PMID-sentid Pub_year Sent_text comp_official_name comp_offset protein_name organism prot_offset 15058963-2 2004 This large molecular "mesh" encases the entire cytoplasm of bacteria, and it is comprised of repeating backbone units of N-acetyl-glucosamine (NAG)-N-acetyl-muramic acid (NAM). N-acetylmuramic acid 148-169 N-acetyl-alpha-glucosaminidase Homo sapiens 121-141 15301246-2 2004 N-acetyl-3-D-glucosaminidase (NAG) activity in urine served as an indicator of proximal tubular damage METHODS: NAG activity was estimated in 21 patients during the course of treatment with infliximab and methotrexate. Methotrexate 205-217 N-acetyl-alpha-glucosaminidase Homo sapiens 0-28 15041069-3 2004 Of 397, 20 subjects (5%) excreted urine Cd between 1.4 microg/g and 3.8 microg/g creatinine and these subjects faced 10-15% increase in the probability of having abnormal urinary excretion of N-acetyl-beta-D-glucosaminidase (NAG-uria). Cadmium 40-42 N-acetyl-alpha-glucosaminidase Homo sapiens 225-228 15041069-4 2004 The prevalence of NAG-uria varied with Cd body burden in a dose-dependent manner (chi2 = 22, P < 0.008). Cadmium 39-41 N-acetyl-alpha-glucosaminidase Homo sapiens 18-21 15041069-5 2004 Also NAG-nuria was one of the three kidney effect markers tested that showed the greatest strength of correlation with urine Cd in both men and women (r = 0.48, P < 0.001). Cadmium 125-127 N-acetyl-alpha-glucosaminidase Homo sapiens 5-8 15714518-1 2005 N-acetylglutamate (NAG) is a unique cofactor that is essential for the conversion of ammonia to urea in the liver. N-acetylglutamic acid 0-17 N-acetyl-alpha-glucosaminidase Homo sapiens 19-22 15714518-1 2005 N-acetylglutamate (NAG) is a unique cofactor that is essential for the conversion of ammonia to urea in the liver. Ammonia 85-92 N-acetyl-alpha-glucosaminidase Homo sapiens 19-22 15714518-1 2005 N-acetylglutamate (NAG) is a unique cofactor that is essential for the conversion of ammonia to urea in the liver. Urea 96-100 N-acetyl-alpha-glucosaminidase Homo sapiens 19-22 15599770-6 2005 NAG/Cr levels correlated with erythrocyte sedimentation rate (r=0.66, P<0.001) and platelet count (r=0.61, P<0.001) and showed a slight correlation with the number of joints with active arthritis in children with polyarticular JIA (r=0.45, P=0.055). Creatinine 4-6 N-acetyl-alpha-glucosaminidase Homo sapiens 0-3 15626645-8 2005 Next, in models of renal function in all workers, uric acid was significantly (p < 0.05) associated with all renal outcomes except NAG. Uric Acid 50-59 N-acetyl-alpha-glucosaminidase Homo sapiens 134-137 15050968-2 2004 2.3.1.1) is a mitochondrial enzyme that catalyzes the formation of N-acetylglutamate (NAG), an essential allosteric activator of carbamylphosphate synthetase I (CPSI). N-acetylglutamic acid 67-84 N-acetyl-alpha-glucosaminidase Homo sapiens 86-89 15050968-10 2004 A structural analog of NAG, carbamylglutamate, has been shown to bind and activate CPSI, and several patients have been reported to respond favorably to this drug (Carbaglu). N-carbamylglutamate 28-45 N-acetyl-alpha-glucosaminidase Homo sapiens 23-26 15050968-10 2004 A structural analog of NAG, carbamylglutamate, has been shown to bind and activate CPSI, and several patients have been reported to respond favorably to this drug (Carbaglu). carglumic acid 164-172 N-acetyl-alpha-glucosaminidase Homo sapiens 23-26 15058963-2 2004 This large molecular "mesh" encases the entire cytoplasm of bacteria, and it is comprised of repeating backbone units of N-acetyl-glucosamine (NAG)-N-acetyl-muramic acid (NAM). N-acetylmuramic acid 148-169 N-acetyl-alpha-glucosaminidase Homo sapiens 143-146 15058963-5 2004 In the present paper, we have devised a synthetic route for the preparation of a fragment of the cell wall comprised of a tetrasaccharide (NAG-NAM-NAG-NAM), along with the two appended peptides. tetrasaccharide 122-137 N-acetyl-alpha-glucosaminidase Homo sapiens 139-142 15058963-5 2004 In the present paper, we have devised a synthetic route for the preparation of a fragment of the cell wall comprised of a tetrasaccharide (NAG-NAM-NAG-NAM), along with the two appended peptides. tetrasaccharide 122-137 N-acetyl-alpha-glucosaminidase Homo sapiens 147-150 12875848-0 2003 The course of phosphorus in the reaction of N-acetyl-L-glutamate kinase, determined from the structures of crystalline complexes, including a complex with an AlF(4)(-) transition state mimic. Phosphorus 14-24 N-acetyl-alpha-glucosaminidase Homo sapiens 44-64 14582958-8 2003 The limit of detection was 17 mug/L NAG in water for the direct competitive enzyme immunoassay. Water 43-48 N-acetyl-alpha-glucosaminidase Homo sapiens 36-39 14582958-9 2003 NAG is also a main metabolite of glufosinate in resistant transgenic plants. phosphinothricin 33-44 N-acetyl-alpha-glucosaminidase Homo sapiens 0-3 14582958-10 2003 The antibodies might be useful for the selective detection of NAG in the presence of the parent compound glufosinate (cross-reactivity 0.13%) and other metabolites. phosphinothricin 105-116 N-acetyl-alpha-glucosaminidase Homo sapiens 62-65 14976384-0 2004 Synergistic effect of N-acetylglucosamine and retinoids on hyaluronan production in human keratinocytes. Hyaluronic Acid 59-69 N-acetyl-alpha-glucosaminidase Homo sapiens 22-41 14976384-5 2004 The copresence of NAG with either of two retinoids, retinoic acid (RA) or retinol, exerted a synergistic effect on HA production. Retinoids 41-50 N-acetyl-alpha-glucosaminidase Homo sapiens 18-21 14976384-5 2004 The copresence of NAG with either of two retinoids, retinoic acid (RA) or retinol, exerted a synergistic effect on HA production. Tretinoin 52-65 N-acetyl-alpha-glucosaminidase Homo sapiens 18-21 14976384-5 2004 The copresence of NAG with either of two retinoids, retinoic acid (RA) or retinol, exerted a synergistic effect on HA production. Tretinoin 67-69 N-acetyl-alpha-glucosaminidase Homo sapiens 18-21 14976384-5 2004 The copresence of NAG with either of two retinoids, retinoic acid (RA) or retinol, exerted a synergistic effect on HA production. Vitamin A 74-81 N-acetyl-alpha-glucosaminidase Homo sapiens 18-21 15116821-5 2004 RESULTS: N-acetyl-beta-D-glucosaminidase indexed to urinary creatinine (U-NAG/crea), a sensitive marker of renal proximal tubular damage, increased similarly in both groups at the end of surgery (two-way ANOVA, p < 0.05). Creatinine 60-70 N-acetyl-alpha-glucosaminidase Homo sapiens 74-77 15116821-5 2004 RESULTS: N-acetyl-beta-D-glucosaminidase indexed to urinary creatinine (U-NAG/crea), a sensitive marker of renal proximal tubular damage, increased similarly in both groups at the end of surgery (two-way ANOVA, p < 0.05). crea 60-64 N-acetyl-alpha-glucosaminidase Homo sapiens 74-77 12875848-1 2003 N-Acetyl-L-glutamate kinase (NAGK), the structural paradigm of the enzymes of the amino acid kinase family, catalyzes the phosphorylation of the gamma-COO(-) group of N-acetyl-L-glutamate (NAG) by ATP. Adenosine Triphosphate 197-200 N-acetyl-alpha-glucosaminidase Homo sapiens 167-187 12875848-1 2003 N-Acetyl-L-glutamate kinase (NAGK), the structural paradigm of the enzymes of the amino acid kinase family, catalyzes the phosphorylation of the gamma-COO(-) group of N-acetyl-L-glutamate (NAG) by ATP. Adenosine Triphosphate 197-200 N-acetyl-alpha-glucosaminidase Homo sapiens 29-32 12875848-2 2003 We determine here the crystal structures of NAGK complexes with MgADP, NAG and the transition-state analog AlF(4)(-); with MgADP and NAG; and with ADP and SO(4)(2-). Adenosine Diphosphate 64-69 N-acetyl-alpha-glucosaminidase Homo sapiens 44-47 12875848-2 2003 We determine here the crystal structures of NAGK complexes with MgADP, NAG and the transition-state analog AlF(4)(-); with MgADP and NAG; and with ADP and SO(4)(2-). Adenosine Diphosphate 123-128 N-acetyl-alpha-glucosaminidase Homo sapiens 44-47 12875848-2 2003 We determine here the crystal structures of NAGK complexes with MgADP, NAG and the transition-state analog AlF(4)(-); with MgADP and NAG; and with ADP and SO(4)(2-). Adenosine Diphosphate 66-69 N-acetyl-alpha-glucosaminidase Homo sapiens 44-47 12875848-3 2003 Comparison of these structures with that of the MgAMPPNP-NAG complex allows to delineate three successive steps during phosphoryl transfer: at the beginning, when the attacking and leaving O atoms and the P atom are imperfectly aligned and the distance between the attacking O atom and the P atom is 2.8A; midway, at the bipyramidal intermediate, with nearly perfect alignment and a distance of 2.3A; and, when the transfer is completed. Adenylyl Imidodiphosphate 48-56 N-acetyl-alpha-glucosaminidase Homo sapiens 57-60 12049639-9 2002 The enzyme secreted by transduced MPS IIIB fibroblasts was endocytosed in deficient cells by the mannose 6-phosphate system. mannose-6-phosphate 97-116 N-acetyl-alpha-glucosaminidase Homo sapiens 34-42 15315013-11 2003 The urinary excretion of NAG and alpha-1M was estimated in the second morning portion of urine and it was presented as NAG/creatinine and alpha-1M/creatinine ratio. Creatinine 123-133 N-acetyl-alpha-glucosaminidase Homo sapiens 25-28 15315013-11 2003 The urinary excretion of NAG and alpha-1M was estimated in the second morning portion of urine and it was presented as NAG/creatinine and alpha-1M/creatinine ratio. Creatinine 147-157 N-acetyl-alpha-glucosaminidase Homo sapiens 25-28 12459178-2 2002 2.3.1.1) is a mitochondrial enzyme catalyzing the formation of N-acetylglutamate (NAG), an essential allosteric activator of carbamylphosphate synthase I (CPSI), the first enzyme of the urea cycle. N-acetylglutamic acid 63-80 N-acetyl-alpha-glucosaminidase Homo sapiens 82-85 12459178-2 2002 2.3.1.1) is a mitochondrial enzyme catalyzing the formation of N-acetylglutamate (NAG), an essential allosteric activator of carbamylphosphate synthase I (CPSI), the first enzyme of the urea cycle. Urea 186-190 N-acetyl-alpha-glucosaminidase Homo sapiens 82-85 12406749-1 2002 Dissolved free and combined N-acetyl-D-glucosamine (NAG) is among the largest pools of amino sugars in the ocean. Amino Sugars 87-99 N-acetyl-alpha-glucosaminidase Homo sapiens 52-55 12406749-3 2002 We studied the distribution and kinetics of NAG uptake by the phosphoenolpyruvate:NAG phosphotransferase systems (PTS) in marine bacterial isolates and natural bacterial assemblages in near-shore waters. Phosphoenolpyruvate 62-81 N-acetyl-alpha-glucosaminidase Homo sapiens 44-47 12406749-8 2002 Carbohydrate competition experiments indicated that glucose, glucosamine, mannose, and fructose were taken up by the same system as NAG. Carbohydrates 0-12 N-acetyl-alpha-glucosaminidase Homo sapiens 132-135 12406749-8 2002 Carbohydrate competition experiments indicated that glucose, glucosamine, mannose, and fructose were taken up by the same system as NAG. Glucose 52-59 N-acetyl-alpha-glucosaminidase Homo sapiens 132-135 12406749-8 2002 Carbohydrate competition experiments indicated that glucose, glucosamine, mannose, and fructose were taken up by the same system as NAG. Glucosamine 61-72 N-acetyl-alpha-glucosaminidase Homo sapiens 132-135 12406749-8 2002 Carbohydrate competition experiments indicated that glucose, glucosamine, mannose, and fructose were taken up by the same system as NAG. Mannose 74-81 N-acetyl-alpha-glucosaminidase Homo sapiens 132-135 12406749-8 2002 Carbohydrate competition experiments indicated that glucose, glucosamine, mannose, and fructose were taken up by the same system as NAG. Fructose 87-95 N-acetyl-alpha-glucosaminidase Homo sapiens 132-135 12406749-9 2002 Sensitivity to the antibiotic and NAG structural analog streptozotocin (STZ) was developed into a culture-independent approach, which demonstrated that approximately one-third of bacteria in natural marine assemblages that were synthesizing DNA took up NAG. Streptozocin 56-70 N-acetyl-alpha-glucosaminidase Homo sapiens 34-37 12406749-9 2002 Sensitivity to the antibiotic and NAG structural analog streptozotocin (STZ) was developed into a culture-independent approach, which demonstrated that approximately one-third of bacteria in natural marine assemblages that were synthesizing DNA took up NAG. Streptozocin 56-70 N-acetyl-alpha-glucosaminidase Homo sapiens 253-256 12406749-9 2002 Sensitivity to the antibiotic and NAG structural analog streptozotocin (STZ) was developed into a culture-independent approach, which demonstrated that approximately one-third of bacteria in natural marine assemblages that were synthesizing DNA took up NAG. Streptozocin 72-75 N-acetyl-alpha-glucosaminidase Homo sapiens 34-37 12406749-9 2002 Sensitivity to the antibiotic and NAG structural analog streptozotocin (STZ) was developed into a culture-independent approach, which demonstrated that approximately one-third of bacteria in natural marine assemblages that were synthesizing DNA took up NAG. Streptozocin 72-75 N-acetyl-alpha-glucosaminidase Homo sapiens 253-256 12458807-5 2002 In patients with recently diagnosed FMF, a marked decrease in U-NAG, U-beta2M and Ua were determined after three months on colchicine therapy. Colchicine 123-133 N-acetyl-alpha-glucosaminidase Homo sapiens 64-67 12058031-1 2002 N-Acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase, also known as "uncovering" enzyme (UCE), is localized in the trans-Golgi network, where it removes a covering N-acetylglucosamine from the mannose 6-phosphate recognition marker on lysosomal acid hydrolases. Acetylglucosamine 178-197 N-acetyl-alpha-glucosaminidase Homo sapiens 37-66 12058031-1 2002 N-Acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase, also known as "uncovering" enzyme (UCE), is localized in the trans-Golgi network, where it removes a covering N-acetylglucosamine from the mannose 6-phosphate recognition marker on lysosomal acid hydrolases. mannose-6-phosphate 207-226 N-acetyl-alpha-glucosaminidase Homo sapiens 37-66 14653309-0 2002 Change in the iso-enzyme profiles of urinary N-acetyl-beta-D-glucosoaminidase in workers exposed to mercury. Mercury 100-107 N-acetyl-alpha-glucosaminidase Homo sapiens 45-77 14653309-1 2002 The iso-enzyme profiles of urinary N-acetyl-beta-D-glucosoaminidase (NAG) were studied in the workers from a chloro-alkaline electrolysis plant that had been continuously exposed to elemental mercury. Mercury 182-199 N-acetyl-alpha-glucosaminidase Homo sapiens 35-67 14653309-1 2002 The iso-enzyme profiles of urinary N-acetyl-beta-D-glucosoaminidase (NAG) were studied in the workers from a chloro-alkaline electrolysis plant that had been continuously exposed to elemental mercury. Mercury 182-199 N-acetyl-alpha-glucosaminidase Homo sapiens 69-72 14653309-3 2002 The activities of urinary NAG in workers exposed to mercury before and after the work break and in the control group were 2.09 +/- 1.03 IU/L; 0.90 +/- 0.52 IU/L and 1.13 +/- 0.35 IU/L, respectively. Mercury 52-59 N-acetyl-alpha-glucosaminidase Homo sapiens 26-29 14653309-10 2002 It is concluded that mercury affected the increased exocytosis of iso-enzyme A and the inhibition of B iso-enzyme of NAG. Mercury 21-28 N-acetyl-alpha-glucosaminidase Homo sapiens 117-120 14653309-11 2002 The increase in activity of urinary NAG in subjects exposed to mercury was a consequence of the increased excretion of A form. Mercury 63-70 N-acetyl-alpha-glucosaminidase Homo sapiens 36-39 14694604-4 2002 Compared with TPA, DOW and control groups, the values of urine N-acetyl-beta-D-glucosaminidase(NAG) and beta 2-2-microglobulim (beta 2-MG) in TPA + EG + DOW group of both men and women increased significantly(P < 0.05, P < 0.01), with(5.68 +/- 4.01) U/mmol Cr and (23.49 +/- 13.44) mg/mol Cr, and(6.68 +/- 4.68) U/mmol Cr and (22.80 +/- 13.00) mg/mol Cr, respectively. terephthalic acid 142-145 N-acetyl-alpha-glucosaminidase Homo sapiens 95-98 11869929-8 2002 Urinary NAG (U/gr creatinine) (4.71 +/- 2.11) was lower than the battery workers (7.39 +/- 4.37), however significantly higher than the normal control group (3.07 +/- 1.20). Creatinine 18-28 N-acetyl-alpha-glucosaminidase Homo sapiens 8-11 11793481-1 2002 MPS III results from a deficiency in one of the four enzymes involved in the degradation of heparan sulfate, with sulfamidase (SGSH) being deficient in MPS IIIA and a-N-acetylglucosaminidase (NAGLU) deficient in MPS IIIB. Heparitin Sulfate 92-107 N-acetyl-alpha-glucosaminidase Homo sapiens 165-190 11763992-8 2001 Serum creatinine transiently decreased rather than increased 14 days after cisplatin and furosemide administration, while NAG excretion increased 3 days after cisplatin and furosemide administration. Furosemide 173-183 N-acetyl-alpha-glucosaminidase Homo sapiens 122-125 11921700-5 2002 Urinary NAG excretion levels of IGT group and control group were 2.89 (1.23-7.97) and 2.22 (0.60-4.93) U/g creatinine, median (range), respectively. Creatinine 107-117 N-acetyl-alpha-glucosaminidase Homo sapiens 8-11 11838319-12 2001 When the urine NAG level becomes high in a patient taking lithium for bipolar disorder, the physician may need to consider lithium-induced renal insufficiency. Lithium 58-65 N-acetyl-alpha-glucosaminidase Homo sapiens 15-18 11838319-12 2001 When the urine NAG level becomes high in a patient taking lithium for bipolar disorder, the physician may need to consider lithium-induced renal insufficiency. Lithium 123-130 N-acetyl-alpha-glucosaminidase Homo sapiens 15-18 11763992-11 2001 Moreover, the first course morning cisplatin and furosemide treatment was associated with less change in NAG excretion (less kidney toxicity) than the first course of evening cisplatin and furosemide treatment. Cisplatin 35-44 N-acetyl-alpha-glucosaminidase Homo sapiens 105-108 11763992-11 2001 Moreover, the first course morning cisplatin and furosemide treatment was associated with less change in NAG excretion (less kidney toxicity) than the first course of evening cisplatin and furosemide treatment. Furosemide 49-59 N-acetyl-alpha-glucosaminidase Homo sapiens 105-108 11763992-12 2001 The second course evening cisplatin and furosemide treatment was associated with an increase in NAG excretion compared to the first course of treatment, while morning cisplatin and furosemide treatment in the second course showed less change in NAG excretion compared to the first course. Cisplatin 26-35 N-acetyl-alpha-glucosaminidase Homo sapiens 96-99 11763992-12 2001 The second course evening cisplatin and furosemide treatment was associated with an increase in NAG excretion compared to the first course of treatment, while morning cisplatin and furosemide treatment in the second course showed less change in NAG excretion compared to the first course. Furosemide 40-50 N-acetyl-alpha-glucosaminidase Homo sapiens 96-99 11763992-12 2001 The second course evening cisplatin and furosemide treatment was associated with an increase in NAG excretion compared to the first course of treatment, while morning cisplatin and furosemide treatment in the second course showed less change in NAG excretion compared to the first course. Furosemide 181-191 N-acetyl-alpha-glucosaminidase Homo sapiens 245-248 9754859-10 1998 A dose-response relation was observed between cumulative toluene exposure and both IgE and NAG excretion. Toluene 57-64 N-acetyl-alpha-glucosaminidase Homo sapiens 91-94 11730274-8 2001 All patients demonstrated significant tubular injury but urinary levels of NAG and RBP were lower in the dopamine group (41%, p=0.057 and 41%, p=0.007, respectively) on the first post-operative day. Dopamine 105-113 N-acetyl-alpha-glucosaminidase Homo sapiens 75-78 11103842-5 2000 The activity of N-acetyl-beta-D-glucosaminidase in urine (U-NAG) was higher in the exposed workers (mean 0.18 U/mmol Cr versus 0.14 U/mmol Cr, P=0.02). Creatinine 117-119 N-acetyl-alpha-glucosaminidase Homo sapiens 60-63 11103842-8 2000 The highest activity of U-NAG was observed in the exposed workers with the lower concentrations of selenium in whole blood. Selenium 99-107 N-acetyl-alpha-glucosaminidase Homo sapiens 26-29 10833408-9 2000 This contrasts with the presence of mannose 6-phosphate on naturally occurring alpha-N-acetylglucosaminidase secreted by diploid human fibroblasts and on recombinant human alpha-l-iduronidase secreted by the same CHO cells. mannose-6-phosphate 36-55 N-acetyl-alpha-glucosaminidase Homo sapiens 79-108 9852385-3 1999 Multiple regression analysis confirmed that the significant independent determinants of NAG/creatinine ratio were age, parity, gestation and fasting state. Creatinine 92-102 N-acetyl-alpha-glucosaminidase Homo sapiens 88-91 9852385-5 1999 The urinary NAG/Cr ratio is influenced by fasting, parity, gestation and age. Chromium 16-18 N-acetyl-alpha-glucosaminidase Homo sapiens 12-15 9832037-1 1998 Sanfilippo syndrome type B or mucopolysaccharidosis type IIIB (MPS IIIB) is one of a group of lysosomal storage disorders that are characterised by the inability to breakdown heparan sulphate. Heparitin Sulfate 175-191 N-acetyl-alpha-glucosaminidase Homo sapiens 30-61 9832037-1 1998 Sanfilippo syndrome type B or mucopolysaccharidosis type IIIB (MPS IIIB) is one of a group of lysosomal storage disorders that are characterised by the inability to breakdown heparan sulphate. Heparitin Sulfate 175-191 N-acetyl-alpha-glucosaminidase Homo sapiens 63-71 11153910-1 2000 Sanfilippo syndrome type B (mucopolysaccharidosis IIIB) is a rare autosomal recessive disorder characterized by the inability to degrade heparan sulfate because of a deficiency of the lysosomal enzyme alpha-N-acetylglucosaminidase (NAGLU). Heparitin Sulfate 137-152 N-acetyl-alpha-glucosaminidase Homo sapiens 201-230 11068184-1 2000 Mucopolysaccharidosis type IIIB (MPS-IIB) is a lysosomal storage disorder characterised by the defective degradation of heparan sulfate due to a deficiency of alpha-N-acetylglucosaminidase (NAG). Heparitin Sulfate 120-135 N-acetyl-alpha-glucosaminidase Homo sapiens 159-188 10758174-5 2000 Single channel conductances to Na(+) (g(Na)) or Cs(+) (g(Cs)) in the SS dimer were smaller than in natural gA. Cesium 57-59 N-acetyl-alpha-glucosaminidase Homo sapiens 31-43 10094189-1 1999 Sanfilippo B syndrome (mucopolysaccharidosis IIIB, MPS IIIB) is caused by a deficiency of alpha-N-acetylglucosaminidase, a lysosomal enzyme involved in the degradation of heparan sulphate. Heparitin Sulfate 171-187 N-acetyl-alpha-glucosaminidase Homo sapiens 51-59 10094189-1 1999 Sanfilippo B syndrome (mucopolysaccharidosis IIIB, MPS IIIB) is caused by a deficiency of alpha-N-acetylglucosaminidase, a lysosomal enzyme involved in the degradation of heparan sulphate. Heparitin Sulfate 171-187 N-acetyl-alpha-glucosaminidase Homo sapiens 90-119 12080715-8 1999 Pre- and post-oral intake of the salt with high dose KI, Hb, ZPP, delta-ALA, PbB, NAG and Rp the people mentioned above had the following indexes, (101.2 and 128) g.L-1 (P = 0.05), (33.5 and 7.7) micrograms.g-1 Hb(P < 0.01), (123.12 and 65.35) mumol.L-1 (P < 0.05), (2.123 and 0.85) mumol.L-1 (P < 0.01), (20.9 and 6.7) U.L-1 (P < 0.01), (1.5 and 0.34) mg.L-1 (P < 0.05) respectively. Salts 33-37 N-acetyl-alpha-glucosaminidase Homo sapiens 82-85 9675717-0 1998 Urinary NAG and GAG as biomarkers of renal effects in exposure to 2-alkoxyalcohols and their acetates. 2-alkoxyalcohols 66-82 N-acetyl-alpha-glucosaminidase Homo sapiens 8-11 9675717-0 1998 Urinary NAG and GAG as biomarkers of renal effects in exposure to 2-alkoxyalcohols and their acetates. Acetates 93-101 N-acetyl-alpha-glucosaminidase Homo sapiens 8-11 8973472-3 1996 The heparan sulfates from patients with Sanfilippo A (deficient in heparan N-sulfatase) and Sanfilippo B (deficient in alpha-N-acetylglucosaminidase) were degraded with heparitinase II producing, besides unsaturated disaccharides, substantial amounts of glucosamine N-sulfate and N-acetylglucosamine, respectively. glucosamine 2-sulfate 254-275 N-acetyl-alpha-glucosaminidase Homo sapiens 119-148 9743814-13 1998 In synovial fluid of patients requiring joint aspiration, treated orally for 10 days with CS (800 mg/day) the hyaluronate concentration and the intrinsic viscosity significantly increased, while collagenolytic activity, phospholipase A2 and N-acetylglucosaminidase (NAG) decreased. Chondroitin Sulfates 90-92 N-acetyl-alpha-glucosaminidase Homo sapiens 241-264 9743814-13 1998 In synovial fluid of patients requiring joint aspiration, treated orally for 10 days with CS (800 mg/day) the hyaluronate concentration and the intrinsic viscosity significantly increased, while collagenolytic activity, phospholipase A2 and N-acetylglucosaminidase (NAG) decreased. Chondroitin Sulfates 90-92 N-acetyl-alpha-glucosaminidase Homo sapiens 266-269 9571353-0 1998 Relationship between serum 1,5-anhydroglucitol and urinary excretion of N-acetylglucosaminidase and albumin determined at onset of NIDDM with 3-year follow-up. 1,5-anhydroglucitol 27-46 N-acetyl-alpha-glucosaminidase Homo sapiens 72-95 9571353-6 1998 The abnormal excretion of NAG and albumin was associated with a change in serum 1,5AG and was quickly reversible when the serum 1,5AG improved. 1,5-anhydroglucitol 80-85 N-acetyl-alpha-glucosaminidase Homo sapiens 26-29 9571353-6 1998 The abnormal excretion of NAG and albumin was associated with a change in serum 1,5AG and was quickly reversible when the serum 1,5AG improved. 1,5-anhydroglucitol 128-133 N-acetyl-alpha-glucosaminidase Homo sapiens 26-29 9571353-8 1998 Urinary NAG was found to be significantly correlated with the fasting plasma level of glucose (FPG; r = 0.512, P < 0.0001), the level of HbA1 (r = 0.351, P = 0.001), and the level of 1,5AG (r = -0.790, P < 0.0001). Glucose 86-93 N-acetyl-alpha-glucosaminidase Homo sapiens 8-11 9443878-0 1998 NAGLU mutations underlying Sanfilippo syndrome type B. Sanfilippo syndrome type B (mucopolysaccharidosis III B) is a rare autosomal recessive disease caused by deficiency of alpha-N-acetylglucosaminidase, one of the enzymes required for the lysosomal degradation of heparan sulfate. Heparitin Sulfate 266-281 N-acetyl-alpha-glucosaminidase Homo sapiens 0-5 9443878-0 1998 NAGLU mutations underlying Sanfilippo syndrome type B. Sanfilippo syndrome type B (mucopolysaccharidosis III B) is a rare autosomal recessive disease caused by deficiency of alpha-N-acetylglucosaminidase, one of the enzymes required for the lysosomal degradation of heparan sulfate. Heparitin Sulfate 266-281 N-acetyl-alpha-glucosaminidase Homo sapiens 174-203 9696344-6 1998 Separation of the NAG isoenzymes by column ion-exchange chromatography on the DEAE-52 cellulose as well as by electrophoresis in 7% polyacrylamide gel confirms the diagnostic value of this enzyme due to the ability of indicating the site of renal damage. deae-52 cellulose 78-95 N-acetyl-alpha-glucosaminidase Homo sapiens 18-21 9696344-6 1998 Separation of the NAG isoenzymes by column ion-exchange chromatography on the DEAE-52 cellulose as well as by electrophoresis in 7% polyacrylamide gel confirms the diagnostic value of this enzyme due to the ability of indicating the site of renal damage. polyacrylamide 132-146 N-acetyl-alpha-glucosaminidase Homo sapiens 18-21 9279185-4 1997 Increased NAG values reflect the degree of perinatal asphyxia more than do beta 2 M. Gentamicin also increased NAG excretion, but to a lesser extent than did perinatal asphyxia. Gentamicins 85-95 N-acetyl-alpha-glucosaminidase Homo sapiens 111-114 8973472-3 1996 The heparan sulfates from patients with Sanfilippo A (deficient in heparan N-sulfatase) and Sanfilippo B (deficient in alpha-N-acetylglucosaminidase) were degraded with heparitinase II producing, besides unsaturated disaccharides, substantial amounts of glucosamine N-sulfate and N-acetylglucosamine, respectively. Heparitin Sulfate 4-20 N-acetyl-alpha-glucosaminidase Homo sapiens 119-148 10649686-0 1998 The effect of N-acetylglucosamine as a substrate for in vitro synthesis of glycosaminoglycans by human peritoneal mesothelial cells and fibroblasts. Glycosaminoglycans 75-93 N-acetyl-alpha-glucosaminidase Homo sapiens 14-33 10649686-2 1998 In contrast to isosmotic concentrations of glucose, NAG increases the synthesis of hyaluronan by mesothelial cells and fibroblasts in a dose-dependent manner. Hyaluronic Acid 83-93 N-acetyl-alpha-glucosaminidase Homo sapiens 52-55 10649686-3 1998 This effect of NAG can be demonstrated in the presence of increased glucose levels in a medium, or in a medium mixed with effluent dialysate obtained from continuous ambulatory peritoneal dialysis (CAPD) patients. Glucose 68-75 N-acetyl-alpha-glucosaminidase Homo sapiens 15-18 10649686-5 1998 Our results demonstrate that NAG is an effective stimulator of the in vitro glycosaminoglycans synthesis by human peritoneal mesothelial cells and fibroblasts. Glycosaminoglycans 76-94 N-acetyl-alpha-glucosaminidase Homo sapiens 29-32 9235547-9 1997 In the course of the 6-months enalapril therapy of hypertension, NAG activity in urine in the group II was declined to normal values, the creatinine concentration in the urine increased in groups I and II, and the blood pressure was significantly reduced. Enalapril 30-39 N-acetyl-alpha-glucosaminidase Homo sapiens 65-68 9235547-10 1997 The results of our study imply that the monitoring of the NAG activity in urine during the enalapril therapy of hypertension, may to be a indicator of protective action of the drug on the kidney and its antihypertensive efficacy. Enalapril 91-100 N-acetyl-alpha-glucosaminidase Homo sapiens 58-61 8973472-3 1996 The heparan sulfates from patients with Sanfilippo A (deficient in heparan N-sulfatase) and Sanfilippo B (deficient in alpha-N-acetylglucosaminidase) were degraded with heparitinase II producing, besides unsaturated disaccharides, substantial amounts of glucosamine N-sulfate and N-acetylglucosamine, respectively. Acetylglucosamine 280-299 N-acetyl-alpha-glucosaminidase Homo sapiens 119-148 8948524-6 1996 Following gentamicin treatment, increased NAG, AAP, and GGT enzymuria were noted at all time points tested. Gentamicins 10-20 N-acetyl-alpha-glucosaminidase Homo sapiens 42-45 8776591-1 1996 Sanfilippo B syndrome is caused by a deficiency of alpha-N-acetylglucosaminidase, a lysosomal enzyme involved in the degradation of heparan sulphate. Heparitin Sulfate 132-148 N-acetyl-alpha-glucosaminidase Homo sapiens 51-80 7669872-1 1995 Plasma glucose, glycated hemoglobin lc (HbAlc), urinary albumin excretion rate (AER) and urinary N-acetyl-glucosaminidase (NAG): creatinine ratio were studied in 100 normotensive diabetic patients with no evidence of overt renal disease and in 45 controls, to find out whether the glycaemic control and incipient nephropathy may influence the urinary excretion of NAG. Creatinine 129-139 N-acetyl-alpha-glucosaminidase Homo sapiens 123-126 8527350-7 1995 Significant elevation (p < 0.05) of the levels of urinary protein, lactate dehydrogenase (LDH), and N-acetyl-B-D-glycosaminidase (NAG) was observed in patients on Minizide during treatment, and these levels remained elevated during the latter part of the study. MINIZIDE 166-174 N-acetyl-alpha-glucosaminidase Homo sapiens 103-131 8527350-7 1995 Significant elevation (p < 0.05) of the levels of urinary protein, lactate dehydrogenase (LDH), and N-acetyl-B-D-glycosaminidase (NAG) was observed in patients on Minizide during treatment, and these levels remained elevated during the latter part of the study. MINIZIDE 166-174 N-acetyl-alpha-glucosaminidase Homo sapiens 133-136 7588670-6 1995 On the second post-operative day, a reduced urinary NAG/creatinine ratio was observed in the diclofenac group when compared to placebo. Diclofenac 93-103 N-acetyl-alpha-glucosaminidase Homo sapiens 52-55 7669872-6 1995 Multiple regression analysis was performed in the whole of diabetics and significant association were identified between urinary NAG excretion and plasma glucose, AER and plasma creatinine (p < 0.0005, r = 0.42). Glucose 154-161 N-acetyl-alpha-glucosaminidase Homo sapiens 129-132 7669872-6 1995 Multiple regression analysis was performed in the whole of diabetics and significant association were identified between urinary NAG excretion and plasma glucose, AER and plasma creatinine (p < 0.0005, r = 0.42). Creatinine 178-188 N-acetyl-alpha-glucosaminidase Homo sapiens 129-132 7669872-7 1995 The diabetics with plasma glucose lower to 140 mg/dl had more important correlation NAG: creatinine ratio-AER (p < 0.0001, r = 0.70). Glucose 26-33 N-acetyl-alpha-glucosaminidase Homo sapiens 84-87 7669872-7 1995 The diabetics with plasma glucose lower to 140 mg/dl had more important correlation NAG: creatinine ratio-AER (p < 0.0001, r = 0.70). Creatinine 89-99 N-acetyl-alpha-glucosaminidase Homo sapiens 84-87 7669872-8 1995 It is concluded that measurement of urinary NAG may be of value in the detection of diabetic nephropathy at a potentially reversible stage if the plasma glucose is take into account. Glucose 153-160 N-acetyl-alpha-glucosaminidase Homo sapiens 44-47 7587910-3 1995 The effects of EPA-E were determined by observing the changes of the index of urine albumin excretion level/urine creatinine (Cr) excretion level (UAI), the ratio of beta 2-microglobulin excretion level/urine Cr excretion level (beta 2-MG/Cr) and the ratio of N-acetyl-D-glucosaminidase excretion level/urine Cr excretion level (NAG/Cr) at 3, 6 and 12 months after the start of the treatment. eicosapentaenoic acid ethyl ester 15-20 N-acetyl-alpha-glucosaminidase Homo sapiens 329-332 8725030-4 1995 Although statistically nonsignificant, a constant mild increase of urinary NAG was observed after PCN, that has to be evaluated with long-term follow-up studies. PREGNENOLONE CARBONITRILE 98-101 N-acetyl-alpha-glucosaminidase Homo sapiens 75-78 7797145-4 1995 During MTX treatment, NAG indices were normal in 5 children and only slightly elevated occasionally in 9 patients. Methotrexate 7-10 N-acetyl-alpha-glucosaminidase Homo sapiens 22-25 7797145-5 1995 Among them, transiently high serum MTX levels (Patient A) or low urinary pH (Patient B) were accompanied by high NAG indices. Methotrexate 35-38 N-acetyl-alpha-glucosaminidase Homo sapiens 113-116 7797145-6 1995 MTX toxicity has been diagnosed in 3 cases, when permanently high NAG indices were in accordance with other clinical signs. Methotrexate 0-3 N-acetyl-alpha-glucosaminidase Homo sapiens 66-69 7915490-6 1994 In group 1, immediately after DIP, the urinary excretion of albumin, gamma-GTP and NAG were significantly increased (p < 0.01, p < 0.01, p < 0.01). dip 30-33 N-acetyl-alpha-glucosaminidase Homo sapiens 69-86 7527629-5 1994 A positive correlation was found between serum creatinine levels and excretion of the tubular enzyme beta NAG (r = 0.36; p < 0.05), but not between creatinine levels and alpha 1-MG or the glomerular markers. Creatinine 47-57 N-acetyl-alpha-glucosaminidase Homo sapiens 106-109 8015825-4 1994 The NAG values obtained with each substrate decreased with age as a result of a concomitant rise in the urinary creatinine concentration. Creatinine 112-122 N-acetyl-alpha-glucosaminidase Homo sapiens 4-7 7999778-7 1994 A correlation was found for both BSA and lysozyme in KAsp, NaGlu, LysHCl, ArgGlu, and LysGlu between the surface tension effect and the observed preferential interactions, indicating that the change in the surface free energy of the protein-containing cavity due to the surface tension increase for water by these amino acid salts contributes dominantly to the observed increase in the chemical potential of the protein by their addition. Water 299-304 N-acetyl-alpha-glucosaminidase Homo sapiens 59-64 7999778-7 1994 A correlation was found for both BSA and lysozyme in KAsp, NaGlu, LysHCl, ArgGlu, and LysGlu between the surface tension effect and the observed preferential interactions, indicating that the change in the surface free energy of the protein-containing cavity due to the surface tension increase for water by these amino acid salts contributes dominantly to the observed increase in the chemical potential of the protein by their addition. amino acid salts 314-330 N-acetyl-alpha-glucosaminidase Homo sapiens 59-64 8305503-5 1994 The BSA-GlcNAc-induced acrosome reaction was inhibited by N-acetylglucosamine (GlcNAc), p-nitrophenyl-GlcNAc, and purified soluble beta-N-acetylglucosaminidase (beta NAG). Acetylglucosamine 8-14 N-acetyl-alpha-glucosaminidase Homo sapiens 166-169 8305503-8 1994 The characteristics of the BSA-GlcNAc induction suggest that the beta NAG molecule may be the mediator of this effect. Acetylglucosamine 31-37 N-acetyl-alpha-glucosaminidase Homo sapiens 70-73 8243412-1 1993 A previous study of 16 pesticide applicators showed that N-acetylglucosaminidase (NAG) excretion during exposure to the soil nematocide, 1,3-dichloropropene (DCP), was correlated with DCP dose and the excretion of its major metabolite, N-acetyl-S-(cis-3-chloroprop-2-enyl)-cysteine (3CNAC). 1,3-dichloro-1-propene 137-156 N-acetyl-alpha-glucosaminidase Homo sapiens 57-80 7487376-3 1994 Urinary NAG activity was determined in 13 patients with various rheumatic diseases during administration of potentially nephrotoxic drugs like nonsteroidal anti-inflammatory drugs (NSAID), aminoglycosides, gold salts, cyclosporin and steroids. Aminoglycosides 189-204 N-acetyl-alpha-glucosaminidase Homo sapiens 8-11 7487376-3 1994 Urinary NAG activity was determined in 13 patients with various rheumatic diseases during administration of potentially nephrotoxic drugs like nonsteroidal anti-inflammatory drugs (NSAID), aminoglycosides, gold salts, cyclosporin and steroids. gold salts 206-216 N-acetyl-alpha-glucosaminidase Homo sapiens 8-11 7487376-3 1994 Urinary NAG activity was determined in 13 patients with various rheumatic diseases during administration of potentially nephrotoxic drugs like nonsteroidal anti-inflammatory drugs (NSAID), aminoglycosides, gold salts, cyclosporin and steroids. Steroids 234-242 N-acetyl-alpha-glucosaminidase Homo sapiens 8-11 7487376-4 1994 The significant decrease of urinary NAG activity was common in patients with recently diagnosed rheumatic diseases, who received steroids. Steroids 129-137 N-acetyl-alpha-glucosaminidase Homo sapiens 36-39 7487376-6 1994 The use of two types of potentially nephrotoxic drugs, like NSAID and gentamicin or NSAID with cyclosporin induced significant augmentation of NAG excretion. Gentamicins 70-80 N-acetyl-alpha-glucosaminidase Homo sapiens 143-146 7487376-6 1994 The use of two types of potentially nephrotoxic drugs, like NSAID and gentamicin or NSAID with cyclosporin induced significant augmentation of NAG excretion. Cyclosporine 95-106 N-acetyl-alpha-glucosaminidase Homo sapiens 143-146 7487376-8 1994 The recognition of high NAG enzymuria permits to reduce dosage or discontinue treatment with potentially nephrotoxic drug prior to irreversible renal insufficiency as shown in the case of a patient with psoriatic arthritis treated with simultaneously administered cyclosporin and diclofenac. Cyclosporine 264-275 N-acetyl-alpha-glucosaminidase Homo sapiens 24-27 7487376-8 1994 The recognition of high NAG enzymuria permits to reduce dosage or discontinue treatment with potentially nephrotoxic drug prior to irreversible renal insufficiency as shown in the case of a patient with psoriatic arthritis treated with simultaneously administered cyclosporin and diclofenac. Diclofenac 280-290 N-acetyl-alpha-glucosaminidase Homo sapiens 24-27 7507714-0 1993 Formamidinium-induced dimer stabilization and flicker block behavior in homo- and heterodimer channels formed by gramicidin A and N-acetyl gramicidin A. formamidine 0-13 N-acetyl-alpha-glucosaminidase Homo sapiens 130-151 7507714-1 1993 Compared to the N-formyl gramicidin A (GA), the N-acetyl gramicidin A (NAG) channel has unchanged conductance in 1 M NH4+ (gamma NN/gamma GG = 1, conductance ratio) but reduced conductance in 1 M K+ (gamma NN/gamma GG = 0.6) methylammonium (gamma NN/gamma GG = 0.3), and formamidinium (gamma NN/gamma GG = 0.1) solutions. n-formyl gramicidin a 16-37 N-acetyl-alpha-glucosaminidase Homo sapiens 48-69 7507714-1 1993 Compared to the N-formyl gramicidin A (GA), the N-acetyl gramicidin A (NAG) channel has unchanged conductance in 1 M NH4+ (gamma NN/gamma GG = 1, conductance ratio) but reduced conductance in 1 M K+ (gamma NN/gamma GG = 0.6) methylammonium (gamma NN/gamma GG = 0.3), and formamidinium (gamma NN/gamma GG = 0.1) solutions. n-formyl gramicidin a 16-37 N-acetyl-alpha-glucosaminidase Homo sapiens 71-74 7507714-1 1993 Compared to the N-formyl gramicidin A (GA), the N-acetyl gramicidin A (NAG) channel has unchanged conductance in 1 M NH4+ (gamma NN/gamma GG = 1, conductance ratio) but reduced conductance in 1 M K+ (gamma NN/gamma GG = 0.6) methylammonium (gamma NN/gamma GG = 0.3), and formamidinium (gamma NN/gamma GG = 0.1) solutions. formamidine 271-284 N-acetyl-alpha-glucosaminidase Homo sapiens 48-69 7507714-1 1993 Compared to the N-formyl gramicidin A (GA), the N-acetyl gramicidin A (NAG) channel has unchanged conductance in 1 M NH4+ (gamma NN/gamma GG = 1, conductance ratio) but reduced conductance in 1 M K+ (gamma NN/gamma GG = 0.6) methylammonium (gamma NN/gamma GG = 0.3), and formamidinium (gamma NN/gamma GG = 0.1) solutions. formamidine 271-284 N-acetyl-alpha-glucosaminidase Homo sapiens 71-74 8243412-1 1993 A previous study of 16 pesticide applicators showed that N-acetylglucosaminidase (NAG) excretion during exposure to the soil nematocide, 1,3-dichloropropene (DCP), was correlated with DCP dose and the excretion of its major metabolite, N-acetyl-S-(cis-3-chloroprop-2-enyl)-cysteine (3CNAC). n-acetyl-s-(cis-3-chloroprop-2-enyl)-cysteine 236-281 N-acetyl-alpha-glucosaminidase Homo sapiens 57-80 8243412-1 1993 A previous study of 16 pesticide applicators showed that N-acetylglucosaminidase (NAG) excretion during exposure to the soil nematocide, 1,3-dichloropropene (DCP), was correlated with DCP dose and the excretion of its major metabolite, N-acetyl-S-(cis-3-chloroprop-2-enyl)-cysteine (3CNAC). n-acetyl-s-(cis-3-chloroprop-2-enyl)-cysteine 236-281 N-acetyl-alpha-glucosaminidase Homo sapiens 82-85 8243412-1 1993 A previous study of 16 pesticide applicators showed that N-acetylglucosaminidase (NAG) excretion during exposure to the soil nematocide, 1,3-dichloropropene (DCP), was correlated with DCP dose and the excretion of its major metabolite, N-acetyl-S-(cis-3-chloroprop-2-enyl)-cysteine (3CNAC). 3cnac 283-288 N-acetyl-alpha-glucosaminidase Homo sapiens 57-80 8243412-1 1993 A previous study of 16 pesticide applicators showed that N-acetylglucosaminidase (NAG) excretion during exposure to the soil nematocide, 1,3-dichloropropene (DCP), was correlated with DCP dose and the excretion of its major metabolite, N-acetyl-S-(cis-3-chloroprop-2-enyl)-cysteine (3CNAC). 3cnac 283-288 N-acetyl-alpha-glucosaminidase Homo sapiens 82-85 8243412-6 1993 Clear dichotomous differences in urinary protein excretion were seen for high versus low exposure (< or > 1.5 mg 3CNAC excretion/day) for NAG and RBP, but not for ALB. 3cnac 119-124 N-acetyl-alpha-glucosaminidase Homo sapiens 144-147 8243412-1 1993 A previous study of 16 pesticide applicators showed that N-acetylglucosaminidase (NAG) excretion during exposure to the soil nematocide, 1,3-dichloropropene (DCP), was correlated with DCP dose and the excretion of its major metabolite, N-acetyl-S-(cis-3-chloroprop-2-enyl)-cysteine (3CNAC). 1,3-dichloro-1-propene 137-156 N-acetyl-alpha-glucosaminidase Homo sapiens 82-85 8243412-1 1993 A previous study of 16 pesticide applicators showed that N-acetylglucosaminidase (NAG) excretion during exposure to the soil nematocide, 1,3-dichloropropene (DCP), was correlated with DCP dose and the excretion of its major metabolite, N-acetyl-S-(cis-3-chloroprop-2-enyl)-cysteine (3CNAC). 1,3-dichloro-1-propene 158-161 N-acetyl-alpha-glucosaminidase Homo sapiens 57-80 8243412-1 1993 A previous study of 16 pesticide applicators showed that N-acetylglucosaminidase (NAG) excretion during exposure to the soil nematocide, 1,3-dichloropropene (DCP), was correlated with DCP dose and the excretion of its major metabolite, N-acetyl-S-(cis-3-chloroprop-2-enyl)-cysteine (3CNAC). 1,3-dichloro-1-propene 158-161 N-acetyl-alpha-glucosaminidase Homo sapiens 82-85 8243412-1 1993 A previous study of 16 pesticide applicators showed that N-acetylglucosaminidase (NAG) excretion during exposure to the soil nematocide, 1,3-dichloropropene (DCP), was correlated with DCP dose and the excretion of its major metabolite, N-acetyl-S-(cis-3-chloroprop-2-enyl)-cysteine (3CNAC). 1,3-dichloro-1-propene 184-187 N-acetyl-alpha-glucosaminidase Homo sapiens 57-80 8243412-1 1993 A previous study of 16 pesticide applicators showed that N-acetylglucosaminidase (NAG) excretion during exposure to the soil nematocide, 1,3-dichloropropene (DCP), was correlated with DCP dose and the excretion of its major metabolite, N-acetyl-S-(cis-3-chloroprop-2-enyl)-cysteine (3CNAC). 1,3-dichloro-1-propene 184-187 N-acetyl-alpha-glucosaminidase Homo sapiens 82-85 1460703-1 1992 The objective of the present study was to assess renal damage, if any, by non-invasive technique, viz NAG activity in urine and GFR in patients on continuous and intermittent rifampicin therapy. Rifampin 175-185 N-acetyl-alpha-glucosaminidase Homo sapiens 102-105 8295156-0 1993 An association between the lysosomal enzyme NAG and urinary free cortisol and platelet imipramine binding. Hydrocortisone 65-73 N-acetyl-alpha-glucosaminidase Homo sapiens 44-47 8295156-0 1993 An association between the lysosomal enzyme NAG and urinary free cortisol and platelet imipramine binding. Imipramine 87-97 N-acetyl-alpha-glucosaminidase Homo sapiens 44-47 8295156-2 1993 In a separate study of healthy controls NAG levels showed a trend toward association with platelet imipramine binding density. Imipramine 99-109 N-acetyl-alpha-glucosaminidase Homo sapiens 40-43 8127069-3 1993 The enzymatic liberation of the fluorochrome from 4-methyl-umbelliferyl-alpha-N-acetylglucosamine 6-sulphate requires the sequential action of the GlcNAc-6S sulphatase and alpha-N-acetylglucosaminidase. 4-methyl-umbelliferyl-alpha-n-acetylglucosamine 6-sulphate 50-108 N-acetyl-alpha-glucosaminidase Homo sapiens 172-201 1460703-5 1992 An additive toxic effect was obvious in patients receiving streptomycin; when the treatment was withdrawn the urinary NAG activity stabilized within 15-21 days. Streptomycin 59-71 N-acetyl-alpha-glucosaminidase Homo sapiens 118-121 1284195-8 1992 The age, sex and race adjusted NAG and alpha 1m showed increasing trend with rising urinary cadmium levels. Cadmium 92-99 N-acetyl-alpha-glucosaminidase Homo sapiens 31-34 1298541-2 1992 In this study a rapid colorimetric assay for human epidermal keratinocyte growth and viability has been developed based on the colour reaction of NAG (p-nitrophenol-N-acetyl-beta-D-glucosaminide). nag 146-149 N-acetyl-alpha-glucosaminidase Homo sapiens 151-194 1793103-3 1991 This study reports on the relationship of PCE in breath and estimates of chronic exposure with the urinary ratios of total urinary protein, albumin, and n-acetyl-glucosaminidase (NAG) to creatinine in dry cleaning workers exposed to PCE. Tetrachloroethylene 233-236 N-acetyl-alpha-glucosaminidase Homo sapiens 179-182 1610104-1 1992 The NAG activity present in urine from newborn babies was assayed using two colorimetric procedures with either MNP-GlcNAc or VRA-GlcNAc as substrate and compared with data obtained with the well established PNP-GlcNAc procedure. 2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose 116-122 N-acetyl-alpha-glucosaminidase Homo sapiens 4-7 1610104-1 1992 The NAG activity present in urine from newborn babies was assayed using two colorimetric procedures with either MNP-GlcNAc or VRA-GlcNAc as substrate and compared with data obtained with the well established PNP-GlcNAc procedure. 5-(4-(2-acetamido-2-deoxyglucopyranosyloxy)-3-methoxyphenylmethylene)-2-thioxothiazolidin-4-one-3-ethanoate 126-136 N-acetyl-alpha-glucosaminidase Homo sapiens 4-7 1610104-1 1992 The NAG activity present in urine from newborn babies was assayed using two colorimetric procedures with either MNP-GlcNAc or VRA-GlcNAc as substrate and compared with data obtained with the well established PNP-GlcNAc procedure. 2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose 130-136 N-acetyl-alpha-glucosaminidase Homo sapiens 4-7 1562355-1 1992 N-Acetyl-L-glutamate synthetase (NAG synthetase) is a mitochondrial matrix enzyme which catalyzes the synthesis of N-acetyl-Lglutamate (NAG), a physiologic activator of the urea cycle enzyme carbamylphosphate synthetase I. Urea 173-177 N-acetyl-alpha-glucosaminidase Homo sapiens 33-36 1562355-1 1992 N-Acetyl-L-glutamate synthetase (NAG synthetase) is a mitochondrial matrix enzyme which catalyzes the synthesis of N-acetyl-Lglutamate (NAG), a physiologic activator of the urea cycle enzyme carbamylphosphate synthetase I. Urea 173-177 N-acetyl-alpha-glucosaminidase Homo sapiens 115-134 1562355-1 1992 N-Acetyl-L-glutamate synthetase (NAG synthetase) is a mitochondrial matrix enzyme which catalyzes the synthesis of N-acetyl-Lglutamate (NAG), a physiologic activator of the urea cycle enzyme carbamylphosphate synthetase I. Urea 173-177 N-acetyl-alpha-glucosaminidase Homo sapiens 136-139 2042807-1 1991 We have studied 122 patients, all younger than 12 months of age, to whom we check the N-acetylglucosaminidase/creatinine (NAG/creatinine) ratio in the first morning urine. Creatinine 110-120 N-acetyl-alpha-glucosaminidase Homo sapiens 122-125 1320220-4 1992 Six patients had a reduction in the signal from N-acetyl groups (NAG) in the stroke area compared with controls, and those with the lowest NAG to phosphocreatine/creatine ratios had the least recovery of function. Phosphocreatine 146-161 N-acetyl-alpha-glucosaminidase Homo sapiens 139-142 1300357-4 1992 On comparing the BT/TT group with controls a significant decrease (P < 0.001) in zymosan dependent NAG release was observed in the former group at 2 hrs culture. benzothiazole 17-19 N-acetyl-alpha-glucosaminidase Homo sapiens 102-105 1300357-4 1992 On comparing the BT/TT group with controls a significant decrease (P < 0.001) in zymosan dependent NAG release was observed in the former group at 2 hrs culture. Zymosan 84-91 N-acetyl-alpha-glucosaminidase Homo sapiens 102-105 1593797-5 1992 Urinary NAG and BMG concentrations were also increased in patients with non-diabetic ketoacidosis, suggesting a toxic effect of ketone bodies to renal tubular cells. Ketones 128-134 N-acetyl-alpha-glucosaminidase Homo sapiens 8-11 1308626-8 1992 The NAG: creatinine ratio was shown to be elevated after 2 days of treatment at 63 mg/kg. Creatinine 9-19 N-acetyl-alpha-glucosaminidase Homo sapiens 4-7 1785334-9 1991 The NAG correlated with the triglycerides. Triglycerides 28-41 N-acetyl-alpha-glucosaminidase Homo sapiens 4-7 1785334-11 1991 The lipid peroxides in the non HDL correlated with the triglyceride, atherogenic index, and NAG. Lipid Peroxides 4-19 N-acetyl-alpha-glucosaminidase Homo sapiens 92-95 2042807-3 1991 The NAG/creatinine values were inversely correlated with age, height and weight. Creatinine 8-18 N-acetyl-alpha-glucosaminidase Homo sapiens 4-7 1793103-3 1991 This study reports on the relationship of PCE in breath and estimates of chronic exposure with the urinary ratios of total urinary protein, albumin, and n-acetyl-glucosaminidase (NAG) to creatinine in dry cleaning workers exposed to PCE. Tetrachloroethylene 42-45 N-acetyl-alpha-glucosaminidase Homo sapiens 153-177 1793103-3 1991 This study reports on the relationship of PCE in breath and estimates of chronic exposure with the urinary ratios of total urinary protein, albumin, and n-acetyl-glucosaminidase (NAG) to creatinine in dry cleaning workers exposed to PCE. Tetrachloroethylene 42-45 N-acetyl-alpha-glucosaminidase Homo sapiens 179-182 1793103-3 1991 This study reports on the relationship of PCE in breath and estimates of chronic exposure with the urinary ratios of total urinary protein, albumin, and n-acetyl-glucosaminidase (NAG) to creatinine in dry cleaning workers exposed to PCE. Creatinine 187-197 N-acetyl-alpha-glucosaminidase Homo sapiens 179-182 2338998-6 1990 SCC and NAG showed significant negative correlations with MAN, GAL and GLU, the latter being the only parameter significantly correlated with each of the other parameters. Galactose 63-66 N-acetyl-alpha-glucosaminidase Homo sapiens 8-11 2035548-8 1991 A positive correlation was found, however, between urinary N-acetyl-b-D-glucosaminidase (NAG) and urinary mercury. Mercury 106-113 N-acetyl-alpha-glucosaminidase Homo sapiens 59-87 2035548-8 1991 A positive correlation was found, however, between urinary N-acetyl-b-D-glucosaminidase (NAG) and urinary mercury. Mercury 106-113 N-acetyl-alpha-glucosaminidase Homo sapiens 89-92 2241187-7 1990 However NAG index rose remarkably when CDDP was treated by CDDP. Cisplatin 39-43 N-acetyl-alpha-glucosaminidase Homo sapiens 8-11 2241187-7 1990 However NAG index rose remarkably when CDDP was treated by CDDP. Cisplatin 59-63 N-acetyl-alpha-glucosaminidase Homo sapiens 8-11 2339202-1 1990 ONO-3708, a thromboxane A2 (TXA2) antagonist, was administered at a dose of 2 micrograms/kg/min by a double blind method as compared with inactive placebo during cardiopulmonary bypass (CPB) procedure to study the changes of thromboxane B2 (TXB2) levels in plasma and urine and N-acetyl-glucosaminidase (NAG) level in urine. ONO 3708 0-8 N-acetyl-alpha-glucosaminidase Homo sapiens 278-302 2339202-1 1990 ONO-3708, a thromboxane A2 (TXA2) antagonist, was administered at a dose of 2 micrograms/kg/min by a double blind method as compared with inactive placebo during cardiopulmonary bypass (CPB) procedure to study the changes of thromboxane B2 (TXB2) levels in plasma and urine and N-acetyl-glucosaminidase (NAG) level in urine. ONO 3708 0-8 N-acetyl-alpha-glucosaminidase Homo sapiens 304-307 2339202-4 1990 The urinary NAG level, increased significantly (P less than 0.01) during CPB the NAG level in ONO-3708 group was significantly low as compared to placebo group. ONO 3708 94-102 N-acetyl-alpha-glucosaminidase Homo sapiens 12-15 2339202-4 1990 The urinary NAG level, increased significantly (P less than 0.01) during CPB the NAG level in ONO-3708 group was significantly low as compared to placebo group. ONO 3708 94-102 N-acetyl-alpha-glucosaminidase Homo sapiens 81-84 2338998-6 1990 SCC and NAG showed significant negative correlations with MAN, GAL and GLU, the latter being the only parameter significantly correlated with each of the other parameters. Glucose 71-74 N-acetyl-alpha-glucosaminidase Homo sapiens 8-11 2316078-2 1990 Following prospective randomization, we examined NAG excretion during cisplatin treatment with/without nephroprotection, after intravenous urography with ionic/non-ionic contrast media, during lower/upper urinary tract infections and before/after extracorporeal shockwave lithotripsy for intrarenal calculi (first-generation equipment used). Cisplatin 70-79 N-acetyl-alpha-glucosaminidase Homo sapiens 49-52 2154066-14 1990 In conclusion, the persistent and progressive changes seen in the biochemical (LDH, TP, BG, NAG) and cellular parameters (total cells, neutrophils and lymphocytes) following silica administration correlated with the fibrotic response which occurred after exposure to this material. Silicon Dioxide 174-180 N-acetyl-alpha-glucosaminidase Homo sapiens 92-95 2302775-1 1990 We have improved the kinetic rate assay method for determining N-acetyl-beta-D-glucosaminidase (EC 3.2.1.30; NAG) activity in urine with use of the synthetic substrate, 2-chloro-4-nitrophenyl-N-acetyl-beta-D-glucosaminide (CNP-NAG), reported previously (Clin Chem 1988;34:2140-2). 2-chloro-4-nitrophenyl-N-acetylglucosaminide 169-221 N-acetyl-alpha-glucosaminidase Homo sapiens 109-112 2302775-1 1990 We have improved the kinetic rate assay method for determining N-acetyl-beta-D-glucosaminidase (EC 3.2.1.30; NAG) activity in urine with use of the synthetic substrate, 2-chloro-4-nitrophenyl-N-acetyl-beta-D-glucosaminide (CNP-NAG), reported previously (Clin Chem 1988;34:2140-2). 2-chloro-4-nitrophenyl-N-acetylglucosaminide 169-221 N-acetyl-alpha-glucosaminidase Homo sapiens 227-230 2302775-4 1990 Reference values for urinary NAG activity determined by the CNP-NAG method were established for untimed urine specimens from 674 healthy volunteers. cnp 60-63 N-acetyl-alpha-glucosaminidase Homo sapiens 29-32 2302775-5 1990 The normal reference interval (mean +/- 2 SD) for NAG: 1.6-15.0 (mean 4.9) U per gram of creatinine. Creatinine 89-99 N-acetyl-alpha-glucosaminidase Homo sapiens 50-53 2316078-6 1990 However, the increase in NAG excretion was less impressive during cisplatin therapy when nephroprotective amino acids were infused, and in the urography group when non-ionic contrast media were used. Cisplatin 66-75 N-acetyl-alpha-glucosaminidase Homo sapiens 25-28 34411609-1 2021 Mucopolysaccharidosis type IIIB (MPS IIIB) is a lysosomal disease caused by mutations in the NAGLU gene encoding alpha-N-acetylglucosaminidase (NAGLU) which degrades heparan sulfate in lysosomes. Heparitin Sulfate 166-181 N-acetyl-alpha-glucosaminidase Homo sapiens 0-31 6331485-5 1984 Similarly, the NAG level in the silicosis patients with matched controls was higher than that in the silica-exposed controls (P less than 0.05). Silicon Dioxide 101-107 N-acetyl-alpha-glucosaminidase Homo sapiens 15-18 34806811-1 2022 Mucopolysaccharidosis type IIIB is a rare autosomal recessive disorder characterized by deficiency of the enzyme N-acetyl-alpha-d-glucosaminidase (NAGLU), caused by biallelic pathogenic variants in the NAGLU gene, which leads to storage of heparan sulfate and a series of clinical consequences which hallmark is neurodegeneration. Heparitin Sulfate 240-255 N-acetyl-alpha-glucosaminidase Homo sapiens 147-152 34606862-7 2022 The fungicides flutriafol and azoxystrobin, the herbicide chlorsulfuron and the insecticide fipronil induced a significant reduction in PN and beta-1,4-N-acetylglucosaminidase activity (P < 0.05) (NAG) in the alkaline loam soil with low organic carbon content i.e. a soil with properties which typically favors pesticide bioavailability and therefore potential toxicity. flutriafol 15-25 N-acetyl-alpha-glucosaminidase Homo sapiens 197-200 34606862-7 2022 The fungicides flutriafol and azoxystrobin, the herbicide chlorsulfuron and the insecticide fipronil induced a significant reduction in PN and beta-1,4-N-acetylglucosaminidase activity (P < 0.05) (NAG) in the alkaline loam soil with low organic carbon content i.e. a soil with properties which typically favors pesticide bioavailability and therefore potential toxicity. azoxystrobin 30-42 N-acetyl-alpha-glucosaminidase Homo sapiens 197-200 34606862-7 2022 The fungicides flutriafol and azoxystrobin, the herbicide chlorsulfuron and the insecticide fipronil induced a significant reduction in PN and beta-1,4-N-acetylglucosaminidase activity (P < 0.05) (NAG) in the alkaline loam soil with low organic carbon content i.e. a soil with properties which typically favors pesticide bioavailability and therefore potential toxicity. chlorsulfuron 58-71 N-acetyl-alpha-glucosaminidase Homo sapiens 197-200 34606862-7 2022 The fungicides flutriafol and azoxystrobin, the herbicide chlorsulfuron and the insecticide fipronil induced a significant reduction in PN and beta-1,4-N-acetylglucosaminidase activity (P < 0.05) (NAG) in the alkaline loam soil with low organic carbon content i.e. a soil with properties which typically favors pesticide bioavailability and therefore potential toxicity. fipronil 92-100 N-acetyl-alpha-glucosaminidase Homo sapiens 197-200 34806811-1 2022 Mucopolysaccharidosis type IIIB is a rare autosomal recessive disorder characterized by deficiency of the enzyme N-acetyl-alpha-d-glucosaminidase (NAGLU), caused by biallelic pathogenic variants in the NAGLU gene, which leads to storage of heparan sulfate and a series of clinical consequences which hallmark is neurodegeneration. Heparitin Sulfate 240-255 N-acetyl-alpha-glucosaminidase Homo sapiens 202-207 34411609-1 2021 Mucopolysaccharidosis type IIIB (MPS IIIB) is a lysosomal disease caused by mutations in the NAGLU gene encoding alpha-N-acetylglucosaminidase (NAGLU) which degrades heparan sulfate in lysosomes. Heparitin Sulfate 166-181 N-acetyl-alpha-glucosaminidase Homo sapiens 33-41 34411609-1 2021 Mucopolysaccharidosis type IIIB (MPS IIIB) is a lysosomal disease caused by mutations in the NAGLU gene encoding alpha-N-acetylglucosaminidase (NAGLU) which degrades heparan sulfate in lysosomes. Heparitin Sulfate 166-181 N-acetyl-alpha-glucosaminidase Homo sapiens 93-98 34411609-1 2021 Mucopolysaccharidosis type IIIB (MPS IIIB) is a lysosomal disease caused by mutations in the NAGLU gene encoding alpha-N-acetylglucosaminidase (NAGLU) which degrades heparan sulfate in lysosomes. Heparitin Sulfate 166-181 N-acetyl-alpha-glucosaminidase Homo sapiens 113-142 34411609-1 2021 Mucopolysaccharidosis type IIIB (MPS IIIB) is a lysosomal disease caused by mutations in the NAGLU gene encoding alpha-N-acetylglucosaminidase (NAGLU) which degrades heparan sulfate in lysosomes. Heparitin Sulfate 166-181 N-acetyl-alpha-glucosaminidase Homo sapiens 144-149 34411609-2 2021 Deficiency in NAGLU results in lysosomal accumulation of glycosaminoglycans (GAGs) and neurological symptoms. Glycosaminoglycans 57-75 N-acetyl-alpha-glucosaminidase Homo sapiens 14-19 34411609-5 2021 MPS IIIB neural stem cells exhibited NAGLU deficiency accompanied with GAG accumulation, as well as lysosomal enlargement and secondary lipid accumulation. Glycosaminoglycans 71-74 N-acetyl-alpha-glucosaminidase Homo sapiens 0-8 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 34114323-9 2021 In multivariate linear regression analyses, older age, lower total cholesterol and higher HIV RNA were independently associated with higher NAG:UCr; older age, lower total cholesterol and lower CD4 cell count were independently associated with higher alpha1-M:UCr. Cholesterol 67-78 N-acetyl-alpha-glucosaminidase Homo sapiens 140-143 34106504-0 2021 Iminosugar-C-glycosides work as pharmacological chaperones of NAGLU, a glycosidase involved in MPS IIIB rare disease. C-glycoside 10-23 N-acetyl-alpha-glucosaminidase Homo sapiens 62-67 34106504-1 2021 Mucopolysaccharidosis type IIIB is a devastating neurological disease caused by a lack of the lysosomal enzyme, alpha -N-acetylglucosaminidase (NAGLU), leading to a toxic accumulation of heparan sulfate. Heparitin Sulfate 188-203 N-acetyl-alpha-glucosaminidase Homo sapiens 113-143 34106504-1 2021 Mucopolysaccharidosis type IIIB is a devastating neurological disease caused by a lack of the lysosomal enzyme, alpha -N-acetylglucosaminidase (NAGLU), leading to a toxic accumulation of heparan sulfate. Heparitin Sulfate 188-203 N-acetyl-alpha-glucosaminidase Homo sapiens 145-150 34106504-3 2021 Capitalizing on the three-dimensional structures of two modest homoiminosugar-based NAGLU inhibitors in complex with bacterial homolog of NAGLU, CpGH89, we have synthesized a library of 17 six-membered iminosugar- C -glycosides mimicking N -acetyl-D-glucosamine and bearing various pseudo-anomeric substituents of both alpha - and beta -configuration. homoiminosugar 63-77 N-acetyl-alpha-glucosaminidase Homo sapiens 84-89 34106504-3 2021 Capitalizing on the three-dimensional structures of two modest homoiminosugar-based NAGLU inhibitors in complex with bacterial homolog of NAGLU, CpGH89, we have synthesized a library of 17 six-membered iminosugar- C -glycosides mimicking N -acetyl-D-glucosamine and bearing various pseudo-anomeric substituents of both alpha - and beta -configuration. homoiminosugar 63-77 N-acetyl-alpha-glucosaminidase Homo sapiens 138-143 34106504-3 2021 Capitalizing on the three-dimensional structures of two modest homoiminosugar-based NAGLU inhibitors in complex with bacterial homolog of NAGLU, CpGH89, we have synthesized a library of 17 six-membered iminosugar- C -glycosides mimicking N -acetyl-D-glucosamine and bearing various pseudo-anomeric substituents of both alpha - and beta -configuration. cpgh89 145-151 N-acetyl-alpha-glucosaminidase Homo sapiens 84-89 34106504-3 2021 Capitalizing on the three-dimensional structures of two modest homoiminosugar-based NAGLU inhibitors in complex with bacterial homolog of NAGLU, CpGH89, we have synthesized a library of 17 six-membered iminosugar- C -glycosides mimicking N -acetyl-D-glucosamine and bearing various pseudo-anomeric substituents of both alpha - and beta -configuration. cpgh89 145-151 N-acetyl-alpha-glucosaminidase Homo sapiens 138-143 34106504-3 2021 Capitalizing on the three-dimensional structures of two modest homoiminosugar-based NAGLU inhibitors in complex with bacterial homolog of NAGLU, CpGH89, we have synthesized a library of 17 six-membered iminosugar- C -glycosides mimicking N -acetyl-D-glucosamine and bearing various pseudo-anomeric substituents of both alpha - and beta -configuration. C-glycoside 214-227 N-acetyl-alpha-glucosaminidase Homo sapiens 138-143 34106504-3 2021 Capitalizing on the three-dimensional structures of two modest homoiminosugar-based NAGLU inhibitors in complex with bacterial homolog of NAGLU, CpGH89, we have synthesized a library of 17 six-membered iminosugar- C -glycosides mimicking N -acetyl-D-glucosamine and bearing various pseudo-anomeric substituents of both alpha - and beta -configuration. Acetylglucosamine 239-262 N-acetyl-alpha-glucosaminidase Homo sapiens 138-143 34092512-0 2021 Role of the urinary N-acetyl-beta-D-glucosaminidase/creatinine (NAG/Cr) ratio in discriminating between true and false pyuria in sterile urine bag specimens. Creatinine 52-62 N-acetyl-alpha-glucosaminidase Homo sapiens 64-67 34165649-0 2021 A GH89 human alpha-N-acetylglucosaminidase (hNAGLU) homologue from gut microbe Bacteroides thetaiotaomicron capable of hydrolyzing heparosan oligosaccharides. heparosan 131-140 N-acetyl-alpha-glucosaminidase Homo sapiens 13-42 34193170-5 2021 RESULTS: As the sensitive biomarkers of renal injury, beta2-MG and NAG were selected to estimate the 95% confidence interval lower limit of the U-Cd benchmark dose (BMDL5) to be 3.07 and 2.98 mug/g Cr, respectively. u-cd 144-148 N-acetyl-alpha-glucosaminidase Homo sapiens 67-70 34165649-0 2021 A GH89 human alpha-N-acetylglucosaminidase (hNAGLU) homologue from gut microbe Bacteroides thetaiotaomicron capable of hydrolyzing heparosan oligosaccharides. heparosan 131-140 N-acetyl-alpha-glucosaminidase Homo sapiens 44-50 34165649-0 2021 A GH89 human alpha-N-acetylglucosaminidase (hNAGLU) homologue from gut microbe Bacteroides thetaiotaomicron capable of hydrolyzing heparosan oligosaccharides. Oligosaccharides 141-157 N-acetyl-alpha-glucosaminidase Homo sapiens 13-42 34165649-0 2021 A GH89 human alpha-N-acetylglucosaminidase (hNAGLU) homologue from gut microbe Bacteroides thetaiotaomicron capable of hydrolyzing heparosan oligosaccharides. Oligosaccharides 141-157 N-acetyl-alpha-glucosaminidase Homo sapiens 44-50 34165649-2 2021 Although structurally and mechanistically similar to the human lysosomal alpha-N-acetylglucosaminidase (hNAGLU) in GH89 which is involved in the degradation of heparan sulfate in the lysosome, the reported bacterial GH89 enzymes characterized so far have no or low activity toward alpha-N-acetylglucosamine-terminated heparosan oligosaccharides, the preferred substrates of hNAGLU. gh89 115-119 N-acetyl-alpha-glucosaminidase Homo sapiens 104-110 34165649-2 2021 Although structurally and mechanistically similar to the human lysosomal alpha-N-acetylglucosaminidase (hNAGLU) in GH89 which is involved in the degradation of heparan sulfate in the lysosome, the reported bacterial GH89 enzymes characterized so far have no or low activity toward alpha-N-acetylglucosamine-terminated heparosan oligosaccharides, the preferred substrates of hNAGLU. gh89 115-119 N-acetyl-alpha-glucosaminidase Homo sapiens 374-380 34165649-2 2021 Although structurally and mechanistically similar to the human lysosomal alpha-N-acetylglucosaminidase (hNAGLU) in GH89 which is involved in the degradation of heparan sulfate in the lysosome, the reported bacterial GH89 enzymes characterized so far have no or low activity toward alpha-N-acetylglucosamine-terminated heparosan oligosaccharides, the preferred substrates of hNAGLU. Heparitin Sulfate 160-175 N-acetyl-alpha-glucosaminidase Homo sapiens 104-110 34165649-2 2021 Although structurally and mechanistically similar to the human lysosomal alpha-N-acetylglucosaminidase (hNAGLU) in GH89 which is involved in the degradation of heparan sulfate in the lysosome, the reported bacterial GH89 enzymes characterized so far have no or low activity toward alpha-N-acetylglucosamine-terminated heparosan oligosaccharides, the preferred substrates of hNAGLU. Heparitin Sulfate 160-175 N-acetyl-alpha-glucosaminidase Homo sapiens 374-380 34165649-2 2021 Although structurally and mechanistically similar to the human lysosomal alpha-N-acetylglucosaminidase (hNAGLU) in GH89 which is involved in the degradation of heparan sulfate in the lysosome, the reported bacterial GH89 enzymes characterized so far have no or low activity toward alpha-N-acetylglucosamine-terminated heparosan oligosaccharides, the preferred substrates of hNAGLU. gh89 216-220 N-acetyl-alpha-glucosaminidase Homo sapiens 104-110 34165649-2 2021 Although structurally and mechanistically similar to the human lysosomal alpha-N-acetylglucosaminidase (hNAGLU) in GH89 which is involved in the degradation of heparan sulfate in the lysosome, the reported bacterial GH89 enzymes characterized so far have no or low activity toward alpha-N-acetylglucosamine-terminated heparosan oligosaccharides, the preferred substrates of hNAGLU. gh89 216-220 N-acetyl-alpha-glucosaminidase Homo sapiens 374-380 34165649-2 2021 Although structurally and mechanistically similar to the human lysosomal alpha-N-acetylglucosaminidase (hNAGLU) in GH89 which is involved in the degradation of heparan sulfate in the lysosome, the reported bacterial GH89 enzymes characterized so far have no or low activity toward alpha-N-acetylglucosamine-terminated heparosan oligosaccharides, the preferred substrates of hNAGLU. heparosan 318-327 N-acetyl-alpha-glucosaminidase Homo sapiens 374-380 34165649-2 2021 Although structurally and mechanistically similar to the human lysosomal alpha-N-acetylglucosaminidase (hNAGLU) in GH89 which is involved in the degradation of heparan sulfate in the lysosome, the reported bacterial GH89 enzymes characterized so far have no or low activity toward alpha-N-acetylglucosamine-terminated heparosan oligosaccharides, the preferred substrates of hNAGLU. Oligosaccharides 328-344 N-acetyl-alpha-glucosaminidase Homo sapiens 374-380 34165649-4 2021 Among these enzymes, a truncated recombinant alpha-N-acetylglucosaminidase from gut symbiotic bacterium Bacteroides thetaiotaomicron 22Bt3590 was found to catalyze the cleavage of the terminal alpha1-4-linked N-acetylglucosamine (GlcNAc) from a heparosan disaccharide with high efficiency. alpha1-4-linked n-acetylglucosamine 194-229 N-acetyl-alpha-glucosaminidase Homo sapiens 45-74 34165649-4 2021 Among these enzymes, a truncated recombinant alpha-N-acetylglucosaminidase from gut symbiotic bacterium Bacteroides thetaiotaomicron 22Bt3590 was found to catalyze the cleavage of the terminal alpha1-4-linked N-acetylglucosamine (GlcNAc) from a heparosan disaccharide with high efficiency. Acetylglucosamine 231-237 N-acetyl-alpha-glucosaminidase Homo sapiens 45-74 34165649-4 2021 Among these enzymes, a truncated recombinant alpha-N-acetylglucosaminidase from gut symbiotic bacterium Bacteroides thetaiotaomicron 22Bt3590 was found to catalyze the cleavage of the terminal alpha1-4-linked N-acetylglucosamine (GlcNAc) from a heparosan disaccharide with high efficiency. heparosan disaccharide 246-268 N-acetyl-alpha-glucosaminidase Homo sapiens 45-74 34165649-6 2021 This bacterial alpha-N-acetylglucosaminidase could be a useful catalyst for heparan sulfate analysis. Heparitin Sulfate 76-91 N-acetyl-alpha-glucosaminidase Homo sapiens 15-44 35483153-1 2022 In this study, the subcritical water hydrolysis of N-acetyl-d-glucosamine (NAG), a monomer of abundant renewable marine biopolymer chitin, for production of value-added chemicals is investigated. Water 31-36 N-acetyl-alpha-glucosaminidase Homo sapiens 75-78 35192834-6 2022 We found that the activities of BG, NAG, and AP were predominately dependent on plant N contents, while the soil LAP activity was tightly related to soil recalcitrant C and N contents. Nitrogen 86-87 N-acetyl-alpha-glucosaminidase Homo sapiens 36-39 35483153-2 2022 The enhanced ionization of water at subcritical conditions (200 C; 50-100 bar), provides enough acidity for deacetylation of NAG resulting in 80% yield of acetic acid along with traces of formic acid, lactic acid, glucose, fructose, 5-hydroxymethylfurfural (5-HMF),etc. Water 27-32 N-acetyl-alpha-glucosaminidase Homo sapiens 126-129 35483153-2 2022 The enhanced ionization of water at subcritical conditions (200 C; 50-100 bar), provides enough acidity for deacetylation of NAG resulting in 80% yield of acetic acid along with traces of formic acid, lactic acid, glucose, fructose, 5-hydroxymethylfurfural (5-HMF),etc. Acetic Acid 156-167 N-acetyl-alpha-glucosaminidase Homo sapiens 126-129 35483153-2 2022 The enhanced ionization of water at subcritical conditions (200 C; 50-100 bar), provides enough acidity for deacetylation of NAG resulting in 80% yield of acetic acid along with traces of formic acid, lactic acid, glucose, fructose, 5-hydroxymethylfurfural (5-HMF),etc. formic acid 189-200 N-acetyl-alpha-glucosaminidase Homo sapiens 126-129 35483153-2 2022 The enhanced ionization of water at subcritical conditions (200 C; 50-100 bar), provides enough acidity for deacetylation of NAG resulting in 80% yield of acetic acid along with traces of formic acid, lactic acid, glucose, fructose, 5-hydroxymethylfurfural (5-HMF),etc. Lactic Acid 202-213 N-acetyl-alpha-glucosaminidase Homo sapiens 126-129 35483153-2 2022 The enhanced ionization of water at subcritical conditions (200 C; 50-100 bar), provides enough acidity for deacetylation of NAG resulting in 80% yield of acetic acid along with traces of formic acid, lactic acid, glucose, fructose, 5-hydroxymethylfurfural (5-HMF),etc. Glucose 215-222 N-acetyl-alpha-glucosaminidase Homo sapiens 126-129 35483153-2 2022 The enhanced ionization of water at subcritical conditions (200 C; 50-100 bar), provides enough acidity for deacetylation of NAG resulting in 80% yield of acetic acid along with traces of formic acid, lactic acid, glucose, fructose, 5-hydroxymethylfurfural (5-HMF),etc. Fructose 224-232 N-acetyl-alpha-glucosaminidase Homo sapiens 126-129 35483153-2 2022 The enhanced ionization of water at subcritical conditions (200 C; 50-100 bar), provides enough acidity for deacetylation of NAG resulting in 80% yield of acetic acid along with traces of formic acid, lactic acid, glucose, fructose, 5-hydroxymethylfurfural (5-HMF),etc. 5-hydroxymethylfurfural 234-257 N-acetyl-alpha-glucosaminidase Homo sapiens 126-129 35483153-2 2022 The enhanced ionization of water at subcritical conditions (200 C; 50-100 bar), provides enough acidity for deacetylation of NAG resulting in 80% yield of acetic acid along with traces of formic acid, lactic acid, glucose, fructose, 5-hydroxymethylfurfural (5-HMF),etc. 5-hydroxymethylfurfural 259-264 N-acetyl-alpha-glucosaminidase Homo sapiens 126-129 35483153-4 2022 A catalyst p-toluenesulfonic acid (p-TsOH) was employed to selectively convert NAG to levulinic acid (LA) via ring opening of 5-HMF previously formed during hydrolysis. 4-toluenesulfonic acid 11-33 N-acetyl-alpha-glucosaminidase Homo sapiens 79-82 35483153-4 2022 A catalyst p-toluenesulfonic acid (p-TsOH) was employed to selectively convert NAG to levulinic acid (LA) via ring opening of 5-HMF previously formed during hydrolysis. 4-toluenesulfonic acid 35-41 N-acetyl-alpha-glucosaminidase Homo sapiens 79-82 35483153-4 2022 A catalyst p-toluenesulfonic acid (p-TsOH) was employed to selectively convert NAG to levulinic acid (LA) via ring opening of 5-HMF previously formed during hydrolysis. levulinic acid 86-100 N-acetyl-alpha-glucosaminidase Homo sapiens 79-82 35483153-6 2022 Subcritical water enables greener conversion of NAG to platform chemicals wherein the selective production can be achieved by tuning the process conditions. Water 12-17 N-acetyl-alpha-glucosaminidase Homo sapiens 48-51 2556907-5 1989 In the patients with MPS IIA and MPS IIIB, the white matter did not show the proper signal intensity, which suggested that myelination was insufficient and that infiltration or deposition of glycosaminoglycan had occurred; this was consistent with the association of these two types with mental retardation. Glycosaminoglycans 191-208 N-acetyl-alpha-glucosaminidase Homo sapiens 33-41 35453363-6 2022 It is known that L-cysteine level is elevated in cells with the Naglu-/- gene mutation and in selected tissues of individuals with MPS IIIB. Cysteine 17-27 N-acetyl-alpha-glucosaminidase Homo sapiens 64-69 35453363-6 2022 It is known that L-cysteine level is elevated in cells with the Naglu-/- gene mutation and in selected tissues of individuals with MPS IIIB. Cysteine 17-27 N-acetyl-alpha-glucosaminidase Homo sapiens 131-139 35453363-7 2022 The level of glutathione and the Naglu-/- cells" antioxidant potential are significantly reduced, as well as the activity of 3-mercaptopyruvate sulfurtransferase (MPST, EC 2.8.1.2) and the level of sulfane sulfur-containing compounds. Hydrogen Sulfide 198-205 N-acetyl-alpha-glucosaminidase Homo sapiens 33-38 35453363-7 2022 The level of glutathione and the Naglu-/- cells" antioxidant potential are significantly reduced, as well as the activity of 3-mercaptopyruvate sulfurtransferase (MPST, EC 2.8.1.2) and the level of sulfane sulfur-containing compounds. Sulfur 206-212 N-acetyl-alpha-glucosaminidase Homo sapiens 33-38 35155448-6 2021 NAGLU is a key enzyme for the degradation of heparan sulfate (HS), and its deficiency could cause lysosomal accumulation and lead to dysfunctions of VECs. Heparitin Sulfate 45-60 N-acetyl-alpha-glucosaminidase Homo sapiens 0-5 35155448-6 2021 NAGLU is a key enzyme for the degradation of heparan sulfate (HS), and its deficiency could cause lysosomal accumulation and lead to dysfunctions of VECs. Heparitin Sulfate 62-64 N-acetyl-alpha-glucosaminidase Homo sapiens 0-5 35157877-7 2022 The amoA-AOA gene abundance, NAG activity, and total carbon (C) content were the main predictors of total N and mineral N accumulated leakage. Nitrogen 106-107 N-acetyl-alpha-glucosaminidase Homo sapiens 29-32 35157877-7 2022 The amoA-AOA gene abundance, NAG activity, and total carbon (C) content were the main predictors of total N and mineral N accumulated leakage. Nitrogen 120-121 N-acetyl-alpha-glucosaminidase Homo sapiens 29-32 35298547-2 2022 Some patients with IC experience a rise in Urinary N-acetyl-beta-D-Glucosaminidase (NAG)/ Creatinine (Cr) ratio, a marker of renal injury, following exercise. Creatinine 102-104 N-acetyl-alpha-glucosaminidase Homo sapiens 84-87 2575679-3 1989 In order to elucidate the relationship between release of these enzymes and renal ischemic injury, we devised an in vitro model of anoxic injuries to renal tubular cells and measured the time-course release of NAG (a lysosomal enzyme), gamma-GTP and LAP (brush border enzymes) at 37 degrees C under five different aerobic and anaerobic conditions (95% O2, 20% O2, 10% O2, 3% O2 and 0% O2). Oxygen 352-354 N-acetyl-alpha-glucosaminidase Homo sapiens 210-213 2575679-3 1989 In order to elucidate the relationship between release of these enzymes and renal ischemic injury, we devised an in vitro model of anoxic injuries to renal tubular cells and measured the time-course release of NAG (a lysosomal enzyme), gamma-GTP and LAP (brush border enzymes) at 37 degrees C under five different aerobic and anaerobic conditions (95% O2, 20% O2, 10% O2, 3% O2 and 0% O2). Oxygen 360-362 N-acetyl-alpha-glucosaminidase Homo sapiens 210-213 2575679-5 1989 In the 3% O2, 10% O2 and 20% O2 groups, NAG, gamma-GTP and LAP were released into the media at a similar rate to that in the 95% O2 group, and anaerobic damage to the renal tubular cells was not observed. Oxygen 18-20 N-acetyl-alpha-glucosaminidase Homo sapiens 40-43 2575679-3 1989 In order to elucidate the relationship between release of these enzymes and renal ischemic injury, we devised an in vitro model of anoxic injuries to renal tubular cells and measured the time-course release of NAG (a lysosomal enzyme), gamma-GTP and LAP (brush border enzymes) at 37 degrees C under five different aerobic and anaerobic conditions (95% O2, 20% O2, 10% O2, 3% O2 and 0% O2). Oxygen 360-362 N-acetyl-alpha-glucosaminidase Homo sapiens 210-213 2575679-3 1989 In order to elucidate the relationship between release of these enzymes and renal ischemic injury, we devised an in vitro model of anoxic injuries to renal tubular cells and measured the time-course release of NAG (a lysosomal enzyme), gamma-GTP and LAP (brush border enzymes) at 37 degrees C under five different aerobic and anaerobic conditions (95% O2, 20% O2, 10% O2, 3% O2 and 0% O2). Oxygen 360-362 N-acetyl-alpha-glucosaminidase Homo sapiens 210-213 2575679-3 1989 In order to elucidate the relationship between release of these enzymes and renal ischemic injury, we devised an in vitro model of anoxic injuries to renal tubular cells and measured the time-course release of NAG (a lysosomal enzyme), gamma-GTP and LAP (brush border enzymes) at 37 degrees C under five different aerobic and anaerobic conditions (95% O2, 20% O2, 10% O2, 3% O2 and 0% O2). Oxygen 360-362 N-acetyl-alpha-glucosaminidase Homo sapiens 210-213 2575679-5 1989 In the 3% O2, 10% O2 and 20% O2 groups, NAG, gamma-GTP and LAP were released into the media at a similar rate to that in the 95% O2 group, and anaerobic damage to the renal tubular cells was not observed. Oxygen 10-12 N-acetyl-alpha-glucosaminidase Homo sapiens 40-43 2575679-5 1989 In the 3% O2, 10% O2 and 20% O2 groups, NAG, gamma-GTP and LAP were released into the media at a similar rate to that in the 95% O2 group, and anaerobic damage to the renal tubular cells was not observed. Oxygen 18-20 N-acetyl-alpha-glucosaminidase Homo sapiens 40-43 2575679-5 1989 In the 3% O2, 10% O2 and 20% O2 groups, NAG, gamma-GTP and LAP were released into the media at a similar rate to that in the 95% O2 group, and anaerobic damage to the renal tubular cells was not observed. Oxygen 18-20 N-acetyl-alpha-glucosaminidase Homo sapiens 40-43 2575679-6 1989 In the 0% O2 group, the NAG in the medium increased from 60 to 180 min at a significantly higher rate than that of the 95% O2 group, and a linear relationship was observed between NAG concentration and incubation time (r = 0.73), although NAG did not increase significantly at 30 min. Oxygen 10-12 N-acetyl-alpha-glucosaminidase Homo sapiens 24-27 2575679-6 1989 In the 0% O2 group, the NAG in the medium increased from 60 to 180 min at a significantly higher rate than that of the 95% O2 group, and a linear relationship was observed between NAG concentration and incubation time (r = 0.73), although NAG did not increase significantly at 30 min. Oxygen 10-12 N-acetyl-alpha-glucosaminidase Homo sapiens 180-183 2575679-6 1989 In the 0% O2 group, the NAG in the medium increased from 60 to 180 min at a significantly higher rate than that of the 95% O2 group, and a linear relationship was observed between NAG concentration and incubation time (r = 0.73), although NAG did not increase significantly at 30 min. Oxygen 10-12 N-acetyl-alpha-glucosaminidase Homo sapiens 180-183 3255304-1 1988 In this new procedure for determining the activity of N-acetyl-beta-D-glucosaminidase (EC 3.2.1.30; NAG) in urine, a new synthetic substrate, 2-chloro-4-nitrophenyl-N-acetyl-beta-D-glucosaminide is used. 2-chloro-4-nitrophenyl-N-acetylglucosaminide 142-194 N-acetyl-alpha-glucosaminidase Homo sapiens 100-103 2782944-5 1989 Four workers had clinically elevated activity of NAG (greater than 4 mU/mg creatinine) in any of their urine collections after baseline. Creatinine 75-85 N-acetyl-alpha-glucosaminidase Homo sapiens 49-52 2782944-7 1989 Dichloropropene air exposure products of greater than 700 mg.min/m3 or excretion of greater than 1.5 mg 3CNAC/d distinguished abnormally high daily excretion of NAG. 1,3-dichloro-1-propene 0-15 N-acetyl-alpha-glucosaminidase Homo sapiens 161-164 2782944-7 1989 Dichloropropene air exposure products of greater than 700 mg.min/m3 or excretion of greater than 1.5 mg 3CNAC/d distinguished abnormally high daily excretion of NAG. 3cnac 104-109 N-acetyl-alpha-glucosaminidase Homo sapiens 161-164 2649143-3 1989 Of the four measures, only urinary NAG and urinary beta 2m showed a strong positive correlation with blood cadmium concentrations (r = 0.49 and 0.43 respectively); NAG showed a weaker correlation with urinary cadmium concentrations (r = 0.35). Cadmium 107-114 N-acetyl-alpha-glucosaminidase Homo sapiens 35-38 2565539-3 1989 The mean NAG value corrected for creatinine in the higher cadmium group (2.95 U/g creatinine) is significantly different from the mean low cadmium group value (0.92 U/g creatinine, p = 0.0083). Cadmium 58-65 N-acetyl-alpha-glucosaminidase Homo sapiens 9-12 2565539-3 1989 The mean NAG value corrected for creatinine in the higher cadmium group (2.95 U/g creatinine) is significantly different from the mean low cadmium group value (0.92 U/g creatinine, p = 0.0083). Creatinine 82-92 N-acetyl-alpha-glucosaminidase Homo sapiens 9-12 2565539-3 1989 The mean NAG value corrected for creatinine in the higher cadmium group (2.95 U/g creatinine) is significantly different from the mean low cadmium group value (0.92 U/g creatinine, p = 0.0083). Creatinine 82-92 N-acetyl-alpha-glucosaminidase Homo sapiens 9-12 2565539-5 1989 NAG and AAP also give significant correlations with cadmium levels in urine (NAG: r = 0.51; p = 0.0001; AAP: r = 0.56; p = 0.0001). Cadmium 52-59 N-acetyl-alpha-glucosaminidase Homo sapiens 0-3 2565539-5 1989 NAG and AAP also give significant correlations with cadmium levels in urine (NAG: r = 0.51; p = 0.0001; AAP: r = 0.56; p = 0.0001). Cadmium 52-59 N-acetyl-alpha-glucosaminidase Homo sapiens 77-80 2565539-8 1989 A dose-response relationship was found between NAG and cadmium and between AAP and cadmium. Cadmium 55-62 N-acetyl-alpha-glucosaminidase Homo sapiens 47-50 2565539-8 1989 A dose-response relationship was found between NAG and cadmium and between AAP and cadmium. Cadmium 83-90 N-acetyl-alpha-glucosaminidase Homo sapiens 47-50 2565539-9 1989 The analysis of this relationship gives estimates of a 10% chance of observing an elevated NAG value at a cadmium level of 6.3 micrograms/g creatinine (8.0 micrograms/l) and a 10% chance of observing an elevated AAP at a cadmium level of 5.0 micrograms/g creatinine (3.4 micrograms/l). Cadmium 106-113 N-acetyl-alpha-glucosaminidase Homo sapiens 91-94 2565539-9 1989 The analysis of this relationship gives estimates of a 10% chance of observing an elevated NAG value at a cadmium level of 6.3 micrograms/g creatinine (8.0 micrograms/l) and a 10% chance of observing an elevated AAP at a cadmium level of 5.0 micrograms/g creatinine (3.4 micrograms/l). Creatinine 140-150 N-acetyl-alpha-glucosaminidase Homo sapiens 91-94 2565539-10 1989 These data indicate elevations of NAG and AAP at urine cadmium levels below the level of 10 micrograms/g creatinine recommended as an upper limit by the 1980 World Health Organization Study Group. Cadmium 55-62 N-acetyl-alpha-glucosaminidase Homo sapiens 34-37 2649143-9 1989 The age adjusted mean urinary NAG excretion showed a significant rise with urinary cadmium of above 3 micrograms/g creatinine. Cadmium 83-90 N-acetyl-alpha-glucosaminidase Homo sapiens 30-33 2649143-9 1989 The age adjusted mean urinary NAG excretion showed a significant rise with urinary cadmium of above 3 micrograms/g creatinine. Creatinine 115-125 N-acetyl-alpha-glucosaminidase Homo sapiens 30-33 2649143-11 1989 With blood cadmium concentrations, the age adjusted mean urinary NAG excretion showed a rise from 1 microgram/l of blood cadmium followed by a plateau between blood cadmium concentrations of 3-10 micrograms/l. Cadmium 11-18 N-acetyl-alpha-glucosaminidase Homo sapiens 65-68 2649143-11 1989 With blood cadmium concentrations, the age adjusted mean urinary NAG excretion showed a rise from 1 microgram/l of blood cadmium followed by a plateau between blood cadmium concentrations of 3-10 micrograms/l. Cadmium 121-128 N-acetyl-alpha-glucosaminidase Homo sapiens 65-68 2649143-11 1989 With blood cadmium concentrations, the age adjusted mean urinary NAG excretion showed a rise from 1 microgram/l of blood cadmium followed by a plateau between blood cadmium concentrations of 3-10 micrograms/l. Cadmium 121-128 N-acetyl-alpha-glucosaminidase Homo sapiens 65-68 2565539-11 1989 Since elevated levels of NAG and AAP in cadmium-exposed workers may reflect chronic renal tubular nephrotoxicity, these findings indicate that cadmium levels below 10 micrograms/g creatinine may be accompanied by subclinical tubular dysfunction, and that WHO guidelines should be interpreted cautiously, particularly with reference to workers who are no longer exposed and may have had higher cadmium body burdens in the past. Cadmium 40-47 N-acetyl-alpha-glucosaminidase Homo sapiens 25-28 2565539-11 1989 Since elevated levels of NAG and AAP in cadmium-exposed workers may reflect chronic renal tubular nephrotoxicity, these findings indicate that cadmium levels below 10 micrograms/g creatinine may be accompanied by subclinical tubular dysfunction, and that WHO guidelines should be interpreted cautiously, particularly with reference to workers who are no longer exposed and may have had higher cadmium body burdens in the past. Cadmium 143-150 N-acetyl-alpha-glucosaminidase Homo sapiens 25-28 2565539-11 1989 Since elevated levels of NAG and AAP in cadmium-exposed workers may reflect chronic renal tubular nephrotoxicity, these findings indicate that cadmium levels below 10 micrograms/g creatinine may be accompanied by subclinical tubular dysfunction, and that WHO guidelines should be interpreted cautiously, particularly with reference to workers who are no longer exposed and may have had higher cadmium body burdens in the past. Cadmium 143-150 N-acetyl-alpha-glucosaminidase Homo sapiens 25-28 3044631-7 1988 Iproplatin appeared marginally more toxic on the basis of elevated NAG and ALP during the second half of the treatment periods compared with the first (P less than 0.01 and less than 0.025, respectively). iproplatin 0-10 N-acetyl-alpha-glucosaminidase Homo sapiens 67-70 3283687-0 1988 [Urinary excretion of N-acetyl-beta-D-glucosaminidase (NAG) and its isoenzyme B as a marker of the nephrotoxicity of gentamicin: re-test from an animal model]. Gentamicins 117-127 N-acetyl-alpha-glucosaminidase Homo sapiens 55-58 3283687-1 1988 A high level of NAG urinary excretion with marked isoenzyme B excretion are commonly considered as an indicator of aminoglycoside nephrotoxicity. Aminoglycosides 115-129 N-acetyl-alpha-glucosaminidase Homo sapiens 16-19 3283687-2 1988 The urinary excretion of NAG following gentamicin treatment was studied in rabbit. Gentamicins 39-49 N-acetyl-alpha-glucosaminidase Homo sapiens 25-28 3283687-8 1988 Surprisingly, the high level of NAG excretion following the administration of gentamicin at 50 mg/kg/j is not accompanied by a marked excretion of isoenzyme B. Gentamicins 78-88 N-acetyl-alpha-glucosaminidase Homo sapiens 32-35 3283687-10 1988 These data indicate that increases in urinary NAG and isoenzyme B excretion following gentamicin treatment in Human are not always reliable indicators of renal tubular cell lysis. Gentamicins 86-96 N-acetyl-alpha-glucosaminidase Homo sapiens 46-49 3756399-6 1986 NAG was spontaneously higher in the patient group and increased significantly after sucrose ingestion in both groups. Sucrose 84-91 N-acetyl-alpha-glucosaminidase Homo sapiens 0-3 2881198-6 1986 NAG and AAP were more frequently elevated during treatment with cyclosporine A (21/29), than with azathioprine (10/23). Cyclosporine 64-78 N-acetyl-alpha-glucosaminidase Homo sapiens 0-3 3264272-3 1988 Increased U-NAG was seen in workers with a U-Hg today of more than 4 micrograms/mmol creat (about 50 micrograms/l: 35 ug/g creat). creat 85-90 N-acetyl-alpha-glucosaminidase Homo sapiens 12-15 3264272-3 1988 Increased U-NAG was seen in workers with a U-Hg today of more than 4 micrograms/mmol creat (about 50 micrograms/l: 35 ug/g creat). creat 123-128 N-acetyl-alpha-glucosaminidase Homo sapiens 12-15 4006900-1 1985 The biosynthesis of alpha-N-acetylglucosaminidase was studied in cultured human kidney carcinoma cells by labeling cells with 35S-methionine, isolation of the enzyme by immunoprecipitation and analysis on gel electrophoresis of the denatured polypeptide(s) and analysis of the native enzyme on linear sucrose gradient centrifugation. 35s-methionine 126-140 N-acetyl-alpha-glucosaminidase Homo sapiens 20-49 3711072-2 1986 In the presence of N-acetyl-D-glucosamine (NAG) and its oligomers [(NAG)n, n = 2 and 3] under the conditions with which about 90% of lysozyme was calculated to form complexes, the formation of Asp-101 modified lysozyme decreased markedly but to different degrees, that is (NAG)3 was the most and NAG the least effective. asp-101 193-200 N-acetyl-alpha-glucosaminidase Homo sapiens 43-46 3886433-4 1985 At physiological levels of ammonia the activation of carbamoyl-phosphate synthetase (EC 6.3.4.16) by N-acetylglutamate (NAG) is important. Ammonia 27-34 N-acetyl-alpha-glucosaminidase Homo sapiens 120-123 3886433-4 1985 At physiological levels of ammonia the activation of carbamoyl-phosphate synthetase (EC 6.3.4.16) by N-acetylglutamate (NAG) is important. N-acetylglutamic acid 101-118 N-acetyl-alpha-glucosaminidase Homo sapiens 120-123 3886433-5 1985 Various levels of NAG corresponded well with changes in the rate of citrulline and urea synthesis. Citrulline 68-78 N-acetyl-alpha-glucosaminidase Homo sapiens 18-21 3886433-5 1985 Various levels of NAG corresponded well with changes in the rate of citrulline and urea synthesis. Urea 83-87 N-acetyl-alpha-glucosaminidase Homo sapiens 18-21 3886433-8 1985 Evidence for arginine in the regulation of NAG synthesis is not as clear as for NAG on carbamoyl phosphate synthetase I. Arginine 13-21 N-acetyl-alpha-glucosaminidase Homo sapiens 43-46 3886433-13 1985 However, it is possible that responses to the effector may vary with time after eating, and it may be this responsiveness that controls the level of NAG and thereby urea synthesis. Urea 165-169 N-acetyl-alpha-glucosaminidase Homo sapiens 149-152 3921297-1 1985 Conditions for assay of alpha-N-acetylglucosaminidase activity in human cultured fibroblasts, cultured amniotic fluid cells, leucocytes, serum, plasma and chorionic villi were studied using the fluorogenic substrate 4-methylumbelliferyl-2-acetamido-2-deoxy-alpha-D-glucopyranoside. 4-methylumbelliferyl 2-acetamido-2-deoxy-beta-D-glucopyranoside 216-280 N-acetyl-alpha-glucosaminidase Homo sapiens 24-53 4006900-1 1985 The biosynthesis of alpha-N-acetylglucosaminidase was studied in cultured human kidney carcinoma cells by labeling cells with 35S-methionine, isolation of the enzyme by immunoprecipitation and analysis on gel electrophoresis of the denatured polypeptide(s) and analysis of the native enzyme on linear sucrose gradient centrifugation. Sucrose 301-308 N-acetyl-alpha-glucosaminidase Homo sapiens 20-49 6494455-5 1984 The ionic, hyperosmolaric megluminamidotrizoate++ caused significantly elevated enzymuria of NAG, AP, and LDH (P less than 0.01) following tubular irrigation, whereas iopamidol showed no significant enzymuria. megluminamidotrizoate++ 26-49 N-acetyl-alpha-glucosaminidase Homo sapiens 93-96 6240800-11 1984 Although the patient was not examined enzymatically, the structure of urinary GAG suggested a defect of alpha-N-acetylglucosaminidase in the patient. Glycosaminoglycans 78-81 N-acetyl-alpha-glucosaminidase Homo sapiens 104-133 6760389-8 1982 Nine out of 11 patients treated with CyA showed one or more increases in NAG excretion, but the number of such episodes did not differ between patients with CyA serum concentrations below 500 ng/ml and those with levels above 500 ng/ml. Cyclosporine 37-40 N-acetyl-alpha-glucosaminidase Homo sapiens 73-76 6547193-3 1984 For the building blocks of the pseudomurein sugar strands, i.e. for the monosaccharides beta-D-N-acetylglucosamine (NAG) and alpha-L-N-acetyltalosaminuronic acid (NAT), both in C1 ring conformation, as well as for their 1,3 and 1,4 linked disaccharides, the favoured conformations were obtained. pseudomurein sugar 31-49 N-acetyl-alpha-glucosaminidase Homo sapiens 88-114 6547193-3 1984 For the building blocks of the pseudomurein sugar strands, i.e. for the monosaccharides beta-D-N-acetylglucosamine (NAG) and alpha-L-N-acetyltalosaminuronic acid (NAT), both in C1 ring conformation, as well as for their 1,3 and 1,4 linked disaccharides, the favoured conformations were obtained. pseudomurein sugar 31-49 N-acetyl-alpha-glucosaminidase Homo sapiens 116-119 6547193-3 1984 For the building blocks of the pseudomurein sugar strands, i.e. for the monosaccharides beta-D-N-acetylglucosamine (NAG) and alpha-L-N-acetyltalosaminuronic acid (NAT), both in C1 ring conformation, as well as for their 1,3 and 1,4 linked disaccharides, the favoured conformations were obtained. Monosaccharides 72-87 N-acetyl-alpha-glucosaminidase Homo sapiens 88-114 6547193-3 1984 For the building blocks of the pseudomurein sugar strands, i.e. for the monosaccharides beta-D-N-acetylglucosamine (NAG) and alpha-L-N-acetyltalosaminuronic acid (NAT), both in C1 ring conformation, as well as for their 1,3 and 1,4 linked disaccharides, the favoured conformations were obtained. Monosaccharides 72-87 N-acetyl-alpha-glucosaminidase Homo sapiens 116-119 6547193-3 1984 For the building blocks of the pseudomurein sugar strands, i.e. for the monosaccharides beta-D-N-acetylglucosamine (NAG) and alpha-L-N-acetyltalosaminuronic acid (NAT), both in C1 ring conformation, as well as for their 1,3 and 1,4 linked disaccharides, the favoured conformations were obtained. Disaccharides 239-252 N-acetyl-alpha-glucosaminidase Homo sapiens 88-114 6547193-4 1984 The helical parameters of sugar strands of both linkage types, which describe the regular structure of the corresponding polysaccharides, poly-(1,3-NAT-NAG) and poly-(1,4-NAT-NAG), were calculated. Sugars 26-31 N-acetyl-alpha-glucosaminidase Homo sapiens 152-155 6547193-4 1984 The helical parameters of sugar strands of both linkage types, which describe the regular structure of the corresponding polysaccharides, poly-(1,3-NAT-NAG) and poly-(1,4-NAT-NAG), were calculated. Sugars 26-31 N-acetyl-alpha-glucosaminidase Homo sapiens 175-178 6547193-5 1984 Both types of polysaccharides poly-(NAG-NAT) considered in this study favoured extended conformations, which in the case of 1,3 linked polymers showed less gain of length per saccharide unit compared to 1,4 linked poly-(NAG-NAT) residues. Polysaccharides 14-29 N-acetyl-alpha-glucosaminidase Homo sapiens 36-39 6547193-5 1984 Both types of polysaccharides poly-(NAG-NAT) considered in this study favoured extended conformations, which in the case of 1,3 linked polymers showed less gain of length per saccharide unit compared to 1,4 linked poly-(NAG-NAT) residues. Polysaccharides 14-29 N-acetyl-alpha-glucosaminidase Homo sapiens 220-223 6547193-5 1984 Both types of polysaccharides poly-(NAG-NAT) considered in this study favoured extended conformations, which in the case of 1,3 linked polymers showed less gain of length per saccharide unit compared to 1,4 linked poly-(NAG-NAT) residues. poly- 30-35 N-acetyl-alpha-glucosaminidase Homo sapiens 36-39 6547193-5 1984 Both types of polysaccharides poly-(NAG-NAT) considered in this study favoured extended conformations, which in the case of 1,3 linked polymers showed less gain of length per saccharide unit compared to 1,4 linked poly-(NAG-NAT) residues. poly- 30-35 N-acetyl-alpha-glucosaminidase Homo sapiens 220-223 6547193-5 1984 Both types of polysaccharides poly-(NAG-NAT) considered in this study favoured extended conformations, which in the case of 1,3 linked polymers showed less gain of length per saccharide unit compared to 1,4 linked poly-(NAG-NAT) residues. Polymers 135-143 N-acetyl-alpha-glucosaminidase Homo sapiens 36-39 6547193-5 1984 Both types of polysaccharides poly-(NAG-NAT) considered in this study favoured extended conformations, which in the case of 1,3 linked polymers showed less gain of length per saccharide unit compared to 1,4 linked poly-(NAG-NAT) residues. Polymers 135-143 N-acetyl-alpha-glucosaminidase Homo sapiens 220-223 6547193-5 1984 Both types of polysaccharides poly-(NAG-NAT) considered in this study favoured extended conformations, which in the case of 1,3 linked polymers showed less gain of length per saccharide unit compared to 1,4 linked poly-(NAG-NAT) residues. poly 14-18 N-acetyl-alpha-glucosaminidase Homo sapiens 36-39 6547193-5 1984 Both types of polysaccharides poly-(NAG-NAT) considered in this study favoured extended conformations, which in the case of 1,3 linked polymers showed less gain of length per saccharide unit compared to 1,4 linked poly-(NAG-NAT) residues. poly 14-18 N-acetyl-alpha-glucosaminidase Homo sapiens 220-223 6547193-6 1984 For a 1,3 linked sugar moiety of pseudomurein every pair of neighbouring peptides attached to glycan chain pointed in favoured conformations approximately to opposite sides of the strands, whereas in a 1,4 linked poly-(NAG-NAT) the peptides protruded approximately to the same side of the glycan moiety. Polysaccharides 289-295 N-acetyl-alpha-glucosaminidase Homo sapiens 219-222 6547193-9 1984 In poly-(1,3-NAG-NAT) the glycan chains possessed a zig-zag-like arrangement, whereas for glycan chains of the murein type relatively flat structures were preferred. Polysaccharides 26-32 N-acetyl-alpha-glucosaminidase Homo sapiens 13-16 6402508-7 1983 When lysosomes deficient in the enzyme alpha-N-acetylglucosaminidase were incubated at 37 degrees C with [3H]acetyl-CoA, tritium was incorporated primarily into glycosaminoglycans. 3h]acetyl-coa 106-119 N-acetyl-alpha-glucosaminidase Homo sapiens 39-68 6402508-7 1983 When lysosomes deficient in the enzyme alpha-N-acetylglucosaminidase were incubated at 37 degrees C with [3H]acetyl-CoA, tritium was incorporated primarily into glycosaminoglycans. Tritium 121-128 N-acetyl-alpha-glucosaminidase Homo sapiens 39-68 6402508-7 1983 When lysosomes deficient in the enzyme alpha-N-acetylglucosaminidase were incubated at 37 degrees C with [3H]acetyl-CoA, tritium was incorporated primarily into glycosaminoglycans. Glycosaminoglycans 161-179 N-acetyl-alpha-glucosaminidase Homo sapiens 39-68 6402508-9 1983 The acetylation of heparan sulfate in alpha-N-acetylglucosaminidase-deficient lysosomes could be stimulated by the addition of 0.5 mM ATP. Heparitin Sulfate 19-34 N-acetyl-alpha-glucosaminidase Homo sapiens 38-67 6402508-9 1983 The acetylation of heparan sulfate in alpha-N-acetylglucosaminidase-deficient lysosomes could be stimulated by the addition of 0.5 mM ATP. Adenosine Triphosphate 134-137 N-acetyl-alpha-glucosaminidase Homo sapiens 38-67 6402508-12 1983 Incorporation of [3H]acetate from [3H]acetyl-CoA into heparan sulfate (by alpha-N-acetylglucosaminidase-deficient lysosomes) and into N-acetylglucosamine (by normal lysosomes) showed a similar concentration dependence. [3h]acetate 17-28 N-acetyl-alpha-glucosaminidase Homo sapiens 74-103 6402508-12 1983 Incorporation of [3H]acetate from [3H]acetyl-CoA into heparan sulfate (by alpha-N-acetylglucosaminidase-deficient lysosomes) and into N-acetylglucosamine (by normal lysosomes) showed a similar concentration dependence. [3h]acetyl-coa 34-48 N-acetyl-alpha-glucosaminidase Homo sapiens 74-103 6402508-12 1983 Incorporation of [3H]acetate from [3H]acetyl-CoA into heparan sulfate (by alpha-N-acetylglucosaminidase-deficient lysosomes) and into N-acetylglucosamine (by normal lysosomes) showed a similar concentration dependence. Heparitin Sulfate 54-69 N-acetyl-alpha-glucosaminidase Homo sapiens 74-103 6421152-1 1984 The biosynthesis of alpha-N-acetylglucosaminidase in normal and Sanfilippo B fibroblasts was studied by labeling cells with [35S]methionine and isolation of the enzyme by immunoprecipitation. Sulfur-35 125-128 N-acetyl-alpha-glucosaminidase Homo sapiens 20-49 6421152-1 1984 The biosynthesis of alpha-N-acetylglucosaminidase in normal and Sanfilippo B fibroblasts was studied by labeling cells with [35S]methionine and isolation of the enzyme by immunoprecipitation. Methionine 129-139 N-acetyl-alpha-glucosaminidase Homo sapiens 20-49 6127169-4 1982 There was a significant increase in the urinary excretion of both enzymes (AAP and NAG) within 2 days of cis-platinum administration (NAG P less than 0.05 and AAP P less than 0.07). Cisplatin 105-117 N-acetyl-alpha-glucosaminidase Homo sapiens 83-86 7171913-3 1982 However, a small number of lithium-treated patients may have evidence of renal damage, identifiable by NAG assay. Lithium 27-34 N-acetyl-alpha-glucosaminidase Homo sapiens 103-106 6802523-0 1982 Detection of the Sanfilippo type B syndrome using radiolabelled oligosaccharides as substrates for the estimation of alpha-N-acetylglucosaminidase. Oligosaccharides 64-80 N-acetyl-alpha-glucosaminidase Homo sapiens 117-146 6802523-4 1982 Alpha-N-Acetylglucosaminidase activity assessed with GlcNAc-IdOA was 12 times higher than the values obtained using GlcNAc-Ido, GlcNAc-anIdo and GlcNAc-Ido(OS). 2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose 53-59 N-acetyl-alpha-glucosaminidase Homo sapiens 0-29 6802523-4 1982 Alpha-N-Acetylglucosaminidase activity assessed with GlcNAc-IdOA was 12 times higher than the values obtained using GlcNAc-Ido, GlcNAc-anIdo and GlcNAc-Ido(OS). Iduronic Acid 60-64 N-acetyl-alpha-glucosaminidase Homo sapiens 0-29 6802523-6 1982 These results demonstrate that a C6 carboxyl group on the adjacent residue to the N-acetylglucosaminide moiety is an important structural requirement in the mechanism of action or binding of alpha-N-acetylglucosaminidase toward alpha-linked N-acetylglucosaminide residues. n-acetylglucosaminide 82-103 N-acetyl-alpha-glucosaminidase Homo sapiens 191-220 6802523-6 1982 These results demonstrate that a C6 carboxyl group on the adjacent residue to the N-acetylglucosaminide moiety is an important structural requirement in the mechanism of action or binding of alpha-N-acetylglucosaminidase toward alpha-linked N-acetylglucosaminide residues. n-acetylglucosaminide 241-262 N-acetyl-alpha-glucosaminidase Homo sapiens 191-220 6802523-9 1982 Alpha-N-Acetylglucosaminidase activity in leucocyte and fibroblast homogenates assayed using GlcNAc-IdOA as substrate clearly distinguished Sanfilippo B patients from normal controls, and Sanfilippo A, C and D patients. 2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose 93-99 N-acetyl-alpha-glucosaminidase Homo sapiens 0-29 6127169-4 1982 There was a significant increase in the urinary excretion of both enzymes (AAP and NAG) within 2 days of cis-platinum administration (NAG P less than 0.05 and AAP P less than 0.07). Cisplatin 105-117 N-acetyl-alpha-glucosaminidase Homo sapiens 134-137 114170-2 1979 Adsorptive endocytosis of alpha-N-acetylglucosaminidase from human urine by isolated rat hepatocytes is inhibited by glycoproteins, polysaccharides and sugars that are known to bind to cell-surface receptors specific for either terminal galactose/N-acetylgalactosamine residues, terminal mannose residues or mannose 6-phosphate residues. Polysaccharides 132-147 N-acetyl-alpha-glucosaminidase Homo sapiens 26-55 7151635-4 1982 The effect of the aminoglycoside on the kidney was studied both by monitoring serum creatinine and the urinary elimination of the lysosomal enzyme N-acetylglucosaminidase (NAG). Aminoglycosides 18-32 N-acetyl-alpha-glucosaminidase Homo sapiens 172-175 7151635-6 1982 A transient elevation was found in NAG urinary excretion in the neonates treated with amikacin. Amikacin 86-94 N-acetyl-alpha-glucosaminidase Homo sapiens 35-38 7329141-2 1981 Urine N-Acetyl-b-d-glucosaminidase (NAG) was expressed in units/mg creatinine in urine. Creatinine 67-77 N-acetyl-alpha-glucosaminidase Homo sapiens 6-34 7329141-2 1981 Urine N-Acetyl-b-d-glucosaminidase (NAG) was expressed in units/mg creatinine in urine. Creatinine 67-77 N-acetyl-alpha-glucosaminidase Homo sapiens 36-39 7324477-1 1981 The urinary excretion of N-acetyl-beta-glucosaminade (NAG) and alanine aminopeptidase (AAP) was measured as an indicator for nephrotoxicity to neomycin and gentamycin in patients after colorectal surgery. Neomycin 143-151 N-acetyl-alpha-glucosaminidase Homo sapiens 25-52 114170-2 1979 Adsorptive endocytosis of alpha-N-acetylglucosaminidase from human urine by isolated rat hepatocytes is inhibited by glycoproteins, polysaccharides and sugars that are known to bind to cell-surface receptors specific for either terminal galactose/N-acetylgalactosamine residues, terminal mannose residues or mannose 6-phosphate residues. Sugars 152-158 N-acetyl-alpha-glucosaminidase Homo sapiens 26-55 114170-2 1979 Adsorptive endocytosis of alpha-N-acetylglucosaminidase from human urine by isolated rat hepatocytes is inhibited by glycoproteins, polysaccharides and sugars that are known to bind to cell-surface receptors specific for either terminal galactose/N-acetylgalactosamine residues, terminal mannose residues or mannose 6-phosphate residues. Galactose 237-246 N-acetyl-alpha-glucosaminidase Homo sapiens 26-55 114170-2 1979 Adsorptive endocytosis of alpha-N-acetylglucosaminidase from human urine by isolated rat hepatocytes is inhibited by glycoproteins, polysaccharides and sugars that are known to bind to cell-surface receptors specific for either terminal galactose/N-acetylgalactosamine residues, terminal mannose residues or mannose 6-phosphate residues. Acetylgalactosamine 249-268 N-acetyl-alpha-glucosaminidase Homo sapiens 26-55 114170-2 1979 Adsorptive endocytosis of alpha-N-acetylglucosaminidase from human urine by isolated rat hepatocytes is inhibited by glycoproteins, polysaccharides and sugars that are known to bind to cell-surface receptors specific for either terminal galactose/N-acetylgalactosamine residues, terminal mannose residues or mannose 6-phosphate residues. Mannose 288-295 N-acetyl-alpha-glucosaminidase Homo sapiens 26-55 114170-2 1979 Adsorptive endocytosis of alpha-N-acetylglucosaminidase from human urine by isolated rat hepatocytes is inhibited by glycoproteins, polysaccharides and sugars that are known to bind to cell-surface receptors specific for either terminal galactose/N-acetylgalactosamine residues, terminal mannose residues or mannose 6-phosphate residues. mannose-6-phosphate 308-327 N-acetyl-alpha-glucosaminidase Homo sapiens 26-55 114170-3 1979 Recognition of alpha-N-acetylglucosaminidase by a cell-surface receptor specific for terminal galactose/N-acetylgalactosamine residues is supported by the observations (a) that neuraminidase pretreatment of the enzyme enhances endocytosis, (b) that beta-galactosidase treatment decreases endocytosis and (c) that neuraminidase pretreatment of hepatocytes decreases alpha-N-acetylglucosaminidase endocytosis. Galactose 94-103 N-acetyl-alpha-glucosaminidase Homo sapiens 15-44 114170-3 1979 Recognition of alpha-N-acetylglucosaminidase by a cell-surface receptor specific for terminal galactose/N-acetylgalactosamine residues is supported by the observations (a) that neuraminidase pretreatment of the enzyme enhances endocytosis, (b) that beta-galactosidase treatment decreases endocytosis and (c) that neuraminidase pretreatment of hepatocytes decreases alpha-N-acetylglucosaminidase endocytosis. Galactose 94-103 N-acetyl-alpha-glucosaminidase Homo sapiens 365-394 114170-4 1979 Recognition of alpha-N-acetylglucosaminidase via receptors recognizing mannose 6-phosphate residues is lost after treatment of the enzyme with alkaline phosphatase and endoglucosaminidase H. The effect of endoglucosaminidase H supports the view that the mannose 6-phosphate residues reside in N-glycosidically linked oligosaccharide side chains of the high-mannose type. mannose-6-phosphate 71-90 N-acetyl-alpha-glucosaminidase Homo sapiens 15-44 114170-4 1979 Recognition of alpha-N-acetylglucosaminidase via receptors recognizing mannose 6-phosphate residues is lost after treatment of the enzyme with alkaline phosphatase and endoglucosaminidase H. The effect of endoglucosaminidase H supports the view that the mannose 6-phosphate residues reside in N-glycosidically linked oligosaccharide side chains of the high-mannose type. mannose-6-phosphate 254-273 N-acetyl-alpha-glucosaminidase Homo sapiens 15-44 114170-4 1979 Recognition of alpha-N-acetylglucosaminidase via receptors recognizing mannose 6-phosphate residues is lost after treatment of the enzyme with alkaline phosphatase and endoglucosaminidase H. The effect of endoglucosaminidase H supports the view that the mannose 6-phosphate residues reside in N-glycosidically linked oligosaccharide side chains of the high-mannose type. glycosidically 295-309 N-acetyl-alpha-glucosaminidase Homo sapiens 15-44 114170-4 1979 Recognition of alpha-N-acetylglucosaminidase via receptors recognizing mannose 6-phosphate residues is lost after treatment of the enzyme with alkaline phosphatase and endoglucosaminidase H. The effect of endoglucosaminidase H supports the view that the mannose 6-phosphate residues reside in N-glycosidically linked oligosaccharide side chains of the high-mannose type. Oligosaccharides 317-332 N-acetyl-alpha-glucosaminidase Homo sapiens 15-44 114170-4 1979 Recognition of alpha-N-acetylglucosaminidase via receptors recognizing mannose 6-phosphate residues is lost after treatment of the enzyme with alkaline phosphatase and endoglucosaminidase H. The effect of endoglucosaminidase H supports the view that the mannose 6-phosphate residues reside in N-glycosidically linked oligosaccharide side chains of the high-mannose type. Mannose 71-78 N-acetyl-alpha-glucosaminidase Homo sapiens 15-44 114170-5 1979 The weak inhibition of endocytosis produced by compounds known to interact with cell-surface receptors specific for mannose residues suggests that this recognition system plays only a minor role in the endocytosis of lysosomal alpha-N-acetylglucosaminidase by hepatocytes. Mannose 116-123 N-acetyl-alpha-glucosaminidase Homo sapiens 227-256 102578-1 1978 alpha-N-Acetylglucosaminidase (EC 3.2.1.50) was purified from human placenta by a four-step procedure including ammonium sulfate precipitation, affinity chromatography with immobilized antibodies against urinary alpha-N-acetylglucosaminidase, gel chromatography and discontinuous gel electrophoresis with a 30% recovery and 26 300-fold purification. Ammonium Sulfate 112-128 N-acetyl-alpha-glucosaminidase Homo sapiens 0-29 428391-0 1979 Isolation and characterization of phosphorylated oligosaccharides from alpha-N-acetylglucosaminidase that are recognized by cell-surface receptors. Oligosaccharides 49-65 N-acetyl-alpha-glucosaminidase Homo sapiens 71-100 428391-9 1979 Loss of alpha-N-acetylglucosaminidase endocytosis after treatment with endoglucosaminidase H indicated that the recognition site of alpha-N-acetylglucosaminidase is located on N-glycosidically linked oligosaccharides of the high mannose type. Nitrogen 14-15 N-acetyl-alpha-glucosaminidase Homo sapiens 132-161 428391-9 1979 Loss of alpha-N-acetylglucosaminidase endocytosis after treatment with endoglucosaminidase H indicated that the recognition site of alpha-N-acetylglucosaminidase is located on N-glycosidically linked oligosaccharides of the high mannose type. linked oligosaccharides 193-216 N-acetyl-alpha-glucosaminidase Homo sapiens 8-37 428391-9 1979 Loss of alpha-N-acetylglucosaminidase endocytosis after treatment with endoglucosaminidase H indicated that the recognition site of alpha-N-acetylglucosaminidase is located on N-glycosidically linked oligosaccharides of the high mannose type. linked oligosaccharides 193-216 N-acetyl-alpha-glucosaminidase Homo sapiens 132-161 428391-9 1979 Loss of alpha-N-acetylglucosaminidase endocytosis after treatment with endoglucosaminidase H indicated that the recognition site of alpha-N-acetylglucosaminidase is located on N-glycosidically linked oligosaccharides of the high mannose type. Mannose 229-236 N-acetyl-alpha-glucosaminidase Homo sapiens 8-37 428391-9 1979 Loss of alpha-N-acetylglucosaminidase endocytosis after treatment with endoglucosaminidase H indicated that the recognition site of alpha-N-acetylglucosaminidase is located on N-glycosidically linked oligosaccharides of the high mannose type. Mannose 229-236 N-acetyl-alpha-glucosaminidase Homo sapiens 132-161 428391-10 1979 Acidic oligosaccharides with an average molecular weight of 2200 were liberated from alpha-N-acetylglucosaminidase by endoglucosaminidase H. These oligosaccharides were susceptible to degradation by alkaline phosphatase, alpha-mannosidase and beta-N-acetylglucosaminidase. Oligosaccharides 7-23 N-acetyl-alpha-glucosaminidase Homo sapiens 85-114 102578-6 1978 Placenta alpha-N-acetylglucosaminidase has an apparent molecular weight of 304 000 and contains 23.4% carbohydrate consisting of glucose, galactose, mannose, hexosamines and neuraminic acid. Carbohydrates 102-114 N-acetyl-alpha-glucosaminidase Homo sapiens 9-38 102578-6 1978 Placenta alpha-N-acetylglucosaminidase has an apparent molecular weight of 304 000 and contains 23.4% carbohydrate consisting of glucose, galactose, mannose, hexosamines and neuraminic acid. Glucose 129-136 N-acetyl-alpha-glucosaminidase Homo sapiens 9-38 102578-6 1978 Placenta alpha-N-acetylglucosaminidase has an apparent molecular weight of 304 000 and contains 23.4% carbohydrate consisting of glucose, galactose, mannose, hexosamines and neuraminic acid. Galactose 138-147 N-acetyl-alpha-glucosaminidase Homo sapiens 9-38 102578-6 1978 Placenta alpha-N-acetylglucosaminidase has an apparent molecular weight of 304 000 and contains 23.4% carbohydrate consisting of glucose, galactose, mannose, hexosamines and neuraminic acid. Mannose 149-156 N-acetyl-alpha-glucosaminidase Homo sapiens 9-38 102578-6 1978 Placenta alpha-N-acetylglucosaminidase has an apparent molecular weight of 304 000 and contains 23.4% carbohydrate consisting of glucose, galactose, mannose, hexosamines and neuraminic acid. Hexosamines 158-169 N-acetyl-alpha-glucosaminidase Homo sapiens 9-38 102578-6 1978 Placenta alpha-N-acetylglucosaminidase has an apparent molecular weight of 304 000 and contains 23.4% carbohydrate consisting of glucose, galactose, mannose, hexosamines and neuraminic acid. Neuraminic Acids 174-189 N-acetyl-alpha-glucosaminidase Homo sapiens 9-38 102578-7 1978 Gel electrophoresis in the presence of 0.1% sodium dodecylsulfate separated placenta alpha-N-acetylglucosaminidase into subunits with molecular weights of 86 500 and 81 000. Sodium Dodecyl Sulfate 44-65 N-acetyl-alpha-glucosaminidase Homo sapiens 85-114 646806-3 1978 The inhibition of alpha-N-acetylglucosaminidase endocytosis by mannose, p-nitrophenyl alpha-d-mannoside and mannose 6-phosphate was shown to be competitive. Mannose 63-70 N-acetyl-alpha-glucosaminidase Homo sapiens 18-47 646806-3 1978 The inhibition of alpha-N-acetylglucosaminidase endocytosis by mannose, p-nitrophenyl alpha-d-mannoside and mannose 6-phosphate was shown to be competitive. p-nitrophenyl alpha-d-mannoside 72-103 N-acetyl-alpha-glucosaminidase Homo sapiens 18-47 646806-3 1978 The inhibition of alpha-N-acetylglucosaminidase endocytosis by mannose, p-nitrophenyl alpha-d-mannoside and mannose 6-phosphate was shown to be competitive. mannose-6-phosphate 108-127 N-acetyl-alpha-glucosaminidase Homo sapiens 18-47 646806-9 1978 Endocytosis of ;low-uptake" forms of alpha-N-acetylglucosaminidase and alpha-mannosidase was likewise susceptible to inhibition by sugar phosphates and by alkaline phosphatase treatment, suggesting that ;low-uptake" forms are either contaminated with ;high-uptake" forms or are internalized via the same route as ;high-uptake" forms. Sugar Phosphates 131-147 N-acetyl-alpha-glucosaminidase Homo sapiens 37-66 33899395-13 2021 Agricultural land use significantly affected the stoichiometry of C:N:P acquiring enzymes in soils by reducing the activity of N-degrading enzymes relative, resulting in the increases of BG:NAG and the decreases of NAG:AP. Nitrogen 68-69 N-acetyl-alpha-glucosaminidase Homo sapiens 190-193 923593-10 1977 Sodium periodate treatment reduces the alpha-N-acetylglucosaminidase recognition by fibroblasts and suggests that the recognition sites on the enzyme are associated with its carbohydrate moiety. metaperiodate 0-16 N-acetyl-alpha-glucosaminidase Homo sapiens 39-68 923593-10 1977 Sodium periodate treatment reduces the alpha-N-acetylglucosaminidase recognition by fibroblasts and suggests that the recognition sites on the enzyme are associated with its carbohydrate moiety. Carbohydrates 174-186 N-acetyl-alpha-glucosaminidase Homo sapiens 39-68 811254-1 1975 We have attempted to detect binding of N-acetylglucosamine (NAG) to alpha-lactalbumin, the B protein of lactose synthetase, under conditions in which binding of NAG to lysozyme, a protein to which alpha-lactalbumin has a significant sequence homology, is observed. Lactose 104-111 N-acetyl-alpha-glucosaminidase Homo sapiens 39-64 811254-1 1975 We have attempted to detect binding of N-acetylglucosamine (NAG) to alpha-lactalbumin, the B protein of lactose synthetase, under conditions in which binding of NAG to lysozyme, a protein to which alpha-lactalbumin has a significant sequence homology, is observed. Lactose 104-111 N-acetyl-alpha-glucosaminidase Homo sapiens 60-63 811254-3 1975 The synthesis of a NAG analogue, N-diazoacetyl-glucosamine (diazoNAG), was carried out, and the molecule was demonstrated to be an active galactose acceptor in the lactose synthetase reaction. n-diazoacetyl-glucosamine 33-58 N-acetyl-alpha-glucosaminidase Homo sapiens 19-22 811254-3 1975 The synthesis of a NAG analogue, N-diazoacetyl-glucosamine (diazoNAG), was carried out, and the molecule was demonstrated to be an active galactose acceptor in the lactose synthetase reaction. diazonag 60-68 N-acetyl-alpha-glucosaminidase Homo sapiens 19-22 811254-3 1975 The synthesis of a NAG analogue, N-diazoacetyl-glucosamine (diazoNAG), was carried out, and the molecule was demonstrated to be an active galactose acceptor in the lactose synthetase reaction. Galactose 138-147 N-acetyl-alpha-glucosaminidase Homo sapiens 19-22 242129-1 1975 Assays for the determination of serum alpha-N-acetylglucosaminidase (EC 3.2.1.50) activity are described employing p-nitrophenyl-N-acetyl-alpha-D-glucosaminide, phenyl-N-acetyl-alpha-D-glucosaminide, and UDP-N-acetylglucosamine as substrates. 4-nitrophenyl-N-acetyl-2-deoxyglucopyranoside 115-159 N-acetyl-alpha-glucosaminidase Homo sapiens 38-67 242129-1 1975 Assays for the determination of serum alpha-N-acetylglucosaminidase (EC 3.2.1.50) activity are described employing p-nitrophenyl-N-acetyl-alpha-D-glucosaminide, phenyl-N-acetyl-alpha-D-glucosaminide, and UDP-N-acetylglucosamine as substrates. phenyl-n-acetyl-alpha-d-glucosaminide 122-159 N-acetyl-alpha-glucosaminidase Homo sapiens 38-67 242129-1 1975 Assays for the determination of serum alpha-N-acetylglucosaminidase (EC 3.2.1.50) activity are described employing p-nitrophenyl-N-acetyl-alpha-D-glucosaminide, phenyl-N-acetyl-alpha-D-glucosaminide, and UDP-N-acetylglucosamine as substrates. Uridine Diphosphate N-Acetylglucosamine 204-227 N-acetyl-alpha-glucosaminidase Homo sapiens 38-67 5253664-5 1969 In addition, the binding to these sites of N-acetyl-D-muramic acid (NAM) and a cell-wall disaccharide, NAG-NAM, have been studied. N-acetylmuramic acid 43-66 N-acetyl-alpha-glucosaminidase Homo sapiens 103-106 5253664-5 1969 In addition, the binding to these sites of N-acetyl-D-muramic acid (NAM) and a cell-wall disaccharide, NAG-NAM, have been studied. Disaccharides 89-101 N-acetyl-alpha-glucosaminidase Homo sapiens 103-106 5253664-7 1969 Binding of synthetic substracts, such as p-nitrophenyl-2-acetamido-4-O-(2-acetamido-2-deoxy-beta-D -glucopyranosyl)-beta-D-glucopyranoside (NAG-Gluc-varphiNO(2)), has also been studied by the magnetic resonance technique described. p-nitrophenyl-2-acetamido-4-o-(2-acetamido-2-deoxy-beta-d -glucopyranosyl)-beta-d-glucopyranoside 41-138 N-acetyl-alpha-glucosaminidase Homo sapiens 140-143 34014949-4 2021 We measured the responses of soil microbial biomass C and N; on soil beta-1,4-glucosidase (BG) and beta-1,4-N-acetylglucosaminidase (NAG) activity; and soil microflora characteristics to N additions gradient with 0 (control), 5 (N5), 10 (N10), and 15 (N15) g N m-2 yr-1. Nitrogen 58-59 N-acetyl-alpha-glucosaminidase Homo sapiens 133-136 33592134-17 2021 Urinary NAG-CR, but not ACR, increased during follow-up. Chromium 12-14 N-acetyl-alpha-glucosaminidase Homo sapiens 8-11 33899395-13 2021 Agricultural land use significantly affected the stoichiometry of C:N:P acquiring enzymes in soils by reducing the activity of N-degrading enzymes relative, resulting in the increases of BG:NAG and the decreases of NAG:AP. Nitrogen 68-69 N-acetyl-alpha-glucosaminidase Homo sapiens 215-218 33839004-1 2021 Mucopolysaccharidosis IIIB (MPS IIIB, Sanfilippo syndrome type B) is caused by a deficiency in alpha-N-acetylglucosaminidase (NAGLU) activity, which leads to the accumulation of heparan sulfate (HS). Heparitin Sulfate 178-193 N-acetyl-alpha-glucosaminidase Homo sapiens 28-36 33729711-7 2022 The effects of different carbon sources, such as glucose, N-acetylglucosamine (NAG), N-acetylgalactosamine (NAGA), and inulin, were compared with results showing that the optimal carbon sources for butyric acid production were NAG, a major component of mucin in the human intestine, and glucose. Carbon 179-185 N-acetyl-alpha-glucosaminidase Homo sapiens 108-111 33713715-8 2021 With respect to Cd and to some extent Cr, beta-2-microglobulin (B2-MG) and N-acetyl-beta-D-glucosaminidase (NAG) are well-established, sensitive, and the most common effect biomarkers to relate Cd or Cr exposure to renal tubular dysfunction. Cadmium 194-196 N-acetyl-alpha-glucosaminidase Homo sapiens 108-111 33713715-8 2021 With respect to Cd and to some extent Cr, beta-2-microglobulin (B2-MG) and N-acetyl-beta-D-glucosaminidase (NAG) are well-established, sensitive, and the most common effect biomarkers to relate Cd or Cr exposure to renal tubular dysfunction. Chromium 200-202 N-acetyl-alpha-glucosaminidase Homo sapiens 108-111 33578883-1 2021 Erroneous conclusions may result from normalization of urine cadmium and N-acetyl-beta-D-glucosaminidase concentrations ([Cd]u and [NAG]u) to the urine creatinine concentration ([cr]u). Creatinine 152-162 N-acetyl-alpha-glucosaminidase Homo sapiens 132-135 33651290-7 2021 Urinary Cd levels were positively correlated with blood Cd levels, urinary 8-OHdG, and NAG levels (r = 0.307, r = 0.185, r = 0.150, p < 0.05), but not correlated with urinary beta2-MG levels (p > 0.05). Cadmium 8-10 N-acetyl-alpha-glucosaminidase Homo sapiens 87-90 33316534-5 2021 UN treatments significantly increased the activity of beta-1,4-glucosidase (BG) but reduced the activities of beta-1,4-N-acetylglucosaminidase (NAG), polyphenol oxidase (PPO), and peroxidase (PER). Nitrogen 1-2 N-acetyl-alpha-glucosaminidase Homo sapiens 144-147 32841436-5 2020 Urine-values of NAG and KIM-1 got related to urinary creatinine. Creatinine 53-63 N-acetyl-alpha-glucosaminidase Homo sapiens 16-19 33409510-1 2021 Aqueous solutions of sodium l-glutamate (NaGlu) in the concentration range 0 < c/M <= 1.90 at 25 C were investigated by dielectric relaxation spectroscopy (DRS) and statistical mechanics (1D-RISM and 3D-RISM calculations) to study the hydration and dynamics of the l-glutamate (Glu-) anion. Sodium Glutamate 21-39 N-acetyl-alpha-glucosaminidase Homo sapiens 41-46 33409510-1 2021 Aqueous solutions of sodium l-glutamate (NaGlu) in the concentration range 0 < c/M <= 1.90 at 25 C were investigated by dielectric relaxation spectroscopy (DRS) and statistical mechanics (1D-RISM and 3D-RISM calculations) to study the hydration and dynamics of the l-glutamate (Glu-) anion. Glutamic Acid 28-39 N-acetyl-alpha-glucosaminidase Homo sapiens 41-46 33372494-3 2021 The results showed that the activities of beta-1,4-N-acetylglucosaminidase (NAG), leucine aminopeptidase (LAP), and alkaline phosphatase (ALP) increased significantly with the increasing years of land abandonment, whereas the activity of beta-1,4-glucosidase (BG) showed the opposite change trend. Nitrogen 51-52 N-acetyl-alpha-glucosaminidase Homo sapiens 76-79 32029103-1 2020 Carbon dots (CDs) were synthesized from p-aminophenol and ethylenediamine via one-step under mild condition and used as a sensitive fluorescent nanoprobe for the activity determination of N-acetyl-beta-d-glucosaminidase (NAG). Carbon 0-6 N-acetyl-alpha-glucosaminidase Homo sapiens 221-224 32578945-0 2020 Untypically mild phenotype of a patient suffering from Sanfilippo syndrome B with the c.638C>T/c.889C>T (p.Pro213Leu/p.Arg297Ter) mutations in the NAGLU gene. pro213leu 107-116 N-acetyl-alpha-glucosaminidase Homo sapiens 147-152 32578945-0 2020 Untypically mild phenotype of a patient suffering from Sanfilippo syndrome B with the c.638C>T/c.889C>T (p.Pro213Leu/p.Arg297Ter) mutations in the NAGLU gene. arg297ter 119-128 N-acetyl-alpha-glucosaminidase Homo sapiens 147-152 32018067-9 2020 Protein content, N-acetyl-b-glucosaminidase (NAG) and myeloperoxidase (MPO) activities were elevated in ocular tissues after disease induction, further decreasing post-treatment with intravitreal thalidomide. Thalidomide 196-207 N-acetyl-alpha-glucosaminidase Homo sapiens 17-43 32018067-9 2020 Protein content, N-acetyl-b-glucosaminidase (NAG) and myeloperoxidase (MPO) activities were elevated in ocular tissues after disease induction, further decreasing post-treatment with intravitreal thalidomide. Thalidomide 196-207 N-acetyl-alpha-glucosaminidase Homo sapiens 45-48 33128529-9 2021 The positive correlation was observed between cadmium exposure and urinary N-acetyl-beta-d-glucosaminidase (NAG) concentrations, and also arsenic and chromium exposure and kidney injury molecule (KIM-1). Cadmium 46-53 N-acetyl-alpha-glucosaminidase Homo sapiens 108-111 31965290-1 2020 INTRODUCTION: Mucopolysaccharidosis (MPS) IIIB is a lysosomal disorder in which a deficiency in alpha-N-acetylglucosaminidase impairs the degradation of heparan sulphate, which accumulates in tissues causing multiple organs dysfunction. Heparitin Sulfate 153-169 N-acetyl-alpha-glucosaminidase Homo sapiens 96-125 32422590-1 2020 Chitin, a long-chain polymer of N-acetyl-D-glucosamine (NAG) and the most abundant natural nitrogen-containing organic material in the world, is far under-utilized than other biomass resources. Chitin 0-6 N-acetyl-alpha-glucosaminidase Homo sapiens 56-59 32422590-1 2020 Chitin, a long-chain polymer of N-acetyl-D-glucosamine (NAG) and the most abundant natural nitrogen-containing organic material in the world, is far under-utilized than other biomass resources. Polymers 21-28 N-acetyl-alpha-glucosaminidase Homo sapiens 56-59 32422590-2 2020 Herein, we demonstrate a highly efficient deoxygenation process to convert chitin monomer, i.e., NAG, into various amines, which are the ubiquitous platform chemicals in chemical industry. Chitin 75-81 N-acetyl-alpha-glucosaminidase Homo sapiens 97-100 32422590-2 2020 Herein, we demonstrate a highly efficient deoxygenation process to convert chitin monomer, i.e., NAG, into various amines, which are the ubiquitous platform chemicals in chemical industry. Amines 115-121 N-acetyl-alpha-glucosaminidase Homo sapiens 97-100 32422590-4 2020 By optimizing the reaction conditions, ~50% yield of various amines was obtained via the selective deoxygenation of NAG. Amines 61-67 N-acetyl-alpha-glucosaminidase Homo sapiens 116-119 31926412-2 2020 Its monomer unit, N-acetyl-D-glucosamine (NAG), contains precious atomic nitrogen and represents a potential feedstock for the manufacture of regenerative organic nitrogen chemicals. Nitrogen 73-81 N-acetyl-alpha-glucosaminidase Homo sapiens 42-45 31926412-2 2020 Its monomer unit, N-acetyl-D-glucosamine (NAG), contains precious atomic nitrogen and represents a potential feedstock for the manufacture of regenerative organic nitrogen chemicals. Nitrogen 163-171 N-acetyl-alpha-glucosaminidase Homo sapiens 42-45 31926412-3 2020 Herein, the conversion of NAG to the platform chemical, 3-acetamido-5-acetylfuran (3A5AF), catalyzed by amino acid ionic liquids, was investigated. 2-acetylfuran 56-81 N-acetyl-alpha-glucosaminidase Homo sapiens 26-29 31926412-3 2020 Herein, the conversion of NAG to the platform chemical, 3-acetamido-5-acetylfuran (3A5AF), catalyzed by amino acid ionic liquids, was investigated. 2-acetylfuran 83-88 N-acetyl-alpha-glucosaminidase Homo sapiens 26-29 32029103-1 2020 Carbon dots (CDs) were synthesized from p-aminophenol and ethylenediamine via one-step under mild condition and used as a sensitive fluorescent nanoprobe for the activity determination of N-acetyl-beta-d-glucosaminidase (NAG). 4-aminophenol 40-53 N-acetyl-alpha-glucosaminidase Homo sapiens 221-224 32029103-2 2020 In this assay, p-nitrophenol was in situ produced from p-nitrophenyl-beta-D-N-acetyl-glucosaminide, which was exclusively hydrolyzed by NAG. 4-nitrophenol 15-28 N-acetyl-alpha-glucosaminidase Homo sapiens 136-139 32029103-2 2020 In this assay, p-nitrophenol was in situ produced from p-nitrophenyl-beta-D-N-acetyl-glucosaminide, which was exclusively hydrolyzed by NAG. 4-nitrophenyl-N-acetyl-2-deoxyglucopyranoside 55-98 N-acetyl-alpha-glucosaminidase Homo sapiens 136-139 31568610-7 2020 According to receiver operating characteristic (ROC) analysis, combining NAG and creatinine showed a significantly increased area under the curve (AUC) compared to creatinine alone (AUC: 0.75 vs 0.87; P < .001). Creatinine 164-174 N-acetyl-alpha-glucosaminidase Homo sapiens 73-76 31622890-7 2020 The U-Cd level in this study was positively correlated with the U-NAG level (r = 0.26, p < 0.01), as the U-Cr level was also positively correlated with the levels of U-NAG, U-RBP, and U-BMG (r = 0.21, 0.33, 0.18, p < 0.01, respectively). u-cd 4-8 N-acetyl-alpha-glucosaminidase Homo sapiens 66-69 31568610-11 2020 NAG presented as an independent AKI predictor beside creatinine, age, the diagnosis of myocardial infarction and mean arterial pressure. Creatinine 53-63 N-acetyl-alpha-glucosaminidase Homo sapiens 0-3 32007031-3 2020 Two residual segments of ABA molecules can interact with one Ag/Cu adatom to form a coordination dimer through the N-Ag/Cu-N coordination bond on different substrates. 4-azidobenzoic acid 25-28 N-acetyl-alpha-glucosaminidase Homo sapiens 115-119 32007031-3 2020 Two residual segments of ABA molecules can interact with one Ag/Cu adatom to form a coordination dimer through the N-Ag/Cu-N coordination bond on different substrates. Copper 64-66 N-acetyl-alpha-glucosaminidase Homo sapiens 115-119 32007031-3 2020 Two residual segments of ABA molecules can interact with one Ag/Cu adatom to form a coordination dimer through the N-Ag/Cu-N coordination bond on different substrates. Copper 120-124 N-acetyl-alpha-glucosaminidase Homo sapiens 115-119 31505350-7 2020 U-NAG levels were significantly negatively associated with the interaction between Cd and Se (B: -0.511, 95% CI: -0.886, -0.136). Cadmium 83-85 N-acetyl-alpha-glucosaminidase Homo sapiens 2-5 31505350-7 2020 U-NAG levels were significantly negatively associated with the interaction between Cd and Se (B: -0.511, 95% CI: -0.886, -0.136). Selenium 90-92 N-acetyl-alpha-glucosaminidase Homo sapiens 2-5 32186110-7 2019 RESULTS: Compared with the results for the dimethyl sulfoxide group, treatment of cells with TDA and emodin showed statistically significant differences in the FITC leakage rate, the apical / basolateral ratio of LDH and GGT, and the secretion of GGT, LDH, NAG and KIM-1. phtiobuzone 93-96 N-acetyl-alpha-glucosaminidase Homo sapiens 257-260 31645877-1 2019 Background: Mucopolysaccharidosis IIIB (MPS IIIB) (Sanfilippo Syndrome Type B; OMIM 252920) is an autosomal recessive metabolic disorder caused by mutations in the NAGLU gene which encode lysosomal enzyme N-acetyl-glucosaminidase, involved in degradation of complex polysaccharide, heparan sulfate. 1-octyl-3-methylimidazolium hexafluorophosphate 79-90 N-acetyl-alpha-glucosaminidase Homo sapiens 40-48 31645877-1 2019 Background: Mucopolysaccharidosis IIIB (MPS IIIB) (Sanfilippo Syndrome Type B; OMIM 252920) is an autosomal recessive metabolic disorder caused by mutations in the NAGLU gene which encode lysosomal enzyme N-acetyl-glucosaminidase, involved in degradation of complex polysaccharide, heparan sulfate. 1-octyl-3-methylimidazolium hexafluorophosphate 79-90 N-acetyl-alpha-glucosaminidase Homo sapiens 164-169 31645877-1 2019 Background: Mucopolysaccharidosis IIIB (MPS IIIB) (Sanfilippo Syndrome Type B; OMIM 252920) is an autosomal recessive metabolic disorder caused by mutations in the NAGLU gene which encode lysosomal enzyme N-acetyl-glucosaminidase, involved in degradation of complex polysaccharide, heparan sulfate. N-acetylchitooligosaccharide 205-213 N-acetyl-alpha-glucosaminidase Homo sapiens 40-48 31645877-1 2019 Background: Mucopolysaccharidosis IIIB (MPS IIIB) (Sanfilippo Syndrome Type B; OMIM 252920) is an autosomal recessive metabolic disorder caused by mutations in the NAGLU gene which encode lysosomal enzyme N-acetyl-glucosaminidase, involved in degradation of complex polysaccharide, heparan sulfate. N-acetylchitooligosaccharide 205-213 N-acetyl-alpha-glucosaminidase Homo sapiens 164-169 31645877-1 2019 Background: Mucopolysaccharidosis IIIB (MPS IIIB) (Sanfilippo Syndrome Type B; OMIM 252920) is an autosomal recessive metabolic disorder caused by mutations in the NAGLU gene which encode lysosomal enzyme N-acetyl-glucosaminidase, involved in degradation of complex polysaccharide, heparan sulfate. Sulfates 290-297 N-acetyl-alpha-glucosaminidase Homo sapiens 40-48 31645877-1 2019 Background: Mucopolysaccharidosis IIIB (MPS IIIB) (Sanfilippo Syndrome Type B; OMIM 252920) is an autosomal recessive metabolic disorder caused by mutations in the NAGLU gene which encode lysosomal enzyme N-acetyl-glucosaminidase, involved in degradation of complex polysaccharide, heparan sulfate. Sulfates 290-297 N-acetyl-alpha-glucosaminidase Homo sapiens 164-169 31590383-9 2019 The false negative rate of urinary DMB ratio using the dye-based method for these 13 patients was 31%, including one MPS I, two MPS IIIB, and one MPS IVA. dimethylmethylene blue 35-38 N-acetyl-alpha-glucosaminidase Homo sapiens 128-136 32186110-7 2019 RESULTS: Compared with the results for the dimethyl sulfoxide group, treatment of cells with TDA and emodin showed statistically significant differences in the FITC leakage rate, the apical / basolateral ratio of LDH and GGT, and the secretion of GGT, LDH, NAG and KIM-1. Emodin 101-107 N-acetyl-alpha-glucosaminidase Homo sapiens 257-260 30657762-7 2019 Similar to neurons and astrocytes, BMN 250 uptake in Sanfilippo B patient fibroblasts is predominantly CI-MPR-mediated, resulting in augmentation of NAGLU activity with doses of enzyme that fall well below the Kuptake (5 nM), which are sufficient to prevent HS accumulation. bmn 250 35-42 N-acetyl-alpha-glucosaminidase Homo sapiens 149-154 31347464-6 2019 Urine NAG index was significantly correlated with urinary fractional excretion of sodium (FENa; rho = 0.76, p < 0.001) and plasma creatinine (rho = 0.74, p = 0.001). Sodium 82-88 N-acetyl-alpha-glucosaminidase Homo sapiens 6-9 31347464-6 2019 Urine NAG index was significantly correlated with urinary fractional excretion of sodium (FENa; rho = 0.76, p < 0.001) and plasma creatinine (rho = 0.74, p = 0.001). fena 90-94 N-acetyl-alpha-glucosaminidase Homo sapiens 6-9 31347464-6 2019 Urine NAG index was significantly correlated with urinary fractional excretion of sodium (FENa; rho = 0.76, p < 0.001) and plasma creatinine (rho = 0.74, p = 0.001). Creatinine 130-140 N-acetyl-alpha-glucosaminidase Homo sapiens 6-9 30920848-4 2019 Results: NAG showed among others significant correlation with N-terminal pro brain natriuretic peptide (NTproBNP), troponin I and creatinine. Creatinine 130-140 N-acetyl-alpha-glucosaminidase Homo sapiens 9-12 31583092-4 2019 Results: Urinary NAG (P = 0.003) and AAP (P = 0.03) following treatment with concomitant fosfomycin were lower than those after treatment with tobramycin and colomycin alone. Fosfomycin 89-99 N-acetyl-alpha-glucosaminidase Homo sapiens 17-20 30635159-1 2019 Mucopolysaccharidosis IIIB is caused by a marked decrease in N-acetyl-alpha-d-glucosaminidase (NAGLU) enzyme activity, which leads to the accumulation of heparan sulfate in key organs, progressive brain atrophy, and neurocognitive decline. Heparitin Sulfate 154-169 N-acetyl-alpha-glucosaminidase Homo sapiens 61-93 30635159-1 2019 Mucopolysaccharidosis IIIB is caused by a marked decrease in N-acetyl-alpha-d-glucosaminidase (NAGLU) enzyme activity, which leads to the accumulation of heparan sulfate in key organs, progressive brain atrophy, and neurocognitive decline. Heparitin Sulfate 154-169 N-acetyl-alpha-glucosaminidase Homo sapiens 95-100 31309128-1 2019 Deficiency in NAGLU disrupts the lysosomal turnover of heparan sulfate (HS), which results in the abnormal accumulation of partially degraded HS in cells and tissues. Heparitin Sulfate 55-70 N-acetyl-alpha-glucosaminidase Homo sapiens 14-19 31309128-1 2019 Deficiency in NAGLU disrupts the lysosomal turnover of heparan sulfate (HS), which results in the abnormal accumulation of partially degraded HS in cells and tissues. Heparitin Sulfate 72-74 N-acetyl-alpha-glucosaminidase Homo sapiens 14-19 31309128-1 2019 Deficiency in NAGLU disrupts the lysosomal turnover of heparan sulfate (HS), which results in the abnormal accumulation of partially degraded HS in cells and tissues. Heparitin Sulfate 142-144 N-acetyl-alpha-glucosaminidase Homo sapiens 14-19 31309128-4 2019 The focus of these studies was to further characterize the ability of NAGLU-IGF2 to clear accumulated HS compared to unmodified NAGLU in primary cellular models of MPS IIIB. Heparitin Sulfate 102-104 N-acetyl-alpha-glucosaminidase Homo sapiens 70-80 31309128-4 2019 The focus of these studies was to further characterize the ability of NAGLU-IGF2 to clear accumulated HS compared to unmodified NAGLU in primary cellular models of MPS IIIB. Heparitin Sulfate 102-104 N-acetyl-alpha-glucosaminidase Homo sapiens 70-75 31309128-5 2019 Here, we establish distinct primary cell models of MPS IIIB with HS accumulation. Heparitin Sulfate 65-67 N-acetyl-alpha-glucosaminidase Homo sapiens 51-59 31309128-8 2019 In contrast, under conditions of limited exposure duration, NAGLU-IGF2 was taken up more rapidly than the unmodified NAGLU into MPS IIIB primary fibroblasts, astrocytes, and cortical neurons, where it efficiently degraded accumulated HS. Heparitin Sulfate 234-236 N-acetyl-alpha-glucosaminidase Homo sapiens 60-70 31309128-8 2019 In contrast, under conditions of limited exposure duration, NAGLU-IGF2 was taken up more rapidly than the unmodified NAGLU into MPS IIIB primary fibroblasts, astrocytes, and cortical neurons, where it efficiently degraded accumulated HS. Heparitin Sulfate 234-236 N-acetyl-alpha-glucosaminidase Homo sapiens 60-65 30848915-1 2019 In microorganisms and plants, N-acetyl-l-glutamate kinase (NAGK) catalyzes the second step in l-arginine synthesis, the phosphorylation of N-Acetyl-l-glutamate (NAG) to give N-acetyl-l-glutamate-5-phosphate. Arginine 94-104 N-acetyl-alpha-glucosaminidase Homo sapiens 139-159 30848915-1 2019 In microorganisms and plants, N-acetyl-l-glutamate kinase (NAGK) catalyzes the second step in l-arginine synthesis, the phosphorylation of N-Acetyl-l-glutamate (NAG) to give N-acetyl-l-glutamate-5-phosphate. Arginine 94-104 N-acetyl-alpha-glucosaminidase Homo sapiens 59-62 30848915-1 2019 In microorganisms and plants, N-acetyl-l-glutamate kinase (NAGK) catalyzes the second step in l-arginine synthesis, the phosphorylation of N-Acetyl-l-glutamate (NAG) to give N-acetyl-l-glutamate-5-phosphate. Arginine 94-104 N-acetyl-alpha-glucosaminidase Homo sapiens 30-50 30848915-6 2019 Lys41 is found to guide phosphate transfer through the interactions with the beta-,gamma-, and gamma-phosphate oxygen atoms of adenosine 5"-triphosphate surrounded by two highly conserved glycine residues (Gly44 and Gly76), while Arg98 helps to position the NAG substrate in the catalytic site, which facilitates the phosphate transfer. Phosphates 24-33 N-acetyl-alpha-glucosaminidase Homo sapiens 258-261 30848915-6 2019 Lys41 is found to guide phosphate transfer through the interactions with the beta-,gamma-, and gamma-phosphate oxygen atoms of adenosine 5"-triphosphate surrounded by two highly conserved glycine residues (Gly44 and Gly76), while Arg98 helps to position the NAG substrate in the catalytic site, which facilitates the phosphate transfer. Oxygen 111-117 N-acetyl-alpha-glucosaminidase Homo sapiens 258-261 30848915-6 2019 Lys41 is found to guide phosphate transfer through the interactions with the beta-,gamma-, and gamma-phosphate oxygen atoms of adenosine 5"-triphosphate surrounded by two highly conserved glycine residues (Gly44 and Gly76), while Arg98 helps to position the NAG substrate in the catalytic site, which facilitates the phosphate transfer. Adenosine Triphosphate 127-152 N-acetyl-alpha-glucosaminidase Homo sapiens 258-261 30848915-6 2019 Lys41 is found to guide phosphate transfer through the interactions with the beta-,gamma-, and gamma-phosphate oxygen atoms of adenosine 5"-triphosphate surrounded by two highly conserved glycine residues (Gly44 and Gly76), while Arg98 helps to position the NAG substrate in the catalytic site, which facilitates the phosphate transfer. Glycine 188-195 N-acetyl-alpha-glucosaminidase Homo sapiens 258-261 30848915-6 2019 Lys41 is found to guide phosphate transfer through the interactions with the beta-,gamma-, and gamma-phosphate oxygen atoms of adenosine 5"-triphosphate surrounded by two highly conserved glycine residues (Gly44 and Gly76), while Arg98 helps to position the NAG substrate in the catalytic site, which facilitates the phosphate transfer. Phosphates 101-110 N-acetyl-alpha-glucosaminidase Homo sapiens 258-261 30238383-11 2019 There were significant associations between elevated glu/Cr and asphyxia or neonatal acute kidney injury, and elevated NAG/Cr and indomethacin use, although these were not confirmed by multivariate analysis. Chromium 123-125 N-acetyl-alpha-glucosaminidase Homo sapiens 119-122 30238383-12 2019 At follow-up, the frequency of elevated NAG/Cr, glu/Cr, UA/Cr, and malb/Cr was reduced but that of elevated Ca/Cr, IgG/Cr, and beta2m/Cr remained similar or increased. Chromium 44-46 N-acetyl-alpha-glucosaminidase Homo sapiens 40-43 30337552-1 2018 N-acetylglutamate synthase deficiency (NAGSD, MIM #237310) is an autosomal recessive disorder of the urea cycle that results from absent or decreased production of N-acetylglutamate (NAG) due to either decreased NAGS gene expression or defective NAGS enzyme. Urea 101-105 N-acetyl-alpha-glucosaminidase Homo sapiens 39-42 30564336-2 2018 Two siblings of a family manifested behavioral abnormalities; hepatosplenomegaly and hypotonia of infantile onset were found to have a novel homozygous frameshift variation, p.Leu280TrpfsTer19 in NAGLU. leu280trpfster19 176-192 N-acetyl-alpha-glucosaminidase Homo sapiens 196-201 30408744-6 2018 RESOURCE DETAILS: Mucopolysaccharidosis IIIB (MPSIII, Sanfilippo syndrome type B) is a pediatric neurodegenerative disorder caused by a deficiency in NAGLU, an enzyme required for lysosomal degradation of heparin sulphate (HS). heparin sulphate 205-221 N-acetyl-alpha-glucosaminidase Homo sapiens 150-155 30408744-6 2018 RESOURCE DETAILS: Mucopolysaccharidosis IIIB (MPSIII, Sanfilippo syndrome type B) is a pediatric neurodegenerative disorder caused by a deficiency in NAGLU, an enzyme required for lysosomal degradation of heparin sulphate (HS). hassio 223-225 N-acetyl-alpha-glucosaminidase Homo sapiens 150-155 30075419-2 2018 The PAMAM dendrimers were modified with L-tryptophan and N-acetyl glucosamine (NAG) for higher drug loading and to utilize GLUT transporters, respectively. Acetylglucosamine 79-82 N-acetyl-alpha-glucosaminidase Homo sapiens 57-77 30337552-2 2018 NAG is essential for the activity of carbamylphosphate synthetase 1 (CPS1), the first and rate-limiting enzyme of the urea cycle. Urea 118-122 N-acetyl-alpha-glucosaminidase Homo sapiens 0-3 30337552-1 2018 N-acetylglutamate synthase deficiency (NAGSD, MIM #237310) is an autosomal recessive disorder of the urea cycle that results from absent or decreased production of N-acetylglutamate (NAG) due to either decreased NAGS gene expression or defective NAGS enzyme. N-acetylglutamic acid 0-17 N-acetyl-alpha-glucosaminidase Homo sapiens 39-42 29445029-13 2018 The decrease in GFRcysC and increase in N-acetyl-ss-glucosaminidase (NAG) and creatinine demonstrate that these biomarkers can quantify cisplatin glomerular and proximal tubular toxicity. Cisplatin 136-145 N-acetyl-alpha-glucosaminidase Homo sapiens 40-67 30205615-3 2018 In this study, natural N-acetyl-d-glucosamine (NAG) was prepared from liquefied chitin. Acetylglucosamine 23-45 N-acetyl-alpha-glucosaminidase Homo sapiens 47-50 30205615-3 2018 In this study, natural N-acetyl-d-glucosamine (NAG) was prepared from liquefied chitin. Chitin 80-86 N-acetyl-alpha-glucosaminidase Homo sapiens 47-50 30205615-7 2018 Furthermore, NAG supplementation significantly lowered alkaline phosphatase levels and increased calcium content in the serum of ovariectomized rats. Calcium 97-104 N-acetyl-alpha-glucosaminidase Homo sapiens 13-16 30205615-9 2018 Moreover, NAG effectively protected osteoblasts from oxidative damage induced by hydrogen peroxide. Hydrogen Peroxide 81-98 N-acetyl-alpha-glucosaminidase Homo sapiens 10-13 29998700-8 2018 RDA analysis showed that soil carbon and nitrogen contents had significant positive relationships with the activities of BG and NAG in the 0-20 cm soil profiles, however, negative relationships were observed in the 20-40 cm soil profiles. Carbon 30-36 N-acetyl-alpha-glucosaminidase Homo sapiens 128-131 29998700-8 2018 RDA analysis showed that soil carbon and nitrogen contents had significant positive relationships with the activities of BG and NAG in the 0-20 cm soil profiles, however, negative relationships were observed in the 20-40 cm soil profiles. Nitrogen 41-49 N-acetyl-alpha-glucosaminidase Homo sapiens 128-131 30182584-6 2018 The results showed that higher levels of N addition significantly decreased dehydrogenase (DHA) and beta-1,4-N-acetylglucosaminidase (NAG) activities by 22.3% and 12.5%, respectively. Nitrogen 41-42 N-acetyl-alpha-glucosaminidase Homo sapiens 100-132 30182584-6 2018 The results showed that higher levels of N addition significantly decreased dehydrogenase (DHA) and beta-1,4-N-acetylglucosaminidase (NAG) activities by 22.3% and 12.5%, respectively. Nitrogen 41-42 N-acetyl-alpha-glucosaminidase Homo sapiens 134-137 29979746-6 2018 To address this problem, we measured enzymatic activities of 164 NAGLU missense VUS in the ExAC dataset and developed a statistical framework for estimating disease incidence with associated confidence intervals. 3-[(3~{a}~{S},4~{S},6~{a}~{R})-4-carboxy-2,3,4,5,6,6~{a}-hexahydro-1~{H}-pyrrolo[2,3-c]pyrrol-3~{a}-yl]propyl-$l^{3}-oxidanyl-bis(oxidanyl)boranuide 80-83 N-acetyl-alpha-glucosaminidase Homo sapiens 65-70 29979746-7 2018 We found that 25% of VUS decreased the activity of NAGLU to levels consistent with Sanfilippo Type B pathogenic alleles. 3-[(3~{a}~{S},4~{S},6~{a}~{R})-4-carboxy-2,3,4,5,6,6~{a}-hexahydro-1~{H}-pyrrolo[2,3-c]pyrrol-3~{a}-yl]propyl-$l^{3}-oxidanyl-bis(oxidanyl)boranuide 21-24 N-acetyl-alpha-glucosaminidase Homo sapiens 51-56 29445029-13 2018 The decrease in GFRcysC and increase in N-acetyl-ss-glucosaminidase (NAG) and creatinine demonstrate that these biomarkers can quantify cisplatin glomerular and proximal tubular toxicity. Cisplatin 136-145 N-acetyl-alpha-glucosaminidase Homo sapiens 69-72 28836185-1 2018 BACKGROUND: In the severe neurodegenerative disorder mucopolysaccharidosis type IIIB (MPSIIIB or Sanfilippo disease type B), deficiency of the lysosomal enzyme N-acetyl-alpha-glucosaminidase (NAGLU) results in accumulation of heparan sulfate. Heparitin Sulfate 226-241 N-acetyl-alpha-glucosaminidase Homo sapiens 160-190 29557043-9 2018 In agreement with previous studies, environmental Cd pollution resulted in elevated Cd accumulation in the bodies of children, and it increased the concentration of NAG in their urine. Cadmium 50-52 N-acetyl-alpha-glucosaminidase Homo sapiens 165-168 29557043-10 2018 Similarly, environmental Cd pollution increased NAG and BMG in the urine of adults. Cadmium 25-27 N-acetyl-alpha-glucosaminidase Homo sapiens 48-51 29557043-11 2018 Multivariate models showed that the urinary excretion of BMG, RBP, and NAG was positively associated with Cd levels in the urine of both children and adults. Cadmium 106-108 N-acetyl-alpha-glucosaminidase Homo sapiens 71-74 29557043-12 2018 The reference thresholds of U-Cd in relation to elevated U-BMG, U-RBP, and U-NAG were higher in children than adults after standardization for other covariates. u-cd 28-32 N-acetyl-alpha-glucosaminidase Homo sapiens 77-80 29881562-1 2018 Homozygous or compound heterozygous mutation in the gene encoding N-alpha-acetylglucosaminidase (NAGLU) on chromosome 17q21 results in Sanfilippo B, resulting in excess accumulation of intralysosomal glycosaminoglycans (mucopolysaccharides) in various tissues. Glycosaminoglycans 220-239 N-acetyl-alpha-glucosaminidase Homo sapiens 66-95 29881562-1 2018 Homozygous or compound heterozygous mutation in the gene encoding N-alpha-acetylglucosaminidase (NAGLU) on chromosome 17q21 results in Sanfilippo B, resulting in excess accumulation of intralysosomal glycosaminoglycans (mucopolysaccharides) in various tissues. Glycosaminoglycans 220-239 N-acetyl-alpha-glucosaminidase Homo sapiens 97-102 28692093-0 2017 Chemoselective ligation reaction of N-acetylglucosamine (NAG) with hydrazide functional probes to determine galactosyltransferase activity by MALDI mass spectrometry. Acetylglucosamine 36-55 N-acetyl-alpha-glucosaminidase Homo sapiens 57-60 28939127-8 2017 A significant and positive correlation was found between urinary melamine concentration and urinary NAG levels (Spearman correlation coefficient, r = 0.157, p = 0.006, n = 309). melamine 65-73 N-acetyl-alpha-glucosaminidase Homo sapiens 100-103 28939127-10 2017 In this group, patients with the highest quartile of urinary melamine concentration had a 3.95-fold risk (95% confidence interval = 1.43-10.94) of high NAG levels (dichotomized by median), compared to the lowest quartile after adjustment. melamine 61-69 N-acetyl-alpha-glucosaminidase Homo sapiens 152-155 28939127-12 2017 In conclusion, urinary melamine is significantly associated with urinary marker of early renal tubular injury, NAG, in urolithiasis patients, especially ones with first stone episode. melamine 23-31 N-acetyl-alpha-glucosaminidase Homo sapiens 111-114 28581831-2 2017 NAG is a precursor of hyaluronic acid, increasing its amount in skin, and consequently, preserving the skin hydration and elasticity. Hyaluronic Acid 22-37 N-acetyl-alpha-glucosaminidase Homo sapiens 0-3 28751108-1 2017 BACKGROUND: The autosomal recessive, neurodegenerative disorder mucopolysaccharidosis type IIIB (MPSIIIB) is caused by a deficiency of the lysosomal enzyme N-acetyl-alpha-glucosaminidase (NAGLU), resulting in accumulation of heparan sulfate. Heparitin Sulfate 225-240 N-acetyl-alpha-glucosaminidase Homo sapiens 156-186 28751108-1 2017 BACKGROUND: The autosomal recessive, neurodegenerative disorder mucopolysaccharidosis type IIIB (MPSIIIB) is caused by a deficiency of the lysosomal enzyme N-acetyl-alpha-glucosaminidase (NAGLU), resulting in accumulation of heparan sulfate. Heparitin Sulfate 225-240 N-acetyl-alpha-glucosaminidase Homo sapiens 188-193 28692093-0 2017 Chemoselective ligation reaction of N-acetylglucosamine (NAG) with hydrazide functional probes to determine galactosyltransferase activity by MALDI mass spectrometry. Isoniazid 67-76 N-acetyl-alpha-glucosaminidase Homo sapiens 57-60 28692093-2 2017 We report here the use of synthetic beta-N-acetylglucosamine (NAG) ligands that contain hydrazide functional groups to determine galactosyltransferase activity by mass spectrometry. Isoniazid 88-97 N-acetyl-alpha-glucosaminidase Homo sapiens 36-60 28692093-2 2017 We report here the use of synthetic beta-N-acetylglucosamine (NAG) ligands that contain hydrazide functional groups to determine galactosyltransferase activity by mass spectrometry. Isoniazid 88-97 N-acetyl-alpha-glucosaminidase Homo sapiens 62-65 28692093-3 2017 With hydrazide-linked beta-d-NAG as the acceptor, the activity of beta-1,4-GT is quantified by matrix-assisted laser desorption/ionization (MALDI)-time-of-flight (TOF) mass spectrometry (MS) with high efficiency. Isoniazid 5-14 N-acetyl-alpha-glucosaminidase Homo sapiens 29-32 28692093-4 2017 Using the disulfide moiety in a 3,3"-dithiodipropionic acid dihydrazide (DTP)-linked beta-d-NAG probe, Au nanoparticles (AuNPs) are employed for enriching DTP-linked beta-d-NAG after enzymatic reaction, and the ligand-bound AuNPs are subsequently deposited on a MALDI plate for analysis. Disulfides 10-19 N-acetyl-alpha-glucosaminidase Homo sapiens 92-95 28692093-4 2017 Using the disulfide moiety in a 3,3"-dithiodipropionic acid dihydrazide (DTP)-linked beta-d-NAG probe, Au nanoparticles (AuNPs) are employed for enriching DTP-linked beta-d-NAG after enzymatic reaction, and the ligand-bound AuNPs are subsequently deposited on a MALDI plate for analysis. Disulfides 10-19 N-acetyl-alpha-glucosaminidase Homo sapiens 173-176 28692093-4 2017 Using the disulfide moiety in a 3,3"-dithiodipropionic acid dihydrazide (DTP)-linked beta-d-NAG probe, Au nanoparticles (AuNPs) are employed for enriching DTP-linked beta-d-NAG after enzymatic reaction, and the ligand-bound AuNPs are subsequently deposited on a MALDI plate for analysis. 3,3"-dithiodipropionic acid dihydrazide 32-71 N-acetyl-alpha-glucosaminidase Homo sapiens 92-95 28692093-4 2017 Using the disulfide moiety in a 3,3"-dithiodipropionic acid dihydrazide (DTP)-linked beta-d-NAG probe, Au nanoparticles (AuNPs) are employed for enriching DTP-linked beta-d-NAG after enzymatic reaction, and the ligand-bound AuNPs are subsequently deposited on a MALDI plate for analysis. 3,3"-dithiodipropionic acid dihydrazide 32-71 N-acetyl-alpha-glucosaminidase Homo sapiens 173-176 28692093-5 2017 In addition, we have demonstrated that a perfluorocarbon (PF) labeled beta-NAG-ligand can be useful for surface-based enzymatic reaction with a perfluorooctadecanethiol (PFDT)-covered gold surface. Fluorocarbons 41-56 N-acetyl-alpha-glucosaminidase Homo sapiens 75-78 28692093-5 2017 In addition, we have demonstrated that a perfluorocarbon (PF) labeled beta-NAG-ligand can be useful for surface-based enzymatic reaction with a perfluorooctadecanethiol (PFDT)-covered gold surface. Fluorocarbons 58-60 N-acetyl-alpha-glucosaminidase Homo sapiens 75-78 28692093-5 2017 In addition, we have demonstrated that a perfluorocarbon (PF) labeled beta-NAG-ligand can be useful for surface-based enzymatic reaction with a perfluorooctadecanethiol (PFDT)-covered gold surface. perfluorooctadecanethiol 144-168 N-acetyl-alpha-glucosaminidase Homo sapiens 75-78 28692093-5 2017 In addition, we have demonstrated that a perfluorocarbon (PF) labeled beta-NAG-ligand can be useful for surface-based enzymatic reaction with a perfluorooctadecanethiol (PFDT)-covered gold surface. pfdt 170-174 N-acetyl-alpha-glucosaminidase Homo sapiens 75-78 28692093-7 2017 This is the first work that uses hydrazide-linked beta-d-NAG for activity analysis, providing a new surface-based MS approach to determine enzyme activity in a potentially high-throughput manner. Isoniazid 33-42 N-acetyl-alpha-glucosaminidase Homo sapiens 57-60 29931914-7 2017 RESULTS: Compared with the control group, the NAG activity of the microwave irradiation group was signifi-cantly increased(P < 0.01), and NAG activity of genistein pre-incubated group was significantly decreased(P < 0.01). Genistein 157-166 N-acetyl-alpha-glucosaminidase Homo sapiens 141-144 29441857-4 2017 In contrast, the hydrogels prepared at 7.0 % and 14.0 % HA concentration showed a less remaining content of NAG equaled to approximately 15.9+-5.4 % and 19.5+-2.6 % respectively. Hyaluronic Acid 56-58 N-acetyl-alpha-glucosaminidase Homo sapiens 108-111 29055942-2 2017 Oral administration of N-carbamoylglutamate (NCG), a synthetic analog of N-acetylglutamate (NAG), successfully decreases plasma ammonia levels in the affected children. N-carbamylglutamate 23-43 N-acetyl-alpha-glucosaminidase Homo sapiens 92-95 29055942-2 2017 Oral administration of N-carbamoylglutamate (NCG), a synthetic analog of N-acetylglutamate (NAG), successfully decreases plasma ammonia levels in the affected children. N-carbamylglutamate 45-48 N-acetyl-alpha-glucosaminidase Homo sapiens 92-95 29055942-2 2017 Oral administration of N-carbamoylglutamate (NCG), a synthetic analog of N-acetylglutamate (NAG), successfully decreases plasma ammonia levels in the affected children. N-acetylglutamic acid 73-90 N-acetyl-alpha-glucosaminidase Homo sapiens 92-95 29055942-2 2017 Oral administration of N-carbamoylglutamate (NCG), a synthetic analog of N-acetylglutamate (NAG), successfully decreases plasma ammonia levels in the affected children. Ammonia 128-135 N-acetyl-alpha-glucosaminidase Homo sapiens 92-95 29055942-7 2017 With EAAT3, the NAG-induced current was sodium-dependent and saturable (Km 409 microM). Sodium 40-46 N-acetyl-alpha-glucosaminidase Homo sapiens 16-19 27668536-7 2016 In 47.37% patients NAG diminished under ciprofloxacin treatment. Ciprofloxacin 40-53 N-acetyl-alpha-glucosaminidase Homo sapiens 19-22 27934952-1 2016 N-acetylglutamate synthase (NAGS; E.C.2.3.1.1) catalyzes the formation of N-acetylglutamate (NAG) from acetyl coenzyme A and glutamate. N-acetylglutamic acid 0-17 N-acetyl-alpha-glucosaminidase Homo sapiens 28-31 27934952-1 2016 N-acetylglutamate synthase (NAGS; E.C.2.3.1.1) catalyzes the formation of N-acetylglutamate (NAG) from acetyl coenzyme A and glutamate. Glutamic Acid 8-17 N-acetyl-alpha-glucosaminidase Homo sapiens 28-31 27934952-2 2016 In microorganisms and plants, NAG is the first intermediate of the L-arginine biosynthesis; in animals, NAG is an allosteric activator of carbamylphosphate synthetase I and III. Arginine 67-77 N-acetyl-alpha-glucosaminidase Homo sapiens 30-33 27934952-2 2016 In microorganisms and plants, NAG is the first intermediate of the L-arginine biosynthesis; in animals, NAG is an allosteric activator of carbamylphosphate synthetase I and III. Arginine 67-77 N-acetyl-alpha-glucosaminidase Homo sapiens 104-107 27668536-8 2016 This observation has the significance of favourable evolution of the tubulointerstitial lesions caused by UTI and lack of nephrotoxic effects; 52.63% cases presented an increase of urinary NAG, a fact that suggests a nephrotoxic effect of ciprofloxacin. Ciprofloxacin 239-252 N-acetyl-alpha-glucosaminidase Homo sapiens 189-192 27606644-7 2016 Significantly higher urinary KIM-1/Cr, L-FABP/Cr, NAG/Cr and NGAL/Cr were found in CD group (p <0.05). Cadmium 83-85 N-acetyl-alpha-glucosaminidase Homo sapiens 50-53 27771289-1 2016 BACKGROUND: N-acetylglutamate synthase (NAGS) plays a key role in the removal of ammonia via the urea cycle by catalyzing the synthesis of N-acetylglutamate (NAG), the obligatory cofactor in the carbamyl phosphate synthetase 1 reaction. Ammonia 81-88 N-acetyl-alpha-glucosaminidase Homo sapiens 40-43 27771289-1 2016 BACKGROUND: N-acetylglutamate synthase (NAGS) plays a key role in the removal of ammonia via the urea cycle by catalyzing the synthesis of N-acetylglutamate (NAG), the obligatory cofactor in the carbamyl phosphate synthetase 1 reaction. Urea 97-101 N-acetyl-alpha-glucosaminidase Homo sapiens 40-43 27771289-1 2016 BACKGROUND: N-acetylglutamate synthase (NAGS) plays a key role in the removal of ammonia via the urea cycle by catalyzing the synthesis of N-acetylglutamate (NAG), the obligatory cofactor in the carbamyl phosphate synthetase 1 reaction. N-acetylglutamic acid 12-29 N-acetyl-alpha-glucosaminidase Homo sapiens 40-43 27771289-3 2016 METHODS: UPLC-MS/MS was used in conjunction with stable isotope (N-acetylglutamic-2,3,3,4,4-d5 acid) dilution for the quantitative detection of NAG produced by the NAGS enzyme. n-acetylglutamic-2,3,3,4,4-d5 acid 65-99 N-acetyl-alpha-glucosaminidase Homo sapiens 144-147 27708787-9 2016 Urinary cadmium (U-Cd), urinary mercury (U-Hg), age, occupation, hypertension, and diabetes had a significant association with higher U-NAG levels. Cadmium 8-15 N-acetyl-alpha-glucosaminidase Homo sapiens 136-139 26980004-3 2016 Of the 20 participants in this study, the urinary NAG/creatinine (Cr) rose from a pre-exercise level of 8.9, 6.7 to 14.3 (mumol/L/mmol Cr; median, IQR) to 12.9, 9.1 to 17.7 post exercise (p = 0.0003, Mann Whitney U test). Creatinine 54-64 N-acetyl-alpha-glucosaminidase Homo sapiens 50-53 26980004-3 2016 Of the 20 participants in this study, the urinary NAG/creatinine (Cr) rose from a pre-exercise level of 8.9, 6.7 to 14.3 (mumol/L/mmol Cr; median, IQR) to 12.9, 9.1 to 17.7 post exercise (p = 0.0003, Mann Whitney U test). Chromium 66-68 N-acetyl-alpha-glucosaminidase Homo sapiens 50-53 26980004-3 2016 Of the 20 participants in this study, the urinary NAG/creatinine (Cr) rose from a pre-exercise level of 8.9, 6.7 to 14.3 (mumol/L/mmol Cr; median, IQR) to 12.9, 9.1 to 17.7 post exercise (p = 0.0003, Mann Whitney U test). Chromium 135-137 N-acetyl-alpha-glucosaminidase Homo sapiens 50-53 26980004-5 2016 Participants with a rise in the NAG/Cr ratio post exercise had a greater ability to increase endothelial reactivity (%; median, IQR; 2.56, 0.1 to 3.7) cf. Chromium 36-38 N-acetyl-alpha-glucosaminidase Homo sapiens 32-35 26980004-9 2016 The mechanism by which the phenotypically distinct sub-group of patients with intermittent claudication who experience a NAG/Cr rise involves complex interactions between systemic oxidative stress and endothelial function. Chromium 125-127 N-acetyl-alpha-glucosaminidase Homo sapiens 121-124 27708787-9 2016 Urinary cadmium (U-Cd), urinary mercury (U-Hg), age, occupation, hypertension, and diabetes had a significant association with higher U-NAG levels. Mercury 32-39 N-acetyl-alpha-glucosaminidase Homo sapiens 136-139 27708787-13 2016 CONCLUSIONS: U-NAG levels seem to be affected by air pollution exposure as well as age, hypertension, diabetes, and even low levels of cadmium and low levels of mercury. Cadmium 135-142 N-acetyl-alpha-glucosaminidase Homo sapiens 15-18 27708787-13 2016 CONCLUSIONS: U-NAG levels seem to be affected by air pollution exposure as well as age, hypertension, diabetes, and even low levels of cadmium and low levels of mercury. Mercury 161-168 N-acetyl-alpha-glucosaminidase Homo sapiens 15-18 27497730-9 2016 In the ACV-treated rats, increased levels of protein (PRO), occult blood (BLD), white blood cell (WBC), and NAG activity in urine were observed, while the urine creatinine and urea nitrogen levels showed a decrease compared with the control. Acyclovir 7-10 N-acetyl-alpha-glucosaminidase Homo sapiens 108-111 27537182-9 2016 Both beta2-MG and NAG were more sensitive than RBP in response to Cd exposure. Cadmium 66-68 N-acetyl-alpha-glucosaminidase Homo sapiens 18-21 27602027-2 2016 Some bacteria use N-acyl-L-homoserine lactone (AHL) mediated quorum sensing (QS) to regulate chitinase production in order to catalyze the cleavage of chitin polymers into water soluble N-acetyl-D-glucosamine (NAG) monomers. n-acyl-l-homoserine lactone 18-45 N-acetyl-alpha-glucosaminidase Homo sapiens 210-213 27602027-2 2016 Some bacteria use N-acyl-L-homoserine lactone (AHL) mediated quorum sensing (QS) to regulate chitinase production in order to catalyze the cleavage of chitin polymers into water soluble N-acetyl-D-glucosamine (NAG) monomers. Chitin 93-99 N-acetyl-alpha-glucosaminidase Homo sapiens 210-213 27602027-2 2016 Some bacteria use N-acyl-L-homoserine lactone (AHL) mediated quorum sensing (QS) to regulate chitinase production in order to catalyze the cleavage of chitin polymers into water soluble N-acetyl-D-glucosamine (NAG) monomers. Water 172-177 N-acetyl-alpha-glucosaminidase Homo sapiens 210-213 27602027-6 2016 Further, this study shows that NAG down-regulates CviR induced violacein production while simultaneously up-regulating CviR dependent extracellular enzymes, suggesting that an unknown NAG dependent regulatory component influences phenotype expression. violacein 63-72 N-acetyl-alpha-glucosaminidase Homo sapiens 31-34 27398022-6 2016 Similarly, urinary NAG levels increased significantly at three hours (3.9 vs. 2.2 IU/mg creatinine; P < 0.001). Creatinine 88-98 N-acetyl-alpha-glucosaminidase Homo sapiens 19-22 27570737-2 2016 Carbamoylphosphate synthetase 1 (CPS1), the first and rate-limiting enzyme of urea cycle, is activated by N-acetylglutamate (NAG), and thus N-acetylglutamate synthase (NAGS) is an essential part of the urea cycle. Urea 78-82 N-acetyl-alpha-glucosaminidase Homo sapiens 125-128 27570737-2 2016 Carbamoylphosphate synthetase 1 (CPS1), the first and rate-limiting enzyme of urea cycle, is activated by N-acetylglutamate (NAG), and thus N-acetylglutamate synthase (NAGS) is an essential part of the urea cycle. N-acetylglutamic acid 106-123 N-acetyl-alpha-glucosaminidase Homo sapiens 125-128 27570737-2 2016 Carbamoylphosphate synthetase 1 (CPS1), the first and rate-limiting enzyme of urea cycle, is activated by N-acetylglutamate (NAG), and thus N-acetylglutamate synthase (NAGS) is an essential part of the urea cycle. Urea 202-206 N-acetyl-alpha-glucosaminidase Homo sapiens 125-128 27570737-3 2016 Although NAGS deficiency is the rarest urea cycle disorder, it is the only one that can be specifically and effectively treated by a drug, N-carbamylglutamate, a stable structural analogous of NAG that activates CPS1. Urea 39-43 N-acetyl-alpha-glucosaminidase Homo sapiens 9-12 27570737-3 2016 Although NAGS deficiency is the rarest urea cycle disorder, it is the only one that can be specifically and effectively treated by a drug, N-carbamylglutamate, a stable structural analogous of NAG that activates CPS1. N-carbamylglutamate 139-158 N-acetyl-alpha-glucosaminidase Homo sapiens 9-12 27398022-9 2016 CONCLUSIONS: Urinary IL-18 and NAG levels increased transiently after administration of gadolinium-based contrast agents in patients with normal renal function. Gadolinium 88-98 N-acetyl-alpha-glucosaminidase Homo sapiens 31-34 26907177-1 2016 BACKGROUND: Mucopolysaccharidosis type IIIB (MPS IIIB) is a rare genetic disorder in which the deficiency of the lysosomal enzyme N-acetyl-alpha-glucosaminidase (NAGLU) results in the accumulation of heparan sulfate (HS), leading to progressive neurocognitive deterioration. Heparitin Sulfate 200-215 N-acetyl-alpha-glucosaminidase Homo sapiens 45-53 27252713-11 2016 Path analysis showed that oxalic acid enhanced potential N mineralization rates indirectly through inducing microbes and NAG activities. Oxalic Acid 26-37 N-acetyl-alpha-glucosaminidase Homo sapiens 121-124 26907177-1 2016 BACKGROUND: Mucopolysaccharidosis type IIIB (MPS IIIB) is a rare genetic disorder in which the deficiency of the lysosomal enzyme N-acetyl-alpha-glucosaminidase (NAGLU) results in the accumulation of heparan sulfate (HS), leading to progressive neurocognitive deterioration. Heparitin Sulfate 200-215 N-acetyl-alpha-glucosaminidase Homo sapiens 130-160 26907177-1 2016 BACKGROUND: Mucopolysaccharidosis type IIIB (MPS IIIB) is a rare genetic disorder in which the deficiency of the lysosomal enzyme N-acetyl-alpha-glucosaminidase (NAGLU) results in the accumulation of heparan sulfate (HS), leading to progressive neurocognitive deterioration. Heparitin Sulfate 200-215 N-acetyl-alpha-glucosaminidase Homo sapiens 162-167 26907177-1 2016 BACKGROUND: Mucopolysaccharidosis type IIIB (MPS IIIB) is a rare genetic disorder in which the deficiency of the lysosomal enzyme N-acetyl-alpha-glucosaminidase (NAGLU) results in the accumulation of heparan sulfate (HS), leading to progressive neurocognitive deterioration. Heparitin Sulfate 217-219 N-acetyl-alpha-glucosaminidase Homo sapiens 45-53 26907177-1 2016 BACKGROUND: Mucopolysaccharidosis type IIIB (MPS IIIB) is a rare genetic disorder in which the deficiency of the lysosomal enzyme N-acetyl-alpha-glucosaminidase (NAGLU) results in the accumulation of heparan sulfate (HS), leading to progressive neurocognitive deterioration. Heparitin Sulfate 217-219 N-acetyl-alpha-glucosaminidase Homo sapiens 130-160 26907177-1 2016 BACKGROUND: Mucopolysaccharidosis type IIIB (MPS IIIB) is a rare genetic disorder in which the deficiency of the lysosomal enzyme N-acetyl-alpha-glucosaminidase (NAGLU) results in the accumulation of heparan sulfate (HS), leading to progressive neurocognitive deterioration. Heparitin Sulfate 217-219 N-acetyl-alpha-glucosaminidase Homo sapiens 162-167 26910785-0 2016 Insulin Receptor Antibody-alpha-N-Acetylglucosaminidase Fusion Protein Penetrates the Primate Blood-Brain Barrier and Reduces Glycosoaminoglycans in Sanfilippo Type B Fibroblasts. glycosoaminoglycans 126-145 N-acetyl-alpha-glucosaminidase Homo sapiens 26-55 26059772-6 2015 Patients with NAG affinity-decreasing mutations might benefit from NAG site saturation therapy with N-carbamyl-L-glutamate (a registered drug, the analog of NAG). N-carbamylglutamate 100-122 N-acetyl-alpha-glucosaminidase Homo sapiens 14-17 30034506-1 2016 Introduction: N-carbamoyl-L-glutamic acid (NCG) is a synthetic analogue of N-acetyl glutamate (NAG) that works effectively as a cofactor for carbamoyl phosphate synthase 1 and enhances ureagenesis by activating the urea cycle. Urea 185-189 N-acetyl-alpha-glucosaminidase Homo sapiens 75-93 30034506-1 2016 Introduction: N-carbamoyl-L-glutamic acid (NCG) is a synthetic analogue of N-acetyl glutamate (NAG) that works effectively as a cofactor for carbamoyl phosphate synthase 1 and enhances ureagenesis by activating the urea cycle. Urea 185-189 N-acetyl-alpha-glucosaminidase Homo sapiens 95-98 25724126-4 2015 RESULTS: Our stratified analysis based on the value of the conventional TIN parameter N-acetylglucosaminidase (NAG) excretion showed that the high-NAG index group (more than median value of NAG-to-Cr ratio, n = 47) demonstrated significantly high FEMg values (p = 0.017). Chromium 197-199 N-acetyl-alpha-glucosaminidase Homo sapiens 111-114 25724126-4 2015 RESULTS: Our stratified analysis based on the value of the conventional TIN parameter N-acetylglucosaminidase (NAG) excretion showed that the high-NAG index group (more than median value of NAG-to-Cr ratio, n = 47) demonstrated significantly high FEMg values (p = 0.017). Chromium 197-199 N-acetyl-alpha-glucosaminidase Homo sapiens 147-150 25724126-4 2015 RESULTS: Our stratified analysis based on the value of the conventional TIN parameter N-acetylglucosaminidase (NAG) excretion showed that the high-NAG index group (more than median value of NAG-to-Cr ratio, n = 47) demonstrated significantly high FEMg values (p = 0.017). Chromium 197-199 N-acetyl-alpha-glucosaminidase Homo sapiens 147-150 30034506-1 2016 Introduction: N-carbamoyl-L-glutamic acid (NCG) is a synthetic analogue of N-acetyl glutamate (NAG) that works effectively as a cofactor for carbamoyl phosphate synthase 1 and enhances ureagenesis by activating the urea cycle. carglumic acid 14-41 N-acetyl-alpha-glucosaminidase Homo sapiens 75-93 30034506-1 2016 Introduction: N-carbamoyl-L-glutamic acid (NCG) is a synthetic analogue of N-acetyl glutamate (NAG) that works effectively as a cofactor for carbamoyl phosphate synthase 1 and enhances ureagenesis by activating the urea cycle. carglumic acid 14-41 N-acetyl-alpha-glucosaminidase Homo sapiens 95-98 30034506-1 2016 Introduction: N-carbamoyl-L-glutamic acid (NCG) is a synthetic analogue of N-acetyl glutamate (NAG) that works effectively as a cofactor for carbamoyl phosphate synthase 1 and enhances ureagenesis by activating the urea cycle. carglumic acid 43-46 N-acetyl-alpha-glucosaminidase Homo sapiens 75-93 30034506-1 2016 Introduction: N-carbamoyl-L-glutamic acid (NCG) is a synthetic analogue of N-acetyl glutamate (NAG) that works effectively as a cofactor for carbamoyl phosphate synthase 1 and enhances ureagenesis by activating the urea cycle. carglumic acid 43-46 N-acetyl-alpha-glucosaminidase Homo sapiens 95-98 26592762-1 2015 Human carbamoyl phosphate synthetase (CPS1), a 1500-residue multidomain enzyme, catalyzes the first step of ammonia detoxification to urea requiring N-acetyl-L-glutamate (NAG) as essential activator to prevent ammonia/amino acids depletion. Ammonia 108-115 N-acetyl-alpha-glucosaminidase Homo sapiens 149-169 26592762-1 2015 Human carbamoyl phosphate synthetase (CPS1), a 1500-residue multidomain enzyme, catalyzes the first step of ammonia detoxification to urea requiring N-acetyl-L-glutamate (NAG) as essential activator to prevent ammonia/amino acids depletion. Ammonia 108-115 N-acetyl-alpha-glucosaminidase Homo sapiens 171-174 26592762-1 2015 Human carbamoyl phosphate synthetase (CPS1), a 1500-residue multidomain enzyme, catalyzes the first step of ammonia detoxification to urea requiring N-acetyl-L-glutamate (NAG) as essential activator to prevent ammonia/amino acids depletion. Urea 134-138 N-acetyl-alpha-glucosaminidase Homo sapiens 149-169 26592762-1 2015 Human carbamoyl phosphate synthetase (CPS1), a 1500-residue multidomain enzyme, catalyzes the first step of ammonia detoxification to urea requiring N-acetyl-L-glutamate (NAG) as essential activator to prevent ammonia/amino acids depletion. Urea 134-138 N-acetyl-alpha-glucosaminidase Homo sapiens 171-174 26592762-1 2015 Human carbamoyl phosphate synthetase (CPS1), a 1500-residue multidomain enzyme, catalyzes the first step of ammonia detoxification to urea requiring N-acetyl-L-glutamate (NAG) as essential activator to prevent ammonia/amino acids depletion. Ammonia 210-217 N-acetyl-alpha-glucosaminidase Homo sapiens 149-169 26592762-1 2015 Human carbamoyl phosphate synthetase (CPS1), a 1500-residue multidomain enzyme, catalyzes the first step of ammonia detoxification to urea requiring N-acetyl-L-glutamate (NAG) as essential activator to prevent ammonia/amino acids depletion. Ammonia 210-217 N-acetyl-alpha-glucosaminidase Homo sapiens 171-174 26592762-2 2015 Here we present the crystal structures of CPS1 in the absence and in the presence of NAG, clarifying the on/off-switching of the urea cycle by NAG. Urea 129-133 N-acetyl-alpha-glucosaminidase Homo sapiens 85-88 26592762-2 2015 Here we present the crystal structures of CPS1 in the absence and in the presence of NAG, clarifying the on/off-switching of the urea cycle by NAG. Urea 129-133 N-acetyl-alpha-glucosaminidase Homo sapiens 143-146 26068232-1 2015 N-acetylglutamate synthase (NAGS) catalyzes the production of N-acetylglutamate (NAG) from acetyl-CoA and L-glutamate. N-acetylglutamic acid 0-17 N-acetyl-alpha-glucosaminidase Homo sapiens 28-31 26068232-1 2015 N-acetylglutamate synthase (NAGS) catalyzes the production of N-acetylglutamate (NAG) from acetyl-CoA and L-glutamate. Acetyl Coenzyme A 91-101 N-acetyl-alpha-glucosaminidase Homo sapiens 28-31 26068232-1 2015 N-acetylglutamate synthase (NAGS) catalyzes the production of N-acetylglutamate (NAG) from acetyl-CoA and L-glutamate. Glutamic Acid 106-117 N-acetyl-alpha-glucosaminidase Homo sapiens 28-31 26059772-6 2015 Patients with NAG affinity-decreasing mutations might benefit from NAG site saturation therapy with N-carbamyl-L-glutamate (a registered drug, the analog of NAG). N-carbamylglutamate 100-122 N-acetyl-alpha-glucosaminidase Homo sapiens 67-70 26059772-6 2015 Patients with NAG affinity-decreasing mutations might benefit from NAG site saturation therapy with N-carbamyl-L-glutamate (a registered drug, the analog of NAG). N-carbamylglutamate 100-122 N-acetyl-alpha-glucosaminidase Homo sapiens 67-70 26059772-9 2015 Molecular dynamics simulations that were restrained according to the observed effects of the mutations are consistent with this hypothesis, providing further backing for this structurally plausible signaling mechanism by which NAG could trigger urea cycle activation via CPS1. Urea 245-249 N-acetyl-alpha-glucosaminidase Homo sapiens 227-230 25378480-8 2015 Furthermore, a very efficient trans-N-acetylglucosaminidase activity was observed when the double mutant was incubated in the presence of NAG-oxazoline as a donor and N-methyl-O-benzyl-N-(beta-d-glucopyranosyl)-hydroxylamine as an acceptor. n-methyl-o-benzyl-n-(beta-d-glucopyranosyl)-hydroxylamine 167-224 N-acetyl-alpha-glucosaminidase Homo sapiens 138-141 25462626-1 2015 A new and efficient solvent free synthesis of 2,4,5-trisubstituted imidazoles (3a-3j) was achieved by N-acetyl glycine (NAG) catalyzed three components condensation of aldehydes, benzil and ammonium acetate. 2,4,5-trisubstituted imidazoles 46-77 N-acetyl-alpha-glucosaminidase Homo sapiens 102-118 25463647-7 2015 Our results showed that eyestalk ablation increased the ecdysteroid content as well as the activities of chitinase and NAG, which were inhibited by cadmium in a concentration-dependent manner; histological examinations demonstrated that eyestalk ablation produced storage particles in the epidermal tissues, which was also reduced by cadmium in a concentration-dependent manner. Cadmium 148-155 N-acetyl-alpha-glucosaminidase Homo sapiens 119-122 25463647-8 2015 Our data suggest that cadmium disrupts endocrine function through inhibiting the secretion of ecdysteroids by the Y-organ and altering with the regulation of chitinase and NAG activity in the epidermis. Cadmium 22-29 N-acetyl-alpha-glucosaminidase Homo sapiens 172-175 25462626-1 2015 A new and efficient solvent free synthesis of 2,4,5-trisubstituted imidazoles (3a-3j) was achieved by N-acetyl glycine (NAG) catalyzed three components condensation of aldehydes, benzil and ammonium acetate. 2,4,5-trisubstituted imidazoles 46-77 N-acetyl-alpha-glucosaminidase Homo sapiens 120-123 25462626-1 2015 A new and efficient solvent free synthesis of 2,4,5-trisubstituted imidazoles (3a-3j) was achieved by N-acetyl glycine (NAG) catalyzed three components condensation of aldehydes, benzil and ammonium acetate. Aldehydes 168-177 N-acetyl-alpha-glucosaminidase Homo sapiens 102-118 25462626-1 2015 A new and efficient solvent free synthesis of 2,4,5-trisubstituted imidazoles (3a-3j) was achieved by N-acetyl glycine (NAG) catalyzed three components condensation of aldehydes, benzil and ammonium acetate. Aldehydes 168-177 N-acetyl-alpha-glucosaminidase Homo sapiens 120-123 25462626-1 2015 A new and efficient solvent free synthesis of 2,4,5-trisubstituted imidazoles (3a-3j) was achieved by N-acetyl glycine (NAG) catalyzed three components condensation of aldehydes, benzil and ammonium acetate. benzil 179-185 N-acetyl-alpha-glucosaminidase Homo sapiens 102-118 25462626-1 2015 A new and efficient solvent free synthesis of 2,4,5-trisubstituted imidazoles (3a-3j) was achieved by N-acetyl glycine (NAG) catalyzed three components condensation of aldehydes, benzil and ammonium acetate. benzil 179-185 N-acetyl-alpha-glucosaminidase Homo sapiens 120-123 25462626-1 2015 A new and efficient solvent free synthesis of 2,4,5-trisubstituted imidazoles (3a-3j) was achieved by N-acetyl glycine (NAG) catalyzed three components condensation of aldehydes, benzil and ammonium acetate. ammonium acetate 190-206 N-acetyl-alpha-glucosaminidase Homo sapiens 102-118 25462626-1 2015 A new and efficient solvent free synthesis of 2,4,5-trisubstituted imidazoles (3a-3j) was achieved by N-acetyl glycine (NAG) catalyzed three components condensation of aldehydes, benzil and ammonium acetate. ammonium acetate 190-206 N-acetyl-alpha-glucosaminidase Homo sapiens 120-123 25256447-8 2015 The concentration of HS in CSF in the patient with the attenuated phenotype of MPS IIIB 2 years after UCBT was very high and in the range of untreated MPS III patients.We conclude that the course of cognitive development, behavioral problems, and absence of biochemical correction in CSF demonstrate the absence of relevant effect of UCBT in MPS III patients, even when performed before clinical onset of CNS disease. Heparitin Sulfate 21-23 N-acetyl-alpha-glucosaminidase Homo sapiens 79-87 25256447-8 2015 The concentration of HS in CSF in the patient with the attenuated phenotype of MPS IIIB 2 years after UCBT was very high and in the range of untreated MPS III patients.We conclude that the course of cognitive development, behavioral problems, and absence of biochemical correction in CSF demonstrate the absence of relevant effect of UCBT in MPS III patients, even when performed before clinical onset of CNS disease. ucbt 102-106 N-acetyl-alpha-glucosaminidase Homo sapiens 79-87 25354943-1 2014 Inborn defects in N-acetylglutamate (NAG) synthase (NAGS) cause a reduction of NAG, an essential cofactor for the initiation of the urea cycle. Urea 132-136 N-acetyl-alpha-glucosaminidase Homo sapiens 37-40 25142083-0 2015 The ratios of urinary beta2-microglobulin and NAG to creatinine vary with age in children. Creatinine 53-63 N-acetyl-alpha-glucosaminidase Homo sapiens 46-49 24326128-4 2014 Adjusted odds ratios for an elevated urinary NAG index (>5.8U/g creatinine) according to the HbA1c (<=5.4%, 5.5%-5.9%, and 6.0%-6.4%) and 1,5-AG tertiles were calculated. Creatinine 67-77 N-acetyl-alpha-glucosaminidase Homo sapiens 45-48 24833032-2 2014 These enzymes were used in a total enzyme-based system to produce pure N-acetylglucosamine (NAG) from chitin. Chitin 102-108 N-acetyl-alpha-glucosaminidase Homo sapiens 71-90 24833032-2 2014 These enzymes were used in a total enzyme-based system to produce pure N-acetylglucosamine (NAG) from chitin. Chitin 102-108 N-acetyl-alpha-glucosaminidase Homo sapiens 92-95 24833032-6 2014 When an enzyme incubation mixture containing a 1:1 (pkat/pkat) activity mixed ratio of endochitinase: NAGase was employed, the maximum yield of N-acetylglucosamine (NAG) obtained was 98% from beta-chitin and 20% from alpha-chitin. beta-chitin 192-203 N-acetyl-alpha-glucosaminidase Homo sapiens 144-163 24833032-6 2014 When an enzyme incubation mixture containing a 1:1 (pkat/pkat) activity mixed ratio of endochitinase: NAGase was employed, the maximum yield of N-acetylglucosamine (NAG) obtained was 98% from beta-chitin and 20% from alpha-chitin. beta-chitin 192-203 N-acetyl-alpha-glucosaminidase Homo sapiens 102-105 24833032-6 2014 When an enzyme incubation mixture containing a 1:1 (pkat/pkat) activity mixed ratio of endochitinase: NAGase was employed, the maximum yield of N-acetylglucosamine (NAG) obtained was 98% from beta-chitin and 20% from alpha-chitin. alpha-chitin 217-229 N-acetyl-alpha-glucosaminidase Homo sapiens 144-163 24833032-6 2014 When an enzyme incubation mixture containing a 1:1 (pkat/pkat) activity mixed ratio of endochitinase: NAGase was employed, the maximum yield of N-acetylglucosamine (NAG) obtained was 98% from beta-chitin and 20% from alpha-chitin. alpha-chitin 217-229 N-acetyl-alpha-glucosaminidase Homo sapiens 102-105 24833032-9 2014 Mass spectroscopic analysis, using electrospray ionisation mass spectrometry (ESI-MS), of the product obtained from beta-chitin after digestion (for 24h) depicted one distinct major molecular ion peak m/z 260.1, a small minor ion peak m/z 481.2, a potassium adduct of NAG and a potassium adduct of two NAG molecules. beta-chitin 116-127 N-acetyl-alpha-glucosaminidase Homo sapiens 268-271 24833032-9 2014 Mass spectroscopic analysis, using electrospray ionisation mass spectrometry (ESI-MS), of the product obtained from beta-chitin after digestion (for 24h) depicted one distinct major molecular ion peak m/z 260.1, a small minor ion peak m/z 481.2, a potassium adduct of NAG and a potassium adduct of two NAG molecules. beta-chitin 116-127 N-acetyl-alpha-glucosaminidase Homo sapiens 302-305 25170411-8 2014 The current results revealed that NAG/creatinine index was significantly higher in all patients with (vesicoureteral reflux, hydronephrosis and pyelonephritis) in comparison with cystitis. Creatinine 38-48 N-acetyl-alpha-glucosaminidase Homo sapiens 34-37 24326128-1 2014 BACKGROUND: To assess the relationship between the serum level of 1,5-anhydroglucitol (1,5-AG), a marker of postprandial hyperglycemia, and the ratio of the urinary activity of N-acetyl-beta-d-glucosaminidase to creatinine (NAG index) in subjects without diabetes mellitus (DM). 1,5-anhydroglucitol 66-85 N-acetyl-alpha-glucosaminidase Homo sapiens 224-227 24326128-1 2014 BACKGROUND: To assess the relationship between the serum level of 1,5-anhydroglucitol (1,5-AG), a marker of postprandial hyperglycemia, and the ratio of the urinary activity of N-acetyl-beta-d-glucosaminidase to creatinine (NAG index) in subjects without diabetes mellitus (DM). 1,5-anhydroglucitol 87-93 N-acetyl-alpha-glucosaminidase Homo sapiens 224-227 24326128-8 2014 CONCLUSION: Poor control of postprandial glucose is related to an elevated urinary NAG index in persons without DM. Glucose 41-48 N-acetyl-alpha-glucosaminidase Homo sapiens 83-86 25170411-1 2014 OBJECTIVES: To assess urinary NAG/ urinary creatinine (NAG/ Cr) ratio in patients with urological abnormalities (normal and abnormal ultrasonography) and compare it with normal healthy children. Creatinine 43-53 N-acetyl-alpha-glucosaminidase Homo sapiens 55-58 23894642-1 2013 N-acetylglutamate synthase (NAGS) catalyzes the conversion of AcCoA and L-glutamate to CoA and N-acetyl-L-glutamate (NAG), an obligate cofactor for carbamyl phosphate synthetase I (CPSI) in the urea cycle. Glutamic Acid 72-83 N-acetyl-alpha-glucosaminidase Homo sapiens 95-115 24266751-6 2014 Glycosaminoglycan storage was reduced by 60% (P<0.001) to near background levels in MPS IIIB cells after treatment with rhNAGLU-IGF-II, with half-maximal correction at concentrations of 3-12 pM. Glycosaminoglycans 0-17 N-acetyl-alpha-glucosaminidase Homo sapiens 87-95 23985742-4 2014 In incubation experiments, we examined community shifts of AGB in response to the addition of N-acetyl-glucosamine (NAG), one of the most abundant aminosugars in aquatic systems. norarginine 59-62 N-acetyl-alpha-glucosaminidase Homo sapiens 94-114 23985742-4 2014 In incubation experiments, we examined community shifts of AGB in response to the addition of N-acetyl-glucosamine (NAG), one of the most abundant aminosugars in aquatic systems. norarginine 59-62 N-acetyl-alpha-glucosaminidase Homo sapiens 116-119 23672714-2 2013 N-Acetylglucosamine (NAG) is the substrate for hyaluronan synthesis, and it also has anti-inflammatory and anti-senescent activity in mesothelial cells. Hyaluronic Acid 47-57 N-acetyl-alpha-glucosaminidase Homo sapiens 0-19 23672714-2 2013 N-Acetylglucosamine (NAG) is the substrate for hyaluronan synthesis, and it also has anti-inflammatory and anti-senescent activity in mesothelial cells. Hyaluronic Acid 47-57 N-acetyl-alpha-glucosaminidase Homo sapiens 21-24 24880489-1 2014 A convenient and efficient new method has been established for the synthesis of dihydropyrimidines by inexpensive and non-toxic N-acetyl glycine (NAG) catalysed reaction of aromatic aldehydes with ethyl acetoacetate and urea/thiourea. dihydropyrimidines 80-98 N-acetyl-alpha-glucosaminidase Homo sapiens 128-144 24880489-1 2014 A convenient and efficient new method has been established for the synthesis of dihydropyrimidines by inexpensive and non-toxic N-acetyl glycine (NAG) catalysed reaction of aromatic aldehydes with ethyl acetoacetate and urea/thiourea. dihydropyrimidines 80-98 N-acetyl-alpha-glucosaminidase Homo sapiens 146-149 24880489-1 2014 A convenient and efficient new method has been established for the synthesis of dihydropyrimidines by inexpensive and non-toxic N-acetyl glycine (NAG) catalysed reaction of aromatic aldehydes with ethyl acetoacetate and urea/thiourea. Aldehydes 182-191 N-acetyl-alpha-glucosaminidase Homo sapiens 128-144 24880489-1 2014 A convenient and efficient new method has been established for the synthesis of dihydropyrimidines by inexpensive and non-toxic N-acetyl glycine (NAG) catalysed reaction of aromatic aldehydes with ethyl acetoacetate and urea/thiourea. Aldehydes 182-191 N-acetyl-alpha-glucosaminidase Homo sapiens 146-149 24880489-1 2014 A convenient and efficient new method has been established for the synthesis of dihydropyrimidines by inexpensive and non-toxic N-acetyl glycine (NAG) catalysed reaction of aromatic aldehydes with ethyl acetoacetate and urea/thiourea. ethyl acetoacetate 197-215 N-acetyl-alpha-glucosaminidase Homo sapiens 128-144 24880489-1 2014 A convenient and efficient new method has been established for the synthesis of dihydropyrimidines by inexpensive and non-toxic N-acetyl glycine (NAG) catalysed reaction of aromatic aldehydes with ethyl acetoacetate and urea/thiourea. ethyl acetoacetate 197-215 N-acetyl-alpha-glucosaminidase Homo sapiens 146-149 24880489-1 2014 A convenient and efficient new method has been established for the synthesis of dihydropyrimidines by inexpensive and non-toxic N-acetyl glycine (NAG) catalysed reaction of aromatic aldehydes with ethyl acetoacetate and urea/thiourea. Urea 220-224 N-acetyl-alpha-glucosaminidase Homo sapiens 128-144 24880489-1 2014 A convenient and efficient new method has been established for the synthesis of dihydropyrimidines by inexpensive and non-toxic N-acetyl glycine (NAG) catalysed reaction of aromatic aldehydes with ethyl acetoacetate and urea/thiourea. Urea 220-224 N-acetyl-alpha-glucosaminidase Homo sapiens 146-149 24880489-1 2014 A convenient and efficient new method has been established for the synthesis of dihydropyrimidines by inexpensive and non-toxic N-acetyl glycine (NAG) catalysed reaction of aromatic aldehydes with ethyl acetoacetate and urea/thiourea. Thiourea 225-233 N-acetyl-alpha-glucosaminidase Homo sapiens 128-144 24880489-1 2014 A convenient and efficient new method has been established for the synthesis of dihydropyrimidines by inexpensive and non-toxic N-acetyl glycine (NAG) catalysed reaction of aromatic aldehydes with ethyl acetoacetate and urea/thiourea. Thiourea 225-233 N-acetyl-alpha-glucosaminidase Homo sapiens 146-149 24266751-1 2014 Enzyme replacement therapy for MPS IIIB (mucopolysaccharidosis type IIIB; also known as Sanfilippo B syndrome) has been hindered by inadequate mannose 6 phosphorylation and cellular uptake of rhNAGLU (recombinant human alpha-N-acetylglucosaminidase). Mannose 143-150 N-acetyl-alpha-glucosaminidase Homo sapiens 31-39 24071376-12 2014 Continuous infusion of nicardipine attenuated the increase in NAG, which is a marker of renal tubular injury, during hypotensive anesthesia with desflurane and remifentanil. Nicardipine 23-34 N-acetyl-alpha-glucosaminidase Homo sapiens 62-65 24071376-12 2014 Continuous infusion of nicardipine attenuated the increase in NAG, which is a marker of renal tubular injury, during hypotensive anesthesia with desflurane and remifentanil. Desflurane 145-155 N-acetyl-alpha-glucosaminidase Homo sapiens 62-65 24071376-12 2014 Continuous infusion of nicardipine attenuated the increase in NAG, which is a marker of renal tubular injury, during hypotensive anesthesia with desflurane and remifentanil. Remifentanil 160-172 N-acetyl-alpha-glucosaminidase Homo sapiens 62-65 23649895-6 2013 Glycerol partially replaces the essential activator N-acetyl-l-glutamate (NAG), opening possibilities for treating CPS1D due to NAG site defects. Glycerol 0-8 N-acetyl-alpha-glucosaminidase Homo sapiens 52-72 23649895-6 2013 Glycerol partially replaces the essential activator N-acetyl-l-glutamate (NAG), opening possibilities for treating CPS1D due to NAG site defects. Glycerol 0-8 N-acetyl-alpha-glucosaminidase Homo sapiens 74-77 23649895-6 2013 Glycerol partially replaces the essential activator N-acetyl-l-glutamate (NAG), opening possibilities for treating CPS1D due to NAG site defects. Glycerol 0-8 N-acetyl-alpha-glucosaminidase Homo sapiens 128-131 23649895-11 2013 NAG and its analogue and orphan drug N-carbamoyl-l-glutamate, protected human CPS1 against proteolytic and thermal inactivation in the presence of MgATP, raising hopes of treating CPS1D by chemical chaperoning with N-carbamoyl-l-glutamate. Adenosine Triphosphate 147-152 N-acetyl-alpha-glucosaminidase Homo sapiens 0-3 23649895-11 2013 NAG and its analogue and orphan drug N-carbamoyl-l-glutamate, protected human CPS1 against proteolytic and thermal inactivation in the presence of MgATP, raising hopes of treating CPS1D by chemical chaperoning with N-carbamoyl-l-glutamate. cps1d 180-185 N-acetyl-alpha-glucosaminidase Homo sapiens 0-3 23649895-11 2013 NAG and its analogue and orphan drug N-carbamoyl-l-glutamate, protected human CPS1 against proteolytic and thermal inactivation in the presence of MgATP, raising hopes of treating CPS1D by chemical chaperoning with N-carbamoyl-l-glutamate. N-carbamylglutamate 215-238 N-acetyl-alpha-glucosaminidase Homo sapiens 0-3 23894642-1 2013 N-acetylglutamate synthase (NAGS) catalyzes the conversion of AcCoA and L-glutamate to CoA and N-acetyl-L-glutamate (NAG), an obligate cofactor for carbamyl phosphate synthetase I (CPSI) in the urea cycle. Glutamic Acid 72-83 N-acetyl-alpha-glucosaminidase Homo sapiens 28-31 23894642-1 2013 N-acetylglutamate synthase (NAGS) catalyzes the conversion of AcCoA and L-glutamate to CoA and N-acetyl-L-glutamate (NAG), an obligate cofactor for carbamyl phosphate synthetase I (CPSI) in the urea cycle. Coenzyme A 64-67 N-acetyl-alpha-glucosaminidase Homo sapiens 95-115 23894642-1 2013 N-acetylglutamate synthase (NAGS) catalyzes the conversion of AcCoA and L-glutamate to CoA and N-acetyl-L-glutamate (NAG), an obligate cofactor for carbamyl phosphate synthetase I (CPSI) in the urea cycle. Coenzyme A 64-67 N-acetyl-alpha-glucosaminidase Homo sapiens 28-31 23894642-1 2013 N-acetylglutamate synthase (NAGS) catalyzes the conversion of AcCoA and L-glutamate to CoA and N-acetyl-L-glutamate (NAG), an obligate cofactor for carbamyl phosphate synthetase I (CPSI) in the urea cycle. Urea 194-198 N-acetyl-alpha-glucosaminidase Homo sapiens 95-115 23894642-1 2013 N-acetylglutamate synthase (NAGS) catalyzes the conversion of AcCoA and L-glutamate to CoA and N-acetyl-L-glutamate (NAG), an obligate cofactor for carbamyl phosphate synthetase I (CPSI) in the urea cycle. Urea 194-198 N-acetyl-alpha-glucosaminidase Homo sapiens 28-31 23725302-1 2013 BACKGROUND: N-acetyl glucosamine (NAG) is a precursor for hyaluronic acid (HA) biosynthesis in the body. Hyaluronic Acid 58-73 N-acetyl-alpha-glucosaminidase Homo sapiens 12-32 23840811-6 2013 This procedure is based on the use of the fluorogenic NAG substrate, 4-Methylumbelliferyl-2-acetamido-2-deoxy-alpha-D-glucopyranoside (MUG), in a one-step cell assay that does not require cell disruption or post-assay normalization and that employs a low number of cells in 96-well plate format. 4-methylumbelliferyl 2-acetamido-2-deoxy-beta-D-glucopyranoside 69-133 N-acetyl-alpha-glucosaminidase Homo sapiens 54-57 23725302-1 2013 BACKGROUND: N-acetyl glucosamine (NAG) is a precursor for hyaluronic acid (HA) biosynthesis in the body. Hyaluronic Acid 58-73 N-acetyl-alpha-glucosaminidase Homo sapiens 34-37 23725302-1 2013 BACKGROUND: N-acetyl glucosamine (NAG) is a precursor for hyaluronic acid (HA) biosynthesis in the body. Hyaluronic Acid 75-77 N-acetyl-alpha-glucosaminidase Homo sapiens 12-32 23725302-1 2013 BACKGROUND: N-acetyl glucosamine (NAG) is a precursor for hyaluronic acid (HA) biosynthesis in the body. Hyaluronic Acid 75-77 N-acetyl-alpha-glucosaminidase Homo sapiens 34-37 23725302-8 2013 The highest effect on skin moisture content was achieved by NAG liposomal prepared using fusion method after 3 h. The difference between moisture content of the skin treated by preparations containing GA (solution and liposomes) and empty liposomes was negligible in all tests and duration times of the experiment. Glucosamine 201-203 N-acetyl-alpha-glucosaminidase Homo sapiens 60-63 24475424-5 2013 RESULTS: There was moderate correlation between NAG and microalbuminuria (r=0,34) in the group of patients treated with Ketoprofen only, while statistically significant correlation (r=0,21) was seen in group of patients with combined use of Methotrexate and Ketoprofen. Ketoprofen 120-130 N-acetyl-alpha-glucosaminidase Homo sapiens 48-51 23667853-1 2013 Mucopolysaccharidosis (MPS) IIIB is a lysosomal storage disorder (LSD) caused by abnormalities of the enzyme alpha-N-acetylglucosaminidase (NAGLU) that is required for degradation of heparan sulfate. Heparitin Sulfate 183-198 N-acetyl-alpha-glucosaminidase Homo sapiens 109-138 23667853-1 2013 Mucopolysaccharidosis (MPS) IIIB is a lysosomal storage disorder (LSD) caused by abnormalities of the enzyme alpha-N-acetylglucosaminidase (NAGLU) that is required for degradation of heparan sulfate. Heparitin Sulfate 183-198 N-acetyl-alpha-glucosaminidase Homo sapiens 140-145 23255614-8 2013 The GSH precursor dipeptide, cysteinyl glycine (cysgly), and the glutamate derivative N-acetyl glutamate (NAG), inhibited uptake of PAH when present in the medium and trans-stimulated uptake of PAH from the intracellular side, indicating that they are hitherto unrecognized transported substrates of OAT1. Glutamic Acid 65-74 N-acetyl-alpha-glucosaminidase Homo sapiens 86-104 23255614-8 2013 The GSH precursor dipeptide, cysteinyl glycine (cysgly), and the glutamate derivative N-acetyl glutamate (NAG), inhibited uptake of PAH when present in the medium and trans-stimulated uptake of PAH from the intracellular side, indicating that they are hitherto unrecognized transported substrates of OAT1. Glutamic Acid 65-74 N-acetyl-alpha-glucosaminidase Homo sapiens 106-109 23255614-8 2013 The GSH precursor dipeptide, cysteinyl glycine (cysgly), and the glutamate derivative N-acetyl glutamate (NAG), inhibited uptake of PAH when present in the medium and trans-stimulated uptake of PAH from the intracellular side, indicating that they are hitherto unrecognized transported substrates of OAT1. p-Aminohippuric Acid 132-135 N-acetyl-alpha-glucosaminidase Homo sapiens 86-104 23255614-8 2013 The GSH precursor dipeptide, cysteinyl glycine (cysgly), and the glutamate derivative N-acetyl glutamate (NAG), inhibited uptake of PAH when present in the medium and trans-stimulated uptake of PAH from the intracellular side, indicating that they are hitherto unrecognized transported substrates of OAT1. p-Aminohippuric Acid 132-135 N-acetyl-alpha-glucosaminidase Homo sapiens 106-109 23255614-8 2013 The GSH precursor dipeptide, cysteinyl glycine (cysgly), and the glutamate derivative N-acetyl glutamate (NAG), inhibited uptake of PAH when present in the medium and trans-stimulated uptake of PAH from the intracellular side, indicating that they are hitherto unrecognized transported substrates of OAT1. p-Aminohippuric Acid 194-197 N-acetyl-alpha-glucosaminidase Homo sapiens 86-104 23255614-8 2013 The GSH precursor dipeptide, cysteinyl glycine (cysgly), and the glutamate derivative N-acetyl glutamate (NAG), inhibited uptake of PAH when present in the medium and trans-stimulated uptake of PAH from the intracellular side, indicating that they are hitherto unrecognized transported substrates of OAT1. p-Aminohippuric Acid 194-197 N-acetyl-alpha-glucosaminidase Homo sapiens 106-109 23109228-1 2013 Lysozyme is a well-studied enzyme that hydrolyzes the beta-(1,4)-glycosidic linkage of N-acetyl-beta-glucosamine (NAG)(n) oligomers. beta-(1,4) 54-64 N-acetyl-alpha-glucosaminidase Homo sapiens 87-112 23109228-1 2013 Lysozyme is a well-studied enzyme that hydrolyzes the beta-(1,4)-glycosidic linkage of N-acetyl-beta-glucosamine (NAG)(n) oligomers. beta-(1,4) 54-64 N-acetyl-alpha-glucosaminidase Homo sapiens 114-117 24475424-6 2013 NAG enzymuria in size, number of patients registered, and time of appearance were greater and appears earlier in the group with the combined use of Methotrexate and Ketoprofen compared with the mono-therapy with Ketoprofen. Methotrexate 148-160 N-acetyl-alpha-glucosaminidase Homo sapiens 0-3 24475424-6 2013 NAG enzymuria in size, number of patients registered, and time of appearance were greater and appears earlier in the group with the combined use of Methotrexate and Ketoprofen compared with the mono-therapy with Ketoprofen. Ketoprofen 165-175 N-acetyl-alpha-glucosaminidase Homo sapiens 0-3 24475424-6 2013 NAG enzymuria in size, number of patients registered, and time of appearance were greater and appears earlier in the group with the combined use of Methotrexate and Ketoprofen compared with the mono-therapy with Ketoprofen. Ketoprofen 212-222 N-acetyl-alpha-glucosaminidase Homo sapiens 0-3 24475424-7 2013 Mean urinary NAG induction was increasing with the concomitant use of Methotrexate and Ketoprofen. Methotrexate 70-82 N-acetyl-alpha-glucosaminidase Homo sapiens 13-16 24475424-7 2013 Mean urinary NAG induction was increasing with the concomitant use of Methotrexate and Ketoprofen. Ketoprofen 87-97 N-acetyl-alpha-glucosaminidase Homo sapiens 13-16 24475424-8 2013 CONCLUSIONS: Methotrexate is more potent NAG inductor than Ketoprofen and provokes greater tubular enzymuria than Ketoprofen. Methotrexate 13-25 N-acetyl-alpha-glucosaminidase Homo sapiens 41-44 22721850-0 2012 Design, synthesis and evaluation of N-acetyl glucosamine (NAG)-PEG-doxorubicin targeted conjugates for anticancer delivery. peg-doxorubicin 63-78 N-acetyl-alpha-glucosaminidase Homo sapiens 36-56 23174579-5 2012 At 24 h after contrast administration, the levels of serum cystatin C, urine beta2-microglobulin and urine NAG were significantly lower in amlodipine group than in the control group, but the other functional parameters showed no significant difference. Amlodipine 139-149 N-acetyl-alpha-glucosaminidase Homo sapiens 107-110 22721850-0 2012 Design, synthesis and evaluation of N-acetyl glucosamine (NAG)-PEG-doxorubicin targeted conjugates for anticancer delivery. peg-doxorubicin 63-78 N-acetyl-alpha-glucosaminidase Homo sapiens 58-61 22721850-2 2012 Toward this objectives, we propose, synthesis of poly(ethylene glycol) (PEG)-doxorubicin (DOX) prodrug conjugates consisting N-acetyl glucosamine (NAG) as a targeting moiety. Polyethylene Glycols 49-70 N-acetyl-alpha-glucosaminidase Homo sapiens 125-145 22721850-2 2012 Toward this objectives, we propose, synthesis of poly(ethylene glycol) (PEG)-doxorubicin (DOX) prodrug conjugates consisting N-acetyl glucosamine (NAG) as a targeting moiety. Polyethylene Glycols 49-70 N-acetyl-alpha-glucosaminidase Homo sapiens 147-150 22721850-2 2012 Toward this objectives, we propose, synthesis of poly(ethylene glycol) (PEG)-doxorubicin (DOX) prodrug conjugates consisting N-acetyl glucosamine (NAG) as a targeting moiety. Polyethylene Glycols 72-76 N-acetyl-alpha-glucosaminidase Homo sapiens 125-145 22721850-2 2012 Toward this objectives, we propose, synthesis of poly(ethylene glycol) (PEG)-doxorubicin (DOX) prodrug conjugates consisting N-acetyl glucosamine (NAG) as a targeting moiety. Polyethylene Glycols 72-76 N-acetyl-alpha-glucosaminidase Homo sapiens 147-150 22721850-2 2012 Toward this objectives, we propose, synthesis of poly(ethylene glycol) (PEG)-doxorubicin (DOX) prodrug conjugates consisting N-acetyl glucosamine (NAG) as a targeting moiety. Doxorubicin 77-88 N-acetyl-alpha-glucosaminidase Homo sapiens 125-145 22721850-2 2012 Toward this objectives, we propose, synthesis of poly(ethylene glycol) (PEG)-doxorubicin (DOX) prodrug conjugates consisting N-acetyl glucosamine (NAG) as a targeting moiety. Doxorubicin 77-88 N-acetyl-alpha-glucosaminidase Homo sapiens 147-150 22721850-2 2012 Toward this objectives, we propose, synthesis of poly(ethylene glycol) (PEG)-doxorubicin (DOX) prodrug conjugates consisting N-acetyl glucosamine (NAG) as a targeting moiety. Doxorubicin 90-93 N-acetyl-alpha-glucosaminidase Homo sapiens 125-145 22721850-2 2012 Toward this objectives, we propose, synthesis of poly(ethylene glycol) (PEG)-doxorubicin (DOX) prodrug conjugates consisting N-acetyl glucosamine (NAG) as a targeting moiety. Doxorubicin 90-93 N-acetyl-alpha-glucosaminidase Homo sapiens 147-150 22721850-6 2012 Interestingly, PEG-DOX conjugate with NAG ligand showed significantly higher cytotoxicity compared to drug conjugate with DOX. peg-dox 15-22 N-acetyl-alpha-glucosaminidase Homo sapiens 38-41 22721850-6 2012 Interestingly, PEG-DOX conjugate with NAG ligand showed significantly higher cytotoxicity compared to drug conjugate with DOX. Doxorubicin 19-22 N-acetyl-alpha-glucosaminidase Homo sapiens 38-41 22721850-7 2012 In addition, the polymer drug conjugate with NAG and DOX showed enhanced internalization and retention effect in cancer cells, compared to free DOX. Doxorubicin 144-147 N-acetyl-alpha-glucosaminidase Homo sapiens 45-48 22721850-8 2012 Thus, with enhanced internalization and targeting ability of PEG conjugate of NAG-DOX has implication in targeted anticancer therapy. Polyethylene Glycols 61-64 N-acetyl-alpha-glucosaminidase Homo sapiens 78-81 22156940-2 2012 Our previous studies in mucopolysaccharidosis type IIIB (MPSIIIB), a disease in which a genetic defect induces the accumulation of undigested heparan sulfate (HS) fragments, led to the hypothesis that abnormal lysosome formation was related to events occurring at the Golgi level. Heparitin Sulfate 142-157 N-acetyl-alpha-glucosaminidase Homo sapiens 57-64 22870359-6 2012 The renal safety was evaluated by changes of blood urea nitrogen (BUN), creatinine and urine N-acetyl-b-glucoseaminidase (NAG)-creatinine ratio at 24 hours and 72 hours after surgery from preoperative level. Creatinine 127-137 N-acetyl-alpha-glucosaminidase Homo sapiens 122-125 22870359-8 2012 However, the BUN and urine NAG-creatinine ratios at 72 hours after surgery were higher in isoflurane anesthesia in some carbon dioxide absorbent groups (P = 0.03 and 0.04, respectively). Creatinine 31-41 N-acetyl-alpha-glucosaminidase Homo sapiens 27-30 22870359-8 2012 However, the BUN and urine NAG-creatinine ratios at 72 hours after surgery were higher in isoflurane anesthesia in some carbon dioxide absorbent groups (P = 0.03 and 0.04, respectively). Isoflurane 90-100 N-acetyl-alpha-glucosaminidase Homo sapiens 27-30 30780843-1 2012 Carglumic acid is a structural analog and the first registered synthetic form of the naturally occurring allosteric activator of the urea cycle, N-acetylglutamate (NAG), which is the product of the enzyme NAG synthase (NAGS). carglumic acid 0-14 N-acetyl-alpha-glucosaminidase Homo sapiens 164-167 30780843-1 2012 Carglumic acid is a structural analog and the first registered synthetic form of the naturally occurring allosteric activator of the urea cycle, N-acetylglutamate (NAG), which is the product of the enzyme NAG synthase (NAGS). Urea 133-137 N-acetyl-alpha-glucosaminidase Homo sapiens 164-167 30780843-1 2012 Carglumic acid is a structural analog and the first registered synthetic form of the naturally occurring allosteric activator of the urea cycle, N-acetylglutamate (NAG), which is the product of the enzyme NAG synthase (NAGS). N-acetylglutamic acid 145-162 N-acetyl-alpha-glucosaminidase Homo sapiens 164-167 30780843-2 2012 Because NAG is essential for the function of carbamoylphosphate synthetase 1 as the first step of the urea cycle, a decreased availability of NAG due to primary or secondary defects of NAGS will affect ammonia detoxification in the urea cycle. Urea 102-106 N-acetyl-alpha-glucosaminidase Homo sapiens 8-11 30780843-2 2012 Because NAG is essential for the function of carbamoylphosphate synthetase 1 as the first step of the urea cycle, a decreased availability of NAG due to primary or secondary defects of NAGS will affect ammonia detoxification in the urea cycle. Urea 102-106 N-acetyl-alpha-glucosaminidase Homo sapiens 142-145 22540123-2 2012 The process consists of a one-step preparation of a novel triazine type glycosyl donor in water and the subsequent transglycosylation to a galactose derivative catalysed by alpha-N-acetylglucosaminidase. Triazines 58-66 N-acetyl-alpha-glucosaminidase Homo sapiens 173-202 22540123-2 2012 The process consists of a one-step preparation of a novel triazine type glycosyl donor in water and the subsequent transglycosylation to a galactose derivative catalysed by alpha-N-acetylglucosaminidase. glycosyl 72-80 N-acetyl-alpha-glucosaminidase Homo sapiens 173-202 22540123-2 2012 The process consists of a one-step preparation of a novel triazine type glycosyl donor in water and the subsequent transglycosylation to a galactose derivative catalysed by alpha-N-acetylglucosaminidase. Water 90-95 N-acetyl-alpha-glucosaminidase Homo sapiens 173-202 22540123-2 2012 The process consists of a one-step preparation of a novel triazine type glycosyl donor in water and the subsequent transglycosylation to a galactose derivative catalysed by alpha-N-acetylglucosaminidase. Galactose 139-148 N-acetyl-alpha-glucosaminidase Homo sapiens 173-202 30780843-2 2012 Because NAG is essential for the function of carbamoylphosphate synthetase 1 as the first step of the urea cycle, a decreased availability of NAG due to primary or secondary defects of NAGS will affect ammonia detoxification in the urea cycle. Urea 232-236 N-acetyl-alpha-glucosaminidase Homo sapiens 8-11 30780843-2 2012 Because NAG is essential for the function of carbamoylphosphate synthetase 1 as the first step of the urea cycle, a decreased availability of NAG due to primary or secondary defects of NAGS will affect ammonia detoxification in the urea cycle. Urea 232-236 N-acetyl-alpha-glucosaminidase Homo sapiens 142-145 30780843-4 2012 In addition, it is approved in Europe for the treatment of acute hyperammonemia in patients with specific organic acidurias that can lead to NAG deficiency secondary to inhibition of NAGS. organic acidurias 106-123 N-acetyl-alpha-glucosaminidase Homo sapiens 141-144 22090394-3 2012 Other members of this enzyme family, such as human NAGLU, are active on heparan. heparan 72-79 N-acetyl-alpha-glucosaminidase Homo sapiens 51-56 22156940-2 2012 Our previous studies in mucopolysaccharidosis type IIIB (MPSIIIB), a disease in which a genetic defect induces the accumulation of undigested heparan sulfate (HS) fragments, led to the hypothesis that abnormal lysosome formation was related to events occurring at the Golgi level. Heparitin Sulfate 159-161 N-acetyl-alpha-glucosaminidase Homo sapiens 57-64 22156940-3 2012 We reproduced the enzyme defect of MPSIIIB in HeLa cells using tetracycline-inducible expression of shRNAs directed against alpha-N-acetylglucosaminidase (NAGLU) and addressed this hypothesis. Tetracycline 63-75 N-acetyl-alpha-glucosaminidase Homo sapiens 35-42 22156940-3 2012 We reproduced the enzyme defect of MPSIIIB in HeLa cells using tetracycline-inducible expression of shRNAs directed against alpha-N-acetylglucosaminidase (NAGLU) and addressed this hypothesis. Tetracycline 63-75 N-acetyl-alpha-glucosaminidase Homo sapiens 124-153 22156940-3 2012 We reproduced the enzyme defect of MPSIIIB in HeLa cells using tetracycline-inducible expression of shRNAs directed against alpha-N-acetylglucosaminidase (NAGLU) and addressed this hypothesis. Tetracycline 63-75 N-acetyl-alpha-glucosaminidase Homo sapiens 155-160 22383952-4 2012 N-acetylglutamate synthase (NAGS) produces a unique cofactor, N-acetylglutamate (NAG), that is essential for the catalytic function of the first and rate-limiting enzyme of ureagenesis, carbamyl phosphate synthetase 1 (CPS1). N-acetylglutamic acid 0-17 N-acetyl-alpha-glucosaminidase Homo sapiens 28-31 23776373-2 2011 The initial and rate-limiting enzyme of the urea cycle, carbamylphosphate synthetase 1 (CPS1), requires an allosteric activator, N-acetylglutamate (NAG). Urea 44-48 N-acetyl-alpha-glucosaminidase Homo sapiens 148-151 21898464-1 2011 N-Acetyl-beta-glucosamine (NAG) is an important moiety of glycoproteins and is involved in many biological functions. nag 27-30 N-acetyl-alpha-glucosaminidase Homo sapiens 0-25 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 N-acetyl-alpha-glucosaminidase Homo sapiens 323-331 21685203-3 2011 In this fatal lysosomal storage disease, defective alpha-N-acetylglucosaminidase interrupts the degradation of heparan sulfate (HS) proteoglycans and induces cell disorders predominating in the central nervous system, causing relentless progression toward severe mental retardation. Heparitin Sulfate 111-126 N-acetyl-alpha-glucosaminidase Homo sapiens 51-80 21685203-3 2011 In this fatal lysosomal storage disease, defective alpha-N-acetylglucosaminidase interrupts the degradation of heparan sulfate (HS) proteoglycans and induces cell disorders predominating in the central nervous system, causing relentless progression toward severe mental retardation. Heparitin Sulfate 128-130 N-acetyl-alpha-glucosaminidase Homo sapiens 51-80 23776373-2 2011 The initial and rate-limiting enzyme of the urea cycle, carbamylphosphate synthetase 1 (CPS1), requires an allosteric activator, N-acetylglutamate (NAG). N-acetylglutamic acid 129-146 N-acetyl-alpha-glucosaminidase Homo sapiens 148-151 23776373-11 2011 Treatment of NAGS deficiency with N-carbamyglutamate, a stable analog of NAG, can restore deficient urea cycle function and normalize blood ammonia in affected patients. n-carbamyglutamate 34-52 N-acetyl-alpha-glucosaminidase Homo sapiens 13-16 23776373-11 2011 Treatment of NAGS deficiency with N-carbamyglutamate, a stable analog of NAG, can restore deficient urea cycle function and normalize blood ammonia in affected patients. Urea 100-104 N-acetyl-alpha-glucosaminidase Homo sapiens 13-16 23776373-11 2011 Treatment of NAGS deficiency with N-carbamyglutamate, a stable analog of NAG, can restore deficient urea cycle function and normalize blood ammonia in affected patients. Ammonia 140-147 N-acetyl-alpha-glucosaminidase Homo sapiens 13-16 21725930-8 2011 CONCLUSIONS: Replacement of glucose with NAG in the dialysis fluid can slow down aging of MC. Methylcholanthrene 90-92 N-acetyl-alpha-glucosaminidase Homo sapiens 41-44 22754010-2 2011 Currently, NAG is being produced by an environment-unfriendly chemical process using chitin, a polysaccharide present in abundance in the exoskeleton of crustaceans, as a substrate. Chitin 85-91 N-acetyl-alpha-glucosaminidase Homo sapiens 11-14 22754010-2 2011 Currently, NAG is being produced by an environment-unfriendly chemical process using chitin, a polysaccharide present in abundance in the exoskeleton of crustaceans, as a substrate. Polysaccharides 95-109 N-acetyl-alpha-glucosaminidase Homo sapiens 11-14 19754428-6 2009 The location of the NAG site is identical to that of the weak bacterial CPS activator IMP (inosine monophosphate) in Escherichia coli CPS, indicating a common origin for these sites and excluding any relatedness to the binding site of the other bacterial CPS activator, ornithine. Inosine Monophosphate 91-112 N-acetyl-alpha-glucosaminidase Homo sapiens 20-23 20303810-1 2010 N-acetylglutamate (NAG) is a unique enzyme cofactor, essential for liver ureagenesis in mammals while it is the first committed substrate for de novo arginine biosynthesis in microorganisms and plants. N-acetylglutamic acid 0-17 N-acetyl-alpha-glucosaminidase Homo sapiens 19-22 20303810-1 2010 N-acetylglutamate (NAG) is a unique enzyme cofactor, essential for liver ureagenesis in mammals while it is the first committed substrate for de novo arginine biosynthesis in microorganisms and plants. Arginine 150-158 N-acetyl-alpha-glucosaminidase Homo sapiens 19-22 20303810-2 2010 The enzyme that produces NAG from glutamate and CoA, NAG synthase (NAGS), is allosterically inhibited by arginine in microorganisms and plants and activated in mammals. Glutamic Acid 34-43 N-acetyl-alpha-glucosaminidase Homo sapiens 25-28 20303810-2 2010 The enzyme that produces NAG from glutamate and CoA, NAG synthase (NAGS), is allosterically inhibited by arginine in microorganisms and plants and activated in mammals. Arginine 105-113 N-acetyl-alpha-glucosaminidase Homo sapiens 25-28 20303810-9 2010 For either condition, N-carbamylglutamate (NCG), a stable functional analog of NAG, was found to either restore or improve the deficient urea-cycle function. N-carbamylglutamate 22-41 N-acetyl-alpha-glucosaminidase Homo sapiens 79-82 20303810-9 2010 For either condition, N-carbamylglutamate (NCG), a stable functional analog of NAG, was found to either restore or improve the deficient urea-cycle function. Urea 137-141 N-acetyl-alpha-glucosaminidase Homo sapiens 79-82 19754428-0 2009 Structural insight on the control of urea synthesis: identification of the binding site for N-acetyl-L-glutamate, the essential allosteric activator of mitochondrial carbamoyl phosphate synthetase. Urea 37-41 N-acetyl-alpha-glucosaminidase Homo sapiens 92-112 19754428-1 2009 NAG (N-acetyl-L-glutamate), the essential allosteric activator of the first urea cycle enzyme, CPSI (carbamoyl phosphate synthetase I), is a key regulator of this crucial cycle for ammonia detoxification in animals (including humans). Urea 76-80 N-acetyl-alpha-glucosaminidase Homo sapiens 0-3 19754428-1 2009 NAG (N-acetyl-L-glutamate), the essential allosteric activator of the first urea cycle enzyme, CPSI (carbamoyl phosphate synthetase I), is a key regulator of this crucial cycle for ammonia detoxification in animals (including humans). Urea 76-80 N-acetyl-alpha-glucosaminidase Homo sapiens 5-25 19754428-1 2009 NAG (N-acetyl-L-glutamate), the essential allosteric activator of the first urea cycle enzyme, CPSI (carbamoyl phosphate synthetase I), is a key regulator of this crucial cycle for ammonia detoxification in animals (including humans). Ammonia 181-188 N-acetyl-alpha-glucosaminidase Homo sapiens 0-3 19754428-1 2009 NAG (N-acetyl-L-glutamate), the essential allosteric activator of the first urea cycle enzyme, CPSI (carbamoyl phosphate synthetase I), is a key regulator of this crucial cycle for ammonia detoxification in animals (including humans). Ammonia 181-188 N-acetyl-alpha-glucosaminidase Homo sapiens 5-25 19754428-6 2009 The location of the NAG site is identical to that of the weak bacterial CPS activator IMP (inosine monophosphate) in Escherichia coli CPS, indicating a common origin for these sites and excluding any relatedness to the binding site of the other bacterial CPS activator, ornithine. Ornithine 270-279 N-acetyl-alpha-glucosaminidase Homo sapiens 20-23 19754428-4 2009 It can tightly accommodate one extended NAG molecule having the delta-COO- at the pocket entry, the alpha-COO- and acetamido groups tightly hydrogen bonded to the pocket, and the terminal methyl of the acetamido substituent surrounded by hydrophobic residues. Hydrogen 140-148 N-acetyl-alpha-glucosaminidase Homo sapiens 40-43 19754428-7 2009 Our findings open the way to the identification of CPSI deficiency patients carrying NAG site mutations, and to the possibility of tailoring the activator to fit a given NAG site mutation, as exemplified here with N-acetyl-L(+/-)-beta-phenylglutamate for the W1410K CPSI mutation. n-acetyl-l(+/-)-beta-phenylglutamate 214-250 N-acetyl-alpha-glucosaminidase Homo sapiens 170-173 19754428-5 2009 This binding mode is supported by the observation of reduced NAG affinity upon mutation of NAG-interacting residues of CPSI (recombinantly expressed using baculovirus/insect cells); by the fine-mapping of the N-chloroacetyl-L-glutamate photoaffinity labelling site of CPSI; and by previously established structure-activity relationships for NAG analogues. n-chloroacetyl-l-glutamate 209-235 N-acetyl-alpha-glucosaminidase Homo sapiens 61-64 19691938-8 2009 Amino sugars such as NAG may competitively bind to CD44, modulating keratinocyte cellular adhesion. Amino Sugars 0-12 N-acetyl-alpha-glucosaminidase Homo sapiens 21-24 19247681-2 2009 In the skin, HA can be synthesized by dermal fibroblasts and N-acetylglucosamine (NAG) is a precursor for HA biosynthesis in the body. Acetylglucosamine 61-80 N-acetyl-alpha-glucosaminidase Homo sapiens 82-85 19691938-10 2009 We propose the use of amino sugars such as NAG as alternative compounds to replace the use of alpha-hydroxy acids in skin care. Amino Sugars 22-34 N-acetyl-alpha-glucosaminidase Homo sapiens 43-46 18581145-8 2008 U(NAG) and U(NAG) to creatinine ratio (U(NAG/CR)) were elevated in all patients with thalassemia compared with the control group (p < 0.001) and were directly correlated to the amount of transfused iron but not to actual ferritin level. Creatinine 21-31 N-acetyl-alpha-glucosaminidase Homo sapiens 13-16 19399896-1 2009 Sanfilippo syndrome type B (MPS III B) is caused by a deficiency of alpha-N-acetylglucosaminidase enzyme (Naglu), leading to accumulation of heparan sulfate (HS), a glycosaminoglycan (GAG), within lysosomes and to eventual progressive cerebral and systemic multiple organ abnormalities. Heparitin Sulfate 141-156 N-acetyl-alpha-glucosaminidase Homo sapiens 28-37 19399896-1 2009 Sanfilippo syndrome type B (MPS III B) is caused by a deficiency of alpha-N-acetylglucosaminidase enzyme (Naglu), leading to accumulation of heparan sulfate (HS), a glycosaminoglycan (GAG), within lysosomes and to eventual progressive cerebral and systemic multiple organ abnormalities. Heparitin Sulfate 158-160 N-acetyl-alpha-glucosaminidase Homo sapiens 28-37 19399896-1 2009 Sanfilippo syndrome type B (MPS III B) is caused by a deficiency of alpha-N-acetylglucosaminidase enzyme (Naglu), leading to accumulation of heparan sulfate (HS), a glycosaminoglycan (GAG), within lysosomes and to eventual progressive cerebral and systemic multiple organ abnormalities. Glycosaminoglycans 165-182 N-acetyl-alpha-glucosaminidase Homo sapiens 28-37 19399896-1 2009 Sanfilippo syndrome type B (MPS III B) is caused by a deficiency of alpha-N-acetylglucosaminidase enzyme (Naglu), leading to accumulation of heparan sulfate (HS), a glycosaminoglycan (GAG), within lysosomes and to eventual progressive cerebral and systemic multiple organ abnormalities. Glycosaminoglycans 184-187 N-acetyl-alpha-glucosaminidase Homo sapiens 28-37 19088067-9 2009 We can exclude alpha1,3-fucosylation of the two peripheral GlcNAcs linked to the trimannosyl core of the acceptor, because the FUT10 fucosylated biantennary N-glycan product loses both terminal GlcNAc residues after digestion with human placenta alpha-N-acetylglucosaminidase. n-glycan 157-165 N-acetyl-alpha-glucosaminidase Homo sapiens 246-275 18338235-1 2008 Hyperammonaemia is common in neonates with branched-chain organic acidaemias, primarily due to the inhibition of N-acetylglutamate (NAG) synthetase; NAG is an activator for carbamylphosphate synthetase I, the first enzyme of the urea cycle. Urea 229-233 N-acetyl-alpha-glucosaminidase Homo sapiens 132-135 18338235-1 2008 Hyperammonaemia is common in neonates with branched-chain organic acidaemias, primarily due to the inhibition of N-acetylglutamate (NAG) synthetase; NAG is an activator for carbamylphosphate synthetase I, the first enzyme of the urea cycle. Urea 229-233 N-acetyl-alpha-glucosaminidase Homo sapiens 149-152 18338235-2 2008 N-Carbamylglutamate, a NAG analogue, has been reported to correct hyperammonaemia in neonates with organic acidaemias. N-carbamylglutamate 0-19 N-acetyl-alpha-glucosaminidase Homo sapiens 23-26 18338235-2 2008 N-Carbamylglutamate, a NAG analogue, has been reported to correct hyperammonaemia in neonates with organic acidaemias. organic acidaemias 99-117 N-acetyl-alpha-glucosaminidase Homo sapiens 23-26 19416848-2 2009 The primary cause is mutation in the NAGLU gene, resulting in deficiency of alpha-N-acetylglucosaminidase and lysosomal accumulation of heparan sulfate. Heparitin Sulfate 136-151 N-acetyl-alpha-glucosaminidase Homo sapiens 37-42 18581145-8 2008 U(NAG) and U(NAG) to creatinine ratio (U(NAG/CR)) were elevated in all patients with thalassemia compared with the control group (p < 0.001) and were directly correlated to the amount of transfused iron but not to actual ferritin level. Creatinine 21-31 N-acetyl-alpha-glucosaminidase Homo sapiens 13-16 17075868-1 2007 In this study three model drugs (N-acetyl-D-glucosamine (NAG), anhydrous caffeine, and propranolol hydrochloride) were agglomerated with starch acetate (SA) by mixing the binary powders on a stainless steel (SS) plate. starch acetate 137-151 N-acetyl-alpha-glucosaminidase Homo sapiens 57-60 17573853-8 2008 Triton X-100 stimulated sperm and epididymal NAG activity but not the enzyme obtained from other sources. Octoxynol 0-12 N-acetyl-alpha-glucosaminidase Homo sapiens 45-48 18047607-4 2007 To identify additional mechanisms by which NAG might affect melanin production, an in vitro genomics experiment was conducted in SkinEthic skin equivalent cultures, which were topically dosed with NAG vs. a vehicle control. Melanins 60-67 N-acetyl-alpha-glucosaminidase Homo sapiens 43-46 18047607-5 2007 Relative to vehicle, NAG reduced melanin production, and the expression of several pigmentation-relevant genes were affected (down-regulated or up-regulated) by NAG treatment. Melanins 33-40 N-acetyl-alpha-glucosaminidase Homo sapiens 21-24 18022595-2 2007 N-acetylglucosamine (NAG) is a solute of the comparable size to glucose, with strong anti-inflammatory properties. Glucose 64-71 N-acetyl-alpha-glucosaminidase Homo sapiens 0-19 18022595-2 2007 N-acetylglucosamine (NAG) is a solute of the comparable size to glucose, with strong anti-inflammatory properties. Glucose 64-71 N-acetyl-alpha-glucosaminidase Homo sapiens 21-24 18022595-7 2007 GLU caused hypertrophy of mesothelial cells (+53% vs control, P < 0.001) and prolonged their population doubling time (+16% vs control, P < 0.01); NAG did not cause significant changes in these parameters. Glutamic Acid 0-3 N-acetyl-alpha-glucosaminidase Homo sapiens 153-156 18022595-8 2007 Healing of mesothelial monolayer after mechanical injury was impaired in GLU treated cells: (-48% vs control, P < 0.001 and -40% vs NAG, P < 0.05). Glutamic Acid 73-76 N-acetyl-alpha-glucosaminidase Homo sapiens 135-138 18022595-10 2007 In the presence of NAG, these parameters were comparable with the control group, but at the same time NAG stimulated synthesis of hyaluronan: +116% versus control, P < 0.001 and + 96% versus GLU, P < 0.01. Hyaluronic Acid 130-140 N-acetyl-alpha-glucosaminidase Homo sapiens 102-105 18022595-10 2007 In the presence of NAG, these parameters were comparable with the control group, but at the same time NAG stimulated synthesis of hyaluronan: +116% versus control, P < 0.001 and + 96% versus GLU, P < 0.01. Glutamic Acid 194-197 N-acetyl-alpha-glucosaminidase Homo sapiens 19-22 18022595-10 2007 In the presence of NAG, these parameters were comparable with the control group, but at the same time NAG stimulated synthesis of hyaluronan: +116% versus control, P < 0.001 and + 96% versus GLU, P < 0.01. Glutamic Acid 194-197 N-acetyl-alpha-glucosaminidase Homo sapiens 102-105 18022595-11 2007 Treatment with GLU resulted in decline of tissue plasminogen activator/plasminogen activator inhibitor-1 (t-PA/PAI-1) ratio by 23% versus control, P < 0.001, whereas NAG increased that parameter by 43%, P < 0.01 versus control. Glutamic Acid 15-18 N-acetyl-alpha-glucosaminidase Homo sapiens 169-172 17679744-10 2007 There was a significantly positive correlation between the NAG values and the change in the blood glucose level (p=0.001), hence diabetic CKD patients should be meticulously followed during Ramadan fasting. Glucose 98-105 N-acetyl-alpha-glucosaminidase Homo sapiens 59-62 16890218-4 2007 Among the women, the NAG and AMG were positively correlated with both the daily mercury intake and mercury levels in hair, toenail, and urine (P<0.01); and, these relations were almost similar when using multiple regression analysis to adjust for possible confounders such as urinary cadmium (0.47+/-0.28 microg/g creatinine) and smoking status. Creatinine 317-327 N-acetyl-alpha-glucosaminidase Homo sapiens 21-24 19099774-6 2008 METHODS: Two fluorigenic substrate (4-methylumbelliferyl-alpha-D-N-sulphoglucosaminide.Na and 4-methylumbelliferyl-alpha-N-acetylglucosaminide) were used for the assay of SGSH and NAGLU activity. 4-methylumbelliferyl-alpha-d-n-sulphoglucosaminide 36-86 N-acetyl-alpha-glucosaminidase Homo sapiens 180-185 24692796-12 2008 Urinary GAG concentration decreased significantly in all 5 patients with MPS IIIA and in 2 patients with MPS IIIB (P = 0.028). Glycosaminoglycans 8-11 N-acetyl-alpha-glucosaminidase Homo sapiens 105-113 17640047-1 2007 Sanfilippo type B is an autosomal recessive mucopolysaccharidosis (MPS IIIB) caused by deficiency of N-acetyl-alpha-D-glucosaminidase, a lysosomal enzyme involved in the degradation of heparan sulfate. Heparitin Sulfate 185-200 N-acetyl-alpha-glucosaminidase Homo sapiens 67-75 17460717-6 2007 infusion of mannitol, to complement the CNS delivery of adeno-associated viral (AAV) vector for treating MPS IIIB in young adult mice. Mannitol 12-20 N-acetyl-alpha-glucosaminidase Homo sapiens 105-113 16890218-4 2007 Among the women, the NAG and AMG were positively correlated with both the daily mercury intake and mercury levels in hair, toenail, and urine (P<0.01); and, these relations were almost similar when using multiple regression analysis to adjust for possible confounders such as urinary cadmium (0.47+/-0.28 microg/g creatinine) and smoking status. Mercury 80-87 N-acetyl-alpha-glucosaminidase Homo sapiens 21-24 16890218-4 2007 Among the women, the NAG and AMG were positively correlated with both the daily mercury intake and mercury levels in hair, toenail, and urine (P<0.01); and, these relations were almost similar when using multiple regression analysis to adjust for possible confounders such as urinary cadmium (0.47+/-0.28 microg/g creatinine) and smoking status. Mercury 99-106 N-acetyl-alpha-glucosaminidase Homo sapiens 21-24 16890218-4 2007 Among the women, the NAG and AMG were positively correlated with both the daily mercury intake and mercury levels in hair, toenail, and urine (P<0.01); and, these relations were almost similar when using multiple regression analysis to adjust for possible confounders such as urinary cadmium (0.47+/-0.28 microg/g creatinine) and smoking status. Cadmium 287-294 N-acetyl-alpha-glucosaminidase Homo sapiens 21-24 17075868-4 2007 Triboelectric measurements showed that when the drugs were in contact with SS, charges of the opposite polarity were generated to SA (+) and caffeine and NAG (-) promoting adhesion. Stainless Steel 75-77 N-acetyl-alpha-glucosaminidase Homo sapiens 154-157 17910281-7 2007 NAG enzymuria (units/mmol creatinine) was increased in both diabetic groups compared to control values (group B: 122 +/- 7, group A: 70 +/- 5, controls 27 +/- 2, all P<0.001). Creatinine 26-36 N-acetyl-alpha-glucosaminidase Homo sapiens 0-3 16616506-2 2006 Replacement of the acetamido group by azidoacetamido group resulted in an inhibitor, N-azidoacetyl-beta-D-glucopyranosylamine (azido-NAG), with a Ki value of 48.7 microM, in the direction of glycogen synthesis. azidoacetamido 38-52 N-acetyl-alpha-glucosaminidase Homo sapiens 133-136 17510888-5 2007 Negligible permeability was observed for NAG in neat solutions of known membrane permeation enhancers ethanol, oleic acid, isopropyl myristate, and isopropyl palmitate, as well as from saturated solutions of NAG in water or phosphate buffer. Water 215-220 N-acetyl-alpha-glucosaminidase Homo sapiens 208-211 17510888-6 2007 Permeability measurements obtained from saturated solutions of NAG in DMSO and phosphate buffer solutions containing ethanol at 2%, 5%, 10%, 25%, and 50% demonstrated excellent permeation. Ethanol 117-124 N-acetyl-alpha-glucosaminidase Homo sapiens 63-66 16844430-12 2007 A highly significant difference in NAG excretion was observed on day 14 for tobramycin vs. colistin (median 2.24 vs. 0.98, p<0.001). Tobramycin 76-86 N-acetyl-alpha-glucosaminidase Homo sapiens 35-38 16844430-17 2007 CONCLUSIONS: Both tobramycin and colistin cause acute renal tubular injury with a significant rise in urinary NAG excretion. Tobramycin 18-28 N-acetyl-alpha-glucosaminidase Homo sapiens 110-113 17510888-1 2007 Transdermal permeation of N-acetyl-D-glucosamine (NAG), a metabolite of glucosamine was examined. Glucosamine 37-48 N-acetyl-alpha-glucosaminidase Homo sapiens 50-53 16829627-1 2006 The glycosidase-recognizing N-acetylglucosamine terminal residue, N-acetylglucosaminidase (NAG), has been repetitively implicated in fertilization. Acetylglucosamine 28-47 N-acetyl-alpha-glucosaminidase Homo sapiens 66-89 16829627-1 2006 The glycosidase-recognizing N-acetylglucosamine terminal residue, N-acetylglucosaminidase (NAG), has been repetitively implicated in fertilization. Acetylglucosamine 28-47 N-acetyl-alpha-glucosaminidase Homo sapiens 91-94 16829627-6 2006 Different NAG-specific reagents-an inhibitor (2-acetamido-2-deoxy-D-glucono-1,5-lactone), a substrate (p-nitrophenyl-N-acetylglucosaminide) and an anti-NAG antibody-were able to impair sperm binding to the ZP when present during these assays. 2-acetamido-2-deoxy-D-glucono-(1,5)-lactone 46-87 N-acetyl-alpha-glucosaminidase Homo sapiens 10-13 16616506-2 2006 Replacement of the acetamido group by azidoacetamido group resulted in an inhibitor, N-azidoacetyl-beta-D-glucopyranosylamine (azido-NAG), with a Ki value of 48.7 microM, in the direction of glycogen synthesis. N-azidoacetyl-beta-D-glucopyranosylamine 85-125 N-acetyl-alpha-glucosaminidase Homo sapiens 133-136 16616506-2 2006 Replacement of the acetamido group by azidoacetamido group resulted in an inhibitor, N-azidoacetyl-beta-D-glucopyranosylamine (azido-NAG), with a Ki value of 48.7 microM, in the direction of glycogen synthesis. Glycogen 191-199 N-acetyl-alpha-glucosaminidase Homo sapiens 133-136 16797334-3 2006 We observed a close relation between urine NAG excretion and urine inorganic fluoride levels in the intraoperative period and early postoperative days. inorganic fluoride 67-85 N-acetyl-alpha-glucosaminidase Homo sapiens 43-46 16804628-7 2006 The serum selenium concentration and serum glutathione peroxidase activity were associated with the activity of N-acetyl-beta-D-glucosaminidase in urine (U-NAG). Selenium 10-18 N-acetyl-alpha-glucosaminidase Homo sapiens 156-159 16804628-8 2006 The results indicate that having higher glutathione peroxidase activity or a higher serum selenium concentration results in a lower excretion of U-NAG. Selenium 90-98 N-acetyl-alpha-glucosaminidase Homo sapiens 147-150 16804628-10 2006 Apparently the well-known association between U-NAG and age could only be found for the participants with a lower selenium status. Selenium 114-122 N-acetyl-alpha-glucosaminidase Homo sapiens 48-51 16804628-11 2006 CONCLUSIONS: Increased activities of U-NAG during ongoing exposure to mercury vapor appear to be reversible upon cessation of exposure. Mercury 70-77 N-acetyl-alpha-glucosaminidase Homo sapiens 39-42 16804628-12 2006 Selenium status has a substantial impact on U-NAG activity and should be considered in studies of U-NAG excretion. Selenium 0-8 N-acetyl-alpha-glucosaminidase Homo sapiens 46-49 16804628-12 2006 Selenium status has a substantial impact on U-NAG activity and should be considered in studies of U-NAG excretion. Selenium 0-8 N-acetyl-alpha-glucosaminidase Homo sapiens 100-103 16321554-10 2006 Processing of NAGS-M to form NAGS-C results in an enzyme with higher catalytic activity and could play a role in the regulation of NAG production, CPSI function, and urea synthesis. cpsi 147-151 N-acetyl-alpha-glucosaminidase Homo sapiens 14-17 16321554-1 2006 N-Acetylglutamate synthase (NAGS, EC 2.3.1.1) is a mitochondrial enzyme that catalyzes the formation of N-acetylglutamate (NAG) from glutamate and acetylcoenzyme A. N-acetylglutamic acid 104-121 N-acetyl-alpha-glucosaminidase Homo sapiens 28-31 16321554-10 2006 Processing of NAGS-M to form NAGS-C results in an enzyme with higher catalytic activity and could play a role in the regulation of NAG production, CPSI function, and urea synthesis. Urea 166-170 N-acetyl-alpha-glucosaminidase Homo sapiens 14-17 16321554-1 2006 N-Acetylglutamate synthase (NAGS, EC 2.3.1.1) is a mitochondrial enzyme that catalyzes the formation of N-acetylglutamate (NAG) from glutamate and acetylcoenzyme A. Glutamic Acid 8-17 N-acetyl-alpha-glucosaminidase Homo sapiens 28-31 16321554-1 2006 N-Acetylglutamate synthase (NAGS, EC 2.3.1.1) is a mitochondrial enzyme that catalyzes the formation of N-acetylglutamate (NAG) from glutamate and acetylcoenzyme A. Acetyl Coenzyme A 147-163 N-acetyl-alpha-glucosaminidase Homo sapiens 28-31 16137227-0 2005 Transplantation of human umbilical cord blood cells benefits an animal model of Sanfilippo syndrome type B. Sanfilippo syndrome type B is caused by alpha-N-acetylglucosaminidase (Naglu) enzyme deficiency leading to an accumulation of undegraded heparan sulfate, a glycosaminoglycan (GAG). Heparitin Sulfate 245-260 N-acetyl-alpha-glucosaminidase Homo sapiens 179-184 16321554-2 2006 NAG is an obligatory activator of carbamylphosphate I (CPSI), the first and a rate limiting enzyme of ureagenesis. carbamylphosphate i 34-53 N-acetyl-alpha-glucosaminidase Homo sapiens 0-3 16321554-2 2006 NAG is an obligatory activator of carbamylphosphate I (CPSI), the first and a rate limiting enzyme of ureagenesis. cpsi 55-59 N-acetyl-alpha-glucosaminidase Homo sapiens 0-3 16343875-1 2006 The aim of this study was to design site specific, controlled release tablets of N-acetyl-d-glucosamine (NAG), maltose monohydrate and maltopentaose by using hydrophobic matrix formers starch acetate (SA) and ethyl cellulose (EC). starch acetate 185-199 N-acetyl-alpha-glucosaminidase Homo sapiens 105-108 16343875-1 2006 The aim of this study was to design site specific, controlled release tablets of N-acetyl-d-glucosamine (NAG), maltose monohydrate and maltopentaose by using hydrophobic matrix formers starch acetate (SA) and ethyl cellulose (EC). starch acetate 201-203 N-acetyl-alpha-glucosaminidase Homo sapiens 105-108 16343875-1 2006 The aim of this study was to design site specific, controlled release tablets of N-acetyl-d-glucosamine (NAG), maltose monohydrate and maltopentaose by using hydrophobic matrix formers starch acetate (SA) and ethyl cellulose (EC). ethyl cellulose 209-224 N-acetyl-alpha-glucosaminidase Homo sapiens 105-108 16343875-1 2006 The aim of this study was to design site specific, controlled release tablets of N-acetyl-d-glucosamine (NAG), maltose monohydrate and maltopentaose by using hydrophobic matrix formers starch acetate (SA) and ethyl cellulose (EC). ethyl cellulose 226-228 N-acetyl-alpha-glucosaminidase Homo sapiens 105-108 16141440-11 2005 A linear correlation between cTnT or NAG and GSSG was found. Glutathione Disulfide 45-49 N-acetyl-alpha-glucosaminidase Homo sapiens 37-40 16236942-12 2005 Serum glucose was independently associated with intestinal injury (urine I-FABP peak, R2 = 42.5%, beta = 114.4 +/- 31.4, significant at p = 0.002; urine L-FABP peak, R2 = 47.3%, beta = 7,714.1 +/- 1,920.9, significant at p = 0.001) and renal injury (urine NAG, R2 = 32.1%, beta = 0.21 +/- 0.07, significant at p = 0.009). Glucose 6-13 N-acetyl-alpha-glucosaminidase Homo sapiens 256-259 16299682-11 2005 There was a significant positive correlation between serum Cys C, urinary NAG, LDH, ALP activities and serum Cr levels. Creatinine 109-111 N-acetyl-alpha-glucosaminidase Homo sapiens 74-77 16299682-12 2005 However, there was an inverse correlation between serum Cys C, urinary NAG, LDH, ALP and CCr and CCG in diabetic patients. cationic colloidal gold 97-100 N-acetyl-alpha-glucosaminidase Homo sapiens 71-74 16213146-5 2006 To compare the binding mode of N-trifluoroacetyl derivative with that of the lead molecule, we also determined the structure of GPb-NAG complex at a higher resolution (1.9 angstroms). Nitrogen 31-32 N-acetyl-alpha-glucosaminidase Homo sapiens 132-135 16553303-1 2006 Activity of tubular lysosomic (N-acetyl-beta-D-glucosaminidase--NAG, its thermostable isoenzyme NAG B and B-galactosidase--beta-GAL) and mitochondrial (L-canavanine: ornithine amidinetransferase--COAT) enzymes were measured in urine of 30 patients with diabetes complicated by diabetic nephropathy (DN). Canavanine 152-164 N-acetyl-alpha-glucosaminidase Homo sapiens 64-67 16553303-2 2006 It was shown that activity of NAG, especially its thermostable isoenzyme NAG B and also beta-GAL in urine of DN patients was higher compare to those in healthy subject. beta-D-galactose 88-96 N-acetyl-alpha-glucosaminidase Homo sapiens 30-33 16538969-0 2006 Urinary N-acetyl B glucosaminidase as an earlier marker of diabetic nephropathy and influence of low-dose perindopril/indapamide combination. Perindopril 106-117 N-acetyl-alpha-glucosaminidase Homo sapiens 8-34 16538969-3 2006 OBJECTIVE: The objective of this study is whether NAG can be used as an early marker of diabetic nephropathy by comparing the urinary NAG levels between healthy controls and diabetic patients and determining changes in urinary NAG excretion after treatment with low-dose combination perindopril (2 mg)/ indapamide (0.625 mg)/o.d. Perindopril 283-294 N-acetyl-alpha-glucosaminidase Homo sapiens 50-53 16538969-3 2006 OBJECTIVE: The objective of this study is whether NAG can be used as an early marker of diabetic nephropathy by comparing the urinary NAG levels between healthy controls and diabetic patients and determining changes in urinary NAG excretion after treatment with low-dose combination perindopril (2 mg)/ indapamide (0.625 mg)/o.d. Indapamide 303-313 N-acetyl-alpha-glucosaminidase Homo sapiens 50-53 16538969-9 2006 The assay defined as fragmentation of 3-cresolsulfonphthaleinyl-N-acetyl-beta-D-glucosaminide molecule by NAG to 3-cresolsulphonphthalein and N-acetylglucosamine molecules and serum creatinine were measured in all groups. 3-cresolsulfonphthaleinyl-N-acetylglucosaminide 38-93 N-acetyl-alpha-glucosaminidase Homo sapiens 106-109 16538969-9 2006 The assay defined as fragmentation of 3-cresolsulfonphthaleinyl-N-acetyl-beta-D-glucosaminide molecule by NAG to 3-cresolsulphonphthalein and N-acetylglucosamine molecules and serum creatinine were measured in all groups. 3-cresolsulphonphthalein 113-137 N-acetyl-alpha-glucosaminidase Homo sapiens 106-109 16538969-9 2006 The assay defined as fragmentation of 3-cresolsulfonphthaleinyl-N-acetyl-beta-D-glucosaminide molecule by NAG to 3-cresolsulphonphthalein and N-acetylglucosamine molecules and serum creatinine were measured in all groups. Acetylglucosamine 142-161 N-acetyl-alpha-glucosaminidase Homo sapiens 106-109 16538969-9 2006 The assay defined as fragmentation of 3-cresolsulfonphthaleinyl-N-acetyl-beta-D-glucosaminide molecule by NAG to 3-cresolsulphonphthalein and N-acetylglucosamine molecules and serum creatinine were measured in all groups. Creatinine 182-192 N-acetyl-alpha-glucosaminidase Homo sapiens 106-109 16538969-15 2006 Perindopril/indapamide administration is effective in reducing urinary NAG excretion in these patients, and this effect seems to be independent from blood pressure and glycemia control. Perindopril 0-11 N-acetyl-alpha-glucosaminidase Homo sapiens 71-74 16538969-15 2006 Perindopril/indapamide administration is effective in reducing urinary NAG excretion in these patients, and this effect seems to be independent from blood pressure and glycemia control. Indapamide 12-22 N-acetyl-alpha-glucosaminidase Homo sapiens 71-74 16137227-0 2005 Transplantation of human umbilical cord blood cells benefits an animal model of Sanfilippo syndrome type B. Sanfilippo syndrome type B is caused by alpha-N-acetylglucosaminidase (Naglu) enzyme deficiency leading to an accumulation of undegraded heparan sulfate, a glycosaminoglycan (GAG). Glycosaminoglycans 283-286 N-acetyl-alpha-glucosaminidase Homo sapiens 179-184