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5'-AMP + H2O
adenosine + phosphate
-
-
-
?
a 5'-ribonucleotide + H2O
a ribonucleoside + phosphate
-
-
-
?
1,N6-ethenoadenosine 5'-phosphate + H2O
1,N6-ethenoadenosine ribonucleoside + phosphate
-
45% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
?
2-(cyclohexylethylthio)adenosine 5'-monophosphate + H2O
2-(cyclohexylethylthio)adenosine + phosphate
-
-
-
-
?
2-(cyclohexylmethylthio)adenosine 5'-monophosphate + H2O
2-(cyclohexylmethylthio)adenosine + phosphate
-
-
-
-
?
2-(cyclohexylthio)adenosine 5'-monophosphate + H2O
2-(cyclohexylthio)adenosine + phosphate
-
-
-
-
?
2-(cyclopentylthio)adenosine 5'-monophosphate + H2O
2-(cyclopentylthio)adenosine + phosphate
-
-
-
-
?
2-(dioxanylethylthio)adenosine 5'-monophosphate + H2O
2-(dioxanylethylthio)adenosine + phosphate
-
-
-
-
?
2-(dioxolanylethylthio)adenosine 5'-monophosphate + H2O
2-(dioxolanylethylthio)adenosine + phosphate
-
-
-
-
?
2-(hexylthio)adenosine 5'-monophosphate + H2O
2-(hexylthio)adenosine + phosphate
-
-
-
-
?
2-(propylthio)adenosine 5'-monophosphate + H2O
2-(propylthio)adenosine + phosphate
-
-
-
-
?
3-beta-ribofuranosyladenine 5'-monophosphate + H2O
3-beta-ribofuranosyladenine + phosphate
-
24% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
?
5'-AMP + H2O
?
-
the enzyme is responsible for the production of adenosine in the cardiac tissue
-
-
?
5'-AMP + H2O
adenosine + phosphate
5'-CMP + H2O
cytidine + phosphate
5'-CMP + xanthosine
XMP + cytidine
-
-
-
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
5'-dCMP + H2O
deoxycytidine + phosphate
5'-dGMP + H2O
deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
-
i.e. 2'-deoxyinosine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
5'-GMP + H2O
guanosine + phosphate
5'-GMP + xanthosine
XMP + guanosine
-
-
-
-
?
5'-IMP + H2O
inosine + phosphate
5'-IMP + xanthosine
XMP + inosine
-
-
-
-
?
5'-UMP + H2O
uridine + phosphate
5'-UMP + xanthosine
XMP + uridine
-
-
-
-
?
5'-XMP + H2O
xanthosine + phosphate
-
-
-
?
6-chloropurine ribonucleoside 5'-monophosphate + H2O
6-chloropurine ribonucleoside + phosphate
-
50% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
?
adenosine 5'-O-thiophosphate + H2O
?
-
6% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
-
?
AMP + H2O
adenosine + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
additional information
?
-
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
664550, 677490, 677509, 678104, 679085, 679669, 681724, 681894, 681897, 682113, 682115, 691398, 692192, 693953, 694138, 715146, 715987, 751791, 752167 -
-
?
5'-AMP + H2O
adenosine + phosphate
-
100% activity
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
most efficiently hydrolyzed substrate
-
-
?
5'-CMP + H2O
cytidine + phosphate
-
-
-
?
5'-CMP + H2O
cytidine + phosphate
-
-
-
?
5'-CMP + H2O
cytidine + phosphate
-
-
-
?
5'-CMP + H2O
cytidine + phosphate
-
-
-
?
5'-CMP + H2O
cytidine + phosphate
-
-
-
?
5'-CMP + H2O
cytidine + phosphate
-
87% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
?
5'-CMP + H2O
cytidine + phosphate
-
65% of the activity with 5'-AMP, brain cytosolic enzyme
-
?
5'-CMP + H2O
cytidine + phosphate
-
36% dephosphorylation in relation to AMP
-
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
20% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
7% of the activity with 5'-AMP, brain cytosolic enzyme
-
-
?
5'-dCMP + H2O
deoxycytidine + phosphate
-
28% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
?
5'-dCMP + H2O
deoxycytidine + phosphate
-
i.e. 2'-deoxycytosine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
-
-
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
55% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
?
5'-GMP + H2O
guanosine + phosphate
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
50% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
?
5'-GMP + H2O
guanosine + phosphate
-
19% of the activity with 5'-AMP
-
?
5'-GMP + H2O
guanosine + phosphate
-
57% dephosphorylation in relation to AMP
-
-
?
5'-IMP + H2O
inosine + phosphate
-
-
-
-
?
5'-IMP + H2O
inosine + phosphate
-
36% of the activity with 5'-AMP, brain cytosolic enzyme
-
-
?
5'-IMP + H2O
inosine + phosphate
-
55% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
-
?
5'-UMP + H2O
uridine + phosphate
-
-
-
?
5'-UMP + H2O
uridine + phosphate
-
-
-
?
5'-UMP + H2O
uridine + phosphate
-
-
-
?
5'-UMP + H2O
uridine + phosphate
-
-
-
?
5'-UMP + H2O
uridine + phosphate
-
-
-
?
5'-UMP + H2O
uridine + phosphate
-
93% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
?
5'-UMP + H2O
uridine + phosphate
-
111% of the activity with 5'-AMP, brain cytosolic enzyme
-
?
5'-UMP + H2O
uridine + phosphate
-
51% dephosphorylation in relation to AMP
-
-
?
additional information
?
-
-
accumulation of Arg, N-acetylarginine, homoarginine and argininic acid do not alter 5'-nucleotidase activity
-
?
additional information
?
-
-
involved in the synthesis of guanine nucleotides from xanthosine
-
-
?
additional information
?
-
-
IMP and GMP are the best phosphate donors for phosphotransferase activity, followed by UMP and CMP
-
-
?
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1-pentyl-1H-benzofuro[3,2-b]pyrrolo[3,2-e]pyridine-3-carbonitrile
-
1-tert-butyl-1H-benzofuro[3,2-b]pyrrolo[3,2-e]pyridine-3-carbonitrile
-
1-tert-butyl-5-chloro-6-(2-hydroxy-5-methylphenyl)-1H-pyrrolo[2,3-b]pyridine-3-carbonitrile
-
1-tert-butyl-5-chloro-6-(2-hydroxyphenyl)-1H-pyrrolo[2,3-b]pyridine-3-carbonitrile
-
2-(3-methyl-1,5-diphenyl-1H-pyrazolo[3,4-b]pyridin-6-yl)phenol
-
2-(5-chloro-1,3-dimethyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-4-methylphenol
-
2-(5-chloro-1,3-dimethyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-5-methoxyphenol
-
2-(5-chloro-1,3-dimethyl-1H-pyrazolo[3,4-b]pyridin-6-yl)phenol
-
2-(5-chloro-3-methyl-1-p-tolyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-4-methylphenol
-
2-(5-chloro-3-methyl-1-p-tolyl-1H-pyrazolo[3,4-b]pyridin-6-yl)phenol
-
2-(5-chloro-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-4-methylphenol
-
2-(5-chloro-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-5-methoxyphenol
-
2-(5-chloro-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridin-6-yl)phenol
-
3,8-dimethyl-1-p-tolyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
-
3,8-dimethyl-1-phenyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
-
3-methyl-1-p-tolyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
-
3-methyl-1-phenyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
-
5-chloro-3-methyl-1-phenyl-6-(2-propoxyphenyl)-1H-pyrazolo[3,4-b]pyridine
-
5-chloro-6-(2-(heptyloxy)phenyl)-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridine
-
5-chloro-6-(2-hydroxy-5-methylphenyl)-2-phenyl-2H-pyrazolo[3,4-b]pyridin-3-ol
-
5-chloro-6-(2-hydroxyphenyl)-2-phenyl-2H-pyrazolo[3,4-b]pyridin-3-ol
-
5-chloro-6-(2-methoxyphenyl)-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridine
-
6-chloro-7-(2-hydroxy-5-methylphenyl)pyrido[2,3-d]pyrimidine-2,4(1H,3H)-dione
-
6-chloro-7-(2-hydroxyphenyl)-1-methylpyrido[2,3-d]pyrimidine-2,4(1H,3H)-dione
-
6-chloro-7-(2-hydroxyphenyl)pyrido[2,3-d]pyrimidine-2,4(1H,3H)-dione
-
7-methoxy-3-methyl-1-phenyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
-
alpha,beta-methylene-ADP
-
1-amino-2-methyl-4-(phenylamino)anthracene-9,10-dione
-
4% inhibition at 1 mM
1-amino-4-(1-anthracenylamino)-9,10-dioxo-9,10 dihydroanthracene-2-sulfonate
-
-
1-amino-4-(1-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
competitive mechanism
1-amino-4-(2,3-dimethylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
39% inhibition at 1 mM
1-amino-4-(2,4-dimethylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
47% inhibition at 1 mM
1-amino-4-(2,5-dimethylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
26% inhibition at 1 mM
1-amino-4-(2-aminophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
47% inhibition at 1 mM
1-amino-4-(2-anthracenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
competitive mechanism
1-amino-4-(2-carboxy-4-chlorophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
52% inhibition at 1 mM
1-amino-4-(2-carboxy-4-fluorophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(2-carboxy-5-chlorophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
27% inhibition at 1 mM
1-amino-4-(2-carboxy-5-fluorophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
60% inhibition at 1 mM
1-amino-4-(2-carboxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(2-ethoxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
56% inhibition at 1 mM
1-amino-4-(2-hydroxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(2-methoxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
9% inhibition at 1 mM
1-amino-4-(2-methyl-1-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(2-methylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
33% inhibition at 1 mM
1-amino-4-(2-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(2-sulfophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
14% inhibition at 1 mM
1-amino-4-(3,4-dimethoxyphenethylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
44% inhibition at 1 mM
1-amino-4-(3-amino-2,4,6-trimethylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(3-amino-4-sulfophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(3-amino-5-carboxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
44% inhibition at 1 mM
1-amino-4-(3-aminophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
31% inhibition at 1 mM
1-amino-4-(3-carboxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
26% inhibition at 1 mM
1-amino-4-(3-methylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(4-amino-3-sulfophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(4-aminophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(4-bromo-2-carboxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
56% inhibition at 1 mM
1-amino-4-(4-bromophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(4-carboxymethylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
26% inhibition at 1 mM
1-amino-4-(4-chlorophenethylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
62% inhibition at 1 mM
1-amino-4-(4-chlorophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(4-ethoxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
31% inhibition at 1 mM
1-amino-4-(4-fluorophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(4-hydroxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(4-methylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(4-phenoxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(4-phenylaminophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
37% inhibition at 1 mM
1-amino-4-(4-sulfophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(5-sulfo-1-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(6-carboxy-2-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(6-sulfo-1-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(8-sulfo-1-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(9-phenanthrenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
58% inhibition at 1 mM
1-amino-4-(benzylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
43% inhibition at 1 mM
1-amino-4-(cyclohexylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
1-amino-4-(cyclopentylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
51% inhibition at 1 mM
1-amino-4-(isopropylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
15% inhibition at 1 mM
1-amino-4-(phenethylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
53% inhibition at 1 mM
1-amino-4-bromo-9,10-dioxo-9,10-dihydroanthracene-2-sulfonic acid
-
-
1-amino-4-[4-(diethoxyphosphoryl)methylphenylamino]-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
28% inhibition at 1 mM
3-(2-(3,4,5-trimethoxybenzylideneamino)thiazol-4-yl)-2Hchromen-2-one
-
-
3-(2-(3-chlorobenzylideneamino)thiazol-4-yl)-2H-chromen-2-one
-
-
3-(2-(3-methoxy-4-phenoxybenzylideneamino)thiazol-4-yl)-2H-chromen-2-one
-
-
3-(2-(3-nitrobenzylideneamino)thiazol-4-yl)-2H-chromen-2-one
-
-
3-(2-(4-bromobenzylideneamino)thiazol-4-yl)-2H-chromen-2-one
-
-
3-(2-(4-chlorobenzylideneamino)thiazol-4-yl)-2H-chromen-2-one
-
-
3-(2-(4-fluorobenzylideneamino)thiazol-4-yl)-2H-chromen-2-one
-
-
3-(2-(furan-2-ylmethyleneamino)thiazol-4-yl)-2H-chromen-2-one
-
-
4-(3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzenesulfonic acid
-
-
5-ethynyl-2',3'-dideoxyuridine
-
-
6-amino-4-hydroxynaphthalene-2-sulfonic acid
-
most potent inhibitor of the screen
adenosine 5'-(alpha,beta-methylene)diphosphate
agglutinin
-
enzyme from glioblastoma cells
-
alpha,beta-methylene ADP
-
-
alpha,beta-methylene-ADP
-
-
alpha/beta-methylene-ADP
-
a specific CD73 inhibitor
alphabeta-methylene ADP
-
0.05 mM
Ammonium molybdate
-
17.6% residual activity at 0.1 mM ammonium molybdate
clomipramine
-
enzymatic activity is decreased by the antidepressant clomipramine after in vitro exposure
Cu2+
-
inhibition of cytosolic and membrane-bound enzyme
L-arginine
-
21% inhibition at 0.1 mM
sertraline
-
enzymatic activity is decreased by the antidepressant sertraline after in vitro exposure
sodium 1-amino-9,10-dioxo-4-(phenylamino)-9,10-dihydroanthracene-2-sulfonate
-
-
tetrasodium 4-[[4-([4-[(4-amino-9,10-dioxo-3-sulfonato-9,10-dihydroanthracen-1-yl)amino]-2-sulfonatophenyl]amino)-6-chloro-1,3,5-triazin-2-yl]amino]benzene-1,2-disulfonate
-
-
adenosine 5'-(alpha,beta-methylene)diphosphate
-
-
adenosine 5'-(alpha,beta-methylene)diphosphate
-
treatment with 0.001 mM adenosine 5'-(alpha,beta-methylene)diphosphate, a competitive ecto-5'-NT/CD73 inhibitor, causes a significant reduction of 30% in glioma cell proliferation, the inhibitory effect on cell proliferation caused by adenosine 5'-(alpha,beta-methylene)diphosphate is reverted by cotreatment with nitrobenzylthioinosine and dipyridamole
ADP
-
-
ADP
-
feed-forward inhibition
ATP
-
-
ATP
-
feed-forward inhibition
Ca2+
-
-
Ca2+
-
gradual decrease in enzyme activity in the presence of 1-6 mM of Ca2+
Co2+
-
inhibition of cytosolic and membrane-bound enzyme
Co2+
-
strong, enzyme from glioblastoma cells
Co2+
-
0.1 mM activate, 4 mM inhibit, plasma membrane enzyme
concanavalin A
-
-
-
concanavalin A
-
enzyme from glioblastoma cells
-
EDTA
-
-
EDTA
-
complete inhibition at 1 mM
EDTA
-
inhibition of cytosolic and membrane-bound enzyme
EDTA
-
3 mM, complete inhibition
EDTA
-
decrease of the enzyme activity in presence of 0.5 mM EDTA
Fe2+
-
plasma membrane enzyme
Fe2+
-
the enzyme is susceptible to Fe2+-ion catalyzed oxidative modification. Among the examined chelators it is only deferoxamine and Na-citrate that exert a fully protective and reactivating ability, among the antioxidants it is only GSH, among the metal cations it is only Mn2+
fluoxetine
-
-
fluoxetine
-
chronic treatment with 10mg/kg fluoxetine causes a 42% inhibition of AMP hydrolysis
Mn2+
-
inhibition of cytosolic and membrane-bound enzyme
Mn2+
-
strong, enzyme from glioblastoma cells
Mn2+
-
0.1 mM activate, 4 mM inhibit, plasma membrane enzyme
Ni2+
-
strong, enzyme from glioblastoma cells
Ni2+
-
plasma membrane enzyme
nortriptyline
-
-
nortriptyline
-
chronic treatment with 10mg/kg nortriptyline causes a 30% inhibition of AMP hydrolysis
Pb2+
-
-
Pb2+
-
plasma membrane enzyme
Zn2+
-
inhibition of cytosolic and membrane-bound enzyme
Zn2+
-
strong, enzyme from glioblastoma cells
additional information
-
endogenous inhibitor from rat tissues
-
additional information
-
not inhibitory: mycophenolic acid
-
additional information
-
in vitro and short-term in vivo treatment with fluoxetine and nortriptyline causes no change in activity
-
additional information
-
not inhibited by levamisole
-
additional information
-
AMP hydrolysis by ecto-5'-nucleotidase is not affected by levamisole and tetramisole
-
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0.00293
1-amino-4-(1-anthracenylamino)-9,10-dioxo-9,10 dihydroanthracene-2-sulfonate
-
-
0.00053
1-amino-4-(1-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00015
1-amino-4-(2-anthracenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00026
1-amino-4-(2-carboxy-4-fluorophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00653
1-amino-4-(2-carboxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00184
1-amino-4-(2-hydroxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00274
1-amino-4-(2-methyl-1-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00147
1-amino-4-(2-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.036
1-amino-4-(3-amino-2,4,6-trimethylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.0252
1-amino-4-(3-amino-4-sulfophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.0123
1-amino-4-(3-methylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.01
1-amino-4-(4-amino-3-sulfophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.000297
1-amino-4-(4-aminophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.0113
1-amino-4-(4-bromophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00481
1-amino-4-(4-chlorophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00567
1-amino-4-(4-fluorophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00062
1-amino-4-(4-hydroxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.36
1-amino-4-(4-methylphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00151
1-amino-4-(4-phenoxyphenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00343
1-amino-4-(4-sulfophenylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.0117
1-amino-4-(5-sulfo-1-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00343
1-amino-4-(6-carboxy-2-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.0153
1-amino-4-(6-sulfo-1-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00605
1-amino-4-(8-sulfo-1-naphthylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00166
1-amino-4-(cyclohexylamino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
-
-
0.00091
ADP
-
in 10 mM HEPES (pH 7.4), 2 mM MgCl2, and 1 mM CaCl2
0.00087
alpha,beta-methylene-ADP
-
in 10 mM HEPES (pH 7.4), 2 mM MgCl2, and 1 mM CaCl2
0.0089
ATP
-
in 10 mM HEPES (pH 7.4), 2 mM MgCl2, and 1 mM CaCl2
0.0152
sodium 1-amino-9,10-dioxo-4-(phenylamino)-9,10-dihydroanthracene-2-sulfonate
-
-
0.00307
tetrasodium 4-[[4-([4-[(4-amino-9,10-dioxo-3-sulfonato-9,10-dihydroanthracen-1-yl)amino]-2-sulfonatophenyl]amino)-6-chloro-1,3,5-triazin-2-yl]amino]benzene-1,2-disulfonate
-
-
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0.00729
1-pentyl-1H-benzofuro[3,2-b]pyrrolo[3,2-e]pyridine-3-carbonitrile
Rattus norvegicus
at pH 7.5 and 37°C
0.00543
1-tert-butyl-1H-benzofuro[3,2-b]pyrrolo[3,2-e]pyridine-3-carbonitrile
Rattus norvegicus
at pH 7.5 and 37°C
0.1
1-tert-butyl-5-chloro-6-(2-hydroxy-5-methylphenyl)-1H-pyrrolo[2,3-b]pyridine-3-carbonitrile
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
1-tert-butyl-5-chloro-6-(2-hydroxyphenyl)-1H-pyrrolo[2,3-b]pyridine-3-carbonitrile
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
2-(3-methyl-1,5-diphenyl-1H-pyrazolo[3,4-b]pyridin-6-yl)phenol
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.0235
2-(5-chloro-1,3-dimethyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-4-methylphenol
Rattus norvegicus
at pH 7.5 and 37°C
0.00203
2-(5-chloro-1,3-dimethyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-5-methoxyphenol
Rattus norvegicus
at pH 7.5 and 37°C
0.1
2-(5-chloro-3-methyl-1-p-tolyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-4-methylphenol
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.0111
2-(5-chloro-3-methyl-1-p-tolyl-1H-pyrazolo[3,4-b]pyridin-6-yl)phenol
Rattus norvegicus
at pH 7.5 and 37°C
0.1
2-(5-chloro-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-4-methylphenol
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.00067
2-(5-chloro-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridin-6-yl)-5-methoxyphenol
Rattus norvegicus
at pH 7.5 and 37°C
0.1
2-(5-chloro-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridin-6-yl)phenol
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
3,8-dimethyl-1-p-tolyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
3,8-dimethyl-1-phenyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
3-methyl-1-p-tolyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.00645
3-methyl-1-phenyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
Rattus norvegicus
at pH 7.5 and 37°C
0.1
5-chloro-3-methyl-1-phenyl-6-(2-propoxyphenyl)-1H-pyrazolo[3,4-b]pyridine
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
5-chloro-6-(2-(heptyloxy)phenyl)-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridine
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
5-chloro-6-(2-hydroxy-5-methylphenyl)-2-phenyl-2H-pyrazolo[3,4-b]pyridin-3-ol
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
5-chloro-6-(2-hydroxyphenyl)-2-phenyl-2H-pyrazolo[3,4-b]pyridin-3-ol
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
5-chloro-6-(2-methoxyphenyl)-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridine
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.00352
6-chloro-7-(2-hydroxy-5-methylphenyl)pyrido[2,3-d]pyrimidine-2,4(1H,3H)-dione
Rattus norvegicus
at pH 7.5 and 37°C
0.00214
6-chloro-7-(2-hydroxyphenyl)-1-methylpyrido[2,3-d]pyrimidine-2,4(1H,3H)-dione
Rattus norvegicus
at pH 7.5 and 37°C
0.1
6-chloro-7-(2-hydroxyphenyl)pyrido[2,3-d]pyrimidine-2,4(1H,3H)-dione
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
7-methoxy-3-methyl-1-phenyl-1H-benzofuro[3,2-b]pyrazolo[4,3-e]pyridine
Rattus norvegicus
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.0773
sulfamic acid
Rattus norvegicus
at pH 7.5 and 37°C
0.027
1-amino-4-bromo-9,10-dioxo-9,10-dihydroanthracene-2-sulfonic acid
Rattus norvegicus
-
pH 7.4, 37°C
0.0443
4-(3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzenesulfonic acid
Rattus norvegicus
-
pH 7.4, 37°C
0.0104
6-amino-4-hydroxynaphthalene-2-sulfonic acid
Rattus norvegicus
-
pH 7.4, 37°C
0.0773
sulfamic acid
Rattus norvegicus
-
at pH 7.4 and 37°C
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Wada, I.; Eto, S.; Himeno, M.; Kato, K.
5'-Nucleotidase in rat liver lysosomes
J. Biochem.
101
1077-1085
1987
Rattus norvegicus
brenda
Lamers, J.M.J.; Heyliger, C.E.; Panagia, V.; Dhalla, N.S.
Properties of 5-nucleotidase in rat heart sarcolemma
Biochim. Biophys. Acta
742
568-575
1983
Rattus norvegicus
brenda
Itoh, R.
Studies on some molecular properties of cytosol 5'-nucleotidase from rat liver
Biochim. Biophys. Acta
716
110-113
1982
Rattus norvegicus
brenda
Naito, Y.; Lowenstein, J.M.
5'-Nucleotidase from rat heart
Biochemistry
20
5188-5194
1981
Rattus norvegicus
brenda
Itoh, R.
Purification and some properties of cytosol 5'-nucleotidase from rat liver
Biochim. Biophys. Acta
657
402-410
1981
Rattus norvegicus
brenda
Newby, A.; Luzio, P.; Hales, C.N.
The properties and extracellular location of 5'-nucleotidase of the rat fat-cell plasma membrane
Biochem. J.
146
625-633
1975
Rattus norvegicus
brenda
Widnell, C.C.
Purification of rat liver 5'-nucleotidase as a complex with sphingomyelin
Methods Enzymol.
32
368-374
1974
Rattus norvegicus
brenda
Gibson, W.B.; Drummond, G.I.
Properties of 5'-nucleotidase from avian heart
Biochemistry
11
223-229
1972
Gallus gallus, Columba livia, Rattus norvegicus, Sturnus vulgaris
brenda
Turnay, J.; Olmo, N.; Navarro, J.M.; Gavilanes, J.G.; Lizarbe, M.A.
Isolation and characterization of the ecto-5'-nucleotidase from a rat glioblastoma cell line
Mol. Cell. Biol.
117
23-33
1992
Rattus norvegicus
brenda
Yegutkin, G.G.
Effects of Triton X-100 and concanavalin A on the properties of 5'-nucleotidase in rat liver and adipose plasma membranes: a role of membrane structure in the regulation of enzyme activity
Membr. Cell Biol.
10
631-638
1997
Rattus norvegicus
brenda
Servos, J.; Reilnder, H.; Zimmermann, H.
Catalytically active soluble ecto-5'-nucleotidase purified after heterologous expression as a tool for drug screening
Drug Develop. Res.
45
269-276
1998
Rattus norvegicus
-
brenda
Orford, M.R.; Saggerson, E.D.
A low-Km 5'-nucleotidase from rat brain cytosolic fraction: purification, kinetic properties, and description of regulation by a novel factor that increases sensitivity to inhibition by ATP and ADP
J. Neurochem.
67
795-804
1996
Rattus norvegicus
brenda
Lai, K.M.; Wong, P.C.L.
A comparison of the properties of 5'-nucleotidase purified from the cytosolic and synaptic plasma membrane fractions of rat forebrain
Int. J. Biochem.
23
1123-1130
1991
Rattus norvegicus
brenda
Rajput, A.; Chakravarthy, B.R.; DSouza, C.J.M.
Isolation and characterization of 5'-nucleotidase inhibitor from rat liver
Indian J. Biochem. Biophys.
29
204-208
1992
Rattus norvegicus
brenda
Garvey, E.P.; Prus, K.L.
A specific inhibitor of heart cytosolic 5'-nucleotidase I attenuates hydrolysis of adenosine 5'-monophosphate in primary rat myocytes
Arch. Biochem. Biophys.
364
235-240
1999
Rattus norvegicus
brenda
Kocic, G.; Pavlovic, D.; Jevtovic, T.; Kocic, R.; Bojic, A.; Vlahovic, P.; Djordjevic, V.; Sokolovic, D.; Djindjic, B.
Oxidative modification of rat liver 5'-nucleotidase: the mechanisms for protection and re-activation
Arch. Physiol. Biochem.
109
323-330
2001
Rattus norvegicus
brenda
Balz, D.; de Souza Wyse, A.T.; Morsch, V.M.; da Silva, A.C.; Vieira, V.L.; Morsch, A.L.; Schetinger, M.R.
In vitro effects of L-arginine and guanidino compounds on NTPDase1 and 5'-nucleotidase activities from rat brain synaptosomes
Int. J. Dev. Neurosci.
21
75-82
2003
Rattus norvegicus
brenda
Vekaria, R.M.; Shirley, D.G.; Sevigny, J.; Unwin, R.J.
Immunolocalization of ectonucleotidases along the rat nephron
Am. J. Physiol.
290
F550-F560
2006
Rattus norvegicus
brenda
Henz, S.L.; Ribeiro, C.G.; Rosa, A.; Chiarelli, R.A.; Casali, E.A.; Sarkis, J.J.
Kinetic characterization of ATP diphosphohydrolase and 5'-nucleotidase activities in cells cultured from submandibular salivary glands of rats
Cell Biol. Int.
30
214-220
2006
Rattus norvegicus
brenda
Barsotti, C.; Pesi, R.; Giannecchini, M.; Ipata, P.L.
Evidence for the involvement of cytosolic 5'-nucleotidase (cN-II) in the synthesis of guanine nucleotides from xanthosine
J. Biol. Chem.
280
13465-13469
2005
Rattus norvegicus
brenda
Satriano, J.; Wead, L.; Cardus, A.; Deng, A.; Boss, G.R.; Thomson, S.C.; Blantz, R.C.
Regulation of ecto-5'-nucleotidase by NaCl and nitric oxide: potential roles in tubuloglomerular feedback and adaptation
Am. J. Physiol. Renal Physiol.
291
F1078-F1082
2006
Rattus norvegicus
brenda
Boeck, C.R.; Kroth, E.H.; Bronzatto, M.J.; Vendite, D.
Effect of the L- or D-aspartate on ecto-5'nucleotidase activity and on cellular viability in cultured neurons: participation of the adenosine A(2A) receptors
Amino Acids
33
439-444
2007
Rattus norvegicus
brenda
Iqbal, J.; Jirovsky, D.; Lee, S.Y.; Zimmermann, H.; Mueller, C.E.
Capillary electrophoresis-based nanoscale assays for monitoring ecto-5'-nucleotidase activity and inhibition in preparations of recombinant enzyme and melanoma cell membranes
Anal. Biochem.
373
129-140
2008
Homo sapiens, Rattus norvegicus
brenda
Babiychuk, E.B.; Draeger, A.
Regulation of ecto-5'-nucleotidase activity via Ca2+-dependent, annexin 2-mediated membrane rearrangement?
Biochem. Soc. Trans.
34
374-376
2006
Rattus norvegicus
brenda
Nedeljkovic, N.; Bjelobaba, I.; Subasic, S.; Lavrnja, I.; Pekovic, S.; Stojkov, D.; Vjestica, A.; Rakic, L.; Stojiljkovic, M.
Up-regulation of ectonucleotidase activity after cortical stab injury in rats
Cell Biol. Int.
30
541-546
2006
Rattus norvegicus
brenda
Bernardi, A.; Bavaresco, L.; Wink, M.R.; Jacques-Silva, M.C.; Delgado-Canedo, A.; Lenz, G.; Battastini, A.M.
Indomethacin stimulates activity and expression of ecto-5'-nucleotidase/CD73 in glioma cell lines
Eur. J. Pharmacol.
569
8-15
2007
Homo sapiens, Rattus norvegicus
brenda
Kittel, A.; Sperlagh, B.; Pelletier, J.; Sevigny, J.; Kirley, T.L.
Transient changes in the localization and activity of ecto-nucleotidases in rat hippocampus following lipopolysaccharide treatment
Int. J. Dev. Neurosci.
25
275-282
2007
Rattus norvegicus
brenda
Pedrazza, E.L.; Senger, M.R.; Rico, E.P.; Zimmermann, F.F.; Pedrazza, L.; de Freitas Sarkis, J.J.; Bonan, C.D.
Fluoxetine and nortriptyline affect NTPDase and 5'-nucleotidase activities in rat blood serum
Life Sci.
81
1205-1210
2007
Rattus norvegicus
brenda
Tamajusuku, A.S.; Carrillo-Sepulveda, M.A.; Braganhol, E.; Wink, M.R.; Sarkis, J.J.; Barreto-Chaves, M.L.; Battastini, A.M.
Activity and expression of ecto-5-nucleotidase/CD73 are increased by thyroid hormones in vascular smooth muscle cells
Mol. Cell. Biochem.
289
65-72
2006
Rattus norvegicus
brenda
Miron, V.R.; Bauermann, L.; Morsch, A.L.; Zanin, R.F.; Correa, M.; da Silva, A.C.; Mazzanti, C.; Morsch, V.M.; Lunkes, G.I.; Schetinger, M.R.
Enhanced NTPDase and 5'-nucleotidase activities in diabetes mellitus and iron-overload model
Mol. Cell. Biochem.
298
101-107
2007
Rattus norvegicus
brenda
Spanevello, R.M.; Mazzanti, C.M.; Kaizer, R.; Zanin, R.; Cargnelutti, D.; Hannel, L.; Correa, M.; Mazzanti, A.; Festugatto, R.; Graca, D.; Schetinger, M.R.; Morsch, V.M.
Apyrase and 5'-nucleotidase activities in synaptosomes from the cerebral cortex of rats experimentally demyelinated with ethidium bromide and treated with interferon-beta
Neurochem. Res.
31
455-462
2006
Rattus norvegicus
brenda
Delwing, D.; Delwing, D.; Goncalves, M.C.; Sarkis, J.J.; Wyse, A.T.
NTPDase and 5'-nucleotidase activities of synaptosomes from hippocampus of rats subjected to hyperargininemia
Neurochem. Res.
32
1209-1216
2007
Rattus norvegicus
brenda
Pochmann, D.; Innocente, A.M.; Cotomacci, G.; Barreto-Chaves, M.L.; Sarkis, J.J.
AMP hydrolysis in soluble and microsomal rat cardiac cell fractions: kinetic characterization and molecular identification of 5'-nucleotidase
Biosci. Rep.
28
267-273
2008
Rattus norvegicus
brenda
Pedrazza, E.L.; Rico, E.P.; Senger, M.R.; Pedrazza, L.; Zimmermann, F.F.; Sarkis, J.J.; Bogo, M.R.; Bonan, C.D.
Ecto-nucleotidase pathway is altered by different treatments with fluoxetine and nortriptyline
Eur. J. Pharmacol.
583
18-25
2008
Rattus norvegicus
brenda
Ruecker, B.; Almeida, M.E.; Libermann, T.A.; Zerbini, L.F.; Wink, M.R.; Sarkis, J.J.
E-NTPDases and ecto-5'-nucleotidase expression profile in rat heart left ventricle and the extracellular nucleotide hydrolysis by their nerve terminal endings
Life Sci.
82
477-486
2008
Rattus norvegicus
brenda
Bavaresco, L.; Bernardi, A.; Braganhol, E.; Cappellari, A.R.; Rockenbach, L.; Farias, P.F.; Wink, M.R.; Delgado-Canedo, A.; Battastini, A.M.
The role of ecto-5'-nucleotidase/CD73 in glioma cell line proliferation
Mol. Cell. Biochem.
319
61-68
2008
Homo sapiens, Rattus norvegicus
brenda
Fuerstenau, C.R.; Trentin, D.d.a..S.; Gossenheimer, A.N.; Ramos, D.B.; Casali, E.A.; Barreto-Chaves, M.L.; Sarkis, J.J.
Ectonucleotidase activities are altered in serum and platelets of L-NAME-treated rats
Blood Cells Mol. Dis.
41
223-229
2008
Rattus norvegicus
brenda
Braun, J.S.
Ecto-5'-nucleotidase-positive cells in the choroid and ciliary body of the rat eye
Anat. Rec. (Hoboken)
293
379-382
2010
Rattus norvegicus
brenda
Schmatz, R.; Mazzanti, C.M.; Spanevello, R.; Stefanello, N.; Gutierres, J.; Maldonado, P.A.; Correa, M.; da Rosa, C.S.; Becker, L.; Bagatini, M.; Goncalves, J.F.; Jaques, J.d.o.s..S.; Schetinger, M.R.; Morsch, V.M.
Ectonucleotidase and acetylcholinesterase activities in synaptosomes from the cerebral cortex of streptozotocin-induced diabetic rats and treated with resveratrol
Brain Res. Bull.
80
371-376
2009
Rattus norvegicus
brenda
Bjelobaba, I.; Stojiljkovic, M.; Lavrnja, I.; Stojkov, D.; Pekovic, S.; Dacic, S.; Laketa, D.; Rakic, L.; Nedeljkovic, N.
Regional changes in ectonucleotidase activity after cortical stab injury in rat
Gen. Physiol. Biophys.
28 Spec No
62-68
2009
Rattus norvegicus
brenda
El-Tayeb, A.; Iqbal, J.; Behrenswerth, A.; Romio, M.; Schneider, M.; Zimmermann, H.; Schrader, J.; Mueller, C.E.
Nucleoside-5'-monophosphates as prodrugs of adenosine A2A receptor agonists activated by ecto-5-nucleotidase
J. Med. Chem.
52
7669-7677
2009
Rattus norvegicus
brenda
Baqi, Y.; Lee, S.Y.; Iqbal, J.; Ripphausen, P.; Lehr, A.; Scheiff, A.B.; Zimmermann, H.; Bajorath, J.; Mueller, C.E.
Development of potent and selective inhibitors of ecto-5-nucleotidase based on an anthraquinone scaffold
J. Med. Chem.
53
2076-2086
2010
Rattus norvegicus
brenda
Shirley, D.G.; Vekaria, R.M.; Sevigny, J.
Ectonucleotidases in the kidney
Purinergic Signal.
5
501-511
2009
Mus musculus, Rattus norvegicus
brenda
Martin-Satue, M.; Lavoie, E.G.; Fausther, M.; Lecka, J.; Aliagas, E.; Kukulski, F.; Sevigny, J.
High expression and activity of ecto-5'-nucleotidase/CD73 in the male murine reproductive tract
Histochem. Cell Biol.
133
659-668
2010
Mus musculus, Mus musculus C57BL/6, Rattus norvegicus
brenda
Bjelobaba, I.; Parabucki, A.; Lavrnja, I.; Stojkov, D.; Dacic, S.; Pekovic, S.; Rakic, L.; Stojiljkovic, M.; Nedeljkovic, N.
Dynamic changes in the expression pattern of ecto-5'-nucleotidase in the rat model of cortical stab injury
J. Neurosci. Res.
89
862-873
2011
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Iqbal, J.; Saeed, A.; Raza, R.; Matin, A.; Hameed, A.; Furtmann, N.; Lecka, J.; Sevigny, J.; Bajorath, J.
Identification of sulfonic acids as efficient ecto-5-nucleotidase inhibitors
Eur. J. Med. Chem.
70
685-691
2013
Homo sapiens, Rattus norvegicus
brenda
Salman, S.; Vollmer, C.; McClelland, G.B.; Nurse, C.A.
Characterization of ectonucleotidase expression in the rat carotid body regulation by chronic hypoxia
Am. J. Physiol. Cell Physiol.
313
C274-C284
2017
Rattus norvegicus (P21588)
brenda
Adzic, M.; Nedeljkovic, N.
Unveiling the role of ecto-5'-nucleotidase/CD73 in astrocyte migration by using pharmacological tools
Front. Pharmacol.
9
153
2018
Rattus norvegicus
brenda
Eguchi, R.; Yamaguchi, S.; Otsuguro, K.I.
Fibroblast growth factor 2 modulates extracellular purine metabolism by upregulating ecto-5'-nucleotidase and adenosine deaminase in cultured rat spinal cord astrocytes
J. Pharmacol. Sci.
139
98-104
2018
Rattus norvegicus (P21588)
brenda
Miliutina, M.; Janke, J.; Hassan, S.; Zaib, S.; Iqbal, J.; Lecka, J.; Sevigny, J.; Villinger, A.; Friedrich, A.; Lochbrunner, S.; Langer, P.
A domino reaction of 3-chlorochromones with aminoheterocycles. Synthesis of pyrazolopyridines and benzofuropyridines and their optical and ecto-5'-nucleotidase inhibitory effects
Org. Biomol. Chem.
16
717-732
2018
Rattus norvegicus (P21588), Homo sapiens (P21589)
brenda
Doleski, P.H.; Mendes, R.E.; Leal, D.B.; Bottari, N.B.; Piva, M.M.; Da Silva, E.S.; Gabriel, M.E.; Lucca, N.J.; Schwertz, C.I.; Giacomim, P.; Morsch, V.M.; Schetinger, M.R.; Baldissera, M.D.; Da Silva, A.S.
Seric and hepatic NTPDase and 5'nucleotidase activities of rats experimentally infected by Fasciola hepatica
Parasitology
143
551-556
2016
Rattus norvegicus
brenda
Saeed, A.; Ejaz, S.; Shehzad, M.; Hassan, S.; Al-Rashida, M.; Lecka, J.; Sevigny, J.; Iqbal, J.
3-(5-(Benzylideneamino)thiazol-3-yl)-2H-chromen-2-ones A new class of alkaline phosphatase and ecto-5'-nucleotidase inhibitors
RSC Adv.
6
21026-21036
2016
Homo sapiens, Rattus norvegicus
-
brenda