Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
acetyl-CoA + 2,3-diaminosuccinate
CoA + ?
-
-
-
?
acetyl-CoA + 3-methyl-L-aspartate
CoA + N-acetyl-3-methyl-L-aspartate
-
-
-
?
acetyl-CoA + glutamate
CoA + N-acetylglutamate
-
[14C]glutamate is acetylated with an approximately 50-fold lower affinity and a similar Vmax compared with aspartate
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartate
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
reaction of EC 2.3.1.1
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamic acid
additional information
?
-
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
highly specific
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
-
-
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
highly specific
-
?
acetyl-CoA + L-aspartate
CoA + N-acetyl-L-aspartic acid
-
decreases in enzyme activity occur in a number of neurological disorders, possible role in neuronal mitochondrial energy metabolism
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamic acid
less than 1% of the activity with L-aspartate
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamic acid
less than 1% of the activity with L-aspartate
-
-
?
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamic acid
-
only 10% activity compared to L-aspartate
-
?
additional information
?
-
-
reduced CoA with acetyl-AMP can substitute for acetyl-CoA, about 50% of activity with acetyl-CoA
-
-
?
additional information
?
-
-
highly specific for L-aspartate with 3% or less active for L-glutamate, L-asparagine, L-glutamine, or aspartate-glutamate dipeptide
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2S)-2-(3-phenylpropanamido)butanedioic acid
-
(2S)-2-(3-phenylpropanamido)pentanedioic acid
-
(2S)-2-[[(benzyloxy)carbonyl]amino]butanedioic acid
-
(2S)-2-[[(benzyloxy)carbonyl]amino]pentanedioic acid
-
4-aminomethyl(N-carboethyl,N-4-carboxy-2,6-dichlorobenzyl)phthalate
-
Acyl-AMP derivatives
-
e.g. acetyl-AMP, butyryl-AMP, strong
-
adenosine 3',5'-monophosphate
truncated bisubstrate analog
adenosine 5'-diphosphate
truncated bisubstrate analog
adenosine 5'-monophosphate
truncated bisubstrate analog
adenosine 5'-triphosphate
truncated bisubstrate analog
CHAPS
-
40% of activity at 12 mM, 10% of activity at 20 mM
cholamido propane sulfonate
-
cyclohexylmaltoside
cymal5, high inhibition at CMC concentration
DMSO
20% inhibition at 40% v/v
glutamate
-
Glutamate is a competitive inhibitor. No inhibition is observed with other amino acids, indicating that the enzyme is specific.
lauryldimethylamine-N-oxide
complete inhibition at CMC concentration
N-(2,6-dibromo-4-carboxybenzyl)-N-carboxyethyl-3,4-dicarboxybenzylamine
-
N-(2,6-dichloro-4-carboxybenzyl)-N-carboxyethyl-3,4-dicarboxybenzylamine
-
N-acetyl-(dimethyl)aspartyl-conjugated CoA
coenzyme A coupled to methylated N-acetyl aspartate, bisubstrate inhibitor
N-acetyl-L-aspartic acid
-
IC50: 0.85 mM
N-acetylaspartate
truncated bisubstrate analog
N-acetylaspartyl-conjugated CoA
coenzyme A coupled to N-acetyl aspartate, bisubstrate inhibitor
N-carbobenzyloxy-L-aspartic acid
-
N-carbobenzyloxy-L-glutamic acid
-
N-chloroacetylaspartate
truncated bisubstrate analog
n-decyl-N,N-dimethylamine-N-oxide
high inhibition at CMC concentration
N-methyl-N-nonanoyl-beta-D-glucosylamine
Mega-9, high inhibition at CMC concentration
n-nonyl-beta-D-glucopyranoside
high inhibition at CMC concentration
N-propionyl-(dimethyl)aspartyl-conjugated CoA
coenzyme A coupled to N-propionyl aspartate, bisubstrate inhibitor
N-[((2-[(tert-butoxycarbonyl)amino]ethyl)sulfanyl)acetyl]-L-aspartic acid
truncated bisubstrate analog
octyl pentaglycol
high inhibition at CMC concentration
octyl tetraglycol
high inhibition at CMC concentration
octylglucoside
high inhibition at CMC concentration
polymaleic anhydride C10
-
polymaleic anhydride C12
-
polymaleic anhydride C16
high inhibition at CMC concentration
polymaleic anhydride C4
high inhibition at CMC concentration
polymaleic anhydride C6
complete inhibition at CMC concentration
polymaleic anhydride C8
-
SDS
complete inhibition at CMC concentration
sodium 2-[(tert-butoxycarbonyl)amino]-3-[(2-([(1S)-1,2-dicarboxyethyl]amino)-2-oxoethyl)sulfanyl]propanoate
truncated bisubstrate analog
sodium 3-[(2-([(1S)-1,2-dicarboxyethyl]amino)-2-oxoethyl)sulfanyl]-2-([(trifluoromethoxy)carbonyl]amino)propanoate
truncated bisubstrate analog
sodium dodecanoyl sarcosine
-
additional information
effect of different detergents on the enzyme activity: non-ionic detergents such as Triton X-100 are less disruptive to protein structures than ionic detergents such as SDS, detergents such as C12E8, Tween 20 and several maltosides caused minimal disruption of the enzyme, with greater than 50% residual activity after incubation with CMC levels of each of these detergents. In contrast, significant loss of activity is observed upon incubation with C8 detergents, cymal5, octylglucoside and some shorter chain polymaleic anhydride (pmal) detergents. Ionic detergent SDS and a zwitterionic detergent lauryldimethylamine-N-oxide cause nearly complete loss of catalytic activity
-
additional information
-
effect of different detergents on the enzyme activity: non-ionic detergents such as Triton X-100 are less disruptive to protein structures than ionic detergents such as SDS, detergents such as C12E8, Tween 20 and several maltosides caused minimal disruption of the enzyme, with greater than 50% residual activity after incubation with CMC levels of each of these detergents. In contrast, significant loss of activity is observed upon incubation with C8 detergents, cymal5, octylglucoside and some shorter chain polymaleic anhydride (pmal) detergents. Ionic detergent SDS and a zwitterionic detergent lauryldimethylamine-N-oxide cause nearly complete loss of catalytic activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Adenocarcinoma
Cancer-Specific Production of N-Acetylaspartate via NAT8L Overexpression in Non-Small Cell Lung Cancer and Its Potential as a Circulating Biomarker.
Alzheimer Disease
Transcriptional regulation of N-acetylaspartate metabolism in the 5xFAD model of Alzheimer's disease: Evidence for neuron-glia communication during energetic crisis.
Canavan Disease
Brain Nat8l Knockdown Suppresses Spongiform Leukodystrophy in an Aspartoacylase-Deficient Canavan Disease Mouse Model.
Canavan Disease
Design and optimization of aspartate N-acetyltransferase inhibitors for the potential treatment of Canavan disease.
Canavan Disease
Discovery of Novel Inhibitors of a Critical Brain Enzyme Using a Homology Model and a Deep Convolutional Neural Network.
Canavan Disease
High Throughput Screening Cascade To Identify Human Aspartate N-Acetyltransferase (ANAT) Inhibitors for Canavan Disease.
Carcinoma
Cancer-Specific Production of N-Acetylaspartate via NAT8L Overexpression in Non-Small Cell Lung Cancer and Its Potential as a Circulating Biomarker.
Carcinoma, Non-Small-Cell Lung
Cancer-Specific Production of N-Acetylaspartate via NAT8L Overexpression in Non-Small Cell Lung Cancer and Its Potential as a Circulating Biomarker.
Carcinoma, Non-Small-Cell Lung
Correction: Cancer-Specific Production of N-Acetylaspartate via NAT8L Overexpression in Non-Small Cell Lung Cancer and Its Potential as a Circulating Biomarker.
Carcinoma, Squamous Cell
Cancer-Specific Production of N-Acetylaspartate via NAT8L Overexpression in Non-Small Cell Lung Cancer and Its Potential as a Circulating Biomarker.
Lung Neoplasms
Bridging the gap between non-targeted stable isotope labeling and metabolic flux analysis.
Lung Neoplasms
Cancer-Specific Production of N-Acetylaspartate via NAT8L Overexpression in Non-Small Cell Lung Cancer and Its Potential as a Circulating Biomarker.
Lung Neoplasms
Correction: Cancer-Specific Production of N-Acetylaspartate via NAT8L Overexpression in Non-Small Cell Lung Cancer and Its Potential as a Circulating Biomarker.
Neoplasms
Bridging the gap between non-targeted stable isotope labeling and metabolic flux analysis.
Neoplasms
Cancer-Specific Production of N-Acetylaspartate via NAT8L Overexpression in Non-Small Cell Lung Cancer and Its Potential as a Circulating Biomarker.
Neoplasms
Role of Increased n-acetylaspartate Levels in Cancer.
Nervous System Diseases
Structure of the Brain N-Acetylaspartate Biosynthetic Enzyme NAT8L Revealed by Computer Modeling.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.92
2,3-diaminosuccinate
pH 7.4, temperature not specified in the publication
0.36
3-methyl-L-aspartate
pH 7.4, temperature not specified in the publication
8.6
L-glutamate
pH 7.4, temperature not specified in the publication
additional information
additional information
-
0.001
acetyl-CoA
wild-type, pH 7.1, 30°C
0.0031
acetyl-CoA
pH 7.4, temperature not specified in the publication
0.009
acetyl-CoA
-
in presence of 0.5 mM CHAPS
0.012
acetyl-CoA
mutant P142A, pH 7.1, 30°C
0.013
acetyl-CoA
-
in presence of 1 mM CHAPS
0.017
acetyl-CoA
mutant S132F/R133F, pH 7.1, 30°C
0.019
acetyl-CoA
mutant R133A, pH 7.1, 30°C
0.058
acetyl-CoA
-
pH 7.1, 37°C
0.082
acetyl-CoA
mutant R81A, pH 7.1, 30°C
0.127
acetyl-CoA
mutant E101A, pH 7.1, 30°C
0.14
acetyl-CoA
mutant R220K, pH 7.1, 30°C
0.4
acetyl-CoA
mutant R220A, pH 7.1, 30°C
0.8 - 1.06
acetyl-CoA
-
pH 7.0, 37°C, slightly varying Km depending on source organelle
0.09
L-aspartate
-
-
0.09
L-aspartate
wild-type, pH 7.1, 30°C
0.095
L-aspartate
mutant P142A, pH 7.1, 30°C
0.128
L-aspartate
mutant S132F/R133F, pH 7.1, 30°C
0.16
L-aspartate
pH 7.4, temperature not specified in the publication
0.166 - 0.174
L-aspartate
-
pH 7.0, 37°C, slightly varying Km depending on source organelle
0.2
L-aspartate
mutant R81A, pH 7.1, 30°C
0.434
L-aspartate
mutant E101A, pH 7.1, 30°C
0.58
L-aspartate
-
pH 7.1, 37°C
1.61
L-aspartate
mutant R220K, pH 7.1, 30°C
3.37
L-aspartate
mutant R220A, pH 7.1, 30°C
additional information
additional information
-
Km value for acetyl-CoA
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.031
(2S)-2-(3-phenylpropanamido)butanedioic acid
pH 7.4, temperature not specified in the publication
0.038
(2S)-2-(3-phenylpropanamido)pentanedioic acid
pH 7.4, temperature not specified in the publication
0.017
(2S)-2-[[(benzyloxy)carbonyl]amino]butanedioic acid
pH 7.4, temperature not specified in the publication
0.012
(2S)-2-[[(benzyloxy)carbonyl]amino]pentanedioic acid
pH 7.4, temperature not specified in the publication
0.0006
4-aminomethyl(N-carboethyl,N-4-carboxy-2,6-dichlorobenzyl)phthalate
pH 7.4, temperature not specified in the publication
2.3
adenosine 3',5'-monophosphate
pH not specified in the publication, temperature not specified in the publication
1.1
adenosine 5'-diphosphate
pH not specified in the publication, temperature not specified in the publication
4
adenosine 5'-monophosphate
pH not specified in the publication, temperature not specified in the publication
0.96
adenosine 5'-triphosphate
pH not specified in the publication, temperature not specified in the publication
0.00077
N-(2,6-dibromo-4-carboxybenzyl)-N-carboxyethyl-3,4-dicarboxybenzylamine
pH 7.4, temperature not specified in the publication
0.00061
N-(2,6-dichloro-4-carboxybenzyl)-N-carboxyethyl-3,4-dicarboxybenzylamine
pH 7.4, temperature not specified in the publication
0.018
N-acetyl-(dimethyl)aspartyl-conjugated CoA
pH not specified in the publication, temperature not specified in the publication
0.56
N-acetyl-L-aspartate
-
-
1.6
N-acetylaspartate
pH not specified in the publication, temperature not specified in the publication
0.000275
N-acetylaspartyl-conjugated CoA
pH not specified in the publication, temperature not specified in the publication
0.017
N-carbobenzyloxy-L-aspartic acid
pH 7.4, temperature not specified in the publication
0.012
N-carbobenzyloxy-L-glutamic acid
pH 7.4, temperature not specified in the publication
0.2
N-chloroacetylaspartate
pH not specified in the publication, temperature not specified in the publication
0.000048
N-propionyl-(dimethyl)aspartyl-conjugated CoA
pH not specified in the publication, temperature not specified in the publication
2.1
N-[((2-[(tert-butoxycarbonyl)amino]ethyl)sulfanyl)acetyl]-L-aspartic acid
pH not specified in the publication, temperature not specified in the publication
0.87
sodium 2-[(tert-butoxycarbonyl)amino]-3-[(2-([(1S)-1,2-dicarboxyethyl]amino)-2-oxoethyl)sulfanyl]propanoate
pH not specified in the publication, temperature not specified in the publication
1.03
sodium 3-[(2-([(1S)-1,2-dicarboxyethyl]amino)-2-oxoethyl)sulfanyl]-2-([(trifluoromethoxy)carbonyl]amino)propanoate
pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
Ki values for various inhibitors
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
C128A
mutation in region 4, 94% of wild-type expression, 88% of wild-type activity
C139A
mutation in region 4, 70% of wild-type expression, 126% of wild-type activity
D168A
mutation in region 5, 46% of wild-type expression, no residual activity
D168E
mutation in region 5, 63% of wild-type expression, 7% of wild-type activity
E101A
mutation in region 3, 97% of wild-type expression, 42% of wild-type activity
E101D
mutation in region 3, 61% of wild-type expression, 99% of wild-type activity
P142A
mutation in region 4, 113% of wild-type expression, 116% of wild-type activity
R133A
mutation in region 4, 78% of wild-type expression, 64% of wild-type activity
R133K
mutation in region 4, 69% of wild-type expression, 89% of wild-type activity
R220A
mutation in region 5, 101% of wild-type expression, 14% of wild-type activity
R220K
mutation in region 5, 104% of wild-type expression, 25% of wild-type activity
R81A
mutation in region 3, 57% of wild-type expression, 37% of wild-type activity
R81K
mutation in region 3, 90% of wild-type expression, 82% of wild-type activity
S132F/R133F
mutation in region 4, 92% of wild-type expression, 41% of wild-type activity
additional information
transfection of truncated forms of isoform NAT8L into HEK-293T cells indicates that the 68 N-terminal residues, i.e. regions 1 and 2, have no importance for the catalytic activity and the subcellular localization of the enzyme. The membrane region, i.e. region 4, is necessary and sufficient to target isoform NAT8L to the endoplasmic reticulum
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Goldstein, F.B.
Biosynthesis of N-acetyl-L-aspartic acid
J. Biol. Chem.
234
2702-2706
1959
Rattus norvegicus
-
brenda
Knizley, H.Jr.
The enzymatic synthesis of N-acetyl-L-aspartic acid by a water-insoluble preparation of a cat brain acetone powder
J. Biol. Chem.
242
4619-4622
1967
Felis catus
brenda
Truckenmiller, M.E.; Namboodiri, M.A.A.; Brownstein, M.J.; Neale, J.H.
N-Acetylation of L-aspartate in the nervous system: differential distribution of a specific enzyme
J. Neurochem.
45
1658-1662
1985
Rattus norvegicus
brenda
Moreno, A.; Ross, B.D.; Bluml, S.
Direct determination of the N-acetyl-L-aspartate synthesis rate in the human brain by (13)C MRS and [1-(13)C]glucose infusion
J. Neurochem.
77
347-350
2001
Homo sapiens
brenda
Lu, Z.H.; Chakraborty, G.; Ledeen, R.W.; Yahya, D.; Wu, G.
N-Acetylaspartate synthase is bimodally expressed in microsomes and mitochondria of brain
Brain Res. Mol. Brain Res.
122
71-78
2004
Rattus norvegicus
brenda
Madhavarao, C.N.; Chinopoulos, C.; Chandrasekaran, K.; Namboodiri, M.A.
Characterization of the N-acetylaspartate biosynthetic enzyme from rat brain
J. Neurochem.
86
824-835
2003
Rattus norvegicus
brenda
Wiame, E.; Tyteca, D.; Pierrot, N.; Collard, F.; Amyere, M.; Noel, G.; Desmedt, J.; Nassogne, M.C.; Vikkula, M.; Octave, J.N.; Vincent, M.F.; Courtoy, P.J.; Boltshauser, E.; van Schaftingen, E.
Molecular identification of aspartate N-acetyltransferase and its mutation in hypoacetylaspartia
Biochem. J.
425
127-136
2010
Danio rerio, Mus musculus, Homo sapiens (Q8N9F0), Homo sapiens
brenda
Tahay, G.; Wiame, E.; Tyteca, D.; Courtoy, P.J.; Van Schaftingen, E.
Determinants of the enzymatic activity and the subcellular localization of aspartate N-acetyltransferase
Biochem. J.
441
105-112
2012
Homo sapiens (Q8N9F0)
brenda
Ariyannur, P.S.; Moffett, J.R.; Manickam, P.; Pattabiraman, N.; Arun, P.; Nitta, A.; Nabeshima, T.; Madhavarao, C.N.; Namboodiri, A.M.
Methamphetamine-induced neuronal protein NAT8L is the NAA biosynthetic enzyme: implications for specialized acetyl coenzyme A metabolism in the CNS
Brain Res.
1335
1-13
2010
Mus musculus (Q3UGX3), Homo sapiens (Q8N9F0), Homo sapiens
brenda
Wang, Q.; Zhao, M.; Parungao, G.G.; Viola, R.E.
Purification and characterization of aspartate N-acetyltransferase: a critical enzyme in brain metabolism
Protein Expr. Purif.
119
11-18
2016
Homo sapiens (Q8N9F0), Homo sapiens
brenda
Huber, K.; Hofer, D.C.; Trefely, S.; Pelzmann, H.J.; Madreiter-Sokolowski, C.; Duta-Mare, M.; Schlager, S.; Trausinger, G.; Stryeck, S.; Graier, W.F.; Kolb, D.; Magnes, C.; Snyder, N.W.; Prokesch, A.; Kratky, D.; Madl, T.; Wellen, K.E.; Bogner-Strauss, J.G.
N-acetylaspartate pathway is nutrient responsive and coordinates lipid and energy metabolism in brown adipocytes
Biochim. Biophys. Acta
1866
337-348
2019
Mus musculus (Q3UGX3)
brenda
Thangavelu, B.; Mutthamsetty, V.; Wang, Q.; Viola, R.E.
Design and optimization of aspartate N-acetyltransferase inhibitors for the potential treatment of Canavan disease
Bioorg. Med. Chem.
25
870-885
2017
Homo sapiens (Q8N9F0), Homo sapiens
brenda
Mutthamsetty, V.; Dahal, G.P.; Wang, Q.; Viola, R.E.
Development of bisubstrate analog inhibitors of aspartate N-acetyltransferase, a critical brain enzyme
Chem. Biol. Drug Des.
95
48-57
2020
Homo sapiens (Q8N9F0), Homo sapiens
brenda
Zand, B.; Previs, R.A.; Zacharias, N.M.; Rupaimoole, R.; Mitamura, T.; Nagaraja, A.S.; Guindani, M.; Dalton, H.J.; Yang, L.; Baddour, J.; Achreja, A.; Hu, W.; Pecot, C.V.; Ivan, C.; Wu, S.Y.; McCullough, C.R.; Gharpure, K.M.; Shoshan, E.; Pradeep, S.; Mangala, L.S.; Rodriguez-Aguayo, C.; Wang, Y.; Nick, A.M.
Role of increased N-acetylaspartate levels in cancer
J. Natl. Cancer Inst.
108
djv426
2016
Homo sapiens (Q8N9F0), Homo sapiens
brenda