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(2R)-2-hydroxy-N-pentadecyl-2-phenylacetamide
-
(2S)-2-hydroxy-N-pentadecyl-2-phenylacetamide
(7E)-N-[(3S)-2-oxoazetidin-3-yl]non-7-enamide
-
(Z)-N-[(S)-2-oxoazetidin-3-yl]non-3-enamide
-
([1,1'-biphenyl]-4-yl)methyl [(2S,3R)-2-methyl-4-oxooxetan-3-yl]carbamate
inhibition through a rapid and noncompetitive mechanism, partially reversible inhibition. The compound reacts with the catalytically active N-terminal Cys126 of human enzyme to form a thioester bond
1-heptyl-3-[(S)-2-oxoazetidin-3-yl]urea
-
1-isothiocyanatopentadecane
2,2-dimethyl-N-[(3S)-2-oxoazetidin-3-yl]nonanamide
-
2,5-dihydroxy-N-pentadecylbenzamide
2-hydroxy-N-pentadecylbenzamide
-
2-methyl-N-[(3S)-2-oxoazetidin-3-yl]nonanamide
-
3,5-dichloro-4-nitropyridine
AM11095, synthetis of the specific brain permeable NAAA inhibitor, a slowly reversible NAAA inhibitor
3-(benzyloxy)propyl [(2S,3R)-2-methyl-4-oxooxetan-3-yl]carbamate
-
3-amino-N-nonanoyl-L-alanine
-
3-[6-(3-chlorophenyl)hexanoyl]-1,3-oxazolidin-2-one
i.e. F215, the NAAA inhibitor F215 is a therapeutic agent for osteoarthritis
4-butyl-N-[(S)-2-oxoazetidin-3-yl]benzamide
-
4-cyclohexylbutyl [(3S)-2-oxoazetidin-3-yl]carbamate
a serine-derived beta-lactam CC-ABP, competitive
4-cyclohexylbutyl-N-[(R)-2-oxoazetidin-3-yl]carbamate
-
4-cyclohexylbutyl-N-[(S)-2-oxoazetidin-3-yl]carbamate
5-((biphenyl-4-yl)methyl)-N,N-dimethyl-2H-tetrazole-2-carboxamide
inhibits the enzyme in a covalent and irreversible manner
5-(4-(4-(5,5-difluoro-1,3,7,9-tetramethyl-5H-4l4,5l4-dipyrrolo[1,2-c:2',1'-f][1,3,2]diazaborinin-10-yl)butyl)-1H-1,2,3-triazol-1-yl)pentyl ((2S,3S)-2-methyl-1-(4-(methylsulfonyl)phenoxy)-4-oxoazetidin-3-yl)carbamate
a N-O-substituted beta-lactam BODIPY-ABP, almost complete inhibition of enzyme NAAA
5-(norbornan-2-ylmethoxy)pentyl N-[(2S,3S)-2-methyl-1-(4-methylsulfonylphenoxy)-4-oxo-azetidin-3-yl]carbamate
a norbornene-derived beta-lactam
5-azidopentyl N-[(2S,3S)-2-methyl-1-(4-methylsulfonylphenoxy)-4-oxo-azetidin-3-yl]carbamate
an azide-beta-lactam
5-cyclohexylpentyl [(2S,3R)-2-methyl-4-oxooxetan-3-yl]carbamate
-
5-phenylpentyl N-[(2S,3R)-2-methyl-4-oxo-oxetan-3-yl]-carbamate
-
5-phenylpentyl [(2S,3R)-2-methyl-4-oxooxetan-3-yl]carbamate
-
5-phenylpentyl-N-[(2S,3R)-2-methyl-4-oxo-oxetan-3-yl]carbamate
7-cyclohexyl-N-[(3S)-2-oxoazetidin-3-yl]heptanamide
-
cyclobutanol
41% inhibition at 0.05 mM
Cyclopentanol
85% inhibition at 0.05 mM
cyclopentyl hexadecanoate
competitive inhibition
heptyl N-[(S)-2-oxoazetidin-3-yl]carbamate
-
N-(2-oxocyclobutyl)nonanamide
-
N-(azetidin-3-yl)nonanamide
-
N-benzyloxycarbonyl-L-serine beta-lactone
inhibits the enzyme in a covalent and irreversible manner
N-pentadecylcyclohexancarboxamide
a potent and selective inhibitor
N-pentadecylnaphthalene-2-carboxamide
-
N-pentadecylpyridine-4-carboxamide
N-[(3R)-2-oxoazetidin-3-yl]nonanamide
-
N-[(3S)-2-oxoazetidin-3-yl]-4-phenylbutanamide
-
N-[(3S)-2-oxoazetidin-3-yl]-5-phenylpentanamide
-
N-[(3S)-2-oxoazetidin-3-yl]-6-phenylhexanamide
-
N-[(3S)-2-oxoazetidin-3-yl]decanamide
-
N-[(3S)-2-oxoazetidin-3-yl]heptanamide
-
N-[(3S)-2-oxoazetidin-3-yl]nonanamide
-
N-[(3S)-2-oxoazetidin-3-yl]octanamide
-
N-[(3S)-2-oxoazetidin-3-yl]undecanamide
-
N-[(3S)-2-oxooxetan-3-yl]-3-phenylpropanamide
-
N-[(S)-2-oxoazetidin-3-yl]-6-phenylhexanamide
-
palmitic acid retro-amides N-pentadecylbenzamide
a potent and selective inhibitor
tert-butyl ((2S,3S)-2-methyl-1-(4-(methylsulfonyl)phenoxy)-4-oxoazetidin-3-yl)carbamate
-
undec-10-ynyl-N-[(3S)-2-oxoazetidin-3-yl]carbamate
ARN14686, design and validation of this derivative of ARN726 as activity-based protein profiling (ABPP) probe for the in vivo detection of NAAA
[2-(ethylsulfonyl)phenyl][(2S)-4-(6-fluoro-1,3-benzothiazol-2-yl)-2-methylpiperazin-1-yl]methanone
ARN19702, a noncovalent benzothiazole-piperazine derivative
(2S)-2-hydroxy-N-pentadecyl-2-phenylacetamide
-
(2S)-2-hydroxy-N-pentadecyl-2-phenylacetamide
a covalent beta-lactam
1-isothiocyanatopentadecane
a potent, competitive, selective, and reversible inhibitor
1-isothiocyanatopentadecane
a potent, selective and reversible inhibitor
2,5-dihydroxy-N-pentadecylbenzamide
-
2,5-dihydroxy-N-pentadecylbenzamide
a non-covalent inhibitor
4-cyclohexylbutyl-N-[(S)-2-oxoazetidin-3-yl]carbamate
-
4-cyclohexylbutyl-N-[(S)-2-oxoazetidin-3-yl]carbamate
ARN726, a beta-lactam that irreversibly reacts with Cys126
4-cyclohexylbutyl-N-[(S)-2-oxoazetidin-3-yl]carbamate
ARN726, the enzyme inhibitor exerts systemic anti-inflammatory effects in mouse models of lung inflammation
4-cyclohexylbutyl-N-[(S)-2-oxoazetidin-3-yl]carbamate
it blocks enzyme NAAA by covalently binding to the enzyme's catalytic cysteine and displays pronounced antiinflammatory properties in human macrophages
5-phenylpentyl-N-[(2S,3R)-2-methyl-4-oxo-oxetan-3-yl]carbamate
-
5-phenylpentyl-N-[(2S,3R)-2-methyl-4-oxo-oxetan-3-yl]carbamate
ARN077, the enzyme inhibitor is active in vivo by topical administration in rodent models of hyperalgesia and allodynia
N-pentadecylpyridine-4-carboxamide
-
N-pentadecylpyridine-4-carboxamide
a covalent beta-lactam
additional information
mechanism of inactivation of human enzyme N-acylethanolamine-hydrolyzing acid amidase with selected inhibitors identified in a fluorescent based assay developed for characterization of both reversible and irreversible inhibitors, kinetic analysis using MALDI-TOF mass spectroscopy, molecular modeling, overview
-
additional information
-
mechanism of inactivation of human enzyme N-acylethanolamine-hydrolyzing acid amidase with selected inhibitors identified in a fluorescent based assay developed for characterization of both reversible and irreversible inhibitors, kinetic analysis using MALDI-TOF mass spectroscopy, molecular modeling, overview
-
additional information
selective alkylation of the enzyme's cysteine residues results in almost complete loss of activity
-
additional information
synthesis and evaluation of a series of N-(2-oxoazetidin-3-yl)amides as a novel class of enzyme inhibitors with good potency and improved physicochemical properties, suitable for systemic administration. No inhibition by 3-phenyl-N-[(S)-2-oxoazetidin-3-yl]propanamide, N-[(3S)-2-oxoazetidin-3-yl][1,1'-biphenyl]-4-carboxamide, N-(2-oxocyclobutyl)nonanamide, N-(azetidin-3-yl)nonanamide, 3-amino-N-nonanoyl-L-alanine, N-[(3S)-2-oxopyrrolidin-3-yl]nonanamide, N-[(S)-1-methyl-2-oxo-azetidin-3-yl]nonanamide, N-methyl-N-[(S)-2-oxoazetidin-3-yl]nonanamide, and (S)-3-(nonylamino)azetidin-2-one
-
additional information
development of two unprecedented NAAA-reactive activity-based probes as research tools for application in the discovery of inhibitors and for the in-depth characterization of NAAA in its cellular environment. Assay with lysosome-enriched extracts from hNAAA-overexpressing HEK-293 cells
-
additional information
identification of N-acylethanolamine-hydrolyzing acid amidase inhibitors able to reduce cell proliferation and migration and cause cell death on different bladder cancer cell lines. Inhibitor design of NAAA palmitic acid-retroamide inhibitors, synthesis, and characterization. Fluorescence high-throughput screening method set-up on human recombinant NAAA, using non-fluorescent but fluorogenic N-(4-methylcoumarin)palmitamide (PAMCA), that also allows to characterize the mechanism of inhibition. Reversibility of the inhibition. The NAAA inhibitors affect bladder cancer cells viability, they can be effective in inducing tumor cell death. But the inhibitors are differently effective of the different cell lines, overview
-
additional information
inhibitor binding analysis using purified and activated human enzyme hNAAA coupled to an azide-PEG3-biotin conjugate to its terminal alkyne using click chemistry, and visualization of protein bands using streptavidin-horseradish peroxidase (HRP)
-
additional information
inhibitor desing and synthesis of a class of beta-lactam derivatives that are potent, selective, and systemically active inhibitors of intracellular NAAA activity, reaction mechanisms via acylation or alkylation of the enzyme, overview
-
additional information
NAAA inhibitors block the substrate-binding site
-
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0.02
(2R)-2-hydroxy-N-pentadecyl-2-phenylacetamide
Homo sapiens
pH and temperature not specified in the publication
0.000006 - 0.078
(2S)-2-hydroxy-N-pentadecyl-2-phenylacetamide
0.00309
(7E)-N-[(3S)-2-oxoazetidin-3-yl]non-7-enamide
Homo sapiens
pH 5.0, 37°C
0.0039
(Z)-N-[(S)-2-oxoazetidin-3-yl]non-3-enamide
Homo sapiens
pH 5.0, 37°C
0.000007
([1,1'-biphenyl]-4-yl)methyl [(2S,3R)-2-methyl-4-oxooxetan-3-yl]carbamate
Homo sapiens
pH and temperature not specified in the publication
0.00576
1-heptyl-3-[(S)-2-oxoazetidin-3-yl]urea
Homo sapiens
pH 5.0, 37°C
0.00035 - 0.0006
1-isothiocyanatopentadecane
0.00076
2,2-dimethyl-N-[(3S)-2-oxoazetidin-3-yl]nonanamide
Homo sapiens
pH 5.0, 37°C
0.00023 - 0.038
2,5-dihydroxy-N-pentadecylbenzamide
0.011
2-hydroxy-N-pentadecylbenzamide
Homo sapiens
pH and temperature not specified in the publication
0.00022
2-methyl-N-[(3S)-2-oxoazetidin-3-yl]nonanamide
Homo sapiens
pH 5.0, 37°C
0.00002
3,5-dichloro-4-nitropyridine
Homo sapiens
pH and temperature not specified in the publication
0.0138
4-butyl-N-[(S)-2-oxoazetidin-3-yl]benzamide
Homo sapiens
pH 5.0, 37°C
0.000027 - 0.000073
4-cyclohexylbutyl-N-[(S)-2-oxoazetidin-3-yl]carbamate
0.0000072 - 0.0000077
5-((biphenyl-4-yl)methyl)-N,N-dimethyl-2H-tetrazole-2-carboxamide
0.00035
5-(4-(4-(5,5-difluoro-1,3,7,9-tetramethyl-5H-4l4,5l4-dipyrrolo[1,2-c:2',1'-f][1,3,2]diazaborinin-10-yl)butyl)-1H-1,2,3-triazol-1-yl)pentyl ((2S,3S)-2-methyl-1-(4-(methylsulfonyl)phenoxy)-4-oxoazetidin-3-yl)carbamate
Homo sapiens
pH 7.4, 37°C
0.00006
5-(norbornan-2-ylmethoxy)pentyl N-[(2S,3S)-2-methyl-1-(4-methylsulfonylphenoxy)-4-oxo-azetidin-3-yl]carbamate
Homo sapiens
pH 7.4, 37°C
0.05
5-phenylpentyl N-[(2S,3R)-2-methyl-4-oxo-oxetan-3-yl]-carbamate
Homo sapiens
pH 4.5, 37°C
0.000007
5-phenylpentyl [(2S,3R)-2-methyl-4-oxooxetan-3-yl]carbamate
Homo sapiens
pH and temperature not specified in the publication
0.000007
5-phenylpentyl-N-[(2S,3R)-2-methyl-4-oxo-oxetan-3-yl]carbamate
Homo sapiens
pH and temperature not specified in the publication
0.00028
7-cyclohexyl-N-[(3S)-2-oxoazetidin-3-yl]heptanamide
Homo sapiens
pH 5.0, 37°C
0.01
cyclopentyl hexadecanoate
Homo sapiens
pH and temperature not specified in the publication
0.00024
heptyl N-[(S)-2-oxoazetidin-3-yl]carbamate
Homo sapiens
pH 5.0, 37°C
0.0017 - 0.0019
N-benzyloxycarbonyl-L-serine beta-lactone
0.045
N-pentadecylbenzamide
Homo sapiens
pH and temperature not specified in the publication
0.034
N-pentadecylbutanamide
Homo sapiens
pH and temperature not specified in the publication
0.1
N-pentadecylnaphthalene-2-carboxamide
Homo sapiens
above, pH and temperature not specified in the publication
0.0004 - 0.098
N-pentadecylpyridine-4-carboxamide
0.0745
N-[(3R)-2-oxoazetidin-3-yl]nonanamide
Homo sapiens
pH 5.0, 37°C
0.0734
N-[(3S)-2-oxoazetidin-3-yl]-4-phenylbutanamide
Homo sapiens
pH 5.0, 37°C
0.0272
N-[(3S)-2-oxoazetidin-3-yl]-5-phenylpentanamide
Homo sapiens
pH 5.0, 37°C
0.0006
N-[(3S)-2-oxoazetidin-3-yl]-6-phenylhexanamide
Homo sapiens
pH 5.0, 37°C
0.00024
N-[(3S)-2-oxoazetidin-3-yl]decanamide
Homo sapiens
pH 5.0, 37°C
0.027
N-[(3S)-2-oxoazetidin-3-yl]heptanamide
Homo sapiens
pH 5.0, 37°C
0.00034
N-[(3S)-2-oxoazetidin-3-yl]nonanamide
Homo sapiens
pH 5.0, 37°C
0.0019
N-[(3S)-2-oxoazetidin-3-yl]octanamide
Homo sapiens
pH 5.0, 37°C
0.0001
N-[(3S)-2-oxoazetidin-3-yl]undecanamide
Homo sapiens
pH 5.0, 37°C
0.0121
N-[(S)-2-oxoazetidin-3-yl]-6-phenylhexanamide
Homo sapiens
pH 5.0, 37°C
0.000006
undec-10-ynyl-N-[(3S)-2-oxoazetidin-3-yl]carbamate
Homo sapiens
pH and temperature not specified in the publication
0.00023
[2-(ethylsulfonyl)phenyl][(2S)-4-(6-fluoro-1,3-benzothiazol-2-yl)-2-methylpiperazin-1-yl]methanone
Homo sapiens
pH 4.5, 37°C, recombinant enzyme
0.000006
(2S)-2-hydroxy-N-pentadecyl-2-phenylacetamide
Homo sapiens
pH 7.4, 37°C
0.078
(2S)-2-hydroxy-N-pentadecyl-2-phenylacetamide
Homo sapiens
pH and temperature not specified in the publication
0.00035
1-isothiocyanatopentadecane
Homo sapiens
recombinant enzyme with substrate N-(4-methyl coumarin)palmitamide, pH not specified in the publication, 37°C
0.00035 - 0.0006
1-isothiocyanatopentadecane
Homo sapiens
pH and temperature not specified in the publication
0.0006
1-isothiocyanatopentadecane
Homo sapiens
recombinant enzyme with substrate N-palmitoylethanolamine, pH not specified in the publication, 37°C
0.00023
2,5-dihydroxy-N-pentadecylbenzamide
Homo sapiens
pH 7.4, 37°C
0.038
2,5-dihydroxy-N-pentadecylbenzamide
Homo sapiens
pH and temperature not specified in the publication
0.000027
4-cyclohexylbutyl-N-[(S)-2-oxoazetidin-3-yl]carbamate
Homo sapiens
pH and temperature not specified in the publication
0.000073
4-cyclohexylbutyl-N-[(S)-2-oxoazetidin-3-yl]carbamate
Homo sapiens
pH 7.4, 37°C
0.0000072
5-((biphenyl-4-yl)methyl)-N,N-dimethyl-2H-tetrazole-2-carboxamide
Homo sapiens
recombinant enzyme with substrate N-palmitoylethanolamine, pH not specified in the publication, 37°C
0.0000077
5-((biphenyl-4-yl)methyl)-N,N-dimethyl-2H-tetrazole-2-carboxamide
Homo sapiens
recombinant enzyme with substrate N-(4-methyl coumarin)palmitamide, pH not specified in the publication, 37°C
0.0017
N-benzyloxycarbonyl-L-serine beta-lactone
Homo sapiens
recombinant enzyme with substrate N-(4-methyl coumarin)palmitamide, pH not specified in the publication, 37°C
0.0019
N-benzyloxycarbonyl-L-serine beta-lactone
Homo sapiens
recombinant enzyme with substrate N-palmitoylethanolamine, pH not specified in the publication, 37°C
0.0004
N-pentadecylpyridine-4-carboxamide
Homo sapiens
pH 7.4, 37°C
0.098
N-pentadecylpyridine-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
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gene NAAA, genotyping, six splice variants (a1, b1, c1, a2, b2, and c2), whereof four major splice variants (a1, a2, b2, and c2) are identified in a human prostate cancer cell line LNCaP, they are composed of exons 1-11, exons 1-10 and 12, exons 1-9 and 12, and exons 1-8 and 12, respectively, quantitative PCR expression analysis, method development for individual quantification. Variants a1 and a2 encode the same full-length NAAA protein, which is catalytically active, while b2 and c2 are translated to C-terminally truncated proteins. Recombinant expression in HEK-293 cells. The truncated forms are detected as catalytically inactive precursor proteins, but not as mature forms, expression of N-terminally FLAG-tagged isoform A of human NAAA, corresponding to splice variant a1, in HEK-293 cells. The mature enzyme form loses the N-terminal FLAG tag
gene Naaa, recombinant expression in HEK-293 cells
gene NAAA, recombinant overexpression in HEK-293 cells
recombinant expression in HEK-293 cells
recombinant expression of the C-terminally His6-tagged enzyme in HEK-293 cells
recombinant expression of the enzyme in HEK-293 cells
recombinant expression of wild-type and mutant enzymes NAAA in Spodoptera frugiperda Sf9 insect cells via baculovirus transfection method, the enzyme is secreted. The endogenous signal peptide comprising the first 28-33 residues is replaced by the melittin signal peptide MKFLVNVALVFMVVYISYIYA followed by a His6-tag DRHHHHHHKL. Constructs encompassed residues 29-359 of NAAA of human enzyme
recombinant overexpression in HEK-293 cell membranes
recombinant stable expression of the His6-tagged zymogen in HEK-293 cells, ammonium chloride treatment stimulates secretion of the lysosomal proteins from the HEK293 cells
expressed in COS-7 cells
-
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Hansen, H.; Lauritzen, L.; Moesgaard, B.; Strand, A.M.; Hansen, H.
Formation of N-acyl-phoshatidylethanolamines and N-acylethanolamines: proposed role in neurotoxicity
Biochem. Pharmacol.
55
719-725
1998
Homo sapiens, Mus sp., Rattus norvegicus
brenda
Fiasella, A.; Nuzzi, A.; Summa, M.; Armirotti, A.; Tarozzo, G.; Tarzia, G.; Mor, M.; Bertozzi, F.; Bandiera, T.; Piomelli, D.
3-Aminoazetidin-2-one derivatives as N-acylethanolamine acid amidase (NAAA) inhibitors suitable for systemic administration
ChemMedChem
9
1602-1614
2014
Homo sapiens (Q02083)
brenda
West, J.; Zvonok, N.; Whitten, K.; Wood, J.; Makriyannis, A.
Mass spectrometric characterization of human N-acylethanolamine-hydrolyzing acid midase
J. Proteome Res.
11
972-981
2012
Homo sapiens (Q02083)
brenda
Bandiera, T.; Ponzano, S.; Piomelli, D.
Advances in the discovery of N-acylethanolamine acid amidase inhibitors
Pharmacol. Res.
86
11-17
2014
Homo sapiens (Q02083), Mus musculus, Rattus norvegicus (Q5KTC7)
brenda
West, J.M.; Zvonok, N.; Whitten, K.M.; Vadivel, S.K.; Bowman, A.L.; Makriyannis, A.
Biochemical and mass spectrometric characterization of human N-acylethanolamine-hydrolyzing acid amidase inhibition
PLoS ONE
7
e43877
2012
Homo sapiens (Q02083), Homo sapiens
brenda
Ribeiro, A.; Pontis, S.; Mengatto, L.; Armirotti, A.; Chiurchiu, V.; Capurro, V.; Fiasella, A.; Nuzzi, A.; Romeo, E.; Moreno-Sanz, G.; Maccarrone, M.; Reggiani, A.; Tarzia, G.; Mor, M.; Bertozzi, F.; Bandiera, T.; Piomelli, D.
A potent systemically active N-acylethanolamine acid amidase inhibitor that suppresses inflammation and human macrophage activation
ACS Chem. Biol.
10
1838-1846
2015
Homo sapiens (Q02083), Mus musculus (Q9D7V9), Mus musculus C57BL/6J (Q9D7V9), Rattus norvegicus (Q5KTC7)
brenda
Romeo, E.; Ponzano, S.; Armirotti, A.; Summa, M.; Bertozzi, F.; Garau, G.; Bandiera, T.; Piomelli, D.
Activity-based probe for N-acylethanolamine acid amidase
ACS Chem. Biol.
10
2057-2064
2015
Homo sapiens (Q02083), Rattus norvegicus (Q5KTC7), Rattus norvegicus Sprague-Dawley (Q5KTC7)
brenda
Sakura, Y.; Tsuboi, K.; Uyama, T.; Zhang, X.; Taoka, R.; Sugimoto, M.; Kakehi, Y.; Ueda, N.
A quantitative study on splice variants of N-acylethanolamine acid amidase in human prostate cancer cells and other cells
Biochim. Biophys. Acta
1861
1951-1958
2016
Homo sapiens (Q02083)
brenda
Vago, R.; Bettiga, A.; Salonia, A.; Ciuffreda, P.; Ottria, R.
Development of new inhibitors for N-acylethanolamine-hydrolyzing acid amidase as promising tool against bladder cancer
Bioorg. Med. Chem.
25
1242-1249
2017
Homo sapiens (Q02083)
brenda
Petracca, R.; Romeo, E.; Baggelaar, M.P.; Artola, M.; Pontis, S.; Ponzano, S.; Overkleeft, H.S.; van der Stelt, M.; Piomelli, D.
Novel activity-based probes for N-acylethanolamine acid amidase
Chem. Commun. (Camb.)
53
11810-11813
2017
Homo sapiens (Q02083)
brenda
Sagheddu, C.; Scherma, M.; Congiu, M.; Fadda, P.; Carta, G.; Banni, S.; Wood, J.T.; Makriyannis, A.; Malamas, M.S.; Pistis, M.
Inhibition of N-acylethanolamine acid amidase reduces nicotine-induced dopamine activation and reward
Neuropharmacology
144
327-336
2019
Homo sapiens (Q02083), Rattus norvegicus (Q6P7S1), Rattus norvegicus Sprague-Dawley (Q6P7S1)
brenda
Zhou, P.; Xiang, L.; Yang, Y.; Wu, Y.; Hu, T.; Liu, X.; Lin, F.; Xiu, Y.; Wu, K.; Lu, C.; Ren, J.; Qiu, Y.; Li, Y.
N-Acylethanolamine acid amidase (NAAA) inhibitor F215 as a novel therapeutic agent for osteoarthritis
Pharmacol. Res.
145
104264
2019
Homo sapiens (Q02083), Rattus norvegicus (Q5KTC7)
brenda
Gorelik, A.; Gebai, A.; Illes, K.; Piomelli, D.; Nagar, B.
Molecular mechanism of activation of the immunoregulatory amidase NAAA
Proc. Natl. Acad. Sci. USA
115
E10032-E10040
2018
Cavia porcellus (H0VCJ6), Homo sapiens (Q02083), Mus musculus (Q9D7V9), Oryctolagus cuniculus (G1T7U7)
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