PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 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. 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 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 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 26592762-2 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 3886433-13 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