PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
20232353-2	2010	MPS IIID is caused by a deficiency of N-acetylglucosamine-6-sulphate sulphatase (GNS), one of the enzymes required for the degradation of heparan sulphate.	Heparitin Sulfate	138-154	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	81-84
22276697-1	2012	Graphene nanosheets (GNS) supporting Pt nanoparticles (PNs) are prepared using perfluorosulfonic acid (PFSA) as a functionalization and anchoring agent.	Graphite	0-8	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	21-24
22276697-1	2012	Graphene nanosheets (GNS) supporting Pt nanoparticles (PNs) are prepared using perfluorosulfonic acid (PFSA) as a functionalization and anchoring agent.	perfluorosulfonic acid	79-101	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	21-24
22276697-1	2012	Graphene nanosheets (GNS) supporting Pt nanoparticles (PNs) are prepared using perfluorosulfonic acid (PFSA) as a functionalization and anchoring agent.	perfluorosulfonic acid	103-107	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	21-24
21910976-2	2011	MPS III results from a deficiency in one of the four enzymes involved in the heparan sulfate degradation, with sulfamidase (SGSH), alpha-N-acetylglucosaminidase (NAGLU), acetyl-coenzyme A: alpha-glucosaminide N-acetyltransferase (HGSNAT), and N-acetylglucosamine-6-sulfatase (GNS) being deficient respectively in MPS IIIA, MPS IIIB, MPS IIIC and MPS IIID.	Heparitin Sulfate	77-92	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	243-274
19650410-1	2009	It is an autosomal recessive lysosomal disorder caused by a deficiency of the N-acetylglucosamine-6-sulphatase (GlcNAc-6S sulphatase, GNS), a hydrolase, which is one of the enzymes involved in heparan sulfate catabolism leading to lysosomal storage.	Heparitin Sulfate	193-208	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	134-137
25708886-1	2015	The twelve-membered tetraazamacrocyclic ligand L1 bears an appended lipoic acid unit, whose disulphide ring is an efficient grafting moiety for the surface of gold nanostars (GNS).	Thioctic Acid	68-79	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	175-178
12573255-1	2003	Mucopolysaccharidosis type IIID (MPS IIID; Sanfilippo syndrome type D; MIM 252940) is caused by deficiency of the activity of N-acetylglucosamine-6-sulfatase (GNS), which is normally required for degradation of heparan sulfate.	Heparitin Sulfate	211-226	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	126-157
12573255-1	2003	Mucopolysaccharidosis type IIID (MPS IIID; Sanfilippo syndrome type D; MIM 252940) is caused by deficiency of the activity of N-acetylglucosamine-6-sulfatase (GNS), which is normally required for degradation of heparan sulfate.	Heparitin Sulfate	211-226	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	159-162
3391615-1	1988	Glucosamine-6-sulphatase (G6S), a lysosomal enzyme found in all cells, is involved in the catabolism of heparin, heparan sulphate, and keratan sulphate.	Heparin	104-111	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	0-24
3391615-1	1988	Glucosamine-6-sulphatase (G6S), a lysosomal enzyme found in all cells, is involved in the catabolism of heparin, heparan sulphate, and keratan sulphate.	Heparin	104-111	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	26-29
3391615-1	1988	Glucosamine-6-sulphatase (G6S), a lysosomal enzyme found in all cells, is involved in the catabolism of heparin, heparan sulphate, and keratan sulphate.	Heparitin Sulfate	113-129	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	0-24
3391615-1	1988	Glucosamine-6-sulphatase (G6S), a lysosomal enzyme found in all cells, is involved in the catabolism of heparin, heparan sulphate, and keratan sulphate.	Heparitin Sulfate	113-129	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	26-29
3391615-1	1988	Glucosamine-6-sulphatase (G6S), a lysosomal enzyme found in all cells, is involved in the catabolism of heparin, heparan sulphate, and keratan sulphate.	Keratan Sulfate	135-151	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	0-24
3391615-1	1988	Glucosamine-6-sulphatase (G6S), a lysosomal enzyme found in all cells, is involved in the catabolism of heparin, heparan sulphate, and keratan sulphate.	Keratan Sulfate	135-151	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	26-29
3391615-3	1988	Regional mapping by in situ hybridization of a 3H-labelled human G6S cDNA probe to human metaphase chromosomes indicated that the G6S gene is localized to chromosome 12 at q14.	Tritium	47-49	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	65-68
3391615-3	1988	Regional mapping by in situ hybridization of a 3H-labelled human G6S cDNA probe to human metaphase chromosomes indicated that the G6S gene is localized to chromosome 12 at q14.	Tritium	47-49	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	130-133
30953815-2	2019	Studies have shown that BPA interferes with the development and functions of the brain, but little is known about the effects of BPA on human glutamatergic neurons (hGNs) at the molecular and cellular levels.	bisphenol A	129-132	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	165-169
30953815-3	2019	We investigated the impact of chronic exposure to BPA to hGNs derived from human embryonic stem cells (hESCs).	bisphenol A	50-53	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	57-61
30953815-4	2019	The results showed that chronic exposure of different concentrations of BPA (0, 0.1, 1.0 and 10 muM) to hGNs for 14 days reduced neurite outgrowth in a concentration-dependent manner.	bisphenol A	72-75	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	104-108
17998446-1	2007	BACKGROUND: Mucopolysaccharidosis type IIID (MPS-IIID), or Sanfilippo syndrome type D, is a rare autosomal recessive lysosomal storage disorder caused by mutations in the N-acetylglucosamine-6-sulfatase (GNS) gene, leading to impaired degradation of heparan sulfate.	Heparitin Sulfate	250-265	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	171-202
9600207-4	1998	Both forms of caprine MPS IIID result from a nonsense mutation and consequent deficiency of lysosomal N-acetylglucosamine 6-sulfatase (G6S) activity and are associated with tissue storage and urinary excretion of heparan sulfate (HS).	Heparitin Sulfate	213-228	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	135-138
9600207-4	1998	Both forms of caprine MPS IIID result from a nonsense mutation and consequent deficiency of lysosomal N-acetylglucosamine 6-sulfatase (G6S) activity and are associated with tissue storage and urinary excretion of heparan sulfate (HS).	Heparitin Sulfate	230-232	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	135-138
2500866-0	1989	Sanfilippo D syndrome: estimation of N-acetylglucosamine-6-sulfatase activity with a radiolabeled monosulfated disaccharide substrate.	Disaccharides	111-123	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	37-68
3196333-1	1988	Glucosamine-6-sulfatase is a lysosomal enzyme which degrades glycosaminoglycans and is deficient in mucopolysaccharidosis type IIID.	Glycosaminoglycans	61-79	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	0-23
26745792-2	2016	The paper reported a facile synthesis of nitrogen-doped multiple graphene aerogel/gold nanostar (termed as N-doped MGA/GNS) and its use as the electrochemical sensing platform for detection of double stranded (dsDNA).	Nitrogen	41-49	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	119-122
26745792-2	2016	The paper reported a facile synthesis of nitrogen-doped multiple graphene aerogel/gold nanostar (termed as N-doped MGA/GNS) and its use as the electrochemical sensing platform for detection of double stranded (dsDNA).	Graphite	65-73	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	119-122
26745792-5	2016	On the other hand, the hybridization with GNS further enhances the electrocatalytic activity towards Fe(CN)6(3-/4-).	fe(cn)6	101-108	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	42-45
26016687-1	2015	In this study, a facile one-pot process for the synthesis of hierarchical VS2/graphene nanosheets (VS2/GNS) composites based on the coincident interaction of VS2 and reduced graphene oxide (rGO) sheets in the presence of cetyltrimethylammonium bromide is developed for the first time.	Graphite	78-86	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	99-106
26016687-1	2015	In this study, a facile one-pot process for the synthesis of hierarchical VS2/graphene nanosheets (VS2/GNS) composites based on the coincident interaction of VS2 and reduced graphene oxide (rGO) sheets in the presence of cetyltrimethylammonium bromide is developed for the first time.	graphene oxide	174-188	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	99-106
26016687-1	2015	In this study, a facile one-pot process for the synthesis of hierarchical VS2/graphene nanosheets (VS2/GNS) composites based on the coincident interaction of VS2 and reduced graphene oxide (rGO) sheets in the presence of cetyltrimethylammonium bromide is developed for the first time.	Cetrimonium	221-251	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	99-106
26016687-5	2015	The excellent electrochemical performance of the composites for reversible Li+ storage should be attributed to the exceptional interaction between VS2 and GNS that enabled fast electron transport between graphene and VS2, facile Li-ion diffusion within the electrode.	Graphite	204-212	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	155-158
26016687-7	2015	The VS2/GNS composites may be promising electrode materials for the next generation of rechargeable lithium ion batteries.	Lithium	100-107	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	8-11
25708886-1	2015	The twelve-membered tetraazamacrocyclic ligand L1 bears an appended lipoic acid unit, whose disulphide ring is an efficient grafting moiety for the surface of gold nanostars (GNS).	disulphide	92-102	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	175-178
25708886-7	2015	500-1500 [CuL1](2+) per GNS depending on the conditions, with PEG-SH remaining in the [Cun(L1@GNS)](2n+) hybrids and imparting them with remarkable stability.	peg-sh	62-68	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	24-27
25708886-8	2015	Comparison of the photothermal and two-photon luminescence (TPL) properties of the GNS between the pegylated GNS and [Cun(L1@GNS)](2n+) revealed that the grafted copper complex does not change them to any extent.	Copper	162-168	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	83-86
25708886-8	2015	Comparison of the photothermal and two-photon luminescence (TPL) properties of the GNS between the pegylated GNS and [Cun(L1@GNS)](2n+) revealed that the grafted copper complex does not change them to any extent.	Copper	162-168	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	109-112
23954926-1	2013	Herein, graphene nanosheets (GNS) were synthesized, by a green and facile method based on reduction by glucose, and characterized.	Graphite	8-16	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	29-32
23954926-1	2013	Herein, graphene nanosheets (GNS) were synthesized, by a green and facile method based on reduction by glucose, and characterized.	Glucose	103-110	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	29-32
23954926-2	2013	Afterwards, a carbon paste electrode (CPE) was modified with GNS by casting and drying GNS on top of the CPE (CPE/GNS).	Carbon	14-20	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	61-64
23954926-2	2013	Afterwards, a carbon paste electrode (CPE) was modified with GNS by casting and drying GNS on top of the CPE (CPE/GNS).	Carbon	14-20	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	87-90
23374371-0	2013	Neutralizing the anticoagulant activity of ultra-low-molecular-weight heparins using N-acetylglucosamine 6-sulfatase.	Heparin	70-78	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	85-116
23374371-7	2013	NG6S removes a single 6-O-sulfo group at the non-reducing end of the ULMWH Arixtra( ) (fondaparinux), effectively removing its ability to bind to antithrombin and preventing its inhibition of coagulation factor Xa.	Fondaparinux	75-82	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	0-4