo sapiens	83-91
3348170-2	1988	Functional assays for heparin cofactor II (HC-II) are based on the inactivation of thrombin by HC-II in the presence of dermatan sulfate (DS).	Dermatan Sulfate	138-140	serpin family D member 1	Homo sapiens	22-41
3348170-2	1988	Functional assays for heparin cofactor II (HC-II) are based on the inactivation of thrombin by HC-II in the presence of dermatan sulfate (DS).	Dermatan Sulfate	138-140	serpin family D member 1	Homo sapiens	43-48
3348170-2	1988	Functional assays for heparin cofactor II (HC-II) are based on the inactivation of thrombin by HC-II in the presence of dermatan sulfate (DS).	Dermatan Sulfate	138-140	coagulation factor II, thrombin	Homo sapiens	83-91
3348170-6	1988	After NaNO2/acetic acid treatment of DS (to inactivate heparin), there was enough residual heparin to cause AT-III interference.	Dermatan Sulfate	37-39	serpin family C member 1	Homo sapiens	108-114
3258496-2	1988	Initial studies demonstrated that murine plasma contains a heparin cofactor II-like inhibitor as shown by the presence of a dermatan sulfate-sensitive thrombin inhibitor.	Dermatan Sulfate	124-140	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	59-78
3258496-2	1988	Initial studies demonstrated that murine plasma contains a heparin cofactor II-like inhibitor as shown by the presence of a dermatan sulfate-sensitive thrombin inhibitor.	Dermatan Sulfate	124-140	coagulation factor II	Mus musculus	151-159
3422640-1	1988	Transforming growth factor beta (TGF-beta) increases up to 20-fold the expression of various forms of chondroitin/dermatan sulfate proteoglycan, the major type of sulfated proteoglycan present in the extracellular matrix and culture medium of various human, rodent, and mink cell types including kidney and lung fibroblasts, lung epithelial cells, preadipocytes, and skeletal muscle myoblasts.	Dermatan Sulfate	114-130	transforming growth factor beta 1	Homo sapiens	0-31
3422640-1	1988	Transforming growth factor beta (TGF-beta) increases up to 20-fold the expression of various forms of chondroitin/dermatan sulfate proteoglycan, the major type of sulfated proteoglycan present in the extracellular matrix and culture medium of various human, rodent, and mink cell types including kidney and lung fibroblasts, lung epithelial cells, preadipocytes, and skeletal muscle myoblasts.	Dermatan Sulfate	114-130	transforming growth factor beta 1	Homo sapiens	33-41
3276308-3	1988	A specific binding of SAP to hyaluronic acid, heparan sulfate, and dermatan sulfate was also confirmed by the fact that these glycosaminoglycans blocked the binding of SAP to agarose, a specific ligand of SAP.	Dermatan Sulfate	67-83	amyloid P component, serum	Homo sapiens	22-25
3276308-3	1988	A specific binding of SAP to hyaluronic acid, heparan sulfate, and dermatan sulfate was also confirmed by the fact that these glycosaminoglycans blocked the binding of SAP to agarose, a specific ligand of SAP.	Dermatan Sulfate	67-83	amyloid P component, serum	Homo sapiens	168-171
3276308-3	1988	A specific binding of SAP to hyaluronic acid, heparan sulfate, and dermatan sulfate was also confirmed by the fact that these glycosaminoglycans blocked the binding of SAP to agarose, a specific ligand of SAP.	Dermatan Sulfate	67-83	amyloid P component, serum	Homo sapiens	168-171
2894851-1	1988	Heparin cofactor II (HCII) is an inhibitor of thrombin in plasma that is activated by dermatan sulfate or heparin.	Dermatan Sulfate	86-102	serpin family D member 1	Homo sapiens	21-25
2894851-1	1988	Heparin cofactor II (HCII) is an inhibitor of thrombin in plasma that is activated by dermatan sulfate or heparin.	Dermatan Sulfate	86-102	coagulation factor II, thrombin	Homo sapiens	46-54
2894851-11	1988	The recombinant HCII formed a complex with 125I-thrombin in a reaction that required the presence of heparin or dermatan sulfate.	Dermatan Sulfate	112-128	serpin family D member 1	Homo sapiens	16-20
2894851-11	1988	The recombinant HCII formed a complex with 125I-thrombin in a reaction that required the presence of heparin or dermatan sulfate.	Dermatan Sulfate	112-128	coagulation factor II, thrombin	Homo sapiens	48-56
3691797-0	1987	Binding of heparin or dermatan sulfate to thrombin is essential for the sulfated polysaccharide-accelerated inhibition of thrombin by heparin cofactor II.	Dermatan Sulfate	22-38	coagulation factor II, thrombin	Homo sapiens	42-50
3374475-4	1988	LPL secretion could also be stimulated by heparan sulfate and dermatan sulfate, but not by hyaluronic acid, chondroitin sulfate or keratan sulfate.	Dermatan Sulfate	62-78	lipoprotein lipase	Rattus norvegicus	0-3
3691797-0	1987	Binding of heparin or dermatan sulfate to thrombin is essential for the sulfated polysaccharide-accelerated inhibition of thrombin by heparin cofactor II.	Dermatan Sulfate	22-38	coagulation factor II, thrombin	Homo sapiens	122-130
3691797-5	1987	These results indicate that the binding of heparin or dermatan sulfate to both thrombin and HC II is required for the sulfated polysaccharide-dependent acceleration of the thrombin inhibition by HC II, and the binding to thrombin is more essential for the reaction.	Dermatan Sulfate	54-70	serpin family D member 1	Homo sapiens	195-200
3691797-0	1987	Binding of heparin or dermatan sulfate to thrombin is essential for the sulfated polysaccharide-accelerated inhibition of thrombin by heparin cofactor II.	Dermatan Sulfate	22-38	serpin family D member 1	Homo sapiens	134-153
3691797-5	1987	These results indicate that the binding of heparin or dermatan sulfate to both thrombin and HC II is required for the sulfated polysaccharide-dependent acceleration of the thrombin inhibition by HC II, and the binding to thrombin is more essential for the reaction.	Dermatan Sulfate	54-70	coagulation factor II, thrombin	Homo sapiens	172-180
3691797-1	1987	Heparin cofactor II (HC II) and thrombin were chemically modified with pyridoxal 5"-phosphate, and their effects on the inhibition of thrombin by HC II in the presence of heparin or dermatan sulfate were studied.	Dermatan Sulfate	182-198	serpin family D member 1	Homo sapiens	0-19
3691797-1	1987	Heparin cofactor II (HC II) and thrombin were chemically modified with pyridoxal 5"-phosphate, and their effects on the inhibition of thrombin by HC II in the presence of heparin or dermatan sulfate were studied.	Dermatan Sulfate	182-198	coagulation factor II, thrombin	Homo sapiens	32-40
3691797-2	1987	The inhibition of thrombin by HC II was enhanced about 7000-fold in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	95-111	coagulation factor II, thrombin	Homo sapiens	18-26
3691797-2	1987	The inhibition of thrombin by HC II was enhanced about 7000-fold in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	95-111	serpin family D member 1	Homo sapiens	30-35
3691797-5	1987	These results indicate that the binding of heparin or dermatan sulfate to both thrombin and HC II is required for the sulfated polysaccharide-dependent acceleration of the thrombin inhibition by HC II, and the binding to thrombin is more essential for the reaction.	Dermatan Sulfate	54-70	coagulation factor II, thrombin	Homo sapiens	79-87
3691797-5	1987	These results indicate that the binding of heparin or dermatan sulfate to both thrombin and HC II is required for the sulfated polysaccharide-dependent acceleration of the thrombin inhibition by HC II, and the binding to thrombin is more essential for the reaction.	Dermatan Sulfate	54-70	serpin family D member 1	Homo sapiens	92-97
3691797-5	1987	These results indicate that the binding of heparin or dermatan sulfate to both thrombin and HC II is required for the sulfated polysaccharide-dependent acceleration of the thrombin inhibition by HC II, and the binding to thrombin is more essential for the reaction.	Dermatan Sulfate	54-70	coagulation factor II, thrombin	Homo sapiens	172-180
3620505-0	1987	Isolation of dermatan sulfate with high heparin cofactor II-mediated thrombin-inhibitory activity from porcine spleen.	Dermatan Sulfate	13-29	coagulation factor II, thrombin	Homo sapiens	69-77
3123254-3	1987	The PF4 kinetics, in the presence of heparan and dermatan sulphate, reflected the different affinities that PF4 has for these GAGs.	Dermatan Sulfate	49-66	platelet factor 4	Homo sapiens	4-7
3123254-3	1987	The PF4 kinetics, in the presence of heparan and dermatan sulphate, reflected the different affinities that PF4 has for these GAGs.	Dermatan Sulfate	49-66	platelet factor 4	Homo sapiens	108-111
3123254-9	1987	Although part of the protamine will displace PF4 from the binding sites of the dermatan sulphate molecule, the remaining part of protamine could probably be bound to this GAG without losing its activity so that, upon subsequent heparin injection, it is immediately neutralized, rendering it unavailable for further PF4 harvesting.	Dermatan Sulfate	79-96	platelet factor 4	Homo sapiens	45-48
3316251-8	1987	Deposition of the fibrin matrix in hepatocyte cultures was arrested by hirudin, by specific heparin oligosaccharides that potentiate thrombin inhibition by antithrombin III, and by dermatan sulfate, an activator of heparin cofactor II-mediated inhibition of thrombin.	Dermatan Sulfate	181-197	serpin family D member 1	Rattus norvegicus	215-234
3433248-3	1987	DS has minimal anticoagulant activity by conventional assays but impairs thrombin generation both in vitro and in ex vivo plasma samples.	Dermatan Sulfate	0-2	coagulation factor II, thrombin	Homo sapiens	73-81
3620505-4	1987	Spleen dermatan sulfate exhibited the highest thrombin-inhibitory activity, which may be related to its high content of the disulfated N-acetylgalactosamine residue.	Dermatan Sulfate	7-23	coagulation factor II, thrombin	Homo sapiens	46-54
3113515-4	1987	The PAI-1 could not be removed by incubating ECM in high salt (2 mol/L NaCl), sugars (1 mol/L galactose, 1 mol/L mannose), glycosaminoglycans (10 mmol/L heparin, 10 mmol/L dermatan sulfate), or epsilon-aminocaproic acid (0.1 mol/L).	Dermatan Sulfate	172-188	serpin family E member 1	Bos taurus	4-9
3619144-6	1987	II is likely that its antithrombin activity in vivo is restricted to the areas rich in dermatan sulfate.	Dermatan Sulfate	87-103	serpin family C member 1	Homo sapiens	22-34
3116701-4	1987	Increasing concentrations of heparin (greater than 0.066 micrograms/mL or 0.01 USP units/mL) and dermatan sulfate (greater than 0.1 micrograms/mL) could be readily demonstrated in undiluted plasma by enhanced formation of complexes of thrombin with antithrombin III and heparin cofactor II respectively.	Dermatan Sulfate	97-113	prothrombin	Oryctolagus cuniculus	235-243
3116701-4	1987	Increasing concentrations of heparin (greater than 0.066 micrograms/mL or 0.01 USP units/mL) and dermatan sulfate (greater than 0.1 micrograms/mL) could be readily demonstrated in undiluted plasma by enhanced formation of complexes of thrombin with antithrombin III and heparin cofactor II respectively.	Dermatan Sulfate	97-113	heparin cofactor 2	Oryctolagus cuniculus	270-289
2954956-0	1987	Isolation and characterization of fibronectin-binding proteoglycan carrying both heparan sulfate and dermatan sulfate chains from human placenta.	Dermatan Sulfate	101-117	fibronectin 1	Homo sapiens	34-45
2948956-0	1987	Ca2+-mediated association of human serum amyloid P component with heparan sulfate and dermatan sulfate.	Dermatan Sulfate	86-102	amyloid P component, serum	Homo sapiens	35-60
2948956-2	1987	The binding of human SAP to heparan sulfate and dermatan sulfate was studied using Sepharose-immobilized SAP.	Dermatan Sulfate	48-64	amyloid P component, serum	Homo sapiens	21-24
2948956-3	1987	The apparent dissociation constants of heparan sulfate and dermatan sulfate for immobilized-SAP were estimated to be approximately 2 X 10(-7) M in the presence of 2 mM CaCl2 at neutral pH and physiological ionic strength.	Dermatan Sulfate	59-75	amyloid P component, serum	Homo sapiens	92-95
2948956-7	1987	The calcium-dependent binding of [3H]heparan sulfate and [3H]dermatan sulfate to SAP was strongly inhibited by heparan sulfate, heparin, and dermatan sulfate.	Dermatan Sulfate	61-77	amyloid P component, serum	Homo sapiens	81-84
2948956-7	1987	The calcium-dependent binding of [3H]heparan sulfate and [3H]dermatan sulfate to SAP was strongly inhibited by heparan sulfate, heparin, and dermatan sulfate.	Dermatan Sulfate	141-157	amyloid P component, serum	Homo sapiens	81-84
3619144-4	1987	Dermatan sulfate and pentosan sulfate but not heparin sulfate increase the rate of thrombin inhibition by HC II.	Dermatan Sulfate	0-16	coagulation factor II, thrombin	Homo sapiens	83-91
3619144-4	1987	Dermatan sulfate and pentosan sulfate but not heparin sulfate increase the rate of thrombin inhibition by HC II.	Dermatan Sulfate	0-16	serpin family D member 1	Homo sapiens	106-111
3619144-11	1987	In contrast, the anticoagulant effect of dermatan sulfate is strictly dependent on HC II.	Dermatan Sulfate	41-57	serpin family D member 1	Homo sapiens	83-88
2432917-4	1986	The anticoagulant activities of heparin and dermatan sulphate were primarily attributable to their ability to enhance thrombin inhibition by AT III and HC II respectively.	Dermatan Sulfate	44-61	coagulation factor II, thrombin	Homo sapiens	118-126
3793724-1	1987	Inhibition of thrombin by heparin cofactor II (HCII) is accelerated by dermatan sulfate, heparan sulfate, and heparin.	Dermatan Sulfate	71-87	coagulation factor II, thrombin	Homo sapiens	14-22
3793724-1	1987	Inhibition of thrombin by heparin cofactor II (HCII) is accelerated by dermatan sulfate, heparan sulfate, and heparin.	Dermatan Sulfate	71-87	serpin family D member 1	Homo sapiens	26-45
3793724-1	1987	Inhibition of thrombin by heparin cofactor II (HCII) is accelerated by dermatan sulfate, heparan sulfate, and heparin.	Dermatan Sulfate	71-87	serpin family D member 1	Homo sapiens	47-51
3793724-6	1987	In contrast, treatment with chondroitinase ABC almost totally abolished the ability of these cells to activate HCII while chondroitinase AC had little or no effect, suggesting that dermatan sulfate was responsible for the activity observed.	Dermatan Sulfate	181-197	serpin family D member 1	Homo sapiens	111-115
3301469-5	1987	Dermatan sulphate, a glycosaminoglycan, specifically activates HCII and increases its thrombin neutralizing activity by over a thousand fold.	Dermatan Sulfate	0-17	serpin family D member 1	Homo sapiens	63-67
3301469-5	1987	Dermatan sulphate, a glycosaminoglycan, specifically activates HCII and increases its thrombin neutralizing activity by over a thousand fold.	Dermatan Sulfate	0-17	coagulation factor II, thrombin	Homo sapiens	86-94
3301469-10	1987	The specificity of dermatan sulphate for HCII has allowed the development of functional assays for this protein.	Dermatan Sulfate	19-36	serpin family D member 1	Homo sapiens	41-45
2432917-4	1986	The anticoagulant activities of heparin and dermatan sulphate were primarily attributable to their ability to enhance thrombin inhibition by AT III and HC II respectively.	Dermatan Sulfate	44-61	serpin family C member 1	Homo sapiens	141-147
2432917-4	1986	The anticoagulant activities of heparin and dermatan sulphate were primarily attributable to their ability to enhance thrombin inhibition by AT III and HC II respectively.	Dermatan Sulfate	44-61	serpin family D member 1	Homo sapiens	152-157
3094551-6	1986	Although total GAG concentrations did not differ between a normolipemic control and the two diet groups, apoB showed a significantly positive correlation with the percent of total GAG that was chondroitin sulfate and a significantly negative correlation with the percent of total GAG that was dermatan sulfate.	Dermatan Sulfate	293-309	apolipoprotein B	Sus scrofa	105-109
2432675-3	1986	The maximum second order rate constant of heparin cofactor II-thrombin reaction in the presence of the fractions of over-10 kDa and 18% sulfur was 2.7 X 10(8) M-1 min-1 that was almost same as in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	223-239	coagulation factor II, thrombin	Homo sapiens	62-70
2432675-3	1986	The maximum second order rate constant of heparin cofactor II-thrombin reaction in the presence of the fractions of over-10 kDa and 18% sulfur was 2.7 X 10(8) M-1 min-1 that was almost same as in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	223-239	CD59 molecule (CD59 blood group)	Homo sapiens	163-168
3816422-2	1986	Two species of dermatan sulphate proteoglycans, called DS-PGI and DS-PGII, have recently been isolated from mature bovine articular cartilages.	Dermatan Sulfate	15-32	decorin	Mus musculus	69-73
3755134-1	1986	Heparin cofactor II (HCII) inhibits thrombin rapidly in human plasma in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	99-115	serpin family D member 1	Homo sapiens	0-19
3755134-1	1986	Heparin cofactor II (HCII) inhibits thrombin rapidly in human plasma in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	99-115	serpin family D member 1	Homo sapiens	21-25
3943552-8	1986	These results support the hypothesis that the mechanism of PMC migration involves fibronectin, collagen and sulfated proteoglycans which contain dermatan sulfate.	Dermatan Sulfate	145-161	fibronectin 1	Mus musculus	82-93
2436525-17	1986	At the two lower concentrations, dermatan sulfate catalyzed formation of thrombin-heparin cofactor II.	Dermatan Sulfate	33-49	coagulation factor II, thrombin	Homo sapiens	73-81
3768894-5	1986	The silkworm lectin had the highest affinity for dermatan sulfate and hyaluronic acid, followed by protuberic acid, heparin, and chondroitin sulfate A.	Dermatan Sulfate	49-65	hemocytin	Bombyx mori	13-19
3755134-1	1986	Heparin cofactor II (HCII) inhibits thrombin rapidly in human plasma in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	99-115	coagulation factor II, thrombin	Homo sapiens	36-44
3755134-2	1986	To determine the minimum structure of dermatan sulfate required to activate HCII, the glycosaminoglycan was partially degraded by sequential treatment with periodate, [3H]borohydride, and sulfuric acid.	Dermatan Sulfate	38-54	serpin family D member 1	Homo sapiens	76-80
3755134-7	1986	Fragments of dermatan sulfate containing a minimum of 12-14 sugar residues accelerated inhibition of thrombin by HCII.	Dermatan Sulfate	13-29	coagulation factor II, thrombin	Homo sapiens	101-109
3755134-7	1986	Fragments of dermatan sulfate containing a minimum of 12-14 sugar residues accelerated inhibition of thrombin by HCII.	Dermatan Sulfate	13-29	serpin family D member 1	Homo sapiens	113-117
3755134-9	1986	These studies suggest that HCII is activated by dermatan sulfate fragments greater than or equal to 12 residues in length that contain a specific octasaccharide sequence required for binding to the inhibitor.	Dermatan Sulfate	48-64	serpin family D member 1	Homo sapiens	27-31
3816422-2	1986	Two species of dermatan sulphate proteoglycans, called DS-PGI and DS-PGII, have recently been isolated from mature bovine articular cartilages.	Dermatan Sulfate	15-32	biglycan	Mus musculus	58-61
2998359-1	1985	Human plasma heparin cofactor II (HCII) inhibits thrombin by rapidly forming a stable, equimolar complex in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	135-151	serpin family D member 1	Homo sapiens	13-32
3841420-4	1985	The biological activity of the HC II was unchanged after labelling as was its migratory pattern by crossed immunoelectrophoresis in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	159-175	serpin family D member 1	Homo sapiens	31-36
2998359-1	1985	Human plasma heparin cofactor II (HCII) inhibits thrombin by rapidly forming a stable, equimolar complex in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	135-151	serpin family D member 1	Homo sapiens	34-38
2998359-1	1985	Human plasma heparin cofactor II (HCII) inhibits thrombin by rapidly forming a stable, equimolar complex in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	135-151	coagulation factor II, thrombin	Homo sapiens	49-57
3863104-2	1985	The rate of thrombin inhibition by heparin cofactor II is accelerated (greater than or equal to 1000-fold) in the presence of the glycosaminoglycans, heparin and dermatan sulfate.	Dermatan Sulfate	162-178	coagulation factor II, thrombin	Homo sapiens	12-20
4041618-1	1985	Heparin cofactor II (HCII) is a glycoprotein in human plasma which inactivates thrombin rapidly in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	126-142	serpin family D member 1	Homo sapiens	0-19
4041618-1	1985	Heparin cofactor II (HCII) is a glycoprotein in human plasma which inactivates thrombin rapidly in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	126-142	serpin family D member 1	Homo sapiens	21-25
4041618-1	1985	Heparin cofactor II (HCII) is a glycoprotein in human plasma which inactivates thrombin rapidly in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	126-142	coagulation factor II, thrombin	Homo sapiens	79-87
4041618-2	1985	We have developed a functional assay for HCII in which inhibition of thrombin by plasma is determined in the presence of dermatan sulfate.	Dermatan Sulfate	121-137	serpin family D member 1	Homo sapiens	41-45
4041618-2	1985	We have developed a functional assay for HCII in which inhibition of thrombin by plasma is determined in the presence of dermatan sulfate.	Dermatan Sulfate	121-137	coagulation factor II, thrombin	Homo sapiens	69-77
3931626-9	1985	We propose that some, if not all, of the sulphated N-acetylhexosamine present in human urine is derived from the action of beta-N-acetylhexosaminidase on sulphated GlcNAc or GalNAc residues at the non-reducing end of keratan sulphate, dermatan sulphate or chondroitin sulphate.	Dermatan Sulfate	235-252	O-GlcNAcase	Homo sapiens	123-150
2411283-0	1985	The importance of thrombin inhibition for the expression of the anticoagulant activities of heparin, dermatan sulphate, low molecular weight heparin and pentosan polysulphate.	Dermatan Sulfate	101-118	coagulation factor II, thrombin	Homo sapiens	18-26
2411283-5	1985	Dermatan sulphate and pentosan polysulphate were more effective as inhibitors of thrombin generation than potentiators of factor Xa inactivation.	Dermatan Sulfate	0-17	coagulation factor II, thrombin	Homo sapiens	81-89
3997823-13	1985	These results suggest that DS-PGI and DS-PGII possess different core proteins and may represent two different species of dermatan sulfate proteoglycans.	Dermatan Sulfate	121-137	glucose-6-phosphate isomerase	Bos taurus	30-33
3989479-4	1985	The sequential application of chondroitinase AC and ABC permits the determination of hyaluronate, the chondroitin sulphate isomers and the dermatan sulphate isomers by high performance liquid chromatographic separation of the products of enzymatic hydrolysis.	Dermatan Sulfate	139-156	ATP binding cassette subfamily B member 6 (Langereis blood group)	Homo sapiens	52-55
3838315-3	1985	In the presence of 67 micrograms/ml of dermatan sulfate, radioactivity was detected in a band which corresponded to the thrombin-HCII complex (Mr = 96,000) upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	Dermatan Sulfate	39-55	coagulation factor II, thrombin	Homo sapiens	120-128
3838315-3	1985	In the presence of 67 micrograms/ml of dermatan sulfate, radioactivity was detected in a band which corresponded to the thrombin-HCII complex (Mr = 96,000) upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	Dermatan Sulfate	39-55	serpin family D member 1	Homo sapiens	129-133
3838315-7	1985	HCII inhibited leukocyte cathepsin G slowly, with a rate constant of 8 X 10(4) M-1 min-1 in the presence of dermatan sulfate.	Dermatan Sulfate	108-124	serpin family D member 1	Homo sapiens	0-4
3838315-8	1985	These results indicate that the protease specificity of HCII is more restricted than that of other plasma protease inhibitors and suggest that the anticoagulant effect of dermatan sulfate is due solely to inhibition of thrombin by HCII.	Dermatan Sulfate	171-187	serpin family D member 1	Homo sapiens	56-60
3838315-8	1985	These results indicate that the protease specificity of HCII is more restricted than that of other plasma protease inhibitors and suggest that the anticoagulant effect of dermatan sulfate is due solely to inhibition of thrombin by HCII.	Dermatan Sulfate	171-187	coagulation factor II, thrombin	Homo sapiens	219-227
3838315-8	1985	These results indicate that the protease specificity of HCII is more restricted than that of other plasma protease inhibitors and suggest that the anticoagulant effect of dermatan sulfate is due solely to inhibition of thrombin by HCII.	Dermatan Sulfate	171-187	serpin family D member 1	Homo sapiens	231-235
6084876-8	1984	When mixed with thrombin in the presence of dermatan sulfate, normal human plasma showed antithrombin activity which was not due to AT III but to HC II only.	Dermatan Sulfate	44-60	coagulation factor II, thrombin	Homo sapiens	16-24
3838317-1	1985	Heparin cofactor II is a plasma protein that inhibits thrombin rapidly in the presence of either heparin or dermatan sulfate.	Dermatan Sulfate	108-124	coagulation factor II, thrombin	Homo sapiens	54-62
3838317-7	1985	Furthermore, the supernatant medium from platelets treated with arachidonic acid to cause secretion of platelet factor 4 prevented inhibition of thrombin by heparin cofactor II in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	207-223	coagulation factor II, thrombin	Homo sapiens	145-153
6084876-8	1984	When mixed with thrombin in the presence of dermatan sulfate, normal human plasma showed antithrombin activity which was not due to AT III but to HC II only.	Dermatan Sulfate	44-60	serpin family C member 1	Homo sapiens	89-101
6084876-8	1984	When mixed with thrombin in the presence of dermatan sulfate, normal human plasma showed antithrombin activity which was not due to AT III but to HC II only.	Dermatan Sulfate	44-60	serpin family D member 1	Homo sapiens	146-151
6437709-0	1984	alpha-L-Iduronidase deficiency in mucopolysaccharidosis type I against a radiolabelled sulfated disaccharide substrate derived from dermatan sulfate.	Dermatan Sulfate	132-148	alpha-L-iduronidase	Homo sapiens	0-19
3838602-0	1985	Histidine-rich glycoprotein inhibits the antithrombin activity of heparin cofactor II in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	116-132	serpin family C member 1	Homo sapiens	41-53
6209821-1	1984	In antithrombin III depleted plasma only a slight reduction was observed in thrombin inhibitory activity due to potentiation by dermatan sulphate or by pentosan polysulphate (SP54).	Dermatan Sulfate	128-145	serpin family C member 1	Homo sapiens	3-19
6395434-3	1984	HCII activity was then determined by measuring the rate of human thrombin inhibition by 3 ways: a) activation with heparin in AT-free plasma, b) activation with dermatan sulfate in normal plasma and c) activation with dermatan sulfate in AT-free plasma.	Dermatan Sulfate	161-177	serpin family D member 1	Homo sapiens	0-4
6395434-3	1984	HCII activity was then determined by measuring the rate of human thrombin inhibition by 3 ways: a) activation with heparin in AT-free plasma, b) activation with dermatan sulfate in normal plasma and c) activation with dermatan sulfate in AT-free plasma.	Dermatan Sulfate	218-234	serpin family D member 1	Homo sapiens	0-4
6395434-3	1984	HCII activity was then determined by measuring the rate of human thrombin inhibition by 3 ways: a) activation with heparin in AT-free plasma, b) activation with dermatan sulfate in normal plasma and c) activation with dermatan sulfate in AT-free plasma.	Dermatan Sulfate	218-234	serpin family C member 1	Homo sapiens	238-240
6206589-0	1984	Inhibition of thrombin-induced platelet aggregation and serotonin release by antithrombin III and heparin cofactor II in the presence of standard heparin, dermatan sulfate and pentosan polysulfate.	Dermatan Sulfate	155-171	coagulation factor II, thrombin	Homo sapiens	14-22
6235872-0	1984	Heparan sulfate and dermatan sulfate inhibit the generation of thrombin activity in plasma by complementary pathways.	Dermatan Sulfate	20-36	coagulation factor II, thrombin	Homo sapiens	63-71
6235872-5	1984	In contrast, dermatan sulfate inhibited thrombin generation in both normal and antithrombin III-depleted plasma.	Dermatan Sulfate	13-29	coagulation factor II, thrombin	Homo sapiens	40-48
6235872-5	1984	In contrast, dermatan sulfate inhibited thrombin generation in both normal and antithrombin III-depleted plasma.	Dermatan Sulfate	13-29	serpin family C member 1	Homo sapiens	79-95
6469965-14	1984	The larger dermatan sulfate proteoglycan (DS-I) is transported to the cell surface from which it is quantitatively released into the medium with a t1/2 of 4-6 h. The smaller DS-PG (DS-II) is metabolized similarly to the HS-PG.	Dermatan Sulfate	11-27	syndecan 2	Rattus norvegicus	220-225
6235872-9	1984	The inhibition of thrombin generation by heparan sulfate and dermatan sulfate thus appears to occur by complementary pathways, both of which may contribute to the anticoagulation of blood in vivo.	Dermatan Sulfate	61-77	coagulation factor II, thrombin	Homo sapiens	18-26
6547786-1	1984	An assay measuring the thrombin inactivating effect of human plasma in the presence of dermatan sulfate (DS) is described.	Dermatan Sulfate	87-103	coagulation factor II, thrombin	Homo sapiens	23-31
6547786-1	1984	An assay measuring the thrombin inactivating effect of human plasma in the presence of dermatan sulfate (DS) is described.	Dermatan Sulfate	105-107	coagulation factor II, thrombin	Homo sapiens	23-31
6547786-2	1984	Test plasma, diluted 1/50, is incubated with human thrombin in the presence of DS.	Dermatan Sulfate	79-81	coagulation factor II, thrombin	Homo sapiens	51-59
6206589-0	1984	Inhibition of thrombin-induced platelet aggregation and serotonin release by antithrombin III and heparin cofactor II in the presence of standard heparin, dermatan sulfate and pentosan polysulfate.	Dermatan Sulfate	155-171	serpin family C member 1	Homo sapiens	77-93
6478830-10	1984	In contrast, cellular fractions dA1-dA3 and medium fraction dA4 were enriched in dermatan sulfate.	Dermatan Sulfate	81-97	anon-A1	Drosophila melanogaster	32-35
6231139-5	1984	Conversely, form B alpha-L-iduronidase could not degrade HS, but could degrade DS.	Dermatan Sulfate	79-81	alpha-L-iduronidase	Homo sapiens	19-38
6478830-10	1984	In contrast, cellular fractions dA1-dA3 and medium fraction dA4 were enriched in dermatan sulfate.	Dermatan Sulfate	81-97	l(1)11Ad	Drosophila melanogaster	60-63
6687802-3	1983	Heparin and dermatan sulfate which were eluted from the affinity column catalyzed the inhibition of thrombin by heparin cofactor II to a greater degree than did the respective unfractionated mucopolysaccharides.	Dermatan Sulfate	12-28	coagulation factor II, thrombin	Homo sapiens	100-108
6548014-4	1984	Heparin cofactor II appears to be the only thrombin inhibitor in plasma that can be activated by dermatan sulfate.	Dermatan Sulfate	97-113	coagulation factor II, thrombin	Homo sapiens	43-51
6687888-0	1983	Activation of heparin cofactor II by dermatan sulfate.	Dermatan Sulfate	37-53	serpin family D member 1	Homo sapiens	14-33
6687888-2	1983	Heparin, dermatan sulfate, and heparan sulfate from bovine liver (in order of decreasing activity) activated HCII.	Dermatan Sulfate	9-25	serpin family D member 1	Homo sapiens	109-113
6423280-0	1983	Selective depolymerisation of dermatan sulfate: production of radiolabelled substrates for alpha-L-iduronidase, sulfoiduronate sulfatase, and beta-D-glucuronidase.	Dermatan Sulfate	30-46	alpha-L-iduronidase	Homo sapiens	91-110
6423280-0	1983	Selective depolymerisation of dermatan sulfate: production of radiolabelled substrates for alpha-L-iduronidase, sulfoiduronate sulfatase, and beta-D-glucuronidase.	Dermatan Sulfate	30-46	glucuronidase beta	Homo sapiens	142-162
6423280-1	1983	Radiolabelled disaccharide substrates for alpha-L-iduronidase, beta-D-glucuronidase, and sulfoiduronate sulfatase have been prepared from dermatan sulfate by application in sequence of N-deacetylation, deaminative cleavage, and reduction with NaBT4.	Dermatan Sulfate	138-154	alpha-L-iduronidase	Homo sapiens	42-61
6423280-1	1983	Radiolabelled disaccharide substrates for alpha-L-iduronidase, beta-D-glucuronidase, and sulfoiduronate sulfatase have been prepared from dermatan sulfate by application in sequence of N-deacetylation, deaminative cleavage, and reduction with NaBT4.	Dermatan Sulfate	138-154	glucuronidase beta	Homo sapiens	63-113
6687888-5	1983	The second order rate constant for the thrombin-HCII reaction reached a maximum value of 6.4 X 10(8) M-1 min-1 in the presence of 250-500 micrograms/ml of dermatan sulfate compared to 3.8 X 10(8) M-1 min-1 in the presence of 40-80 micrograms/ml of heparin.	Dermatan Sulfate	155-171	coagulation factor II, thrombin	Homo sapiens	39-47
6687888-5	1983	The second order rate constant for the thrombin-HCII reaction reached a maximum value of 6.4 X 10(8) M-1 min-1 in the presence of 250-500 micrograms/ml of dermatan sulfate compared to 3.8 X 10(8) M-1 min-1 in the presence of 40-80 micrograms/ml of heparin.	Dermatan Sulfate	155-171	serpin family D member 1	Homo sapiens	48-52
6687888-5	1983	The second order rate constant for the thrombin-HCII reaction reached a maximum value of 6.4 X 10(8) M-1 min-1 in the presence of 250-500 micrograms/ml of dermatan sulfate compared to 3.8 X 10(8) M-1 min-1 in the presence of 40-80 micrograms/ml of heparin.	Dermatan Sulfate	155-171	CD59 molecule (CD59 blood group)	Homo sapiens	105-110
6687888-5	1983	The second order rate constant for the thrombin-HCII reaction reached a maximum value of 6.4 X 10(8) M-1 min-1 in the presence of 250-500 micrograms/ml of dermatan sulfate compared to 3.8 X 10(8) M-1 min-1 in the presence of 40-80 micrograms/ml of heparin.	Dermatan Sulfate	155-171	CD59 molecule (CD59 blood group)	Homo sapiens	200-205
6687888-6	1983	When 125I-thrombin was incubated with plasma in the presence of greater than or equal to 100 micrograms/ml of dermatan sulfate, the protease became complexed exclusively with HCII, suggesting that HCII is the only thrombin inhibitor in human plasma that can be activated by dermatan sulfate.	Dermatan Sulfate	110-126	coagulation factor II, thrombin	Homo sapiens	10-18
6687888-6	1983	When 125I-thrombin was incubated with plasma in the presence of greater than or equal to 100 micrograms/ml of dermatan sulfate, the protease became complexed exclusively with HCII, suggesting that HCII is the only thrombin inhibitor in human plasma that can be activated by dermatan sulfate.	Dermatan Sulfate	274-290	coagulation factor II, thrombin	Homo sapiens	10-18
6218163-10	1983	A variety of mucopolysaccharides were able to inhibit interaction of C1q with 125I-LMW-Hep, the most effective being heparan sulfate and dermatan sulfate.	Dermatan Sulfate	137-153	complement C1q C chain	Homo sapiens	69-72
7225714-2	1981	2 Only dermatan sulphate preparations of considerable heparin content potentiate AT III inhibition of thrombin, factor Xa and plasmin.	Dermatan Sulfate	7-24	serpin family C member 1	Homo sapiens	81-87
6130961-7	1983	The activities of two lysosomal hydrolases (arylsulfatase A and arylsulfatase B) involved in the metabolism of sulfatide and dermatan sulfate were measured in confluent cultures.	Dermatan Sulfate	125-141	arylsulfatase A	Felis catus	44-79
7326032-9	1981	The data obtained indicate that the epimerization of D-glucuronosyl to L-iduronosyl residues during biosynthesis of dermatan sulphate involves an abstraction of the C-5 hydrogen of the uronosyl residue.	Dermatan Sulfate	116-133	complement C5	Homo sapiens	165-168
7225714-2	1981	2 Only dermatan sulphate preparations of considerable heparin content potentiate AT III inhibition of thrombin, factor Xa and plasmin.	Dermatan Sulfate	7-24	coagulation factor II, thrombin	Homo sapiens	102-110
7225714-2	1981	2 Only dermatan sulphate preparations of considerable heparin content potentiate AT III inhibition of thrombin, factor Xa and plasmin.	Dermatan Sulfate	7-24	coagulation factor X	Homo sapiens	112-121
7225714-2	1981	2 Only dermatan sulphate preparations of considerable heparin content potentiate AT III inhibition of thrombin, factor Xa and plasmin.	Dermatan Sulfate	7-24	plasminogen	Homo sapiens	126-133
522483-3	1979	One of these, called lectin-2, interacts with specific glycosaminoglycans, especially heparin and dermatan sulfate.	Dermatan Sulfate	98-114	galectin 3	Gallus gallus	21-27
6452123-2	1980	Lipoprotein lipase (EC 3.1.1.34), which was previously shown to bind to immobilized heparin, was now found to bind also to heparan sulphate and dermatan sulphate and to some extent to chondroitin sulphate.	Dermatan Sulfate	144-161	lipoprotein lipase	Rattus norvegicus	0-18
6773589-4	1980	The glycosaminoglycan fraction obtained from the AB-CBF1-MCT-1 mastocytoma cultured in vitro consisted predominantly of dermatan sulfate-like material.	Dermatan Sulfate	120-136	recombination signal binding protein for immunoglobulin kappa J region	Mus musculus	52-56
641404-3	1978	CTAP-I from lymphocytes and CTAP-III from platelets markedly stimulated 35SO4= incorporation into chondroitin 4/6 sulfate and dermatan sulfate synthesized by human synovial, dermal, and cartilage connective tissue cells in vitro.	Dermatan Sulfate	126-142	pro-platelet basic protein	Homo sapiens	28-36
102641-3	1978	This patient exhibited a high level of urinary excretion of dermatan sulfate and heparan sulfate, which could be interpreted in terms of her low alpha-L-iduronidase activity.	Dermatan Sulfate	60-76	alpha-L-iduronidase	Homo sapiens	145-164
656058-2	1978	The order of strength of inhibition at pH4 was: heparin greater than chondroitin 4-sulphate = chondroitin 6-sulphate greater than dermatan sulphate.	Dermatan Sulfate	130-147	prolyl 4-hydroxylase, transmembrane	Homo sapiens	39-42
154210-2	1978	The degradation of dermatan sulphate and heparan sulphate is disturbed due to alpha-L-iduronidase deficiency, leading to intracellular storage and excessive urinary secretion of these substances.	Dermatan Sulfate	19-36	alpha-L-iduronidase	Homo sapiens	78-97
1093849-0	1975	Beta-N-acetylhexosaminidase active on dermatan sulfate.	Dermatan Sulfate	38-54	O-GlcNAcase	Homo sapiens	0-27
409573-2	1977	We have demonstrated complete inhibition of GM1 ganglioside beta-galactosidase activity in vitro by both heparan sulfate and dermatan sulfate, but the effect on lactosylceramide and galactosylceramide hydrolysis was less marked.	Dermatan Sulfate	125-141	galactosidase beta 1	Homo sapiens	60-78
1156366-9	1975	To determine the location of L-IdUA-SO4 residues along the copolymeric chain dermatan sulphate was digested with testicular hyaluronidase.	Dermatan Sulfate	77-94	hemopexin	Sus scrofa	124-137
1156366-15	1975	To study the distribution of L-IdUA-SO4-containing periods in relation to blocks of IdUA-GalNAc-SO4 periods different fractions of hyaluronidase-degraded dermatan sulphate were degraded separately.	Dermatan Sulfate	154-171	hemopexin	Sus scrofa	131-144
1093849-3	1975	It is concluded that normal human serum possesses an exo-beta-N-acetylhexosaminidase active on dermatan sulfate.	Dermatan Sulfate	95-111	O-GlcNAcase	Homo sapiens	57-84
4376944-11	1974	Chemically desulphated dermatan sulphate was found to be a poor substrate for the chondroitinase-ABC enzyme.	Dermatan Sulfate	23-40	galactosamine (N-acetyl)-6-sulfatase	Sus scrofa	82-96
4376944-12	1974	Moreover, digestion with chondroitinase-ABC of chondroitinase-AC-degraded dermatan sulphate released periodate-resistant iduronic acid-containing oligosaccharides.	Dermatan Sulfate	74-91	galactosamine (N-acetyl)-6-sulfatase	Sus scrofa	25-39
4376944-12	1974	Moreover, digestion with chondroitinase-ABC of chondroitinase-AC-degraded dermatan sulphate released periodate-resistant iduronic acid-containing oligosaccharides.	Dermatan Sulfate	74-91	galactosamine (N-acetyl)-6-sulfatase	Sus scrofa	47-61
4376944-2	1974	Dermatan sulphate was degraded by testicular hyaluronidase and an oversulphated fraction was isolated by ion-exchange chromatography.	Dermatan Sulfate	0-17	hemopexin	Sus scrofa	45-58
5038324-4	1972	The growth of tumour cells which were injected subcutaneously after in vitro incubation with chondroitinase-ABC or -AC solution was decreased when compared with that of sham-treated cells.The injection of 1 ml of chondroitin sulphate A and chondroitin sulphate C solution prior to tumour inoculation into the same site promoted the tumour growth, while growth-stimulating effect of chondroitin sulphate B was ambiguous.	Dermatan Sulfate	382-404	galactosamine (N-acetyl)-6-sulfatase	Homo sapiens	93-107
13709087-0	1961	In vitro effects heparin and chondroitin sulfuric acid B on the generation of thrombin.	Dermatan Sulfate	29-56	coagulation factor II, thrombin	Homo sapiens	78-86
33742537-2	2022	Endocan is a soluble dermatan sulphate proteoglycan expressed by endothelium of blood vessels.	Dermatan Sulfate	21-38	endothelial cell specific molecule 1	Homo sapiens	0-7
33997316-4	2021	Previously, we reported that biglycan, a small leucine-rich dermatan sulfate proteoglycan, intensifies ALK5-Smad2/3 signaling by TGF-beta1 and downregulates syndecan-4 expression in vascular endothelial cells.	Dermatan Sulfate	60-76	biglycan	Bos taurus	29-37
33997316-4	2021	Previously, we reported that biglycan, a small leucine-rich dermatan sulfate proteoglycan, intensifies ALK5-Smad2/3 signaling by TGF-beta1 and downregulates syndecan-4 expression in vascular endothelial cells.	Dermatan Sulfate	60-76	SMAD family member 2	Bos taurus	108-115
33623064-4	2021	Dermatan sulphate was correlated with soluble syndecan-1, and inversely correlated with blood pressure and activated partial thromboplastin time.	Dermatan Sulfate	0-17	syndecan 1	Homo sapiens	46-56
33623064-7	2021	The results show that an interplay between syndecan-1 and dermatan sulphate contributes to sFlt1 induced blood pressure elevation in pre-eclampsia.	Dermatan Sulfate	58-75	FMS-like tyrosine kinase 1	Mus musculus	91-96
32785657-6	2021	Subjecting NRK-52E cells to HG milieu significantly decreased sGAG levels more so of chondroitin/dermatan sulfate, which is significantly prevented when HG is co-treated with AMPK activator.	Dermatan Sulfate	97-113	protein kinase AMP-activated catalytic subunit alpha 2	Rattus norvegicus	175-179
32601684-1	2021	Loss-of-function variants in CHST14 cause a dermatan 4-O-sulfotransferase deficiency named musculocontractural Ehlers-Danlos syndrome-CHST14 (mcEDS-CHST14), resulting in complete depletion of the dermatan sulfate moiety of decorin glycosaminoglycan (GAG) chains, which is replaced by chondroitin sulfate.	Dermatan Sulfate	196-212	carbohydrate sulfotransferase 14	Mus musculus	29-35
32730567-6	2021	Dermatan 4 sulfotransferase 1, which transfers sulfate to the C-4 hydroxyl group of N-acetylgalactosamine of DS, contributes to neuronal differentiation of mouse neural progenitor cells.	Dermatan Sulfate	109-111	carbohydrate sulfotransferase 14	Mus musculus	0-29
32730567-9	2021	In mESCs, DS promoted neuronal differentiation by activation of extracellular signal-regulated kinase 1/2 and also accelerated neurite outgrowth.	Dermatan Sulfate	10-12	mitogen-activated protein kinase 1	Homo sapiens	64-105
32856704-4	2020	Recently, we identified and characterized the lysosomal enzyme arylsulfatase K (Arsk) exhibiting glucuronate-2-sulfatase activity as needed for the degradation of heparan sulfate (HS), chondroitin sulfate (CS) and dermatan sulfate (DS).	Dermatan Sulfate	214-230	arylsulfatase K	Mus musculus	63-78
33380731-6	2020	We found that intense removal of chondroitin sulfate (CS) and dermatan sulfate chains by chondroitinase ABC reduced the speed and decreased the strength of adhesion of HeLa cells.	Dermatan Sulfate	62-78	galactosamine (N-acetyl)-6-sulfatase	Homo sapiens	89-103
33131383-1	2020	Versican is a large chondroitin sulfate/dermatan sulfate proteoglycan belonging to the aggrecan/lectican family.	Dermatan Sulfate	40-56	versican	Homo sapiens	0-8
32710940-3	2020	Endocan is a soluble dermatan sulfate proteoglycan mainly secreted by the activated endothelium.	Dermatan Sulfate	21-37	endothelial cell specific molecule 1	Homo sapiens	0-7
33572941-2	2021	IDUA catalyzes the degradation of the glycosaminoglycans dermatan and heparan sulfate (DS and HS, respectively).	Dermatan Sulfate	57-65	alpha-L-iduronidase	Homo sapiens	0-4
33319323-1	2021	Mucopolysaccharidosis type I (MPS I) is a lysosomal storage disease caused by a mutation in the IDUA gene, which codes alpha-L-iduronidase (IDUA), a lysosomal hydrolase that degrades two glycosaminoglycans (GAGs): heparan sulfate (HS) and dermatan sulfate (DS).	Dermatan Sulfate	239-255	iduronidase, alpha-L	Mus musculus	96-100
33319323-1	2021	Mucopolysaccharidosis type I (MPS I) is a lysosomal storage disease caused by a mutation in the IDUA gene, which codes alpha-L-iduronidase (IDUA), a lysosomal hydrolase that degrades two glycosaminoglycans (GAGs): heparan sulfate (HS) and dermatan sulfate (DS).	Dermatan Sulfate	239-255	iduronidase, alpha-L	Mus musculus	140-144
33319323-1	2021	Mucopolysaccharidosis type I (MPS I) is a lysosomal storage disease caused by a mutation in the IDUA gene, which codes alpha-L-iduronidase (IDUA), a lysosomal hydrolase that degrades two glycosaminoglycans (GAGs): heparan sulfate (HS) and dermatan sulfate (DS).	Dermatan Sulfate	257-259	iduronidase, alpha-L	Mus musculus	96-100
33319323-1	2021	Mucopolysaccharidosis type I (MPS I) is a lysosomal storage disease caused by a mutation in the IDUA gene, which codes alpha-L-iduronidase (IDUA), a lysosomal hydrolase that degrades two glycosaminoglycans (GAGs): heparan sulfate (HS) and dermatan sulfate (DS).	Dermatan Sulfate	257-259	iduronidase, alpha-L	Mus musculus	140-144
33425887-2	2020	The diverse functions of CS/DS can be mainly attributed to their high structural variability.	Dermatan Sulfate	28-30	citrate synthase	Homo sapiens	25-27
33425887-4	2020	CS/DS-degrading enzymes with different specific activities are irreplaceable tools that could be used to solve this problem.	Dermatan Sulfate	3-5	citrate synthase	Homo sapiens	0-2
33425887-5	2020	Depending on the site of action, CS/DS-degrading enzymes can be classified as glycosidic bond-cleaving enzymes and sulfatases from animals and microorganisms.	Dermatan Sulfate	36-38	citrate synthase	Homo sapiens	33-35
33425887-6	2020	As discussed in this review, a few of the identified enzymes, particularly those from bacteria, have wildly applied to the basic studies and applications of CS/DS, such as disaccharide composition analysis, the preparation of bioactive oligosaccharides, oligosaccharide sequencing, and potential medical application, but these do not fulfill all of the needs in terms of the structural complexity of CS/DS.	Dermatan Sulfate	160-162	citrate synthase	Homo sapiens	157-159
33425887-6	2020	As discussed in this review, a few of the identified enzymes, particularly those from bacteria, have wildly applied to the basic studies and applications of CS/DS, such as disaccharide composition analysis, the preparation of bioactive oligosaccharides, oligosaccharide sequencing, and potential medical application, but these do not fulfill all of the needs in terms of the structural complexity of CS/DS.	Dermatan Sulfate	160-162	citrate synthase	Homo sapiens	400-402
33425887-6	2020	As discussed in this review, a few of the identified enzymes, particularly those from bacteria, have wildly applied to the basic studies and applications of CS/DS, such as disaccharide composition analysis, the preparation of bioactive oligosaccharides, oligosaccharide sequencing, and potential medical application, but these do not fulfill all of the needs in terms of the structural complexity of CS/DS.	Dermatan Sulfate	403-405	citrate synthase	Homo sapiens	157-159
33425887-6	2020	As discussed in this review, a few of the identified enzymes, particularly those from bacteria, have wildly applied to the basic studies and applications of CS/DS, such as disaccharide composition analysis, the preparation of bioactive oligosaccharides, oligosaccharide sequencing, and potential medical application, but these do not fulfill all of the needs in terms of the structural complexity of CS/DS.	Dermatan Sulfate	403-405	citrate synthase	Homo sapiens	400-402
32222457-3	2020	We have now characterized the responses and intracellular signals elicited by mechanical activation in human mast cells expressing p.C492Y-ADGRE2 and attached to dermatan sulfate, a ligand for ADGRE2.	Dermatan Sulfate	162-178	adhesion G protein-coupled receptor E2	Homo sapiens	193-199
32623553-1	2020	Hunter syndrome or mucopolysaccharidosis type II (MPS II) is an X-linked recessive disease caused by the deficiency of iduronate 2-sulfatase (IDS), leading to storage of undegraded heparan and dermatan sulfate.	Dermatan Sulfate	193-209	iduronate 2-sulfatase	Mus musculus	119-140
32623553-1	2020	Hunter syndrome or mucopolysaccharidosis type II (MPS II) is an X-linked recessive disease caused by the deficiency of iduronate 2-sulfatase (IDS), leading to storage of undegraded heparan and dermatan sulfate.	Dermatan Sulfate	193-209	iduronate 2-sulfatase	Mus musculus	142-145
32856704-4	2020	Recently, we identified and characterized the lysosomal enzyme arylsulfatase K (Arsk) exhibiting glucuronate-2-sulfatase activity as needed for the degradation of heparan sulfate (HS), chondroitin sulfate (CS) and dermatan sulfate (DS).	Dermatan Sulfate	214-230	arylsulfatase K	Mus musculus	80-84
32856704-4	2020	Recently, we identified and characterized the lysosomal enzyme arylsulfatase K (Arsk) exhibiting glucuronate-2-sulfatase activity as needed for the degradation of heparan sulfate (HS), chondroitin sulfate (CS) and dermatan sulfate (DS).	Dermatan Sulfate	232-234	arylsulfatase K	Mus musculus	63-78
32856704-4	2020	Recently, we identified and characterized the lysosomal enzyme arylsulfatase K (Arsk) exhibiting glucuronate-2-sulfatase activity as needed for the degradation of heparan sulfate (HS), chondroitin sulfate (CS) and dermatan sulfate (DS).	Dermatan Sulfate	232-234	arylsulfatase K	Mus musculus	80-84
32664626-6	2020	As shown by microarray analysis, the expression of the arylsulfatase G (ARSG) in pulmonary artery smooth muscle cells increased after silencing the arylsulfatase B gene, but the expression of genes encoding other enzymes involved in the degradation of dermatan sulfate did not.	Dermatan Sulfate	252-268	arylsulfatase G	Homo sapiens	72-76
32664626-0	2020	A Possible Role for Arylsulfatase G in Dermatan Sulfate Metabolism.	Dermatan Sulfate	39-55	arylsulfatase G	Homo sapiens	20-35
32785987-1	2020	BACKGROUND: Mucopolysaccharidosis type I (MPS-I) is a lysosomal storage disorder caused by a deficiency of the enzyme alpha-l-iduronidase, leading to accumulation of undegraded dermatan and heparan sulfates in the cells and secondary multiorgan dysfunction.	Dermatan Sulfate	177-185	alpha-L-iduronidase	Canis lupus familiaris	118-137
32664626-8	2020	Together, these results lead us to propose that arylsulfatase G can take part in DS degradation; therefore, it can affect the functioning of the cells with a silenced arylsulfatase B gene.	Dermatan Sulfate	81-83	arylsulfatase G	Homo sapiens	48-63
32664626-4	2020	The viability of pulmonary artery smooth muscle cells with a silenced ARSB gene was stimulated by the dermatan sulfate.	Dermatan Sulfate	102-118	arylsulfatase B	Homo sapiens	70-74
32664626-6	2020	As shown by microarray analysis, the expression of the arylsulfatase G (ARSG) in pulmonary artery smooth muscle cells increased after silencing the arylsulfatase B gene, but the expression of genes encoding other enzymes involved in the degradation of dermatan sulfate did not.	Dermatan Sulfate	252-268	arylsulfatase G	Homo sapiens	55-70
32664626-8	2020	Together, these results lead us to propose that arylsulfatase G can take part in DS degradation; therefore, it can affect the functioning of the cells with a silenced arylsulfatase B gene.	Dermatan Sulfate	81-83	arylsulfatase B	Homo sapiens	167-182