PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
3346674-1	1988	N-Acetylated-alpha-linked acidic dipeptidase (NAALADase) is a Cl- dependent, membrane bound, metallopeptidase that cleaves the endogenous neuropeptide N-acetyl-L-aspartyl-L-glutamate (NAAG) in vitro.	Ac-Asp-Glu(3-)	151-182	folate hydrolase 1B (pseudogene)	Homo sapiens	0-44
34684866-1	2021	We report the results of a computational study of the hydrolysis reaction mechanism of N-acetyl-l-aspartyl-l-glutamate (NAAG) catalyzed by glutamate carboxypeptidase II.	Ac-Asp-Glu(3-)	87-118	folate hydrolase 1	Homo sapiens	139-168
3346674-1	1988	N-Acetylated-alpha-linked acidic dipeptidase (NAALADase) is a Cl- dependent, membrane bound, metallopeptidase that cleaves the endogenous neuropeptide N-acetyl-L-aspartyl-L-glutamate (NAAG) in vitro.	Ac-Asp-Glu(3-)	151-182	folate hydrolase 1B (pseudogene)	Homo sapiens	46-55
27589333-3	2016	Radiolabeled peptide targeting technologies have rapidly evolved over the last decade and have focused on the successful development of radiolabeled small molecules that act as inhibitors to the binding of the N-acetyl-l-aspartyl-l-glutamate (NAAG) substrate to the PSMA molecule.	Ac-Asp-Glu(3-)	210-241	folate hydrolase 1	Homo sapiens	266-270
3667587-2	1987	High performance liquid chromatography studies documented the presence of an enzyme activity, N-acetylated alpha-linked acidic dipeptidase (NAALA dipeptidase), in rat brain membranes that cleaves the endogenous brain dipeptide, N-acetyl-L-aspartyl-L-glutamate to N-acetyl-aspartate and glutamate.	Ac-Asp-Glu(3-)	228-259	folate hydrolase 1	Rattus norvegicus	94-138
24647901-1	2014	BACKGROUND: Glutamate carboxypeptidase II (GCPII) is a transmembrane enzyme that cleaves N-acetyl-L-aspartyl-L-glutamate (NAAG) in the brain.	Ac-Asp-Glu(3-)	89-120	folate hydrolase 1	Homo sapiens	12-41
24647901-1	2014	BACKGROUND: Glutamate carboxypeptidase II (GCPII) is a transmembrane enzyme that cleaves N-acetyl-L-aspartyl-L-glutamate (NAAG) in the brain.	Ac-Asp-Glu(3-)	89-120	folate hydrolase 1	Homo sapiens	43-48
17714508-3	2007	To complement and extend the structural studies, we constructed a model of GCPII in complex with its substrate, N-acetyl-l-aspartyl-l-glutamate, which enabled us to predict additional amino acid residues interacting with the bound substrate, and used site-directed mutagenesis to assess the contribution of individual residues for substrate/inhibitor binding and enzymatic activity of GCPII.	Ac-Asp-Glu(3-)	112-143	folate hydrolase 1	Homo sapiens	75-80
23891752-1	2013	We recently reported that glutamate carboxypeptidase II (GCPII) has a new physiological function degrading amyloid-beta (Abeta), distinct from its own hydrolysis activity in N-acetyl-L-aspartyl-L-glutamate (NAAG); however, its underlying mechanism remains undiscovered.	Ac-Asp-Glu(3-)	174-205	folate hydrolase 1	Homo sapiens	26-55
23891752-1	2013	We recently reported that glutamate carboxypeptidase II (GCPII) has a new physiological function degrading amyloid-beta (Abeta), distinct from its own hydrolysis activity in N-acetyl-L-aspartyl-L-glutamate (NAAG); however, its underlying mechanism remains undiscovered.	Ac-Asp-Glu(3-)	174-205	folate hydrolase 1	Homo sapiens	57-62
23525279-5	2013	GCPII is a zinc exopeptidase that cleaves glutamate from N-acetyl-L-aspartyl-L-glutamate in the central nervous system and from pteroylpoly-gamma-glutamate in the jejunum.	Ac-Asp-Glu(3-)	57-88	folate hydrolase 1	Homo sapiens	0-5
19301871-2	2009	The hydrolysis of N-acetyl-l-aspartyl-l-glutamate (N-Ac-Asp-Glu), the natural dipeptidic substrate of the GCPII, is intimately involved in cellular signaling within the mammalian nervous system, but the exact mechanism of this reaction has not yet been determined.	Ac-Asp-Glu(3-)	18-49	folate hydrolase 1	Homo sapiens	106-111
17714508-3	2007	To complement and extend the structural studies, we constructed a model of GCPII in complex with its substrate, N-acetyl-l-aspartyl-l-glutamate, which enabled us to predict additional amino acid residues interacting with the bound substrate, and used site-directed mutagenesis to assess the contribution of individual residues for substrate/inhibitor binding and enzymatic activity of GCPII.	Ac-Asp-Glu(3-)	112-143	folate hydrolase 1	Homo sapiens	385-390
16467855-1	2006	Membrane-bound glutamate carboxypeptidase II (GCPII) is a zinc metalloenzyme that catalyzes the hydrolysis of the neurotransmitter N-acetyl-L-aspartyl-L-glutamate (NAAG) to N-acetyl-L-aspartate and L-glutamate (which is itself a neurotransmitter).	Ac-Asp-Glu(3-)	131-162	folate hydrolase 1	Homo sapiens	15-44
16467855-1	2006	Membrane-bound glutamate carboxypeptidase II (GCPII) is a zinc metalloenzyme that catalyzes the hydrolysis of the neurotransmitter N-acetyl-L-aspartyl-L-glutamate (NAAG) to N-acetyl-L-aspartate and L-glutamate (which is itself a neurotransmitter).	Ac-Asp-Glu(3-)	131-162	folate hydrolase 1	Homo sapiens	46-51
15152093-2	2004	The GCPII form expressed in the central nervous system, termed NAALADase, is responsible for the cleavage of N-acetyl-L-aspartyl-L-glutamate (NAAG) yielding free glutamate in the synaptic cleft, and is implicated in various pathologic conditions associated with glutamate excitotoxicity.	Ac-Asp-Glu(3-)	109-140	folate hydrolase 1	Homo sapiens	4-9
15837926-2	2005	PSMA acts as a glutamate carboxypeptidase (GCPII) on small molecule substrates, including folate, the anticancer drug methotrexate, and the neuropeptide N-acetyl-l-aspartyl-l-glutamate.	Ac-Asp-Glu(3-)	153-184	folate hydrolase 1	Homo sapiens	0-4
15837926-2	2005	PSMA acts as a glutamate carboxypeptidase (GCPII) on small molecule substrates, including folate, the anticancer drug methotrexate, and the neuropeptide N-acetyl-l-aspartyl-l-glutamate.	Ac-Asp-Glu(3-)	153-184	folate hydrolase 1	Homo sapiens	43-48
15837926-5	2005	Elucidation of the PSMA structure combined with docking studies and a proposed catalytic mechanism provides insight into the recognition of inhibitors and the natural substrate N-acetyl-l-aspartyl-l-glutamate.	Ac-Asp-Glu(3-)	177-208	folate hydrolase 1	Homo sapiens	19-23
15152093-2	2004	The GCPII form expressed in the central nervous system, termed NAALADase, is responsible for the cleavage of N-acetyl-L-aspartyl-L-glutamate (NAAG) yielding free glutamate in the synaptic cleft, and is implicated in various pathologic conditions associated with glutamate excitotoxicity.	Ac-Asp-Glu(3-)	109-140	folate hydrolase 1	Homo sapiens	63-72
11755246-1	2002	Intracerebroventricular administration of N-acetyl-L-aspartyl-L-glutamate (NAAG), an agonist at group II metabotropic and NR1/NR2D-containing N-methyl-D-aspartate (NMDA) ionotropic glutamate receptors, increased the permeability of the blood-brain barrier (BBB) to serum albumin in the striatum, but produced no similar effects in the entorhinal cortex or in the hippocampal formation.	Ac-Asp-Glu(3-)	42-73	glutamate ionotropic receptor NMDA type subunit 1	Rattus norvegicus	122-125
15027864-1	2004	The neuropeptidase glutamate carboxypeptidase II (GCPII) hydrolyzes N-acetyl-L-aspartyl-L-glutamate (NAAG) to liberate N-acetylaspartate and glutamate.	Ac-Asp-Glu(3-)	68-99	folate hydrolase 1	Homo sapiens	19-48
15027864-1	2004	The neuropeptidase glutamate carboxypeptidase II (GCPII) hydrolyzes N-acetyl-L-aspartyl-L-glutamate (NAAG) to liberate N-acetylaspartate and glutamate.	Ac-Asp-Glu(3-)	68-99	folate hydrolase 1	Homo sapiens	50-55
11755246-1	2002	Intracerebroventricular administration of N-acetyl-L-aspartyl-L-glutamate (NAAG), an agonist at group II metabotropic and NR1/NR2D-containing N-methyl-D-aspartate (NMDA) ionotropic glutamate receptors, increased the permeability of the blood-brain barrier (BBB) to serum albumin in the striatum, but produced no similar effects in the entorhinal cortex or in the hippocampal formation.	Ac-Asp-Glu(3-)	42-73	glutamate ionotropic receptor NMDA type subunit 2D	Rattus norvegicus	126-130
9501243-1	1998	N-acetylated alpha-linked acidic dipeptidase (NAALADase) hydrolyzes acidic peptides, such as the abundant neuropeptide N-acetyl-alpha-L-aspartyl-L-glutamate (NAAG), thereby generating glutamate.	Ac-Asp-Glu(3-)	119-156	folate hydrolase 1	Rattus norvegicus	0-44
10085079-1	1999	Hydrolysis of the neuropeptide N-acetyl-L-aspartyl-L-glutamate (NAAG) by N-acetylated alpha-linked acidic dipeptidase (NAALADase) to release glutamate may be important in a number of neurodegenerative disorders in which excitotoxic mechanisms are implicated.	Ac-Asp-Glu(3-)	31-62	folate hydrolase 1B (pseudogene)	Homo sapiens	73-117
10085079-1	1999	Hydrolysis of the neuropeptide N-acetyl-L-aspartyl-L-glutamate (NAAG) by N-acetylated alpha-linked acidic dipeptidase (NAALADase) to release glutamate may be important in a number of neurodegenerative disorders in which excitotoxic mechanisms are implicated.	Ac-Asp-Glu(3-)	31-62	folate hydrolase 1B (pseudogene)	Homo sapiens	119-128
9755050-2	1998	In the present study we characterize the transport function of the rat brain PEPT2, with special emphasis on electrophysiological properties and interaction with N-acetyl-L-aspartyl-L-glutamate (NAAG).	Ac-Asp-Glu(3-)	162-193	solute carrier family 15 member 2 L homeolog	Xenopus laevis	77-82
9501243-1	1998	N-acetylated alpha-linked acidic dipeptidase (NAALADase) hydrolyzes acidic peptides, such as the abundant neuropeptide N-acetyl-alpha-L-aspartyl-L-glutamate (NAAG), thereby generating glutamate.	Ac-Asp-Glu(3-)	119-156	folate hydrolase 1	Rattus norvegicus	46-55
2250024-2	1990	N-Acetylated alpha-linked acidic dipeptidase (NAALA dipeptidase) is a membrane-bound metallopeptidase that cleaves glutamate from the endogenous neuropeptide N-acetyl-L-aspartyl-L-glutamate.	Ac-Asp-Glu(3-)	158-189	folate hydrolase 1	Rattus norvegicus	0-44
1944768-6	1991	The regional distribution of brain NAG differs from that of NAA and resembles that of N-acetyl-L-aspartyl-L-glutamate (NAAG), suggesting that NAG and NAAG are related.	Ac-Asp-Glu(3-)	86-117	neuroblastoma amplified sequence	Gallus gallus	35-38