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Information on EC 5.6.2.2 - DNA topoisomerase (ATP-hydrolysing) and Organism(s) Homo sapiens and UniProt Accession P11388

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EC Tree
IUBMB Comments
The enzyme can introduce negative superhelical turns into double-stranded circular DNA. One unit has nicking-closing activity, and another catalyses super-twisting and hydrolysis of ATP (cf. EC 5.6.2.1 DNA topoisomerase).
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P11388
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
ATP-dependent breakage, passage and rejoining of double-stranded DNA
Synonyms
atpase, topoisomerase ii, dna gyrase, topo ii, gyrase, top2a, dna topoisomerase ii, topoisomerase iialpha, topo iialpha, topoisomerase ii alpha, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DNA topoisomerase 2alpha
-
DNA topoisomerase IIalpha
-
DNA topoisomeraseIIalpha
-
hTopoIIalpha
-
topo2alpha
-
Topoisomerase II
-
topoisomerase II alpha
-
topoisomerase IIalpha
-
type 2 DNA topoisomerase
-
deoxyribonucleic acid topoisomerase IIalpha
-
-
DNA gyrase
-
-
-
-
DNA Top IIbeta
-
-
DNA Topo II
-
-
DNA topo IIalpha
-
-
DNA topoisomerase II
DNA topoisomerase II alpha
-
-
DNA topoisomerase II beta
-
-
DNA topoisomerase IIalpha
-
-
DNA topoisomerase IIbeta
-
-
DNA topoisomerase type II
-
-
-
-
DNA topoisomerases II
-
-
DNA-topoisomerase II
-
-
DNA-topoisomerase II-alpha
-
-
DNATop2A
-
-
Isomerase, deoxyribonucleate topo-, II
-
-
-
-
microrchidia protein
-
-
MORC1
-
-
NP170 proteins
-
-
-
-
Nuclear proteins 170,000-mol.wt.
-
-
-
-
Protein Gp39
-
-
-
-
Protein Gp52
-
-
-
-
Protein Gp60
-
-
-
-
Proteins , NP170 (specific proteins and subclasses nuclear protein, 170,000-mol.-wt.)
-
-
-
-
PsTopII
-
-
-
-
tIIalpha
-
-
Top2alpha
-
-
Top2b
-
-
topIIalpha
-
-
topo II
topo II alpha
-
-
topo II-alpha
-
-
Topo IIalpha
Topo IIbeta
topo-IIalpha
-
-
TOPOII
topoIIalpha
topoIIbeta
topoisomerase 2 alpha
-
-
Topoisomerase II
topoisomerase II alpha
topoisomerase IIalpha
topoisomerase IIbeta
Topoisomerase type II
-
-
-
-
toposiomerase II
-
-
type II DNA topoisomerase
-
-
type II topoisomerase
-
-
Type II-DNA-topoisomerase
-
-
-
-
type IIalpha DNA topoisomerase
-
-
type-II topoisomerase
-
-
additional information
-
topoisomerase II is an ATPase belonging to the GHKL family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP-dependent breakage, passage and rejoining of double-stranded DNA
show the reaction diagram
catalytic residue is Y815, active site structure includes residues Q789, D799, A801, S802, R804, and Y805
ATP-dependent breakage, passage and rejoining of double-stranded DNA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
DNA topoisomerase (ATP-hydrolysing)
The enzyme can introduce negative superhelical turns into double-stranded circular DNA. One unit has nicking-closing activity, and another catalyses super-twisting and hydrolysis of ATP (cf. EC 5.6.2.1 DNA topoisomerase).
CAS REGISTRY NUMBER
COMMENTARY hide
142805-56-9
-
80449-01-0
formerly not distinguished from EC 5.99.1.2
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + catenated kinetoplast DNA
ADP + phosphate + decatenated kinetoplast DNA
show the reaction diagram
-
-
-
?
ATP + negatively supercoiled pUC19 DNA
ADP + phosphate + relaxed pUC19 DNA
show the reaction diagram
-
-
-
?
ATP + supercoiled pBR322 plasmid DNA
ADP + phosphate + relaxed pBR322 plasmid DNA
show the reaction diagram
-
-
-
?
supercoiled DNA + ATP
relaxed DNA + ADP + phosphate
show the reaction diagram
-
-
-
?
supercoiled DNA + ATP + H2O
?
show the reaction diagram
substrate is supercoiled scpBR322 plasmid DNA. Topo2a creates transient breaks in supercoiled DNA in an ATP-dependent manner resulting in DNA relaxation
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
show the reaction diagram
-
-
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
show the reaction diagram
-
-
-
?
supercoiled pBR322 DNA + ATP + H2O
relaxed pBR322 DNA + ADP + phosphate
show the reaction diagram
-
-
-
?
ATP + catenated kinetoplast DNA
ADP + phosphate + decatenated kinetoplast DNA
show the reaction diagram
-
-
-
-
?
ATP + decatenated DNA
ADP + phosphate + catenated DNA
show the reaction diagram
-
-
-
-
?
ATP + knotted supercoiled DNA
ADP + phosphate + unknotted relaxed DNA
show the reaction diagram
-
-
-
-
?
ATP + negatively supercoiled pBR322 DNA
ADP + phosphate + relaxed pBR322 DNA
show the reaction diagram
-
-
-
-
?
ATP + negatively supercoiled pER8:hemagglutinin plasmid DNA
ADP + phosphate + relaxed pER8:hemagglutinin plasmid DNA
show the reaction diagram
-
-
-
-
?
ATP + relaxed pBR322 DNA
ADP + phosphate + supercoiled pBR322 DNA
show the reaction diagram
-
-
-
-
?
ATP + supercoiled plasmid pNO1
ADP + phosphate + relaxed plasmid pNO1
show the reaction diagram
-
-
-
-
?
ATP + supercoiled pUC19 DNA
ADP + phosphate + nicked pUC19 DNA
show the reaction diagram
-
-
-
-
?
ATP + supercoiled pUC19 DNA
ADP + phosphate + relaxed pUC19 DNA
show the reaction diagram
-
-
-
-
?
catenated kDNA + ATP + H2O
unlinked monomer kDNA + ADP + phosphate
show the reaction diagram
-
-
-
?
DNA + ATP
?
show the reaction diagram
-
cleavage requires coupling to ATP hydrolysis
-
-
?
DNA + ATP + H2O
DNA + ADP + phosphate
show the reaction diagram
double-stranded DNA + ATP + H2O
?
show the reaction diagram
-
ATP-dependent breakage, passage, and rejoining of double-stranded DNA
-
-
?
dsDNA + ATP + H2O
?
show the reaction diagram
four-way junction DNA + ATP + H2O
?
show the reaction diagram
-
binds and cleaves four-way junction DNA in vitro, topoisomerase IIbeta has a 4fold higher affinity for the four-way junction than for the linear duplex, the enzyme binds to the centre of the duplex, the four-way junction contains the sequence of a 40 bp linear duplex (containing a single topoisomerase cleavage site) along to adjacent arms, with the cleavage site straddling the point of strand exchange, the remaining two arms are comprised of sequences which do not contain topoisomerase cleavage sites, except that a potential m-AMSA-inducible cleavage site is introduced across the junction of these two arms
-
?
kinetoplast DNA + ATP
?
show the reaction diagram
-
decatenation
-
?
kinetoplast DNA + ATP + H2O
?
show the reaction diagram
negatively supercoiled DNA + ATP + H2O
?
show the reaction diagram
-
relaxation
-
?
negatively supercoiled pBR322 DNA + ATP + H2O
?
show the reaction diagram
-
breakage, passage, decatenation, and rejoining of negatively supercoiled pBR322 DNA, recombinant wild-type and truncation mutant Top2alphaDELTA1175, mechanisms
-
-
?
negatively supercoiled pHOTI plasmid DNA + ATP + H2O
?
show the reaction diagram
-
-
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
show the reaction diagram
pBR322 DNA + ATP + H2O
?
show the reaction diagram
-
decatenation, relaxation and cleavage of pBR322 DNA
-
-
?
plasmid DNA + ATP + H2O
?
show the reaction diagram
-
cleavage of plasmid DNA
-
-
?
plasmid DNA pRYG + ATP + H2O
?
show the reaction diagram
-
cleavage of plasmid DNA pRYG
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
show the reaction diagram
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
show the reaction diagram
supercoiled pBR 322 plasmid DNA + ATP + H2O
relaxed pBR 322 plasmid DNA + ADP + phosphate
show the reaction diagram
-
-
-
-
?
supercoiled pBR322 + ATP
?
show the reaction diagram
-
relaxation
-
?
supercoiled pBR322 DNA
?
show the reaction diagram
-
cleavage of supercoiled pBR322 DNA
-
-
?
supercoiled pKMp27 DNA + ATP + H2O
?
show the reaction diagram
-
relaxation of supercoiled pKMp27 DNA
-
-
?
supercoiled plasmid DNA + ATP + H2O
relaxed DNA + ADP + phosphate
show the reaction diagram
-
-
-
?
supercoiled plasmid pBR322 DNA + ATP
?
show the reaction diagram
-
relaxation of supercoiled DNA
-
?
supercoiled pRYG DNA + ATP + H2O
?
show the reaction diagram
theta-174 phage DNA + ATP + H2O
?
show the reaction diagram
-
unknotting of theta-174 phage DNA
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
supercoiled DNA + ATP
relaxed DNA + ADP + phosphate
show the reaction diagram
-
-
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
show the reaction diagram
-
-
-
?
supercoiled pBR322 DNA + ATP + H2O
relaxed pBR322 DNA + ADP + phosphate
show the reaction diagram
-
-
-
?
DNA + ATP + H2O
DNA + ADP + phosphate
show the reaction diagram
-
cleavage, relaxation, decatenation, and religation of DNA
-
-
?
dsDNA + ATP + H2O
?
show the reaction diagram
-
breakage, passage, decatenation, and rejoining of dsDNA
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
slightly activating above 5 mM
Cd2+
-
activates up to 1 mM, inhibits above 1 mM
Co2+
-
highly activating at 1-5 mM, enhances DNA cleavage mediated by topoisomerase II alpha in vitro and in cultured cells, 6-13fold higher activity in DNA cleavage compared to Mg2+, but reduced DNA ligation activity
Sr2+
-
slightly activating above 5 mM
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3-(6-methoxynaphthalen-2-yl)phenyl)methanol
-
(4-(6-methoxynaphthalen-2-yl)phenyl)methanol
-
1,4-benzoquinone
-
1,4-Naphthoquinone
-
1-(2-hydroxy-5-(6-hydroxynaphthalen-2-yl)-3-nitrophenyl)ethanone
-
1-(2-hydroxy-5-(6-methoxynaphthalen-2-yl)-3-nitrophenyl)ethanone
-
1-(4-(6-methoxynaphthalen-2-yl)phenyl)ethanol
-
-
1-(hydroxymethyl)-3-(2-hydroxypropan-2-yl)-2-(5-methoxy-9H-beta-carbolin-1-yl)-cyclopentanol
-
1-methyl-3-(2-hydroxypropan-2-yl)-2-(5-methoxy-9H-beta-carbolin-1-yl)-cyclopentanol
-
10-chloro-7-(3-(dimethylamino)propyl)-3-methoxybenzo[a]phenazin-5(7H)- one
-
10-chloro-7-(3-(dimethylamino)propyl)benzo[a]phenazin-5(7H)-one
-
2-(2-hydroxy-5-(6-hydroxynaphthalen-2-yl)phenyl)acetic acid
-
2-(2-hydroxyethyl)-5-(6-methoxynaphthalen-2-yl)phenol
-
2-(3,4-dimethoxyphenyl)-6-methoxynaphthalene
-
2-(4-(6-methoxynaphthalen-2-yl)phenyl)acetic acid
-
2-(4-chlorophenyl)-N-cyclohexylimidazo[1,2-a]pyrazin-3-amine
-
2-(4-chlorophenyl)imidazo[1,2-a]pyrazin-3-amine
-
2-(4-chlorophenyl)imidazo[1,2-a]pyridin-3-amine
-
2-(4-methoxyphenyl)imidazo[1,2-a]pyrazin-3-amine
-
2-(6-hydroxynaphthalen-2-yl)-4-methylbenzoic acid
-
2-acetoxy-5-(6-methoxynaphthalen-2-yl)benzyl acetate
-
2-hydroxy-3-methoxy-5-(6-methoxynaphthalen-2-yl)benzaldehyde
-
2-hydroxy-4-(6-hydroxynaphthalen-2-yl)benzoic acid
-
2-hydroxy-5-(6-hydroxynaphthalen-2-yl )-3-methoxybenzaldehyde
-
2-hydroxy-5-(6-hydroxynaphthalen-2-yl)benzaldehyde
-
2-hydroxy-5-(6-hydroxynaphthalen-2-yl)benzoic acid
-
2-hydroxy-5-(6-methoxynaphthalen-2-yl)benzoic acid
-
2-methoxy-5-(6-methoxynaphthalen-2-yl)benzaldehyde
-
2-methoxy-6-(3-(trifluoromethyl)phenyl)naphthalene
-
2-methoxy-6-(4-(trifluoromethyl)phenyl)naphthalene
-
2-methoxy-6-(4-nitro-3-(trifluoromethyl)phenyl)naphthalene
-
2-methyl-N-methyl-5-demethyl ellipticinium iodide
the compound inhibits DNA cleavage without altering the ability of topoisomerase IIalpha to bind its DNA substrate
3,8-dimethyl-5-(propan-2-yl)-6-[(prop-2-en-1-yl)oxy]naphthalene-1,2-dione
-
3,8-dimethyl-6-(octyloxy)-5-(propan-2-yl)naphthalene-1,2-dione
-
3,8-dimethyl-6-[(3-methylbut-2-en-1-yl)oxy]-5-(propan-2-yl)naphthalene-1,2-dione
-
3,8-dimethyl-6-[[(2Z)-3-phenylprop-2-en-1-yl]oxy]-5-(propan-2-yl)naphthalene-1,2-dione
-
3-[(10-methoxybenzo[a]phenazin-5-yl)oxy]-N,N-dimethylpropan-1-amine
-
4,7-dimethyl-5,6-dioxo-1-(propan-2-yl)-5,6-dihydronaphthalen-2-yl 2-chlorobenzoate
-
4,7-dimethyl-5,6-dioxo-1-(propan-2-yl)-5,6-dihydronaphthalen-2-yl 2-methoxybenzoate
-
4,7-dimethyl-5,6-dioxo-1-(propan-2-yl)-5,6-dihydronaphthalen-2-yl 4-methoxybenzoate
-
4,7-dimethyl-5,6-dioxo-1-(propan-2-yl)-5,6-dihydronaphthalen-2-yl benzoate
-
4,7-dimethyl-5,6-dioxo-1-(propan-2-yl)-5,6-dihydronaphthalen-2-yl butanoate
-
4,7-dimethyl-5,6-dioxo-1-(propan-2-yl)-5,6-dihydronaphthalen-2-yl decanoate
-
4,7-dimethyl-5,6-dioxo-1-(propan-2-yl)-5,6-dihydronaphthalen-2-yl hexanoate
-
4,7-dimethyl-5,6-dioxo-1-(propan-2-yl)-5,6-dihydronaphthalen-2-yl octanoate
-
4-(3-amino-6-bromoimidazo[1,2-a]pyridin-2-yl)benzonitrile
-
4-(6-hydroxynaphthalen-2-yl)benzene-1,2-diol
-
4-(6-methoxynaphthalen-2-yl)-2-methylaniline
-
4-(6-methoxynaphthalen-2-yl)aniline
-
4-(6-methoxynaphthalen-2-yl)phenol
-
4-hydroxy-3-(6-hydroxynaphthalen-2-yl)benzaldehyde
-
4-hydroxy-3-(6-methoxynaphthalen-2-yl)benzaldehyde
-
4-[2-(tert-butylamino)imidazo[1,2-a]pyrimidin-3-yl]benzonitrile
-
4-[3-(tert-butylamino)imidazo[1,2-a]pyrazin-2-yl]benzoic acid
-
4-[3-(tert-butylamino)imidazo[1,2-a]pyridin-2-yl]benzoic acid
-
4-[3-(tert-butylamino)imidazo[1,2-a]pyridin-2-yl]benzonitrile
-
6-(3,4-dimethoxyphenyl)naphthalen-2-ol
-
6-(3-(hydroxymethyl)phenyl)naphthalen-2-ol
-
6-(4-(1-hydroxyethyl)phenyl)naphthalen-2-ol
-
6-(4-(hydroxymethyl)phenyl)naphthalen-2-ol
-
6-(4-amino-3-methylphenyl)naphthalen-2-ol
-
6-(4-aminophenyl)naphthalen-2-ol
-
6-(4-hydroxy-3-(2-hydroxyethyl)phenyl)naphthalen-2-ol
-
6-(4-hydroxy-3-(hydroxymethyl)phenyl)naphthalen-2-ol
-
6-(4-hydroxyphenyl)naphthalen-2-ol
-
6-(4-nitro-3-(trifluoromethyl)phenyl)naphthalen-2-ol
-
6-(benzyloxy)-3,8-dimethyl-5-(propan-2-yl)naphthalene-1,2-dione
-
6-(dodecyloxy)-3,8-dimethyl-5-(propan-2-yl)naphthalene-1,2-dione
-
6-butoxy-3,8-dimethyl-5-(propan-2-yl)naphthalene-1,2-dione
-
6-chloro-2-(pyridin-2-yl)imidazo[1,2-a]pyridin-3-amine
-
6-ethoxy-3,8-dimethyl-5-(propan-2-yl)naphthalene-1,2-dione
-
6-methoxy-3,8-dimethyl-5-(propan-2-yl)naphthalene-1,2-dione
-
6-[(2-phenylethyl)sulfanyl]-9H-purin-2-amine
-
6-[(cyclopentylsulfanyl)methyl]-N2-(4-fluorophenyl)-1,3,5-triazine-2,4-diamine
-
6-[[(1-cyclopentyl-1H-tetrazol-5-yl)sulfanyl]methyl]-N2-(4-fluorophenyl)-1,3,5-triazine-2,4-diamine
-
6-[[(2E)-3,7-dimethylocta-2,6-dien-1-yl]oxy]-3,8-dimethyl-5-(propan-2-yl)naphthalene-1,2-dione
-
6-[[(5-cyclopropyl-1,3,4-oxadiazol-2-yl)sulfanyl]methyl]-N2-(4-fluorophenyl)-1,3,5-triazine-2,4-diamine
-
7-(2-(4-methylpiperazin-1-yl)ethyl)benzo[a]phenazin-5(7H)-one
-
7-(2-(diethylamino)ethyl)benzo[a]phenazin-5(7H)-one
-
7-(2-(dimethylamino)ethyl)-3-methoxybenzo[a]phenazin-5(7H)-one
-
7-(2-(dimethylamino)ethyl)benzo[a]phenazin-5(7H)-one
-
7-(2-(piperidin-1-yl)ethyl)benzo[a]phenazin-5(7H)-one
-
7-(2-morpholinoethyl)benzo[a]phenazin-5(7H)-one
-
7-(3-(4-methylpiperazin-1-yl)propyl)benzo[a]phenazin-5(7H)-one
-
7-(3-(diethylamino)propyl)-3-methoxybenzo[a]phenazin-5(7H)-one
-
7-(3-(diethylamino)propyl)benzo[a]phenazin-5(7H)-one
-
7-(3-(dimethylamino)propyl)-10-methoxybenzo[a]phenazin-5(7H)-one
-
7-(3-(dimethylamino)propyl)-2-methoxybenzo[a]phenazin-5(7H)-one
-
7-(3-(dimethylamino)propyl)-3,10-dimethoxybenzo[a]phenazin-5(7H)-one
-
7-(3-(dimethylamino)propyl)-3,9-dimethoxybenzo[a]phenazin-5(7H)-one
-
7-(3-(dimethylamino)propyl)-3-methoxybenzo[a]phenazin-5(7H)-one
-
7-(3-(dimethylamino)propyl)-9-methoxybenzo[a]phenazin-5(7H)-one
-
7-(3-(dimethylamino)propyl)benzo[a]phenazin-5(7H)-one
-
7-(3-(dimethylamino)propyl)benzo[f]pyrido[2,3-b]quinoxalin-5(7H)-one
-
7-(3-(piperidin-1-yl)propyl)benzo[a]phenazin-5(7H)-one
-
7-(3-(piperidin-1-yl)propyl)benzo[f]pyrido[2,3-b]quinoxalin-5(7H)-one
-
7-(3-(pyrrolidin-1-yl)propyl)benzo[a]phenazin-5(7H)-one
-
7-(3-morpholinopropyl)benzo[a]phenazin-5(7H)-one
-
7-(4-(diethylamino)butyl)benzo[a]phenazin-5(7H)-one
-
7-(4-(dimethylamino)butyl)benzo[a]phenazin-5(7H)-one
-
7-propylbenzo[a]phenazin-5(7H)-one
-
Aclarubicin
i.e. NCI0654508
benzo[a]phenazine
-
camptothecin
-
chartreusin
-
chromomycin A3
-
Ciprofloxacin
a topoisomerase II inhibitor
detorubicin
-
distel (1+)
-
ellipticine
i.e. 5,11-dimethyl-6H-pyrido[4,3-b]carbazole
elsamicin A
-
ethyl 2-(4-chlorophenyl)-3-(cyclohexylamino)-1H-imidazo[1,2-b]pyrazole-7-carboxylate
-
ethyl 3-(tert-butylamino)-2-(4-chlorophenyl)-1H-imidazo[1,2-b]pyrazole-7-carboxylate
-
ethyl 3-amino-2-(4-chlorophenyl)-1H-imidazo[1,2-b]pyrazole-7-carboxylate
-
etoposide
marcellomycin
-
methyl 2-(2-hydroxy-4-(6-methoxynaphthalen-2-yl)phenyl)acetate
-
methyl 2-(2-hydroxy-5-(6-hydroxynaphthalen-2-yl)phenyl)acetate
-
methyl 2-(4-(6-methoxynaphthalen-2-yl)phenyl)acetate
-
methyl 2-hydroxy-2-(4-(6-methoxynaphthalen-2-yl)phenyl)acetate
-
methyl 2-hydroxy-4-(6-methoxynaphthalen-2-yl)benzoate
-
methyl 2-hydroxy-5-(6-methoxynaphthalen-2-yl)benzoate
-
methyl 3-(6-hydroxynaphthalen-2-yl)-4-methylbenzoate
-
methyl 3-(6-methoxynaphthalen-2-yl)-4-methylbenzoate
-
methyl 4-(6-methoxynaphthalen-2-yl)benzoate
-
methyl 4-hydroxy-3-(6-hydroxynaphthalen-2-yl)benzoate
-
methyl 4-hydroxy-3-(6-methoxynaphthalen-2-yl)benzoate
-
mithramycin
-
N-methyl-5-demethyl ellipticine
the compound inhibits DNA cleavage without altering the ability of topoisomerase IIalpha to bind its DNA substrate
N-tert-butyl-2-(1H-pyrrol-2-yl)imidazo[1,2-a]pyridin-3-amine
-
N-tert-butyl-2-(2-chlorophenyl)imidazo[1,2-a]pyrazin-3-amine
-
N-tert-butyl-2-(3-methoxyphenyl)imidazo[1,2-a]pyrazin-3-amine
-
N-tert-butyl-2-(4-chlorophenyl)-7-methylimidazo[1,2-a]pyridin-3-amine
-
N-tert-butyl-2-(4-chlorophenyl)-9H-imidazo[1,2-a]benzimidazol-3-amine
-
N-tert-butyl-2-(4-chlorophenyl)imidazo[1,2-a]pyrazin-3-amine
-
N-tert-butyl-2-(4-chlorophenyl)imidazo[1,2-a]pyridin-3-amine
-
N-tert-butyl-2-(4-chlorophenyl)imidazo[1,2-a]pyrimidin-3-amine
-
N-tert-butyl-2-(naphthalen-1-yl)imidazo[1,2-a]pyridin-3-amine
-
N-tert-butyl-2-(pyridin-2-yl)imidazo[1,2-a]pyridin-3-amine
-
N-tert-butyl-2-phenylimidazo[1,2-a]pyrazin-3-amine
-
N-tert-butyl-2-phenylimidazo[1,2-a]pyridin-3-amine
-
N-tert-butyl-2-propylimidazo[1,2-a]pyridin-3-amine
-
N-tert-butyl-2-[4-(dimethylamino)phenyl]imidazo[1,2-a]pyridin-3-amine
-
N-tert-butyl-6-chloro-2-(4-chlorophenyl)imidazo[1,2-a]pyridin-3-amine
-
N-tert-butyl-6-chloro-2-(4-fluorophenyl)imidazo[1,2-a]pyridin-3-amine
-
N-tert-butylimidazo[1,2-a]pyrazin-3-amine
-
N-tert-butylimidazo[1,2-a]pyridin-3-amine
-
N2-(1,3-benzothiazol-6-yl)-N6-cycloheptyl-5,9-dihydro-4H-purine-2,6-diamine
-
N2-(1,3-benzothiazol-6-yl)-N6-tert-butyl-5,9-dihydro-4H-purine-2,6-diamine
-
N2-(4-fluorophenyl)-6-[[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl]-1,3,5-triazine-2,4-diamine
-
N2-(4-fluorophenyl)-6-[[(1-propyl-1H-imidazol-2-yl)sulfanyl]methyl]-1,3,5-triazine-2,4-diamine
-
N2-(4-fluorophenyl)-6-[[(1H-tetrazol-5-yl)sulfanyl]methyl]-1,3,5-triazine-2,4-diamine
-
N6-tert-butyl-8-ethyl-N2-[2-[2-(morpholin-4-yl)ethoxy]quinolin-6-yl]-5,9-dihydro-4H-purine-2,6-diamine
-
NCI0007535
-
NCI0009223
-
NCI0107678
-
NCI0245021
-
NCI0402956
-
NCI0603831
-
NCI0694885
-
piroxantrone
-
quercetin
a topoisomerase IIalpha inhibitor
salvicine
suramin
a topoisomerase IIalpha inhibitor
teloxantrone
-
valrubicin
-
variamycin
-
[4-amino-6-(4-fluoroanilino)-1,3,5-triazin-2-yl]methyl 4-methylpiperazine-1-carbodithioate
-
[4-amino-6-(4-fluoroanilino)-1,3,5-triazin-2-yl]methyl cyclohexyl(methyl)carbamodithioate
-
[4-amino-6-(4-fluoroanilino)-1,3,5-triazin-2-yl]methyl morpholine-4-carbodithioate
-
[4-amino-6-(4-methoxyanilino)-1,3,5-triazin-2-yl]methyl morpholine-4-carbodithioate
-
[4-amino-6-(4-methoxyanilino)-1,3,5-triazin-2-yl]methyl piperidine-1-carbodithioate
-
(+)-9-demethyleleutherin
-
-
(+)-deoxyeleutherin
-
-
(-)-deoxyeleutherin
-
-
(-)-epicatechin
-
98% inhibition at 0.1 mM
(-)-epigallocatechin
-
redox-dependent topoisomerase II poison
(-)-epigallocatechin gallate
(1,1',1''-[(6,9-dihydroporphyrin-5,10,15-triyl-k2N22,N24)tris(benzene-4,1-diyloxyethane-2,1-diyl)]tris[1-methylpiperidiniumato(2-)])copper(3+)
-
strong inhibition
(1R,1'R,6S,6'S,7R,7'R,11bR,11b'R)-1,1',7,7'-tetrakis(4-hydroxyphenyl)-1,1',6,6',7,7',11b,11b'-octahydro-6,6'-bi-2-oxadibenzo[cd,h]azulene-4,4',8,8',10,10'-hexol
-
comparison with inhibition of HindIII enzyme
(1R,1'R,6S,6'S,7S,7'S,11bR,11b'R)-1,1',7,7'-tetrakis(4-hydroxyphenyl)-1,1',6,6',7,7',11b,11b'-octahydro-6,6'-bi-2-oxadibenzo[cd,h]azulene-4,4',8,8',10,10'-hexol
-
comparison with inhibition of HindIII enzyme
(1R,3R)-8-methoxy-1-methyl-5,10-dioxo-3,4,5,10-tetrahydro-1H-benzo[g]isochromene-3-carboxylic acid
-
-
(1R,3S)-1,3,8-trimethyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(1R,3S)-7,9-dimethoxy-1,3,6-trimethyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(2E)-1,3-bis[4-(oxiran-2-ylmethoxy)phenyl]prop-2-en-1-one
-
inhibition in vivo in cancer cells, IC50 values, overview
(2E)-1,3-bis[4-(thiiran-2-ylmethoxy)phenyl]prop-2-en-1-one
-
inhibition in vivo in cancer cells, IC50 values, overview
(2E)-1-(4-methoxyphenyl)-3-[4-(oxiran-2-ylmethoxy)phenyl]prop-2-en-1-one
-
inhibition in vivo in cancer cells, IC50 values, overview
(2E)-1-(4-methoxyphenyl)-3-[4-(thiiran-2-ylmethoxy)phenyl]prop-2-en-1-one
-
inhibition in vivo in cancer cells, IC50 values, overview
(2E)-1-[2,4-bis(thiiran-2-ylmethoxy)phenyl]-3-(4-methoxyphenyl)prop-2-en-1-one
-
inhibition in vivo in cancer cells, IC50 values, overview
(2E)-1-[4-(3-chloro-2-hydroxypropoxy)phenyl]-3-(4-methoxyphenyl)prop-2-en-1-one
-
inhibition in vivo in cancer cells, IC50 values, overview
(2E)-2-(1,3-benzothiazol-2-ylmethylidene)-N,N-dimethylhydrazinecarbothioamide
-
-
(2E)-2-(1,3-benzothiazol-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-2-(1,8-naphthyridin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-2-(1-benzothiophen-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-2-(benzo[h][1,6]naphthyridin-5-ylmethylidene)-N,N-dimethylhydrazinecarbothioamide
-
-
(2E)-2-(benzo[h][1,6]naphthyridin-5-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-2-(quinolin-2-ylmethylidene)-N-[2-(trifluoromethyl)phenyl]hydrazinecarbothioamide
-
-
(2E)-2-(quinolin-2-ylmethylidene)-N-[4-(trifluoromethyl)phenyl]hydrazinecarbothioamide
-
-
(2E)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-2-(quinoxalin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-2-(thieno[2,3-b]pyridin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-2-[(3,4-dimethylthieno[2,3-b]thiophen-2-yl)methylidene]hydrazinecarbothioamide
-
-
(2E)-3-(4-methoxyphenyl)-1-[4-(oxiran-2-ylmethoxy)phenyl]prop-2-en-1-one
-
inhibition in vivo in cancer cells, IC50 values, overview
(2E)-3-(4-methoxyphenyl)-1-[4-(thiiran-2-ylmethoxy)phenyl]prop-2-en-1-one
-
inhibition in vivo in cancer cells, IC50 values, overview
(2E)-3-[2-methoxy-4-(oxiran-2-ylmethoxy)phenyl]-1-[4-(oxiran-2-ylmethoxy)phenyl]prop-2-en-1-one
-
inhibition in vivo in cancer cells, IC50 values, overview
(2E)-3-[4-(3-chloro-2-hydroxypropoxy)phenyl]-1-(4-methoxyphenyl)prop-2-en-1-one
-
inhibition in vivo in cancer cells, IC50 values, overview
(2E)-N,N-dimethyl-2-(1,8-naphthyridin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N,N-dimethyl-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
exhibits broad antiproliferative activity arresting synchronized cells at the M-phase, also exhibits iron chelator activity, and topoisomerase IIalpha catalytic inhibition, the latter due to direct interaction with the ATPase domain, blocks of ATP hydroly
(2E)-N,N-dimethyl-2-(quinoxalin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N,N-dimethyl-2-(thieno[2,3-b]pyridin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(2-bromophenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(2-fluorophenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(2-methoxy-5-methylphenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(2-methoxyphenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(2-methylphenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(3-bromophenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(3-chlorophenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(3-fluorophenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(3-methoxyphenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(3-methylphenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(4-bromophenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(4-chlorophenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(4-cyanophenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(4-fluorophenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(4-methoxyphenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(4-methylphenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(4-methylphenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarboxamide
-
-
(2E)-N-benzyl-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-phenyl-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-[2',6'-di(propan-2-yl)biphenyl-4-yl]-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2R,2'S,3'S)-3'-(3,5-dihydroxyphenyl)-2,2'-bis(4-hydroxyphenyl)-4-[(E)-2-(4-hydroxyphenyl)ethenyl]-2,2',3,3'-tetrahydro-3,4'-bi-1-benzofuran-6,6'-diol
-
comparison with inhibition of HindIII enzyme
(2R,3S)-2-(3,5-dihydroxyphenyl)-1-[(S)-hydroxy(4-hydroxyphenyl)methyl]-3-(4-hydroxyphenyl)-2,3-dihydro-1H-indene-4,6-diol
-
comparison with inhibition of HindIII enzyme
(2S)-2-(2-hydroxypropan-2-yl)-2,5-dimethyl-8,10-bis[(2-methyloxiran-2-yl)methoxy]-1,2-dihydro-11H-furo[3,2-a]xanthen-11-one
-
-
(2S,3R,4S,6R)-4-amino-2-methyl-6-((3-(2-phenyl-1-tosyl-1H-indol-3-yl)prop-2-yn-1-yl)oxy)tetrahydro-2H-pyran-3-ol
-
103% inhibition at 0.1 mM
(2S,3R,4S,6R)-4-amino-2-methyl-6-((3-(2-phenylbenzofuran-3-yl)prop-2-yn-1-yl)oxy)tetrahydro-2H-pyran-3-ol
-
5.5% inhibition at 0.1 mM
(2S,3R,4S,6R)-4-amino-2-methyl-6-((3-(2-phenylbenzo[b]thiophen-3-yl)prop-2-yn-1-yl)oxy)tetrahydro-2H-pyran-3-ol
-
22.2% inhibition at 0.1 mM
(2S,3R,4S,6R)-4-amino-2-methyl-6-(3-(2-phenyl-1H-indol-3-yl)prop-2-ynyloxy)tetrahydro-2H-pyran-3-ol
-
55.5% inhibition at 0.1 mM
(2S,3S,6R)-2-methyl-6-(3-(2-phenyl-1-tosyl-1H-indol-3-yl)prop-2-ynyloxy)tetrahydro-2H-pyran-3-amine
-
86.2% inhibition at 0.1 mM
(2S,3S,6R)-2-methyl-6-(3-(2-phenyl-1H-indol-3-yl)prop-2-ynyloxy)tetrahydro-2H-pyran-3-amine
-
39.5% inhibition at 0.1 mM
(2S,3S,6R)-2-methyl-6-(3-(2-phenylbenzo[b]thiophen-3-yl)prop-2-ynyloxy)tetrahydro-2H-pyran-3-amine
-
16.4% inhibition at 0.1 mM
(3,3',3''-[(6,9-dihydroporphyrin-5,10,15-triyl-k2N22,N24)tris(benzene-4,1-diyloxy)]tris(N,N,N-trimethylpropan-1-aminiumato)(2-))copper(3+)
-
strong inhibition
(3,5-dimethoxybenzene)-propynoic acid
-
-
(3,5-dimethoxybenzene)-propynoic acid methyl ester
-
-
(3R,4R,4aS,5S,9bS,10S)-4-(3,5-dihydroxyphenyl)-3,5,10-tris(4-hydroxyphenyl)-3,4,4a,5,9b,10-hexahydro-11-oxabenzo[5,6]cyclohepta[1,2,3,4-jkl]-as-indacene-2,6,8-triol
-
comparison with inhibition of HindIII enzyme
(3S)-3-methyl-7,9-bis(propan-2-yloxy)-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(3S)-7,9-dihydroxy-3-methyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(3S)-7,9-dimethoxy-3-methyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(3S)-9-hydroxy-7-methoxy-3-methyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(3S,4S,4aR,5S,9bS,10S)-4-(3,5-dihydroxyphenyl)-3,5,10-tris(4-hydroxyphenyl)-3,4,4a,5,9b,10-hexahydro-11-oxabenzo[5,6]cyclohepta[1,2,3,4-jkl]-as-indacene-2,6,8-triol
-
comparison with inhibition of HindIII enzyme
(4bR,5R,9S,10S,11R,12R)-10-(3,5-dihydroxyphenyl)-5,9,12-tris(4-hydroxyphenyl)-4b,5,9,10,11,12-hexahydrobenzo[6,7]cyclohepta[1,2,3-cd]furo[3,2-f][1]benzofuran-1,3,11-triol
-
comparison with inhibition of HindIII enzyme
(4Z,7Z,10Z,13Z,16Z,19Z)-henicosa-4,7,10,13,16,19-hexaenoic acid
-
IC50 is 0.05 mM for inhibition of decatenation of kinetoplast DNA
(5R,5aR,8aS,9S)-5-(4-hydroxy-3,5-dimethoxyphenyl)-9-(1H-pyrrolo[2,3-b]pyridin-6-ylamino)-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-5-(4-hydroxy-3,5-dimethoxyphenyl)-9-(4H-1,2,4-triazol-3-ylamino)-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-5-(4-hydroxy-3,5-dimethoxyphenyl)-9-(9H-purin-6-ylamino)-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-5-(4-hydroxy-3,5-dimethoxyphenyl)-9-(imidazo[1,2-a]pyridin-8-ylamino)-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-5-(4-hydroxy-3,5-dimethoxyphenyl)-9-{[3-(methylamino)pyridin-2-yl]amino}-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-5-(4-hydroxy-3,5-dimethoxyphenyl)-9-{[3-(piperidin-1-ylmethyl)phenyl]amino}-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
molecular docking to MDR protein
(5R,5aR,8aS,9S)-5-(4-hydroxy-3,5-dimethoxyphenyl)-9-{[3-(pyrrolidin-1-ylmethyl)phenyl]amino}-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-5-(4-hydroxy-3,5-dimethoxyphenyl)-9-{[4-(piperidin-1-ylmethyl)phenyl]amino}-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-5-(4-hydroxy-3,5-dimethoxyphenyl)-9-{[4-(pyrrolidin-1-ylmethyl)phenyl]amino}-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-9-({3-[(diethylamino)methyl]phenyl}amino)-5-(4-hydroxy-3,5-dimethoxyphenyl)-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-9-({4-[(diethylamino)methyl]phenyl}amino)-5-(4-hydroxy-3,5-dimethoxyphenyl)-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-9-[(5,6-diphenyl-1,2,4-triazin-3-yl)amino]-5-(4-hydroxy-3,5-dimethoxyphenyl)-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-9-[(6-aminopyridin-2-yl)amino]-5-(4-hydroxy-3,5-dimethoxyphenyl)-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoic acid
-
irreversible inhibition, IC50 is 0.01 mM for inhibition of decatenation of kinetoplast DNA, effects on thermal transition of dsDNA, overview
(6aR,12aR)-11-(2,3-dihydroxypropoxy)-12a-hydroxy-2,3,9-trimethoxy-6a,12a-dihydrochromeno[3,4-b]chromen-12(6H)-one
-
-
(6aR,12aR)-11-(3-chloro-2-hydroxypropoxy)-12a-hydroxy-2,3,9-trimethoxy-6a,12a-dihydrochromeno[3,4-b]chromen-12(6H)-one
-
-
(6aR,12aR)-11-[3-(benzylamino)-2-hydroxypropoxy]-12a-hydroxy-2,3,9-trimethoxy-6a,12a-dihydrochromeno[3,4-b]chromen-12(6H)-one
-
-
(6aR,12aR)-11-[3-[bis(2-hydroxyethyl)amino]-2-hydroxypropoxy]-12a-hydroxy-2,3,9-trimethoxy-6a,12a-dihydrochromeno[3,4-b]chromen-12(6H)-one
-
-
(6aR,12aR)-12a-hydroxy-11-(2-hydroxy-3-methoxypropoxy)-2,3,9-trimethoxy-6a,12a-dihydrochromeno[3,4-b]chromen-12(6H)-one
-
-
(6aR,12aR)-12a-hydroxy-11-(2-hydroxy-3-[[2-(morpholin-4-yl)ethyl]amino]propoxy)-2,3,9-trimethoxy-6a,12a-dihydrochromeno[3,4-b]chromen-12(6H)-one
-
-
(6aR,12aR)-12a-hydroxy-11-[2-hydroxy-3-(morpholin-4-yl)propoxy]-2,3,9-trimethoxy-6a,12a-dihydrochromeno[3,4-b]chromen-12(6H)-one
-
-
(6aR,12aR)-12a-hydroxy-11-[2-hydroxy-3-[(2-hydroxy-2-phenylethyl)amino]propoxy]-2,3,9-trimethoxy-6a,12a-dihydrochromeno[3,4-b]chromen-12(6H)-one
-
-
(6aR,12aR)-12a-hydroxy-11-[2-hydroxy-3-[(2-phenylethyl)amino]propoxy]-2,3,9-trimethoxy-6a,12a-dihydrochromeno[3,4-b]chromen-12(6H)-one
-
-
(6aR,12aR)-12a-hydroxy-2,3,9-trimethoxy-11-(oxiran-2-ylmethoxy)-6a,12a-dihydrochromeno[3,4-b]chromen-12(6H)-one
-
-
(9-([2-(1H-indol-3-yl)ethyl]amino)acridin-3-yl)(4-methylpiperazin-1-yl)methanone
-
-
(9-([2-(1H-indol-3-yl)ethyl]amino)acridin-4-yl)(4-methylpiperazin-1-yl)methanone
-
-
(9-[(1-benzylpiperidin-4-yl)amino]acridin-3-yl)(4-methylpiperazin-1-yl)methanone
-
-
(9S,12S,13S)-trihydroxy-(10E)-octadecenoic acid
-
97% inhibition at 0.1 mM
1,3,5-trihydroxy-4-methoxy-9H-xanthen-9-one
-
-
1,3-benzodioxole-5-carbaldehyde
-
-
1,3-bis(oxiran-2-ylmethoxy)-9H-xanthen-9-one
-
inhibition in vivo in cancer cells, IC50 values, overview
1,4-benzoquinone
1,4-hydroquinone
1,5-dihydroxy-3-methoxy-2,4-bis(3-methylbut-2-en-1-yl)-9H-xanthen-9-one
-
-
1,7-dihydroxy-9H-xanthen-9-one
-
-
1-(2,2-dibromoethenyl)-3,5-dimethoxybenzene
-
-
1-(2,2-dibromoethenyl)-4-methoxybenzene
-
-
1-(2-hydroxy-3-[[(6aR,12aR)-12a-hydroxy-2,3,9-trimethoxy-12-oxo-6,6a,12,12a-tetrahydrochromeno[3,4-b]chromen-11-yl]oxy]propyl)piperidin-4-one
-
-
1-(4-methoxybenzyl)-1H-[1,2,3]triazolo[4,5-g]-phthalazine-4,9-dione
-
-
1-benzenesulfonyl-3-chloropropenyl-1H-indole
-
-
1-benzenesulfonyl-5-benzyloxy-3-chloropropenyl-1H-indole
-
-
1-ethoxycarbonyl-naphthoquinone-[2,3-d]indolizidine-6,11-dione
-
0.1 mg/ml, 32.1% inhibition of relaxation
1-ethyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
-
-
1-ethyl-3-(benzimidazol-2-yl)-6,8-difluoro-7-(3-methylpiperazin-1-yl)-4(1H)-quinolone
-
18% and 13% inhibition at 0.1 mM and 0.02 mM, respectively
1-ethyl-3-(benzimidazol-2-yl)-6-fluoro-7-(1-piperazin-1-yl)-1,8-naphthyridine-4(1H)-one
-
8% and 30% inhibition at 0.02 mM and 0.1 mM, respectively
1-ethyl-3-(benzimidazol-2-yl)-6-fluoro-7-(piperazin-1-yl)-4(1H)-quinolone
-
8.5% and 7% inhibition at 0.02 mM and 0.1 mM, respectively
1-hydroxy-3-(2',3'-epoxypropoxy)thioxanthone
-
21% inhibition at 0.1 mM
1-hydroxy-3-(3'-chloro-2'-hydroxy-1'-propoxy)thioxanthone
-
84% inhibition at 0.1 mM
1-hydroxy-3-(3'-chloro-2'-thioyl-1'-propoxy)thioxanthone
-
16% inhibition at 0.1 mM
1-hydroxy-3-(oxiran-2-ylmethoxy)-9H-xanthen-9-one
-
-
1-hydroxy-3-[2-hydroxy-3-(2-hydroxyethoxy)propoxy]-9H-xanthen-9-one
-
89.25% inhibition at 0.1 mM
1-hydroxy-3-[2-hydroxy-3-(propylamino)propoxy]-9H-xanthen-9-one
-
100% inhibition at 0.1 mM. ATPase inhibitory activity, molecular docking, overview. The compound shows a stable binding pattern to the ATP-binding domain of topo II
1-hydroxy-3-[2-hydroxy-3-[(2-hydroxyethyl)amino]propoxy]-9H-xanthen-9-one
-
100% inhibition at 0.1 mM
1-hydroxy-3-[2-hydroxy-3-[(2-hydroxyethyl)sulfanyl]propoxy]-9H-xanthen-9-one
-
63.75% inhibition at 0.1 mM
1-hydroxy-3-[2-hydroxy-3-[(3-hydroxypropyl)amino]propoxy]-9H-xanthen-9-one
-
100% inhibition at 0.1 mM
1-hydroxy-3-[2-hydroxy-3-[(3-hydroxypropyl)sulfanyl]propoxy]-9H-xanthen-9-one
-
68% inhibition at 0.1 mM
1-iso-butyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
-
-
1-iso-propyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
-
-
1-methyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
-
-
1-n-butyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
-
-
1-n-propyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
-
-
1-[(1,1-dioxo-2,3-dihydro-1H-1l6-thiophen-3-yl)(ethyl)amino]-1-oxopropan-2-yl 1H-indazole-3-carboxylate
-
-
1-[4-[(methanesulfonyl)amino]phenyl]-1-oxopropan-2-yl 1H-indazole-3-carboxylate
-
-
10'(Z),13'(E),15'(E)-heptadecatrienyl hydroquinone
-
i.e. HQ17(3), the cysteine-reactive alkyl hydroquinone modifies topoisomerase IIalpha, enhances DNA breakage, and induces apoptosis in cancer cells, it is attributed to topoisomerase IIalpha poisoning and the induction of oxidative damage. Irreversibly inhibits Topo IIalpha activity in vitro and is more cytotoxic in leukemia HL-60 cells than in Topo IIalpha-deficient variant HL-60/MX2 cell. HQ17(3) reacts with Cys427, Cys733, and Cys997 of recombinant Topo IIalpha in vitro, whereas it reacts with Cys427 of cellular Topo IIalpha in Huh7 hepatoma cells. The cells, HQ17(3) treatment causes prompt inhibition of DNA synthesis and consequently induces the expression of DNA damage-related genes DDIT3, GADD45A, and GADD45G. Topo IIalpha inhibition, apoptosis, and oxidative stress account for cytotoxicity caused by HQ17(3). Pretreatment of Huh7 cells with N-acetylcysteine partially attenuates mitochondrial membrane damage, DNA breakage, and caspase activation, but does not diminish HQ17(3)-induced cell death
11-(4-Cyanoanilino)azatoxin
-
-
1H-[1,2,3]triazolo[4,5,-g]phthalazine-4,9-dione
-
-
2,2'-(4-phenylpyridine-2,6-diyl)diphenol
-
42.7% inhibition at 0.1 mM
2,2'-bis(8-formyl-1,6,7-trihydroxy-5-isopropyl-3-methylnaphthalene)
-
i.e. gossypol, belongs to the class II compounds which interfere with the catalytic function of topoisomerases without generating strand breaks
2,3-dimethoxy-9-(2-dimethylaminoethoxy)-6-(2-dimethylaminoethyl)-6H-indeno[1,2-c]isoquinolin-5,11-dione
-
-
2,3-dimethoxy-9-(2-dimethylaminoethoxy)-6-(3-dimethylaminopropyl)-6H-indeno[1,2-c]isoquinolin-5,11-dione
-
-
2,4-di(furan-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2,4-di(furan-2-yl)-5H-chromeno[4,3-b]pyridine
2,4-di(pyridin-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2,4-di(pyridin-2-yl)-5H-chromeno[4,3-b]pyridine
2,4-di(thiophen-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2,4-di(thiophen-2-yl)-5H-chromeno[4,3-b]pyridine
2,4-di(thiophen-3-yl)-5H-chromeno[4,3-b]pyridine
-
-
2,4-diphenyl-5,6-dihydrobenzo[h]quinoline
-
-
2,4-diphenyl-5H-chromeno[4,3-b]pyridine
2-(2,6-diphenylpyridin-4-yl)phenol
-
-
2-(2-chlorophenyl)-4-(furan-2-yl)-6-(3-methylthiophen-2-yl) pyridine
-
33.2% inhibition at 0.1 mM
2-(2-chlorophenyl)-6-(5-chlorothiophen-2-yl)-4-(furan-3-yl) pyridine
-
38% inhibition at 0.02 mM
2-(2-chlorophenyl)benzo-1,4-quinone
-
inhibits DNA religation by isoform IIalpha by blocking the N-terminal gate of the enzyme by cross-linking cross-linking its two protomer subunits
2-(3,5-dichlorophenyl)benzo-1,4-quinone
-
inhibits DNA religation by isoform IIalpha by blocking the N-terminal gate of the enzyme by cross-linking cross-linking its two protomer subunits
2-(3-(2-(dimethylamino)ethylamino)propyl)-6-(dodecylamino)-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-(3-(2-(dimethylamino)ethylamino)propyl)-6-(octylamino)-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-(3-(4-methylpiperazin-1-yl)propyl)-6-(octylamino)-1H-benzo-[de]isoquinoline-1,3(2H)-dione
-
-
2-(3-(dimethylamino)propyl)-6-(methylamino)-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-(3-(dimethylamino)propyl)-6-(octylamino)-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-(3-chlorophenyl)-6-(5-chlorothiophen-2-yl)-4-(furan-3-yl) pyridine
-
51% inhibition at 0.02 mM
2-(3-chlorophenyl)benzo-1,4-quinone
-
inhibits DNA religation by isoform IIalpha by blocking the N-terminal gate of the enzyme by cross-linking cross-linking its two protomer subunits
2-(3-fluorophenylamino)-5-(3-hydroxyphenyl)-1,3,4-thiadiazole
-
DNA topoisomerase II catalytic inhibitor
2-(4,6-diphenylpyridin-2-yl)phenol
-
-
2-(4-bromophenylamino)-5-(2,4-dichlorophenyl)-1,3,4-thiadiazole
-
DNA topoisomerase II poison
2-(4-chlorophenyl)-4-(furan-2-yl)-6-(3-methylthiophen-2-yl) pyridine
-
18% inhibition at 0.02 mM
2-(4-chlorophenyl)-4-(furan-3-yl)-6-(3-methylthiophen-2-yl) pyridine
-
33.8% inhibition at 0.1 mM
2-(4-chlorophenyl)-6-(5-chlorothiophen-2-yl)-4-(furan-2-yl) pyridine
-
48.4% inhibition at 0.02 mM
2-(4-chlorophenyl)-6-(5-chlorothiophen-2-yl)-4-(furan-3-yl) pyridine
-
57% inhibition at 0.02 mM
2-(4-chlorophenyl)benzo-1,4-quinone
2-(4-fluorophenylamino)-5-(2,4-dichlorophenyl)-1,3,4-thiadiazole
-
DNA topoisomerase II poison
2-(4-hydroxy-3-methoxyphenyl)chromenylium-3,5,7-triol
-
anthocyanidin, inhibition of isozyme IIbeta decatenation activity
2-(4-phenyl-2,2'-bipyridin-6-yl)phenol
-
-
2-(4-phenyl-2,3'-bipyridin-6-yl)phenol
-
-
2-(4-phenyl-2,4'-bipyridin-6-yl)phenol
-
-
2-(5-chlorothiophen-2-yl)-4-(furan-3-yl)-6-(5-methylfuran-2-yl) pyridine
-
54% inhibition at 0.02 mM
2-(5-chlorothiophen-2-yl)-4-(furan-3-yl)-6-m-tolylpyridine
-
38% inhibition at 0.02 mM
2-(5-chlorothiophen-2-yl)-4-(furan-3-yl)-6-o-tolylpyridine
-
49% inhibition at 0.02 mM
2-(5-chlorothiophen-2-yl)-4-(furan-3-yl)-6-p-tolylpyridine
-
54% inhibition at 0.02 mM
2-(5-chlorothiophen-2-yl)-6-(furan-2-yl)-4-(furan-3-yl)pyridine
-
48.6% inhibition at 0.02 mM
2-(6-phenyl-2,2'-bipyridin-4-yl)phenol
-
-
2-(6-phenyl-2,3'-bipyridin-4-yl)phenol
-
-
2-(6-phenyl-2,4'-bipyridin-4-yl)phenol
-
-
2-(furan-2-yl)-4-(furan-3-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2-(furan-2-yl)-4-(furan-3-yl)-6-(3-methylthiophen-2-yl)pyridine
-
36% inhibition at 0.02 mM
2-(furan-2-yl)-4-(pyridin-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2-(furan-2-yl)-4-(pyridin-2-yl)-5H-chromeno[4,3-b]pyridine
2-(furan-2-yl)-4-(pyridin-3-yl)-5H-chromeno[4,3-b]pyridine
2-(furan-2-yl)-4-(thiophen-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2-(furan-2-yl)-4-(thiophen-2-yl)-5H-chromeno[4,3-b]pyridine
2-(furan-2-yl)-4-(thiophen-3-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2-(furan-2-yl)-4-phenyl-5,6-dihydrobenzo[h]quinoline
-
-
2-(furan-2-yl)-4-phenyl-5H-chromeno[4,3-b]pyridine
2-(pyridin-2-yl)-4-(pyridin-3-yl)-5H-chromeno[4,3-b]pyridine
2-(pyridin-2-yl)-4-(thiophen-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2-(pyridin-2-yl)-4-(thiophen-2-yl)-5H-chromeno[4,3-b]pyridine
2-(pyridin-2-yl)-4-(thiophen-3-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2-(thiophen-2-yl)-4-(thiophen-3-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2-([[6-(benzylsulfanyl)-4-oxo-4,5-dihydro-1,3,5-triazin-2-yl]sulfanyl]methyl)benzonitrile
-
-
2-Amino-1-(1-benzyl-piperidin-4-yl)-4,9-dioxo-3a,4,9,9a-tetrahydro-1H-benzo[f]indole-3-carboxylic acid ethyl ester
-
0.1 mg/ml, 17.0% inhibition of relaxation
2-Amino-1-(2-bromo-ethyl)-4,9-dioxo-3a,4,9,9a-tetrahydro-1H-benzo[f]indole-3-carboxylic acid ethyl ester
-
0.1 mg/ml, 43.4% inhibition of relaxation
2-Amino-1-(2-hydroxy-ethyl)-4,9-dioxo-3a,4,9,9a-tetrahydro-1H-benzo[f]indole-3-carboxylic acid ethyl ester
-
0.1 mg/ml, 7.8% inhibition of relaxation
2-Amino-1-(4-amino-phenyl)-4,9-dioxo-3a,4,9,9a-tetrahydro-1H-benzo[f]indole-3-carboxylic acid ethyl ester
-
0.1 mg/ml, 7.8% inhibition of relaxation
2-Amino-1-(4-fluoro-phenyl)-4,9-dioxo-3a,4,9,9a-tetrahydro-1H-benzo[f]indole-3-carboxylic acid ethyl ester
-
0.1 mg/ml, 28.3% inhibition of relaxation
2-Amino-1-benzyl-4,9-dioxo-3a,4,9,9a-tetrahydro-1H-benzo[f]indole-3-carboxylic acid ethyl ester
-
0.1 mg/ml, 9.4% inhibition of relaxation
2-Amino-1-cyclohexyl-4,9-dioxo-3a,4,9,9a-tetrahydro-1H-benzo[f]indole-3-carboxylic acid ethyl ester
-
0.1 mg/ml, 7.8% inhibition of relaxation
2-Amino-1-isopropyl-4,9-dioxo-3a,4,9,9a-tetrahydro-1H-benzo[f]indole-3-carboxylic acid ethyl ester
-
0.1 mg/ml, 5.9% inhibition of relaxation
2-amino-3-ethoxycarbonyl-N-(4-fluorophenyl)benz[f]indole-4,9-dione
-
potent inhibitor
2-amino-3-ethoxycarbonyl-N-methyl-benz[f]indole-4,9-dione
-
0.1 mg/ml, 9.8% inhibition of relaxation
2-Amino-4,9-dioxo-1-p-tolyl-3a,4,9,9a-tetrahydro-1H-benzo[f]indole-3-carboxylic acid ethyl ester
-
0.1 mg/ml, 41.2% inhibition of relaxation
2-Amino-4,9-dioxo-1-phenyl-3a,4,9,9a-tetrahydro-1H-benzo[f]indole-3-carboxylic acid ethyl ester
-
0.1 mg/ml, 21.6% inhibition of relaxation
2-chloro-3-[2-(dimethylamino)isopropoxy]benzo-[b]naphtho[2,3-d]furan-6,11-dione
-
0.05 mM, 88% inhibition. Comparison of cytotoxicity against various human cancer cells
2-dodecyl-6-(2-(4-methylpiperazin-1-yl)ethylamino)-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-dodecyl-6-(octylamino)-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-ethyl-2H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
-
-
2-hydroxy-3-ethoxycarbonyl-N-(3,4-dimethylphenyl)-benz[f]indole-4,9-dione
-
0.1 mg/ml, 17.0% inhibition of relaxation
2-iso-butyl-2H-[1,2,3] triazolo[4,5-g]phthalazine-4,9-dione
-
-
2-iso-propyl-2H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
-
-
2-methyl-2H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
-
-
2-n-butyl-2H-[1,2,3] triazolo[4,5-g]phthalazine-4,9-dione
-
-
2-n-propyl-2H-[1,2,3] triazolo[4,5-g]phthalazine-4,9-dione
-
-
2-oxo-2-(3-sulfamoylanilino)ethyl 1H-indazole-3-carboxylate
-
-
2-phenyl-4-(pyridin-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2-phenyl-4-(pyridin-2-yl)-5H-chromeno[4,3-b]pyridine
2-phenyl-4-(pyridin-3-yl)-5H-chromeno[4,3-b]pyridine
2-phenyl-4-(thiophen-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2-phenyl-4-(thiophen-2-yl)-5H-chromeno[4,3-b]pyridine
2-phenyl-4-(thiophen-3-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2-phenyl-4-(thiophen-3-yl)-5H-chromeno[4,3-b]pyridine
2-[(1,1-dioxo-1l6-thiolan-3-yl)(ethyl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
-
-
2-[(1,1-dioxo-1l6-thiolan-3-yl)(methyl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
-
-
2-[(1,1-dioxo-1l6-thiolan-3-yl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
-
-
2-[(1,1-dioxo-2,3-dihydro-1H-1l6-thiophen-3-yl)(2-methylpropyl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
-
-
2-[(10Z,13E,15E)-heptadeca-10,13,15-trien-1-yl]benzene-1,4-diol
-
irreversible inhibition of Topo IIalpha activity through the accumulation of Topo II-DNA cleavable complexes
2-[(3-carbamoylthiophen-2-yl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
-
-
2-[(butan-2-yl)(1,1-dioxo-2,3-dihydro-1H-1l6-thiophen-3-yl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
-
-
2-[4-(methanesulfonyl)piperazin-1-yl]-2-oxoethyl 1H-indazole-3-carboxylate
-
-
2-[4-phenyl-6-(thiophen-2-yl)pyridin-2-yl]phenol
-
-
2-[4-phenyl-6-(thiophen-3-yl)pyridin-2-yl]phenol
-
-
2-[6-(furan-2-yl)-4-phenylpyridin-2-yl]phenol
-
-
2-[benzyl(1,1-dioxo-2,3-dihydro-1H-1l6-thiophen-3-yl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
-
-
25,26,27-tris-nor-3beta-methoxylanost-9(11)-en-24-oic acid
-
-
3,3'-(4-phenylpyridine-2,6-diyl)diphenol
-
86.5% inhibition at 0.1 mM
3,4,5-trimethoxybenzaldehyde
-
-
3,4,5-trimethoxyphenylpropynoic-3-(1-benzenesulfonyl-1H-indol-3-yl)-allyl ester
-
-
3,4-dimethoxybenzaldehyde
-
-
3,4-dimethoxyphenylpropynoic-3-(1-benzenesulfonyl-1Hindol-3-yl)-allyl ester
-
-
3,4-methylenedioxyphenylpropynoic-3-(1-benzenesulfonyl-1H-indol-3-yl)-allyl ester
-
-
3,5-dimethoxybenzaldehyde
-
-
3,5-dimethoxyphenylpropynoic-3-(1-benzenesulfonyl-1H-indol-3-yl)-allyl ester
-
-
3-(1,3-benzodioxol-5-yl)prop-2-ynoic acid
-
-
3-(2,6-diphenylpyridin-4-yl)phenol
-
68.2% inhibition at 0.1 mM
3-(2-dimethylaminoethoxy)-6-(2-dimethylaminoethylamino)indeno[2,1-c]quinolin-7-one
-
-
3-(2-phenyl-1-benzofuran-3-yl)prop-2-yn-1-yl 3-amino-2,3,6-trideoxy-b-D-arabino-hexopyranoside
-
6.5% inhibition at 0.1 mM
3-(2-phenyl-1-benzothiophen-3-yl)prop-2-yn-1-yl 3-amino-2,3,6-trideoxy-b-D-arabino-hexopyranoside
-
5.8% inhibition at 0.1 mM
3-(2-phenyl-1H-indol-3-yl)prop-2-yn-1-yl 3-amino-2,3,6-trideoxy-b-D-arabino-hexopyranoside
-
7.1% inhibition at 0.1 mM
3-(2-pyrrolidin-1-ylethoxy)-6-(2-pyrrolidin-1-ylethylamino)indeno[2,1-c]quinolin-7-one
-
-
3-(3,4,5-trimethoxyphenyl)prop-2-ynoic acid
-
-
3-(3,4-dimethoxyphenyl)prop-2-ynoic acid
-
-
3-(3-dimethylaminopropoxy)-6-(3-dimethylaminopropylamino)indeno[2,1-c]quinolin-7-one
-
-
3-(4,6-diphenylpyridin-2-yl)phenol
-
48.4% inhibition at 0.1 mM
3-(4-chlorophenyl)benzo-1,2-quinone
-
inhibits DNA religation by isoform IIalpha by blocking the N-terminal gate of the enzyme by cross-linking cross-linking its two protomer subunits
3-(4-methoxyphenyl)prop-2-ynoic acid
-
-
3-(4-phenyl-2,2'-bipyridin-6-yl)phenol
-
-
3-(4-phenyl-2,3'-bipyridin-6-yl)phenol
-
-
3-(4-phenyl-2,4'-bipyridin-6-yl)phenol
-
3.6% inhibition at 0.1 mM
3-(6-phenyl-2,2'-bipyridin-4-yl)phenol
-
48.1% inhibition at 0.1 mM
3-(6-phenyl-2,3'-bipyridin-4-yl)phenol
-
37.1% inhibition at 0.1 mM
3-(6-phenyl-2,4'-bipyridin-4-yl)phenol
-
42.8% inhibition at 0.1 mM
3-([[6-(benzylsulfanyl)-4-oxo-4,5-dihydro-1,3,5-triazin-2-yl]sulfanyl]methyl)benzonitrile
-
-
3-hydroxy-6-(2-dimethylaminoethylamino)indeno[2,1-c]quinolin-7-one
-
-
3-hydroxy-6-(2-pyrrolidin-1-ylethylamino)indeno[2,1-c]quinolin-7-one
-
-
3-hydroxy-6-(3-dimethylaminopropylamino)indeno[2,1-c]quinolin-7-one
-
-
3-Methoxy-5-(6-oxo-5,8,8a,9-tetrahydro-1,3,7-trioxa-5a-aza-dicyclopenta[b,g]naphthalen-5-yl)-[1,2]benzoquinone
-
inhibits decatenation, inhibition due to stabilization of the topoisomerase II-DNA covalent binary complex, the nonintercalative specific inhibitor stabilizes the cleavable complex
3-oxolanost-9(11)-ene-24S,25-diol
-
IC50: 0.186 mM
3-thiiranylmethyloxy-1-hydroxy-5-azaxanthone
-
19.5% and 9% inhibition at 0.1 mM and 0.02 mM, respectively
3-[(1E)-3-chloroprop-1-en-1-yl]-1-(phenylsulfonyl)-1H-indole
-
-
3-[1-[(4-methylphenyl)sulfonyl]-2-phenyl-1H-indol-3-yl]prop-2-yn-1-yl 3-amino-2,3,6-trideoxy-b-D-arabino-hexopyranoside
-
101% inhibition at 0.1 mM
3-[2-(diethylamino)ethoxy]benzo[b]naphtho[2,3-d]-furan-6,11-dione
-
0.05 mM, 91% inhibition. Comparison of cytotoxicity against various human cancer cells
3-[2-(dimethylamino)isopropoxy]benzo[b]naphtho[2,3-d]furan-6,11-dione
-
0.05 mM, 84% inhibition. Comparison of cytotoxicity against various human cancer cells
3-[2-(dimethylamino)propoxy]benzo[b]naphtho[2,3-d]furan-6,11-dione
-
0.05 mM, 100% inhibition. Comparison of cytotoxicity against various human cancer cells
3-[2-(furan-2-yl)-6-phenylpyridin-4-yl]phenol
-
47.5% inhibition at 0.1 mM
3-[2-phenyl-6-(thiophen-2-yl)pyridin-4-yl]phenol
-
57.5% inhibition at 0.1 mM
3-[2-phenyl-6-(thiophen-3-yl)pyridin-4-yl]phenol
-
52.6% inhibition at 0.1 mM
3-[3-[(2-chloroethyl)sulfanyl]-2-hydroxypropoxy]-1-hydroxy-9H-xanthen-9-one
-
45.33% inhibition at 0.1 mM
3-[3-[bis(2-hydroxyethyl)amino]-2-hydroxypropoxy]-1-hydroxy-9H-xanthen-9-one
-
100% inhibition at 0.1 mM
3-[4-phenyl-6-(thiophen-2-yl)pyridin-2-yl]phenol
-
53.8% inhibition at 0.1 mM
3-[4-phenyl-6-(thiophen-3-yl)pyridin-2-yl]phenol
-
51.8% inhibition at 0.1 mM
3-[6-(furan-2-yl)-4-phenylpyridin-2-yl]phenol
-
51.6% inhibition at 0.1 mM
3alpha-corosolic acid
3beta-corosolic acid
-
IC50: 0.049 mM
4'-chlorobiphenyl-2,5-diol
-
inhibits DNA religation by isoform IIalpha by blocking the N-terminal gate of the enzyme by cross-linking cross-linking its two protomer subunits
4,4'-(4-phenylpyridine-2,6-diyl)diphenol
-
76.8% inhibition at 0.1 mM
4-(2,2-dibromoethenyl)-1,2-dimethoxybenzene
-
-
4-(2,6-diphenylpyridin-4-yl)phenol
-
-
4-(3,4,5-trimethoxyphenyl)-1,5-dihydro-3H-furo[3,4-b]carbazol-3-one
-
-
4-(4,6-diphenylpyridin-2-yl)phenol
-
27.6% inhibition at 0.1 mM
4-(4-chlorophenyl)benzo-1,2-quinone
-
inhibits DNA religation by isoform IIalpha by blocking the N-terminal gate of the enzyme by cross-linking cross-linking its two protomer subunits
4-(4-phenyl-2,2'-bipyridin-6-yl)phenol
-
-
4-(4-phenyl-2,3'-bipyridin-6-yl)phenol
-
18.6% inhibition at 0.1 mM
4-(4-phenyl-2,4'-bipyridin-6-yl)phenol
-
-
4-(5-chlorofuran-2-yl)-2-(3-chlorophenyl)-6-(3-methylthiophen-2-yl) pyridine
-
36% inhibition at 0.02 mM
4-(5-chlorofuran-2-yl)-2-(3-chlorophenyl)-6-(5-chlorothiophen-2-yl) pyridine
-
41% inhibition at 0.02 mM
4-(5-chlorofuran-2-yl)-2-(4-chlorophenyl)-6-(3-methylthiophen-2-yl) pyridine
-
40% inhibition at 0.02 mM
4-(5-chlorofuran-2-yl)-2-(4-chlorophenyl)-6-(5-chlorothiophen-2-yl) pyridine
-
43% inhibition at 0.02 mM
4-(5-chlorofuran-2-yl)-2-(5-chlorothiophen-2-yl)-6-(furan-2-yl) pyridine
-
40% inhibition at 0.02 mM
4-(5-chlorofuran-2-yl)-2-(5-chlorothiophen-2-yl)-6-p-tolylpyridine
-
41% inhibition at 0.02 mM
4-(5-chlorofuran-2-yl)-2-(furan-2-yl)-6-(3-methylthiophen-2-yl) pyridine
-
31% inhibition at 0.02 mM
4-(5-chlorofuran-2-yl)-6-(3-methylthiophen-2-yl)-2,3'-bipyridine
-
25.5% inhibition at 0.02 mM
4-(6-phenyl-2,2'-bipyridin-4-yl)phenol
-
-
4-(6-phenyl-2,3'-bipyridin-4-yl)phenol
-
-
4-(6-phenyl-2,4'-bipyridin-4-yl)phenol
-
8.4% inhibition at 0.1 mM
4-(benzylsulfanyl)-6-[[(2-fluorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
4-(benzylsulfanyl)-6-[[(3-chlorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
4-(furan-2-yl)-2-(pyridin-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
4-(furan-2-yl)-2-(pyridin-2-yl)-5H-chromeno[4,3-b]pyridine
4-(furan-2-yl)-2-(thiophen-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
4-(furan-2-yl)-2-(thiophen-2-yl)-5H-chromeno [4,3-b]pyridine
-
14.1% inhibition at 0.1 mM
4-(furan-2-yl)-2-(thiophen-2-yl)-5H-chromeno[4,3-b]pyridine
-
-
4-(furan-2-yl)-2-phenyl-5,6-dihydrobenzo[h]quinoline
-
-
4-(furan-2-yl)-2-phenyl-5H-chromeno[4,3-b]pyridine
4-(furan-3-yl)-2-(pyridin-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
4-(furan-3-yl)-2-(thiophen-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
4-(furan-3-yl)-2-(thiophen-2-yl)-5H-chromeno[4,3-b]pyridine
4-(furan-3-yl)-2-phenyl-5,6-dihydrobenzo[h]quinoline
-
-
4-(furan-3-yl)-2-phenyl-5H-chromeno[4,3-b]pyridine
4-(furan-3-yl)-6-(thiophene-2-yl)-[2,4']-bipyridyl
-
significant inhibitory effects on human DNA Topo II at 20 microM and 100 microM concentration
4-(furan-3-yl)-6-(thiophene-3-yl)-[2,4']-bipyridyl
-
significant inhibitory effects on human DNA Topo II at 20 microM and 100 microM concentration
4-(pyridin-2-yl)-2-(thiophen-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
4-(pyridin-2-yl)-2-(thiophen-2-yl)-5H-chromeno[4,3-b]pyridine
4-(pyridin-2-yl)-2-(thiophen-3-yl)-5H-chromeno[4,3-b]pyridine
-
25.3% inhibition at 0.1 mM
4-(thiophene-3-yl)-6-(thiophene-2-yl)-[2,2']-bipyridyl
-
weak inhibitory effects on human DNA Topo II compared to etoposide
4-(thiophene-3-yl)-6-(thiophene-2-yl)-[2,4']-bipyridyl
-
weak inhibitory effects on human DNA Topo II when compared to etoposide
4-([[6-(benzylsulfanyl)-4-oxo-4,5-dihydro-1,3,5-triazin-2-yl]sulfanyl]methyl)-3-fluorobenzonitrile
-
-
4-([[6-(benzylsulfanyl)-4-oxo-4,5-dihydro-1,3,5-triazin-2-yl]sulfanyl]methyl)benzonitrile
-
-
4-methoxybenzaldehyde
-
-
4-methoxyphenylpropynoic-3-(1-benzenesulfonyl-1Hindol-3-yl)-allyl ester
-
-
4-N-(2-pyrazinecarboxylic) amino-4'-demethylepipodophyllotoxin
-
-
4-N-(3,4,5-trihydroxybenzoic) amino-4'-demethylepipodophyllotoxin
-
-
4-N-(5-methylpyrazine-2-carboxylic)amino-4'-demethylepipodophyllotoxin
-
-
4-N-(theophylline-7-acetic) amino-4'-demethylepipodophyllotoxin
-
-
4-O-(2-pyrazinecarboxylic)-4'-demethylepipodophyllotoxin
-
-
4-O-(2-quinoline carboxylic)-4'-demethylepipodophyllotoxin
-
-
4-O-(5-methylpyrazine-2-carboxylic)-4'-demethylepipodophyllotoxin
-
-
4-O-(fluoroquinolonic)-4'-demethylepipodophyllotoxin
-
-
4-O-(theophylline-7-acetic)-4'-demethylepipodophyllotoxin
-
-
4-phenyl-2-(pyridin-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
4-phenyl-2-(pyridin-2-yl)-5H-chromeno[4,3-b]pyridine
4-phenyl-2-(thiophen-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
4-phenyl-2-(thiophen-2-yl)-5H-chromeno[4,3-b]pyridine
4-[2-(furan-2-yl)-6-phenylpyridin-4-yl]phenol
-
30.2% inhibition at 0.1 mM
4-[2-phenyl-6-(thiophen-2-yl)pyridin-4-yl]phenol
-
-
4-[2-phenyl-6-(thiophen-3-yl)pyridin-4-yl]phenol
-
-
4-[3-[ethyl(methyl)amino]propyl]furo[3,2-c]phenanthridine-5,10,11(4H)-trione
-
-
4-[4-phenyl-6-(thiophen-2-yl)pyridin-2-yl]phenol
-
35.4% inhibition at 0.1 mM
4-[4-phenyl-6-(thiophen-3-yl)pyridin-2-yl]phenol
-
38.3% inhibition at 0.1 mM
4-[6-(furan-2-yl)-4-phenylpyridin-2-yl]phenol
-
35.2% inhibition at 0.1 mM
5,8-dihydroxy-4-methoxy-3,6-bis(3-methylbut-2-en-1-yl)-4a,9a-dihydro-1H-xanthene-1,2,9-trione
-
-
5-(2,2-dibromoethenyl)-1,2,3-trimethoxybenzene
-
-
5-(2,2-dibromoethenyl)-1,3-benzodioxole
-
-
5-methoxy-1,3-bis[(2-methyloxiran-2-yl)methoxy]-7-(oxiran-2-ylmethyl)-9H-xanthen-9-one
-
-
5-methoxy-1,3-bis[(2-methyloxiran-2-yl)methoxy]-7-(propan-2-yl)-9H-xanthen-9-one
-
-
6'-(thiophene-2-yl)-[3,4',2',4'']-terpyridine
-
significant inhibitory effects on human DNA Topo II at 20 microM and 100 microM concentration
6'-(thiophene-2-yl)-[4,2',4',4'']-terpyridine
-
significant inhibitory effects on human DNA Topo II at 20 microM and 100 microM concentration
6,11-dihydroxy-3,3-dimethyl-5-(3-methylbut-2-en-1-yl)-3H,7H-pyrano[2,3-c]xanthen-7-one
-
-
6,8-bis(oxiran-2-ylmethoxy)benzo[b][1,8]naphthyridin-5(10H)-one
-
9% and 13% inhibition at 0.02 mM and 0.1 mM, respectively
6,8-bis(thiiran-2-ylmethoxy)benzo[b][1,8]naphthyridin-5(10H)-one
-
8.5% and 7% inhibition at 0.02 mM and 0.1 mM, respectively
6-(2-(2-(dimethylamino)ethylamino)ethylamino)-2-dodecyl-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
6-(2-(2-(dimethylamino)ethylamino)ethylamino)-2-octyl-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
6-(2-(4-methylpiperazin-1-yl)ethylamino)-2-octyl-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
6-(2-(dimethylamino)ethylamino)-2-dodecyl-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
6-(2-dimethylaminoethyl)-6H-indeno[1,2-c]isoquinolin-5,11-dione
-
-
6-(3-dimethylaminopropyl)-6H-indeno[1,2-c]isoquinolin-5,11-dione
-
-
6-(5-chlorothiophen-2-yl)-4-(furan-3-yl)-2,2'-bipyridine
-
39% inhibition at 0.02 mM
6-(5-chlorothiophen-2-yl)-4-(furan-3-yl)-2,3'-bipyridine
-
41% inhibition at 0.02 mM
6-(benzylsulfanyl)-4-(butylsulfanyl)-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-(phenylsulfanyl)-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-(propylsulfanyl)-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[(cyclobutylmethyl)sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[(cyclopropylmethyl)sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[[(2-chlorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[[(2-fluorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[[(2-methoxyphenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[[(2-nitrophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[[(3-chlorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[[(3-methoxyphenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[[(3-nitrophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[[(4-chlorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[[(4-fluorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[[(4-nitrophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(dodecylamino)-2-(3-(4-methylpiperazin-1-yl)propyl)-1H-benzo-[de]isoquinoline-1,3(2H)-dione
-
-
6-(furan-2-yl)-4-(furan-3-yl)-[2,2']-bipyridyl
-
significant inhibitory effects on human DNA Topo II at 20 microM and 100 microM concentration
6-(furan-2-yl)-4-(furan-3-yl)-[2,4']-bipyridyl
-
significant inhibitory effects on human DNA Topo II at 20 microM and 100 microM concentration
6-(furan-2-yl)-4-(thiophene-2-yl)-[2,4']-bipyridyl
-
weak inhibitory effects on human DNA Topo II compared to etoposide
6-(furan-2-yl)-4-(thiophene-3-yl)-[2,4']-bipyridyl
-
significant inhibitory effects on human DNA Topo II at 20 microM and 100 microM concentration
6-(furan-2-yl)-[3,4',2',4'']-terpyridine
-
weak inhibitory effects on human DNA Topo II compared to etoposide
6-aminohexanoyl-L-lysyl-6-aminohexanoyl amide
-
-
6-deoxyclitoriacetal
-
-
6-hydroxy-8-(thiiran-2-ylmethoxy)-5H-chromeno[2,3-b]pyridin-5-one
-
inhibition in vivo in cancer cells, IC50 values, overview
6-hydroxy-8-(thiiran-2-ylmethoxy)benzo[b][1,8]naphthyridin-5(10H)-one
-
8% and 9% inhibition at 0.02 mM and 0.1 mM, respectively
6-methoxy-7,8-methylenedioxycoumarin
-
57% inhibition at 0.1 mM
6-[(2-phenylethyl)sulfanyl]-9H-purin-2-amine
-
-
6-[2-(dimethylamino)ethyl]-8-hydroxy-5H-indeno[1,2-c]isoquinoline-5,11(6H)-dione
-
moderate inhibition
6-[2-(dimethylamino)ethyl]-8-[3-(dimethylamino)propoxy]-5H-indeno[1,2-c]isoquinoline-5,11(6H)-dione
-
strong inhibition
6-[3-(dimethylamino)propyl]-8-hydroxy-5H-indeno[1,2-c]isoquinoline-5,11(6H)-dione
-
moderate inhibition
6-[4-(dimethylamino)butyl]-8-[2-(dimethylamino)ethoxy]-5H-indeno[1,2-c]isoquinoline-5,11(6H)-dione
-
weak inhibition
6-[4-(dimethylamino)butyl]-8-[3-(dimethylamino)propoxy]-5H-indeno[1,2-c]isoquinoline-5,11(6H)-dione
-
weak inhibition
7-chloro-1,3-dihydroxyacridone
-
at both 0.2 mM and 0.1 mM, preincubation with the enzyme prior to the addition of DNA leads to the complete loss of DNA binding
7-methoxyeleutherin
-
-
8-(2-(diethylamino)ethoxy)benzofuro[3,2-g]quinoline-5,11-dione
-
0.05 mM, 100% inhibition. Comparison of cytotoxicity against various human cancer cells
8-(2-dimethylaminoethoxy)-6-(2-dimethylaminoethyl)-6H-indeno[1,2-c]isoquinolin-5,11-dione
-
-
8-(2-dimethylaminoethoxy)-6-(3-dimethylaminopropyl)-6Hindeno[1,2-c]isoquinolin-5,11-dione
-
-
8-[2-(dimethylamino)ethoxy]-6-[2-(dimethylamino)ethyl]-5H-indeno[1,2-c]isoquinoline-5,11(6H)-dione
-
very strong inhibition
8-[3-(dimethylamino)propoxy]-6-[3-(dimethylamino)propyl]-5H-indeno[1,2-c]isoquinoline-5,11(6H)-dione
-
strong inhibition
9-(2-dimethylaminoethoxy)-6-(2-dimethylaminoethyl)-6H-indeno[1,2-c]isoquinolin-5,11-dione
-
-
9-(2-dimethylaminoethoxy)-6-(3-dimethylaminopropyl)-6Hindeno[1,2-c]isoquinolin-5,11-dione
-
-
9-(2-pyrrolidin-1-ylethoxy)-6-(2-pyrrolidin-1-ylethyl)-6H-indeno[1,2-c]isoquinolin-5,11-dione
-
-
9-(4-hydroxy-3,5-dimethoxyphenyl)-8-oxo-5,5a,6,8,8a,9-hexahydro-2H-furo[3',4':6,7]naphtho[2,3-d][1,3]dioxol-5-yl 4,6-O-ethylidenehexopyranoside
-
-
9-benzenesulfonyl-4-(3,4,5-trimethoxyphenyl)-1,5-dihydro-H-furo[3,4-b]carbazol-3-one
-
-
9-benzenesulfonyl-4-(3,4-dimethoxyphenyl)-1,5-dihydro-3H-furo[3,4-b]carbazol-3-one
-
-
9-benzenesulfonyl-4-(3,4-methylenedioxyphenyl)-1,5-dihydro-3H-furo[3,4-b]carbazol-3-one
-
-
9-benzenesulfonyl-4-(3,5-dimethoxyphenyl)-1,5-dihydro-3H-furo[3,4-b]carbazol-3-one
-
-
9-benzenesulfonyl-4-(4-methoxyphenyl)-1,5-dihydro-3Hfuro[3,4-b]carbazol-3-one
-
-
9-hydroxy-6-(2-dimethylaminoethyl)-6H-indeno[1,2-c]isoquinolin-5,11-dione
-
-
9-hydroxy-6-(3-dimethylaminopropyl)-6H-indeno[1,2-c]isoquinolin-5,11-dione
-
-
aclacinomycin A
-
-
Aclarubicin
actinomycins
-
-
-
adenylyl-imidodiphosphate
-
i.e. AMP-PNP. In mixtures of AMP-PNP and ATP, the double-strand passage reaction of the enzyme gets blocked and progressively fewer entanglements are relaxed. A total replacement of ATP by AMP-PNP results in a temporal increase in elasticity at higher frequencies, but no transition to an elastic gel with fixed cross-links
ADP
-
traps the wild-type enzyme in the closed clamp formation, which shows no ATPase activity
adriamycin
alpha-lapachone
-
inhibits initial non-covalent binding of topoisomerase II to DNA and, in addition, induces religation of DNA breaks, irreversible
alpha-viniferin-13-O-beta-glucopyranoside
-
comparison with inhibition of HindIII enzyme
amonafide
-
-
amsacrine
anthocyanidins
-
modulate the enzyme activity and affect cellular DNA integrity, high enzyme inhibition by anthocyanidins with vicinal hydroxyl groups like delphinidin or cyanidin, competitive to ethidium bromide in DNA intercalation
apigenin
-
inhibition of enzyme-mediated religation of DNA
Aroclor 1254
-
-
aurintricarboxylic acid
-
-
azalactone ferrocene
-
inhibition of enzyme activity and anti-HIV-1 activity in Sup-T1 cells at nanomolar concentrations. Complete inhibition of proviral DNA synthesis as well as the formation of pre-integration complexes
-
Barminomycin-like anthracyclines
-
-
BAY 50-7950
-
IC50: 15 mg/l, no substantial inhibitory activity
BAY 50-7952
-
IC50: 60 mg/l, no substantial inhibitory activity
Benzene
-
enzyme inhibition by benzene and its metabolites represents a potential mechanism by which benzene can induce its chromosome-altering and leukemogenic effects
Benzisoquinolinediones
-
-
-
benzoquinone
benzoquinone mustard compounds
-
induce the formation of DNA-protein complexes, quantitative structure-activity analysis, inhibition mechanism, overview
-
beta-lapachone
-
inhibits by inducing religation and dissociation of the enzyme from DNA in presence of ATP, irreversible
betulinic acid
-
IC50: 0.08 mM
bis(2,2-dichloro-6-[[2-(hydroxy-kO)benzylidene]amino-kN]-4H-1,3,2-benzodioxastannin-4-onato)copper(2+)
-
-
bis(2-hydroxy-5-[[2-(hydroxy-kO)benzylidene]amino-kN]benzoato)copper(2+)
-
-
bis(acridin-4-ylmethyl)cyanamide
-
comparison with inhibition of calpain, chymotrypsin, cathepsin B, trypsin
Bisantrene
-
efficiency in patients with breast cancer and acute leukemia
bisdioxopiperazine
C11-substituted derivatives of azaelliptitoxin
-
-
camptothecin
Ciprofloxacin
-
40fold higher selectivity for Leishmania panamensis enzyme over human macrophage enzyme
colchiceinamide
-
and analogues, 0.1 mM
conjugated docosahexanoic acid
-
IC50 is 0.01 mM for inhibition of decatenation of kinetoplast DNA
-
conjugated eicosapentaenoic acid
-
irreversible inhibition, IC50 is 0.0025 mM for inhibition of decatenation of kinetoplast DNA, effects on thermal transition of dsDNA, overview
coralyne
-
potent inhibitor of both human and leishmania panamensis enzyme
corosolic acid
-
IC50: 0.043 mM
CP-115953
-
-
curcumin sulfate
i.e. diferuloylmethane sulfate
cyanidin
-
anthocyanidin, complete inhibition of enzyme, isozyme IIalpha and IIbeta, decatenation activity at 0.01 mM, no stabilization of the DNA-enzyme intermediate in contrast to topoisomerase poisons
cyclocurcumin
-
dactinomycin
-
i.e. actinomycin D
daunomycin
-
i.e. daunorubicin
daunorubicin
delphinidin
-
anthocyanidin, complete inhibition of enzyme, isozyme IIalpha and IIbeta, decatenation activity at 0.01 mM, no stabilization of the DNA-enzyme intermediate in contrast to topoisomerase poisons
deoxynanaomycin A
-
-
dexrazoxane
DMP 840
-
synonym bisnafide
doxorubicin
doxorubin
-
i.e. adriamycin
EDTA
-
at 77 mM
eleutherin
ellagic acid
-
15.7fold higher selectivity human macrophage for enzyme over Leishmania panamensis enzyme
ellipticine
-
ellipticines
-
-
enoxacin
-
592fold higher selelctivity for Leishmania panamensis enzyme over human macrophage enzyme
EO9
-
inhibition mechanism
epicatechin gallate
-
-
epirubicin
-
a so called topoisomerase poison, which stabilizes the enzyme-linked double-strand break, that is otherwise transient and rapidly religated
etoposide
etoposide quinone
-
etoposide quinone inhibits ATP hydrolysis by topoisomerase IIalpha
FEITPEKNPQ
-
inhibits human topoisomerase II activity through binding to the active site of the CTD domain
fomitellic acid A
-
0.1 mM, 95% inhibition
fomitellic acid B
-
0.1 mM, 95% inhibition
geldanamycin
-
geldanamycin suppresses the ATPase activity of the enzyme
genistein
hemsleyanol
-
comparison with inhibition of HindIII enzyme
hexamethyleneimine
-
the presence of the formamidino group in the molecule reduced its ability to stimulate DNA cleavage byDNA topoisomerase II, which is not a primary cellular target for the compound
Hoechst 33258
-
bis-imidazole derivative
Hoechst 33342
-
bis-imidazole derivative
hydroquinone
-
hydroquinone inhibits topoII at the DNA binding stage as well as in the closed clamp stage in the catalytic cycle, thereby interfering with either the binding to, or the release of, DNA from the enzyme, inhibition mechanism, overview
hypericin
-
inhibits DNA relaxation activity, potent antagonist of cleavage complex stabilization by chemotherapeutics etoposide and amsacrine
ICRF 187
-
inhibits ATP hydrolysis
ICRF 193
-
inhibits ATP hydrolysis
ICRF-187
ICRF-193
ICRF187
-
catalytic inhibitor
ICRF193
-
catalytic inhibitor
idarubicin
-
-
IETWNPNNKP
-
inhibits human topoisomerase II activity through binding to the active site of the CTD domain
kaempferol
-
-
licochalcone A
-
-
licochalcone E
-
-
lithocholic acid
-
IC50: 0.015 mM, the lithocholic interaction interface has a pocket comprised of three amino acids, Lys720, Leu760 and Thr791
LU 79553
-
synonym elinafide
luteolin
-
inhibition of enzyme-mediated religation of DNA
lyoniside
-
12% inhibition at 0.1 mM
malvidin
-
anthocyanidin, inhibition of isozyme IIbeta decatenation activity
mAMSA
-
inhibits the religation step and traps Top2 as a covalent complex with the enzyme covalently bound to DNA with broken DNA strands
maslinic acid
-
IC50: 0.092 mM
meglumine antimoniate
-
14% inhibition at 0.0033 mM
menadione
-
inhibition mechanism
Merbarone
Merocil
-
-
Merodantoin
-
-
meso-2,3-Bis(3,5-dioxopiperazine-1-yl)butane
-
-
methyl 3-(1,3-benzodioxol-5-yl)prop-2-ynoate
-
-
methyl 3-(3,4,5-trimethoxyphenyl)prop-2-ynoate
-
-
methyl 3-(3,4-dimethoxyphenyl)prop-2-ynoate
-
-
methyl 3-(4-methoxyphenyl)prop-2-ynoate
-
-
methyl N-(4'-(9-acridinylamino)-2-methoxy-phenyl)carbamate hydrochloride
-
methyl N-(4'-(9-acridinylamino)-phenyl) carbamate hydrochloride
-
mitonafide
-
-
mitoxanthrone
-
-
Mitoxantrone
MJ-238
-
-
MJ-III-65
-
-
morpholine
-
amine derivative of doxorubicin, the presence of the formamidino group in the molecule reduces its ability to stimulate DNA cleavage by DNA topoisomerase II, which is not a primary cellular target for the compound
myricetin
N,N'-bis[2-(5-nitro-1,3-dioxo-2,3-dihydro-1H-benz[de]-isoquinolin-2-yl)]butylaminoethyl-2-propanediamine
-
-
N,N'-bis[2-(5-nitro-1,3-dioxo-2,3-dihydro-1H-benz[de]-isoquinolin-2-yl)]propane-2-ethanediamine
-
-
N,N'-diphenyl-N-[(2E)-3-phenylprop-2-en-1-yl]-urea
-
-
N,N,N',N'-tetrakis(acridin-4-ylmethyl)butane-1,4-diamine
-
compound shows in addition in vitro proteasome inhibition properties. Comparison with inhibition of calpain, chymotrypsin, cathepsin B, trypsin
N,N,N',N'-tetrakis(acridin-4-ylmethyl)ethane-1,2-diamine
-
comparison with inhibition of calpain, chymotrypsin, cathepsin B, trypsin
N,N,N',N'-tetrakis[(7-bromo-9-chloroacridin-4-yl)methyl]butane-1,4-diamine
-
comparison with inhibition of calpain, chymotrypsin, cathepsin B, trypsin
N,N,N',N'-tetrakis[(9-aminoacridin-4-yl)methyl]ethane-1,2-diamine
-
compound shows in addition in vitro proteasome inhibition properties. Comparison with inhibition of calpain, chymotrypsin, cathepsin B, trypsin
N,N-diethyl-9-([2-(1H-indol-3-yl)ethyl]amino)acridine-3-carboxamide
-
-
N,N-dimethyl(6-methyl-10,11-dioxo-10,11-dihydrophenanthro[1,2-b]furan-1-yl)methanaminium (2E)-3-carboxyprop-2-enoate
-
-
-
N-(4'-(9-acridinylamino)-3-methoxy-phenyl) methane sulfonamide
-
N-(4-chlorophenyl)-N-[(2E)-3-phenylprop-2-en-1-yl]urea
-
-
N-(4-fluorphenyl)-N-[(2E)-3-phenylprop-2-en-1-yl]urea
-
-
N-(4-methoxyphenyl)-N-[(2E)-3-phenylprop-2-en-1-yl]urea
-
-
N-(4-methylphenyl)-N-[(2E)-3-phenylprop-2-en-1-yl]urea
-
-
N-(acridin-1-ylmethyl)-N,N',N'-tris(acridin-2-ylmethyl)octane-1,8-diamine
-
comparison with inhibition of calpain, chymotrypsin, cathepsin B, trypsin
N-([3-[(methanesulfonyl)amino]phenyl]methyl)-1H-indazole-3-carboxamide
-
-
N-([4-[(methylsulfamoyl)methyl]phenyl]methyl)-1H-indazole-3-carboxamide
-
-
N-benzyladriamycin
-
inhibits by preventing the initial non-covalent binding of topoisomerase II to DNA
N-Trifluoroacetyldoxorubicin-14 valerate
-
-
N-[1-(1H-indazole-3-carbonyl)piperidin-4-yl]methanesulfonamide
-
-
N-[1-(1H-indazole-3-carbonyl)piperidin-4-yl]methanesulfonohydrazide
-
-
N-[1-(1H-indazole-3-carbonyl)piperidin-4-yl]propane-1-sulfonamide
-
-
N-[3-[(methanesulfonyl)amino]propyl]-1H-indazole-3-carboxamide
-
-
N-[4-[(methanesulfonyl)amino]-3-methylphenyl]-1H-indazole-3-carboxamide
-
-
N-[4-[(methanesulfonyl)amino]phenyl]-1H-indazole-3-carboxamide
-
-
N2-(1,3-benzothiazol-6-yl)-N6-cyclohexyl-9H-purine-2,6-diamine
-
-
N2-(1,3-benzothiazol-6-yl)-N6-tert-butyl-9H-purine-2,6-diamine
-
-
N2-(4-fluorophenyl)-6-[[(1H-1,2,4-triazol-5-yl)sulfanyl]methyl]-1,3,5-triazine-2,4-diamine
-
-
N6-tert-butyl-8-ethyl-N2-[2-[2-(morpholin-4-yl)ethoxy]quinolin-6-yl]-5,9-dihydro-4H-purine-2,6-diamine
-
-
nanaomycin A
-
-
neoamphimedine
-
a marine alkaloid from Xestospongia sp., potently inhibits TopoIIalpha-dependent DNA decatenation in the presence of Metnase , circumvents DNA repair protein metnase-enhanced DNA topoisomerase IIalpha activity through ATP-competitive inhibition by binding ata the N-terminal ATPase sites of TopoIIalpha, key interactions observed with neoamphimedine are a network of hydrogen bonds with Ser148, Ser149, and Asn150, and with Asn91 through an ordered water molecule , molecular modeling, oveview
novobiocin
-
inhibits the ATPase activity
NSC727357
-
-
nudiposide
-
9% inhibition at 0.1 mM
o-Quinone analogues of podophyllotoxin possessing various C-4 beta-aniline moieties
-
-
-
oleanolic acid
-
IC50: 0.081 mM
pelargonidin
-
anthocyanidin, inhibition of isozyme IIbeta decatenation activity
Pentamidine
-
17.6fold higher selectivity for Leishmania panamensis enzyme over human macrophage enzyme
Pirarubicin
-
-
podophyllotoxin
-
-
potassium antimonyl tartrate
-
10% inhibition at 0.0033 mM
procyanidin B2
-
potentiating interactions between procyanidin B2 and epicatechin gallate, myricetin and resveratrol
prodigiosin
-
red pigment of Serratia marcescens with apoptotic activity, anti-tumor drug, induces Cu2+-mediated pH-dependent DNA damage, inhibits the enzyme in vitro and in vivo by binding and intercalation with the DNA
quercetin
radicicol
-
radicicol suppresses the ATPase activity of the enzyme
razoxane
-
the ATPase inhibitor does not affect the DNA relaxation and catenation activities of the enzyme
resveratrol
Ro-61-6653
-
IC50: 60 mg/l, no substantial inhibitory activity
ruthenium benzene
-
inhibition of enzyme activity and anti-HIV-1 activity in Sup-T1 cells at nanomolar concentrations. Complete inhibition of proviral DNA synthesis as well as the formation of pre-integration complexes
S-[6-(benzylsulfanyl)-4-oxo-4,5-dihydro-1,3,5-triazin-2-yl] hydrogen carbonothioate
-
-
S35047
-
a phenyl derivative of 8-[2-(dialkylamino)ethoxy]-2,3-dimethoxy-5H-10H-indenol[1,2-b]indol-10-one-O-propynyl-oxime core structure, inhibition of topoisomerase II, intercalation with DNA causes cytoxic activity
S35794
-
a derivative of 8-[2-(dialkylamino)ethoxy]-2,3-dimethoxy-5H-10H-indenol[1,2-b]indol-10-one-O-propynyl-oxime core structure, inhibition of topoisomerase II, intercalation with DNA causes cytoxic activity
S36699
-
a derivative of 8-[2-(dialkylamino)ethoxy]-2,3-dimethoxy-5H-10H-indenol[1,2-b]indol-10-one-O-propynyl-oxime core structure, inhibition of topoisomerase II, intercalation with DNA causes cytoxic activity
S36888
-
a derivative of 8-[2-(dialkylamino)ethoxy]-2,3-dimethoxy-5H-10H-indenol[1,2-b]indol-10-one-O-propynyl-oxime core structure, inhibition of topoisomerase II, intercalation with DNA causes cytoxic activity
S36889
-
a derivative of 8-[2-(dialkylamino)ethoxy]-2,3-dimethoxy-5H-10H-indenol[1,2-b]indol-10-one-O-propynyl-oxime core structure, inhibition of topoisomerase II, intercalation with DNA causes cytoxic activity
salicylic acid
-
salicylic acid suppresses the ATPase and decatenation but not relaxation activity of the enzyme
scopoletin
-
16% inhibition at 0.1 mM
SDS
-
0.5%
Selenite
-
selenite induces topoisomerase II-DNA complexes in K562 cells
Sitafloxacin
-
-
sodium antimonyl(III) gluconate
-
IC50 is 0.0028 mM
sodium orthovanadate
-
inhibits the ATPase activity of the wild-type enzyme, 50% inhibition at 0.005 mM, traps the enzyme in a salt-stable closed conformation, i.e. the closed clamp, no inhibition of mutant Y50F
sodium stibogluconate
-
IC50 is 0.0027 mM
Symadex
-
i.e. C-1311, reduced inhibition of the enzyme in vincristine-resistant cells
tanshinone-1
-
less than 10% inhibition at 0.005 mM
TAS-103
-
-
Teniposide
tert-butoxycarbonyl-(L-lysyl-benzyloxycarbonyl)-6-aminohexanoyl amide
-
-
tert-butoxycarbonyl-6-aminohexanoyl-(L-lysyl-benzyloxycarbonyl)-6-aminohexanoyl amide
-
-
tert-butoxycarbonyl-6-aminohexanoyl-(L-lysyl-benzyloxycarbonyl)-methoxy-6-aminohexanoate
-
-
tert-butoxycarbonyl-6-aminohexanoyl-L-lysyl-methoxy-6-aminohexanoate
-
-
tert-butoxycarbonyl-L-lysyl-6-aminohexanoyl amide
-
-
thiomorpholide amido methyl ferrocene
-
inhibition of enzyme activity and anti-HIV-1 activity in Sup-T1 cells at nanomolar concentrations. Complete inhibition of proviral DNA synthesis as well as the formation of pre-integration complexes
-
thysanone
-
-
trovafloxacin
-
-
ursolic acid
vanadate
-
inhibition of wild-type enzyme, no inhibition of mutant R162K, R162Q and Y165S, inhibition mechanism
ventiloquinone L
-
-
VFDGEL
-
inhibits human topoisomerase II activity through binding to the active site of the CTD domain
zinc bis(2-[(E)-[(2,2-dichloro-4-oxo-4H-1,3,2-benzodioxastannin-6-yl)imino]methyl]phenolate)
-
-
zinc bis(2-[(E)-[(3-carboxy-4-hydroxyphenyl)imino]methyl]phenolate)
-
-
[4-amino-6-(4-fluoroanilino)-1,3,5-triazin-2-yl]methyl morpholine-4-carbodithioate
-
-
[4-amino-6-(4-methoxyanilino)-1,3,5-triazin-2-yl]methyl morpholine-4-carbodithioate
-
-
{1,1',1'',1'''-[(1,4-dihydroporphyrin-5,10,15,20-tetrayl-k4N21,N22,N23,N24)tetrakis(benzene-4,1-diylmethanediyl)]tetrakis[1-methylpiperidiniumato(2-)]}nickel(4+) tetraiodide
-
strong inhibition
{2,2',2'',2''',2'''',2''''',2'''''',2'''''''-[(5,28-dihydro-29H,31H-tetrabenzoporphine-2,3,9,10,16,17,23,24-octayl-k4N29,N30,N31,N32)octasulfanediyl]octakis(N,N-diethyl-N-methylethanaminiumato)(2-)}zinc(8+) octaiodide
-
strong inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,4-benzoquinone
-
a topoisomerase II poison in vivo and in vitro, enhances cleavage activity, inhibits ligation activity, at 0.025 mM, 1,4-hydroquinone has a higher inhibitory effect on ligation activity but a lower effect on cleavage activity compared to 1,4-benzoquinone
1,4-hydroquinone
-
physiological precursor of 1,4-benzoquinone, a topoisomerase II poison, enhances cleavage activity, inhibits ligation activity, at 0.25 mM, alters the enzyme's cleavage site specificity, 1,4-hydroquinone has a higher inhibitory effect on ligation activity but a lower effect on cleavage activity compared to 1,4-benzoquinone
2-(2-chlorophenyl)benzo-1,4-quinone
-
enhances DNA cleavage by isoform IIalpha
2-(3,5-dichlorophenyl)benzo-1,4-quinone
-
enhances DNA cleavage by isoform IIalpha
2-(3-chlorophenyl)benzo-1,4-quinone
-
enhances DNA cleavage by isoform IIalpha
2-(4-chlorophenyl)benzo-1,4-quinone
-
enhances DNA cleavage by isoform IIalpha up to 7fold
3-(4-chlorophenyl)benzo-1,2-quinone
-
enhances DNA cleavage by isoform IIalpha
4'-chlorobiphenyl-2,5-diol
-
enhances DNA cleavage by isoform IIalpha
4-(4-chlorophenyl)benzo-1,2-quinone
-
enhances DNA cleavage by isoform IIalpha
apigenin
-
0.05 mM, 5fold increase in DNA-cleavage activity for isoform II beta, 2fold increase for isoform II alpha
DNA
-
stability of the enzyme's closed clamp conformation may influence DNA-stimulated ATP hydrolysis
DNA repair protein metnase
-
enhances TopoIIalpha activity and increases resistance to TopoII? poisons
-
E1A
-
an adenovirus type 5-based vector that contains E1A, but lacks E1B and E3, specifically enhances the promoter activity by 3.5fold, which leads to increased enzyme expression, overview
-
etoposide
-
0.05 mM, 10fold increase in DNA-cleavage activity for isoform II beta, 6fold increase for isoform II alpha
genistein
-
0.05 mM, 8fold increase in DNA-cleavage activity for isoform II beta, 5fold increase for isoform II alpha
HMGB1
-
chromatin-associated protein, promotes enzyme-mediated catenation of circular DNA, relaxation of negatively supercoiled DNA--------------------------------- and decatenation of kinetoplast DNA. Interaction with enzyme requires both HMG-box domains of HMGB1. A mutant of HMGB1 which cannot change DNA topology stimulates DNA decatenation by enzyme indistinguishably from the wild-type protein
-
luteolin
-
0.05 mM, 7fold increase in DNA-cleavage activity for isoform II beta, 3fold increase for isoform II alpha
myricetin
-
0.05 mM, 7fold increase in DNA-cleavage activity for isoform II beta, 4fold increase for isoform II alpha
p38gamma
-
but not p38alpha MAPK is specifically activated by treatment of breast cancer cells with topoisomerase II drug in intrinsically sensitive but not resistant cells, whereas paclitaxel (Taxol) does not have this effect. The activated p38gamma in turn phosphorylates and stabilizes the topoisomerase II protein, and this enhances the growth inhibition by Topo II drugs. p38gamma activity is necessary and sufficient for Topo IIalpha expression, the drug-p38gamma-Topo IIalpha axis is only detected in intrinsically sensitive but not resistant cells
-
p53 tumor suppressor
-
stimulates the catalytic activity by enhancing the rate of ATP hydrolysis
-
PIASy
-
small ubiquitin-like modifier ligase for topoisomerase 2 alpha
-
protein kinase C delta
-
interaction with enzyme in an S-phase specific manner. Interaction is required for stabilization and catalytic activation of enzyme in response to DNA damage, inhibition of protein kinase C delta activity attenuates DNA damage-induced activation of topoisomerase II alpha. aberrant activation of enzyme by protein kinase C delta is associated with induction of apoptosis upon exposure to genotoxic agents
-
quercetin
-
0.05 mM, 7fold increase in DNA-cleavage activity for isoform II beta, 4fold increase for isoform II alpha
small ubiquitin-like modifier 1
-
required for the mitotic function of the enzyme
-
small ubiquitin-like modifier 2
-
required for the mitotic function of the enzyme
-
small ubiquitin-like modifier 3
-
required for the mitotic function of the enzyme
-
Somatostatin
-
elevates topoisomerase II alpha expression
vanadate
-
slight activation of mutant L169F
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000012
Supercoiled DNA
pH 8.0, temperature not specified in the publication, recombinant topo2alpha
-
0.3 - 0.5
ATP
0.21 - 0.94
DNA
additional information
additional information
-
ATP hydrolysis kinetics for wild-type and Y50F mutant enzyme
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3 - 2.7
ATP
0.5 - 3.6
ATP
0.6 - 3.38
DNA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0494
3beta-corosolic acid
-
-
0.0108
ursolic acid
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
6-[(cyclopentylsulfanyl)methyl]-N2-(4-fluorophenyl)-1,3,5-triazine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
1
6-[[(1-cyclopentyl-1H-tetrazol-5-yl)sulfanyl]methyl]-N2-(4-fluorophenyl)-1,3,5-triazine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
1
6-[[(5-cyclopropyl-1,3,4-oxadiazol-2-yl)sulfanyl]methyl]-N2-(4-fluorophenyl)-1,3,5-triazine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
0.00007 - 0.02645
camptothecin
0.1695 - 0.797
Ciprofloxacin
0.021 - 0.0589
etoposide
1
N2-(4-fluorophenyl)-6-[[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl]-1,3,5-triazine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
1
N2-(4-fluorophenyl)-6-[[(1-propyl-1H-imidazol-2-yl)sulfanyl]methyl]-1,3,5-triazine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
0.337
N2-(4-fluorophenyl)-6-[[(1H-tetrazol-5-yl)sulfanyl]methyl]-1,3,5-triazine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
0.0036 - 0.0277
quercetin
0.0003 - 0.021
suramin
0.00006 - 0.00891
VP-16
1
[4-amino-6-(4-fluoroanilino)-1,3,5-triazin-2-yl]methyl 4-methylpiperazine-1-carbodithioate
Homo sapiens
pH and temperature not specified in the publication
1
[4-amino-6-(4-fluoroanilino)-1,3,5-triazin-2-yl]methyl cyclohexyl(methyl)carbamodithioate
Homo sapiens
pH and temperature not specified in the publication
0.139
[4-amino-6-(4-fluoroanilino)-1,3,5-triazin-2-yl]methyl morpholine-4-carbodithioate
Homo sapiens
pH and temperature not specified in the publication
0.229
[4-amino-6-(4-methoxyanilino)-1,3,5-triazin-2-yl]methyl morpholine-4-carbodithioate
Homo sapiens
pH and temperature not specified in the publication
1
[4-amino-6-(4-methoxyanilino)-1,3,5-triazin-2-yl]methyl piperidine-1-carbodithioate
Homo sapiens
pH and temperature not specified in the publication
6
(1R,1'R,6S,6'S,7R,7'R,11bR,11b'R)-1,1',7,7'-tetrakis(4-hydroxyphenyl)-1,1',6,6',7,7',11b,11b'-octahydro-6,6'-bi-2-oxadibenzo[cd,h]azulene-4,4',8,8',10,10'-hexol
Homo sapiens
-
pH 7.9, 30°C
4
(1R,1'R,6S,6'S,7S,7'S,11bR,11b'R)-1,1',7,7'-tetrakis(4-hydroxyphenyl)-1,1',6,6',7,7',11b,11b'-octahydro-6,6'-bi-2-oxadibenzo[cd,h]azulene-4,4',8,8',10,10'-hexol
Homo sapiens
-
pH 7.9, 30°C
5
(2R,2'S,3'S)-3'-(3,5-dihydroxyphenyl)-2,2'-bis(4-hydroxyphenyl)-4-[(E)-2-(4-hydroxyphenyl)ethenyl]-2,2',3,3'-tetrahydro-3,4'-bi-1-benzofuran-6,6'-diol
Homo sapiens
-
pH 7.9, 30°C
7
(2R,3S)-2-(3,5-dihydroxyphenyl)-1-[(S)-hydroxy(4-hydroxyphenyl)methyl]-3-(4-hydroxyphenyl)-2,3-dihydro-1H-indene-4,6-diol
Homo sapiens
-
pH 7.9, 30°C
0.00083
(2S)-2-(2-hydroxypropan-2-yl)-2,5-dimethyl-8,10-bis[(2-methyloxiran-2-yl)methoxy]-1,2-dihydro-11H-furo[3,2-a]xanthen-11-one
Homo sapiens
-
pH and temperature not specified in the publication, predicted value
3
(3R,4R,4aS,5S,9bS,10S)-4-(3,5-dihydroxyphenyl)-3,5,10-tris(4-hydroxyphenyl)-3,4,4a,5,9b,10-hexahydro-11-oxabenzo[5,6]cyclohepta[1,2,3,4-jkl]-as-indacene-2,6,8-triol
Homo sapiens
-
pH 7.9, 30°C
6
(3S,4S,4aR,5S,9bS,10S)-4-(3,5-dihydroxyphenyl)-3,5,10-tris(4-hydroxyphenyl)-3,4,4a,5,9b,10-hexahydro-11-oxabenzo[5,6]cyclohepta[1,2,3,4-jkl]-as-indacene-2,6,8-triol
Homo sapiens
-
pH 7.9, 30°C
5
(4bR,5R,9S,10S,11R,12R)-10-(3,5-dihydroxyphenyl)-5,9,12-tris(4-hydroxyphenyl)-4b,5,9,10,11,12-hexahydrobenzo[6,7]cyclohepta[1,2,3-cd]furo[3,2-f][1]benzofuran-1,3,11-triol
Homo sapiens
-
pH 7.9, 30°C
0.05
(4Z,7Z,10Z,13Z,16Z,19Z)-henicosa-4,7,10,13,16,19-hexaenoic acid
Homo sapiens
-
IC50 is 0.05 mM for inhibition of decatenation of kinetoplast DNA
0.01
(5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoic acid
Homo sapiens
-
irreversible inhibition, IC50 is 0.01 mM for inhibition of decatenation of kinetoplast DNA, effects on thermal transition of dsDNA, overview
0.00058
1,3,5-trihydroxy-4-methoxy-9H-xanthen-9-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00069
1,5-dihydroxy-3-methoxy-2,4-bis(3-methylbut-2-en-1-yl)-9H-xanthen-9-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00058
1,7-dihydroxy-9H-xanthen-9-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0286
1-(4-methoxybenzyl)-1H-[1,2,3]triazolo[4,5-g]-phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.0556
1-ethyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.0298
1-iso-butyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.0333
1-iso-propyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.039
1-methyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.0432
1-n-butyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.049
1-n-propyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.4767
1-[(1,1-dioxo-2,3-dihydro-1H-1l6-thiophen-3-yl)(ethyl)amino]-1-oxopropan-2-yl 1H-indazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0256
1-[4-[(methanesulfonyl)amino]phenyl]-1-oxopropan-2-yl 1H-indazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0528
1H-[1,2,3]triazolo[4,5,-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.522
2-([[6-(benzylsulfanyl)-4-oxo-4,5-dihydro-1,3,5-triazin-2-yl]sulfanyl]methyl)benzonitrile
Homo sapiens
-
at pH 7.9 and 37°C
0.0615
2-ethyl-2H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.0194
2-iso-butyl-2H-[1,2,3] triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.0545
2-iso-propyl-2H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.0556
2-methyl-2H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.0648
2-n-butyl-2H-[1,2,3] triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.0444
2-n-propyl-2H-[1,2,3] triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.0268
2-oxo-2-(3-sulfamoylanilino)ethyl 1H-indazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0242
2-[(1,1-dioxo-1l6-thiolan-3-yl)(ethyl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.1963
2-[(1,1-dioxo-1l6-thiolan-3-yl)(methyl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0289
2-[(1,1-dioxo-1l6-thiolan-3-yl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.2146
2-[(1,1-dioxo-2,3-dihydro-1H-1l6-thiophen-3-yl)(2-methylpropyl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
1
2-[(3-carbamoylthiophen-2-yl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
Homo sapiens
-
IC50 above 1.0 mM, pH and temperature not specified in the publication
1
2-[(butan-2-yl)(1,1-dioxo-2,3-dihydro-1H-1l6-thiophen-3-yl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
Homo sapiens
-
IC50 above 1.0 mM, pH and temperature not specified in the publication
0.06454
2-[4-(methanesulfonyl)piperazin-1-yl]-2-oxoethyl 1H-indazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0236
2-[benzyl(1,1-dioxo-2,3-dihydro-1H-1l6-thiophen-3-yl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.528
3-([[6-(benzylsulfanyl)-4-oxo-4,5-dihydro-1,3,5-triazin-2-yl]sulfanyl]methyl)benzonitrile
Homo sapiens
-
at pH 7.9 and 37°C
0.186
3-oxolanost-9(11)-ene-24S,25-diol
Homo sapiens
-
IC50: 0.186 mM
0.00119
3-[2-(dimethylamino)propoxy]benzo[b]naphtho[2,3-d]furan-6,11-dione
Homo sapiens
-
-
0.083 - 0.089
3alpha-corosolic acid
0.049
3beta-corosolic acid
Homo sapiens
-
IC50: 0.049 mM
0.4858
4-([[6-(benzylsulfanyl)-4-oxo-4,5-dihydro-1,3,5-triazin-2-yl]sulfanyl]methyl)-3-fluorobenzonitrile
Homo sapiens
-
at pH 7.9 and 37°C
0.1534
4-([[6-(benzylsulfanyl)-4-oxo-4,5-dihydro-1,3,5-triazin-2-yl]sulfanyl]methyl)benzonitrile
Homo sapiens
-
at pH 7.9 and 37°C
0.00071
5,8-dihydroxy-4-methoxy-3,6-bis(3-methylbut-2-en-1-yl)-4a,9a-dihydro-1H-xanthene-1,2,9-trione
Homo sapiens
-
pH and temperature not specified in the publication, predicted value
0.00079
5-methoxy-1,3-bis[(2-methyloxiran-2-yl)methoxy]-7-(oxiran-2-ylmethyl)-9H-xanthen-9-one
Homo sapiens
-
pH and temperature not specified in the publication, predicted value
0.00075
5-methoxy-1,3-bis[(2-methyloxiran-2-yl)methoxy]-7-(propan-2-yl)-9H-xanthen-9-one
Homo sapiens
-
pH and temperature not specified in the publication, predicted value
0.0006
6,11-dihydroxy-3,3-dimethyl-5-(3-methylbut-2-en-1-yl)-3H,7H-pyrano[2,3-c]xanthen-7-one
Homo sapiens
-
pH and temperature not specified in the publication
0.2347
6-(benzylsulfanyl)-4-(butylsulfanyl)-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
1
6-(benzylsulfanyl)-4-(phenylsulfanyl)-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
1
6-(benzylsulfanyl)-4-(propylsulfanyl)-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
1
6-(benzylsulfanyl)-4-[(cyclobutylmethyl)sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
0.481
6-(benzylsulfanyl)-4-[(cyclopropylmethyl)sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
0.0941
6-(benzylsulfanyl)-4-[[(2-chlorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
0.0725
6-(benzylsulfanyl)-4-[[(2-fluorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
1
6-(benzylsulfanyl)-4-[[(2-methoxyphenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
IC50 above 1.0 mM, at pH 7.9 and 37°C
0.3767
6-(benzylsulfanyl)-4-[[(2-nitrophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
0.0576
6-(benzylsulfanyl)-4-[[(3-chlorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
0.4853
6-(benzylsulfanyl)-4-[[(3-methoxyphenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
0.4883
6-(benzylsulfanyl)-4-[[(3-nitrophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
0.2193
6-(benzylsulfanyl)-4-[[(4-chlorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
0.1466
6-(benzylsulfanyl)-4-[[(4-fluorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
0.3859
6-(benzylsulfanyl)-4-[[(4-nitrophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
0.00068
8-(2-(diethylamino)ethoxy)benzofuro[3,2-g]quinoline-5,11-dione
Homo sapiens
-
-
0.002
aclacinomycin A
Homo sapiens
-
-
4
alpha-viniferin-13-O-beta-glucopyranoside
Homo sapiens
-
pH 7.9, 30°C
0.08
betulinic acid
Homo sapiens
-
IC50: 0.08 mM
0.0065
bis(acridin-4-ylmethyl)cyanamide
Homo sapiens
-
pH 8.0
1.999
Ciprofloxacin
Homo sapiens
-
pH 8.0, 37°C
0.01
conjugated docosahexanoic acid
Homo sapiens
-
IC50 is 0.01 mM for inhibition of decatenation of kinetoplast DNA
-
0.0025
conjugated eicosapentaenoic acid
Homo sapiens
-
irreversible inhibition, IC50 is 0.0025 mM for inhibition of decatenation of kinetoplast DNA, effects on thermal transition of dsDNA, overview
0.074
coralyne
Homo sapiens
-
pH 8.0, 37°C
0.043
corosolic acid
Homo sapiens
-
IC50: 0.043 mM
8.5
daunorubicin
Homo sapiens
-
pH 7.9, 30°C
0.0263
ellagic acid
Homo sapiens
-
pH 8.0, 37°C
1.485
enoxacin
Homo sapiens
-
pH 8.0, 37°C
0.000029
epicatechin gallate
Homo sapiens
-
pH 8.0, 37°C
0.05 - 0.0929
etoposide
2.4
FEITPEKNPQ
Homo sapiens
-
in 50 mM Tris-HCl (pH 8.0)
1
hemsleyanol
Homo sapiens
-
pH 7.9, 30°C
0.0002
ICRF-193
Homo sapiens
-
at 37°C
4
IETWNPNNKP
Homo sapiens
-
in 50 mM Tris-HCl (pH 8.0)
0.015
lithocholic acid
Homo sapiens
-
IC50: 0.015 mM, the lithocholic interaction interface has a pocket comprised of three amino acids, Lys720, Leu760 and Thr791
0.092
maslinic acid
Homo sapiens
-
IC50: 0.092 mM
0.002
Mitoxantrone
Homo sapiens
-
-
0.000039
myricetin
Homo sapiens
-
pH 8.0, 37°C
0.0043
N,N,N',N'-tetrakis(acridin-4-ylmethyl)butane-1,4-diamine
Homo sapiens
-
pH 8.0
0.0057
N,N,N',N'-tetrakis(acridin-4-ylmethyl)ethane-1,2-diamine
Homo sapiens
-
pH 8.0
0.0002
N,N,N',N'-tetrakis[(7-bromo-9-chloroacridin-4-yl)methyl]butane-1,4-diamine
Homo sapiens
-
pH 8.0
0.0009
N,N,N',N'-tetrakis[(9-aminoacridin-4-yl)methyl]ethane-1,2-diamine
Homo sapiens
-
pH 8.0
0.0004
N-(acridin-1-ylmethyl)-N,N',N'-tris(acridin-2-ylmethyl)octane-1,8-diamine
Homo sapiens
-
pH 8.0
0.5
N-([3-[(methanesulfonyl)amino]phenyl]methyl)-1H-indazole-3-carboxamide
Homo sapiens
-
IC50 above 0.5 mM, pH and temperature not specified in the publication
0.5
N-([4-[(methylsulfamoyl)methyl]phenyl]methyl)-1H-indazole-3-carboxamide
Homo sapiens
-
IC50 above 0.5 mM, pH and temperature not specified in the publication
0.0251
N-[1-(1H-indazole-3-carbonyl)piperidin-4-yl]methanesulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0139
N-[1-(1H-indazole-3-carbonyl)piperidin-4-yl]methanesulfonohydrazide
Homo sapiens
-
pH and temperature not specified in the publication
0.5
N-[1-(1H-indazole-3-carbonyl)piperidin-4-yl]propane-1-sulfonamide
Homo sapiens
-
IC50 above 0.5 mM, pH and temperature not specified in the publication
0.3819
N-[3-[(methanesulfonyl)amino]propyl]-1H-indazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.5
N-[4-[(methanesulfonyl)amino]-3-methylphenyl]-1H-indazole-3-carboxamide
Homo sapiens
-
IC50 above 0.5 mM, pH and temperature not specified in the publication
0.0458
N-[4-[(methanesulfonyl)amino]phenyl]-1H-indazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0084
N2-(1,3-benzothiazol-6-yl)-N6-cyclohexyl-9H-purine-2,6-diamine
Homo sapiens
-
-
0.0017
N2-(1,3-benzothiazol-6-yl)-N6-tert-butyl-9H-purine-2,6-diamine
Homo sapiens
-
-
0.0005 - 0.002
neoamphimedine
0.081
oleanolic acid
Homo sapiens
-
IC50: 0.081 mM
1.426
Pentamidine
Homo sapiens
-
pH 8.0, 37°C
0.0045
procyanidin B2
Homo sapiens
-
pH 8.0, 37°C
0.0889
quercetin
Homo sapiens
-
pH 8.0, 37°C
0.0657
resveratrol
Homo sapiens
-
pH 8.0, 37°C
1
S-[6-(benzylsulfanyl)-4-oxo-4,5-dihydro-1,3,5-triazin-2-yl] hydrogen carbonothioate
Homo sapiens
-
at pH 7.9 and 37°C
0.0028
sodium antimonyl(III) gluconate
Homo sapiens
-
IC50 is 0.0028 mM
0.0027
sodium stibogluconate
Homo sapiens
-
IC50 is 0.0027 mM
0.02149
tanshinone-1
Homo sapiens
-
at pH 8.0 and 37°C
0.036
ursolic acid
Homo sapiens
-
IC50: 0.036 mM
7.9
VFDGEL
Homo sapiens
-
in 50 mM Tris-HCl (pH 8.0)
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
ATPase and topoisomerase inhibition assay at
6.9
-
assay at
7.1
-
in vivo cytotoxic assay at
7.3
-
assay at
7.4
-
assay at
7.4 - 8
-
assay at, dependent on reaction step
7.8
-
in vitro assay at
7.9 - 8
-
assay at
8.3
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
DNA binding assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
strong correlation of isoform TopoIIalpha level with the progression of DNA damage after peroxide-mediated DNA damage and double-strand breaks. Isoform TopoIIbeta expression is correlated with the DNA double strand breaks repair activity of cells in Ku70, Werner’s helicase and pol-beta dependent pathways
Manually annotated by BRENDA team
-
spatio-temporal expression pattern of DNA Top IIbeta, overview
Manually annotated by BRENDA team
-
leukemia cell
Manually annotated by BRENDA team
-
primary. Topo-IIalpha expression in the gastric adenocarcinoma is positively correlated with tumor location in the gastric cardia, intestinal histological type, late age onset of gastric adenocarcinoma, and male gender, but with no other clinicopathological parameters or with survival, overview
Manually annotated by BRENDA team
-
vincristine-selected multidrug-resistant HL-60 cells
Manually annotated by BRENDA team
-
resitant to topoisomerase II inhibitors
Manually annotated by BRENDA team
-
a hepatocyte-derived cellular carcinoma cell line
Manually annotated by BRENDA team
-
a human cutaneous T cell lymphoma cell line
Manually annotated by BRENDA team
-
non-small-cell lung cancer cell line, cell line with innate etoposide-resistance mediated by cytoplasmic localization of topoisomerase II alpha, 2 enzyme forms, a large and a small one, overview
Manually annotated by BRENDA team
-
lung cancer cell line
Manually annotated by BRENDA team
-
adriamycin-resistant K562 cell line
Manually annotated by BRENDA team
-
a colon adenocarcinoma cell line
Manually annotated by BRENDA team
-
melanoma cells
Manually annotated by BRENDA team
-
a gastric cancer cell line
Manually annotated by BRENDA team
-
Top IIbeta is highly expressed in differentiating cerebellar neurons
Manually annotated by BRENDA team
-
renal carcinoma cells
Manually annotated by BRENDA team
-
Ewing's sarcoma cell line
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
DNA Top IIbeta is localized in the nucleolus during interphase, and in the cytoplasm during mitosis
Manually annotated by BRENDA team
-
in the brain at embryonic stage
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
topoisomerase II poisons generate DNA damage, in addition to inhibition of enzyme activity, and cause delay of cell cycle progression due to DNA damage checkpoints
metabolism
-
mechanistically link of DNA topoisomerase IIbeta-dependent dsDNA breaks and the components of the DNA damage and repair machinery in regulated gene transcription
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TOP2A_HUMAN
1531
0
174385
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
174400
predicted from amino acid sequence
160000
-
x * 170000, HeLa cell enzyme, SDS-PAGE, x * 160000, large truncated INER-37 cell enzyme, SDS-PAGE, x * 65460, small INER-37 cell enzyme, SDS-PAGE
170000
174000
-
Topo IIalpha, SDS-PAGE
175000
-
x * 175000, SDS-PAGE
183000
-
Topo IIbeta, SDS-PAGE
65460
-
x * 170000, HeLa cell enzyme, SDS-PAGE, x * 160000, large truncated INER-37 cell enzyme, SDS-PAGE, x * 65460, small INER-37 cell enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
dimer
homodimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
acetylation of specific sites involved in the allosteric regulation of the enzyme provide a mechanism for modulation of its catalytic activity
phosphoprotein
-
phosphoprotein
sumoylation
-
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis, overview
-
homology-based structure model of segment of amino acids 724-771 forming the alpha2 helix turn helix module with a compact alpha2betaalpha3talpha4 conformation. The helical content of human alpha2 helix turn helix module in solution is similar to that of its couterpart with yeast topoiaomerase II in the solid state. The segment self-associates into dimers. alpha2 helix turn helix module, helix turn helix and alpha4, but not alpha3 segments, bind effectively to DNA
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K168A
the mutant exhibits 7fold impaired DNA cleavage activity and no decatenation activity compared to the wild type enzyme
A772P
-
site-directed mutagenesis, mutation of a residue of the alpha-helix region responsible for anti-cancer drug sensitivity, about 10% activity compared to the recombinant wild-type enzyme in strain JN394t2-4
C170A
-
potential site of quinone adduction. Mutant does not show reduced sensitivity to benzoquinone
C392A
-
potential site of quinone adduction. Mutant shows 50% reduced sensitivity to benzoquinone and displays 2fold faster rates of DNA religation than wild-type. Mutation does not affect the ability of benzoquinone to block the N-terinal gate of the enzyme
C405A
-
potential site of quinone adduction. Mutant shows 50% reduced sensitivity to benzoquinone and displays 2fold faster rates of DNA religation than wild-type. Mutation does not affect the ability of benzoquinone to block the N-terinal gate of the enzyme
C455A
F775P
-
site-directed mutagenesis, mutation of a residue of the alpha-helix region responsible for anti-cancer drug sensitivity, inactive mutant
H759A
-
site-directed mutagenesis, mutation of a residue of the alpha-helix region responsible for anti-cancer drug sensitivity, the mutant shows reduced decatenation activity and amounts of etoposide-induced cleavable complexes compared to the wild-type enzyme
H759P
-
site-directed mutagenesis, mutation of a residue of the alpha-helix region responsible for anti-cancer drug sensitivity, the mutant shows about 50% reduced decatenation activity and amounts of etoposide-induced cleavable complexes compared to the wild-type enzyme
I769P
-
site-directed mutagenesis, mutation of a residue of the alpha-helix region responsible for anti-cancer drug sensitivity, nearly inactive mutant
L169F
L169I
L771P
-
site-directed mutagenesis, mutation of a residue of the alpha-helix region responsible for anti-cancer drug sensitivity, nearly inactive mutant
M762P
-
site-directed mutagenesis, mutation of a residue of the alpha-helix region responsible for anti-cancer drug sensitivity, mutant activity is similar to the wild-type activity
M765P
-
site-directed mutagenesis, mutation of a residue of the alpha-helix region responsible for anti-cancer drug sensitivity, nearly inactive mutant
M766P
-
site-directed mutagenesis, mutation of a residue of the alpha-helix region responsible for anti-cancer drug sensitivity, inactive mutant
N770P
-
site-directed mutagenesis, mutation of a residue of the alpha-helix region responsible for anti-cancer drug sensitivity, the mutant shows 30% reduced decatenation activity and amounts of etoposide-induced cleavable complexes compared to the wild-type enzyme
N774P
-
site-directed mutagenesis, mutation of a residue of the alpha-helix region responsible for anti-cancer drug sensitivity, mutant activity is similar to the wild-type activity
P732L
tenfold less sensitive to inhibitor N-(4’-(9-acridinylamino)-3-methoxy-phenyl) methane sulfonamide than wild-type with crossresistance to inhibitors etoposide, ellipticine, methyl N-(4’-(9-acridinylamino)-2-methoxy-phenyl)carbamate hydrochloride, methyl N-(4’-(9-acridinylamino)-phenyl) carbamate hydrochloride, doxorubicin. Mutant is functional with reduced strand passage activies and altered DNA binding. It has drastically altered cleavage properties cleaving a 40 bp DNA substrate in presence of Mg2+ at different postions from wild-type, with no cleavage in presence of Ca2+
Q773P
-
site-directed mutagenesis, mutation of a residue of the alpha-helix region responsible for anti-cancer drug sensitivity, mutant activity is similar to the wild-type activity
R162K
R162Q
R804A
-
site-directed mutagenesis, residue next to active site tyrosine, mutation only slightly influences the ligation reaction
S1106A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme, during recombinant expression in enzyme-depleted HTETOP cells
S1247A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme, during recombinant expression in enzyme-depleted HTETOP cells
S1354A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme, during recombinant expression in enzyme-depleted HTETOP cells
S1393A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme, during recombinant expression in enzyme-depleted HTETOP cells
S1395A
-
site-directed mutagenesis, phosphorylation site mutant that shows unaltered decatenation activity compared to the wild-type topo IIbeta
S1545A
-
site-directed mutagenesis, phosphorylation site mutant that shows unaltered decatenation activity compared to the wild-type topo IIbeta
S165R
-
the mutation leads to truncations at the 3' end of the coding sequence of topoIIalpha and topoIIbeta with impaired enzyme function
T1426A
-
site-directed mutagenesis, phosphorylation site mutant that shows unaltered decatenation activity compared to the wild-type topo IIbeta
T1426A/S1545A
-
site-directed mutagenesis, phosphorylation site mutant that shows unaltered decatenation activity compared to the wild-type topo IIbeta
T767P
-
site-directed mutagenesis, mutation of a residue of the alpha-helix region responsible for anti-cancer drug sensitivity, mutant activity is similar to the wild-type activity
Y165S
Y656F
-
site-directed mutagenesis, phosphorylation site mutant that shows reduced decatenation activity compared to the wild-type topo IIbeta
Y805A
-
site-directed mutagenesis, active site residue mutant, mutant shows reduced ligation activity compared to the wild-type enzyme
Y805C
-
site-directed mutagenesis, active site residue mutant, mutant shows increased ligation activity compared to the wild-type enzyme
Y805F
Y805H
-
site-directed mutagenesis, active site residue mutant, mutant shows increased ligation activity compared to the wild-type enzyme
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49.2
melting temperature of the wild type ATPase domain
25
-
24 h, stable
37
-
activity begins to decrease after 8 h incubation
4
-
25 h, stable
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged isozyme topo2alpha from Sf9 insect cells by nuclei preparation, glutathione affinity chromatography, and gel filtration
His-Trap HP affinity column chromatography, StrepTactin column chromatography, and SPX200 gel filtration
-
native enzyme partially from Hut 78 cells by nuclear extract preparation
-
partial
-
recombinant His-tagged wild-type and mutant topo IIbeta proteins from Saccharomyces cerevisiae by nickel affinity chromatography
-
recombinant isozymes IIalpha and IIbeta from Saccharomyces cerevisiae to at least 95% homogeneity
-
topoisomerase IIbeta
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme DNA sequence analysis
expressed in Saccharomyces cerevisiae and in BHK-21 cells
expression of GST-tagged isozyme topo2alpha in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
co-overexpression of Topo IIalpha with p38gamma protein in primary breast cancer cells using adenoviral-mediated gene delivery, expression of FLAG-tagged enzyme in 293T cells
-
expressed in DC-3F cells
-
expressed in Saccharomyces cerevisiae JELDELTAtop1 cells
-
expressed in Saccharomyces cerevisiae strain JEL1
-
expression as topoisomerase IIalpha glutathione S-transferase fusion protein
-
expression of GFP-tagged enzyme in mutant enzyme-depleted HTETOP cells
-
expression of His-tagged wild-type and mutant topo IIbeta proteins in Saccharomyces cerevisiae
-
expression of isozymes IIalpha and IIbeta in Saccharomyces cerevisiae
-
expression of topoisomerase IIalpha in Saccharomyces cerevisiae
-
expression of wild-type and mutant enzymes in drug-permeable yeast strain JN394t2-4 and in the temperature-sensitive strain SD1-4
-
expression of wild-type and mutant enzymes in Saccharomyces cerevisiae
-
expression of wild-type and truncation mutant Top2alphaDELTA1175 in Saccharomyces cerevisiae strain JEL-1DELTAtop1
-
gene Top IIbeta is located to chromosome 3p24
-
gene TOP2A, tissue microarray expression analysis
-
isoform IIalpha and isoform IIbeta
-
oligohistidine-tagged recombinant domains of topoisomerase IIalpha overexpressed in Escherichia coli
-
overexpression of isozyme IIalpha in Saccharomyces cerevisiae
-
overexpression of wild-type and mutant enzyme in yeast JELt1 cells
-
overexpression of wild-type and mutant enzymes in Saccharomyces cerevisiae strain JelDELTATop1
-
silencing of the enzyme by transfection of HeLA cells with RNA duplexes of 21 nucleotides in length for each of the isozymes alpha and beta, i.e alpha siRNA-1, alpha siRNA-2, beta siRNA-1, and beta siRNA-2, transfection results in specific silencing of isozyme IIalpha, not of isozyme IIbeta
-
topoisomerase II alpha is expressed in Sf21 cells
-
topoisomerase IIbeta overexpressed in Saccharomyces cerevisiae
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme expression is transiently induced up to 11fold by interleukin-2 at 1000 U/ml after 10 h
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
use of triple-helical DNA structures for targeting enzyme-mediated cleavage to DNA specific sequences and use of drug-triplex-forming oligonucleotides to investgate enzyme mechanism
drug development
medicine
pharmacology
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Andersen, A.H.; Bendixen, C.; Westergaard, O.
DNA topoisomerases
DNA Replication in eucaryotic cells, Cold Spring Harbor Laboratory Press
587-617
1996
Bacteria, Saccharomyces cerevisiae, eukaryota, Homo sapiens, Mus musculus
-
Manually annotated by BRENDA team
Vosberg, H.P.
DNA topoisomerases: enzymes that control DNA conformation
Curr. Top. Microbiol. Immunol.
114
19-102
1985
Bacillus subtilis, Bacteria, Tequatrovirus T4, Bos taurus, Drosophila melanogaster, Escherichia coli, eukaryota, Homo sapiens, Micrococcus luteus, Pseudomonas aeruginosa, Rattus norvegicus, Xenopus laevis
Manually annotated by BRENDA team
Akasaka, T.; Kurosaka, S.; Uchida, Y.; Tanaka, M.; Sato, K.; Hayakawa, I.
Antibacterial activities and inhibitory effects of sitafloxacin (DU-6859a) and its optical isomers against type II topoisomerases
Antimicrob. Agents Chemother.
42
1284-1287
1998
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Insaf, S.; Danks, M.K.; Witiak, D.T.
Structure-function analysis of DNA topoisomerase II inhibitors
Curr. Med. Chem.
3
437-466
1996
Saccharomyces cerevisiae, eukaryota, Homo sapiens, Mammalia
-
Manually annotated by BRENDA team
Austin, C.A.; Marsh, K.L.; Wasserman, R.A.; Willmore, E.; Sayer, P.J.; Wang, J.C.; Fisher, L.M.
Expression, domain structure, and enzymatic properties of an active recombinant human DNA topoisomerase IIbeta
J. Biol. Chem.
270
15739-15746
1995
Homo sapiens
Manually annotated by BRENDA team
Boege, F.; Gieseler, F.; Muller, M.; Biersack, H.; Meyer, P.
Activation of topoisomerase II during partial purification by heparin-Sepharose chromatography
J. Chromatogr.
625
67-71
1992
Homo sapiens
Manually annotated by BRENDA team
Sato, M.; Ishida, R.; Narita, T.; Kato, J.I.; Ikeda, H.; Fukazawa, H.; Andoh, T.
Interaction of the DNA topoisomerase II catalytic inhibitor meso-2,3-bis(3,5-dioxopiperazine-1-yl)butane (ICRF-193), a bisdioxopiperazine derivative, with the conserved region(s) of eukaryotic but not prokaryotic enzyme
Biochem. Pharmacol.
54
545-550
1997
Bos taurus, Brassica oleracea, Drosophila melanogaster, Escherichia coli, Homo sapiens, Schizosaccharomyces pombe, Xenopus laevis
Manually annotated by BRENDA team
Catchpoole, D.R.; Stewart, B.W.
Inhibition of topoisomerase II by aurintricarboxylic acid: implications for mechanisms of apoptosis
Anticancer Res.
14
853-856
1994
Homo sapiens
Manually annotated by BRENDA team
Tepe, J.J.; Madalengoitia, J.S.; Slunt, K.M.; Werbovetz, K.W.; Spoors, P.G.; Macdonald, T.L.
Inhibition of DNA topoisomerase II by azaelliptitoxins functionalized in the variable substituent domain
J. Med. Chem.
39
2188-2196
1996
Homo sapiens
Manually annotated by BRENDA team
Wells, N.J.; Fry, A.M.; Guano, F.; Norbury, C.; Hickinson, I.D.
Cell cycle phase-specific phosphorylation of human topoisomerase II alpha. Evidence of a role for protein kinase C
J. Biol. Chem.
270
28357-28363
1995
Homo sapiens
Manually annotated by BRENDA team
Zhang, Y.L.; Shen, Y.C.; Wang, Z.Q.; Chen, H.X.; Guo, X.; Cheng, Y.C.; Lee, K.H.
Antitumor agents, 130, novel 4 beta-arylamino derivatives of 3',4'-didemethoxy-3',4'-dioxo-4-deoxypodophyllotoxin as potent inhibitors of human DNA topoisomerase II
J. Nat. Prod.
55
1100-1111
1992
Homo sapiens
Manually annotated by BRENDA team
Mizushina, Y.; Ikuta, A.; Endoh, K.; Oshige, M.; Kasai, N.; Kamiya, K.; Satake, T.; Takazawa, H.; Morita, H.; Tomiyasu, H.; Yoshida, H.; Sugawara, F.; Sakaguchi, K.
Inhibition of DNA polymerases and DNA topoisomerase II by triterpenes produced by plant callus
Biochem. Biophys. Res. Commun.
305
365-373
2003
Homo sapiens
Manually annotated by BRENDA team
Mizushina, Y.; Iida, A.; Ohta, K.; Sugawara, F.; Sakaguchi, K.
Novel triterpenoids inhibit both DNA polymerase and DNA topoisomerase
Biochem. J.
350
757-763
2000
Homo sapiens
-
Manually annotated by BRENDA team
Vance, J.R.; Bastow, K.F.
Inhibition of DNA topoisomerase II catalytic activity by the antiviral agents 7-chloro-1,3-dihydroxyacridone and 1,3,7-trihydroxyacridone
Biochem. Pharmacol.
58
703-708
1999
Homo sapiens
Manually annotated by BRENDA team
Krishnan, P.; Bastow, K.F.
Novel mechanisms of DNA topoisomerase II inhibition by pyranonaphthoquinone derivatives-eleutherin, alpha lapachone, and beta lapachone
Biochem. Pharmacol.
60
1367-1379
2000
Homo sapiens
Manually annotated by BRENDA team
Lothstein, L.; Suttle, D.P.; Roaten, J.F.; Koseki, Y.; Israel, M.; Sweatman, T.W.
Catalytic inhibition of DNA topoisomerase II by N-benzyladriamycin (AD 288)
Biochem. Pharmacol.
60
1621-1628
2000
Homo sapiens
Manually annotated by BRENDA team
Peebles, K.A.; Baker, R.K.; Kurz, E.U.; Schneider, B.J.; Kroll, D.J.
Catalytic inhibition of human DNA topoisomerase IIalpha by hypericin, a naphthodianthrone from St. John's wort (Hypericum perforatum)
Biochem. Pharmacol.
62
1059-1070
2001
Homo sapiens
Manually annotated by BRENDA team
Renodon-Corniere, A.; Jensen, L.H.; Nitiss, J.L.; Jensen, P.B.; Sehested, M.
Analysis of bisdioxopiperazine dexrazoxane binding to human DNA topoisomerase II alpha: decreased binding as a mechanism of drug resistance
Biochemistry
42
9749-9754
2003
Homo sapiens
Manually annotated by BRENDA team
Guan, J.; Zhu, X.K.; Tachibana, Y.; Bastow, K.F.; Brossi, A.; Hamel, E.; Lee, K.H.
Antitumor agents. Part 186: Synthesis and biological evaluation of demethylcolchiceinamide analogues as cytotoxic DNA topoisomerase II inhibitors
Bioorg. Med. Chem.
6
2127-2131
1998
Homo sapiens
Manually annotated by BRENDA team
Park, H.J.; Lee, H.J.; Lee, E.J.; Hwang, H.J.; Shin, S.H.; Suh, M.E.; Kim, C.; Kim, H.J.; Seo, E.K.; Lee, S.K.
Cytotoxicity and DNA topoisomerase inhibitory activity of benz[f]indole-4,9-dione analogs
Biosci. Biotechnol. Biochem.
67
1944-1949
2003
Homo sapiens
Manually annotated by BRENDA team
Iida, A.; Kano, M.; Kubota, Y.; Koga, K.; Tomioka, K.
Podophyllotoxin aza-analogue, a novel DNA topoisomerase II inhibitor
Chem. Pharm. Bull.
48
486-489
2000
Homo sapiens
Manually annotated by BRENDA team
Mizushina, Y.; Kasai, N.; Sugawara, F.; Iida, A.; Yoshida, H.; Sakaguchi, K.
Three-dimensional structural model analysis of the binding site of lithocholic acid, an inhibitor of DNA polymerase beta and DNA topoisomerase II
J. Biochem.
130
657-664
2001
Homo sapiens
Manually annotated by BRENDA team
Kwon, Y.; Shin, B.S.; Chung, I.K.
The p53 tumor suppressor stimulates the catalytic activity of human topoisomerase IIa by enhancing the rate of ATP hydrolysis
J. Biol. Chem.
275
18503-18510
2000
Homo sapiens
Manually annotated by BRENDA team
Skouboe, C.; Bjergbaek, L.; Oestergaard, V.H.; Larsen, M.K.; Knudsen, B.R.; Andersen, A.H.
A Human topoisomerase IIa heterodimer with only one ATP binding site can go through successive catalytic cycles
J. Biol. Chem.
278
5768-5774
2003
Homo sapiens
Manually annotated by BRENDA team
Rudolph, J.; Theis, H.; Hanke, R.; Endermann, R.; Johannsen, L.; Geschke, F.U.
seco-Cyclothialidines: new concise synthesis, inhibitory activity toward bacterial and human DNA topoisomerases, and antibacterial properties
J. Med. Chem.
44
619-626
2001
Homo sapiens
Manually annotated by BRENDA team
West, K.L.; Austin, C.A.
Human DNA topoisomerase IIbeta binds and cleaves four-way junction DNA in vitro
Nucleic Acids Res.
27
984-992
1999
Homo sapiens
Manually annotated by BRENDA team
Wada, S.I.; Iida, A.; Tanaka, R.
Triterpene constituents from the stem bark of Pinus luchuensis and their DNA topoisomerase II inhibitory effect
Planta Med.
67
659-664
2001
Homo sapiens
Manually annotated by BRENDA team
Yonezawa, Y.; Tsuzuki, T.; Eitsuka, T.; Miyazawa, T.; Hada, T.; Uryu, K.; Murakami-Nakai, C.; Ikawa, H.; Kuriyama, I.; Takemura, M.; Oshige, M.; Yoshida, H.; Sakaguchi, K.; Mizushina, Y.
Inhibitory effect of conjugated eicosapentaenoic acid on human DNA topoisomerases I and II
Arch. Biochem. Biophys.
435
197-206
2005
Homo sapiens
Manually annotated by BRENDA team
Sorensen, T.K.; Grauslund, M.; Jensen, P.B.; Sehested, M.; Jensen, L.H.
Separation of bisdioxopiperazine- and vanadate resistance in topoisomerase II
Biochem. Biophys. Res. Commun.
334
853-860
2005
Homo sapiens
Manually annotated by BRENDA team
Bal, C.; Baldeyrou, B.; Moz, F.; Lansiaux, A.; Colson, P.; Kraus-Berthier, L.; Leonce, S.; Pierre, A.; Boussard, M.F.; Rousseau, A.; Wierzbicki, M.; Bailly, C.
Novel antitumor indenoindole derivatives targeting DNA and topoisomerase II
Biochem. Pharmacol.
68
1911-1922
2004
Homo sapiens
Manually annotated by BRENDA team
Bromberg, K.D.; Velez-Cruz, R.; Burgin, A.B.; Osheroff, N.
DNA ligation catalyzed by human topoisomerase II alpha
Biochemistry
43
13416-13423
2004
Homo sapiens
Manually annotated by BRENDA team
Baldwin, E.L.; Byl, J.A.; Osheroff, N.
Cobalt enhances DNA cleavage mediated by human topoisomerase II alpha in vitro and in cultured cells
Biochemistry
43
728-735
2004
Homo sapiens
Manually annotated by BRENDA team
Dickey, J.S.; Osheroff, N.
Impact of the C-terminal domain of topoisomerase IIalpha on the DNA cleavage activity of the human enzyme
Biochemistry
44
11546-11554
2005
Homo sapiens
Manually annotated by BRENDA team
Hasinoff, B.B.; Wu, X.; Begleiter, A.; Guziec, L.J.; Guziec, F.Jr.; Giorgianni, A.; Yang, S.; Jiang, Y.; Yalowich, J.C.
Structure-activity study of the interaction of bioreductive benzoquinone alkylating agents with DNA topoisomerase II
Cancer Chemother. Pharmacol.
57
221-233
2006
Homo sapiens
Manually annotated by BRENDA team
de Lucio, B.; Manuel, V.; Barrera-Rodriguez, R.
Characterization of human NSCLC cell line with innate etoposide-resistance mediated by cytoplasmic localization of topoisomerase II alpha
Cancer Sci.
96
774-783
2005
Homo sapiens
Manually annotated by BRENDA team
Habermeyer, M.; Fritz, J.; Barthelmes, H.U.; Christensen, M.O.; Larsen, M.K.; Boege, F.; Marko, D.
Anthocyanidins modulate the activity of human DNA topoisomerases I and II and affect cellular DNA integrity
Chem. Res. Toxicol.
18
1395-1404
2005
Homo sapiens
Manually annotated by BRENDA team
Lindsey, R.H., Jr.; Bender, R.P.; Osheroff, N.
Effects of benzene metabolites on DNA cleavage mediated by human topoisomerase II alpha: 1,4-hydroquinone is a topoisomerase II poison
Chem. Res. Toxicol.
18
761-770
2005
Homo sapiens
Manually annotated by BRENDA team
Jo, J.Y.; Gonzalez de Mejia, E.; Lila, M.A.
Effects of grape cell culture extracts on human topoisomerase II catalytic activity and characterization of active fractions
J. Agric. Food Chem.
53
2489-2498
2005
Homo sapiens
Manually annotated by BRENDA team
Vaughn, J.; Huang, S.; Wessel, I.; Sorensen, T.K.; Hsieh, T.; Jensen, L.H.; Jensen, P.B.; Sehested, M.; Nitiss, J.L.
Stability of the topoisomerase II closed clamp conformation may influence DNA-stimulated ATP hydrolysis
J. Biol. Chem.
280
11920-11929
2005
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
McClendon, A.K.; Rodriguez, A.C.; Osheroff, N.
Human topoisomerase IIalpha rapidly relaxes positively supercoiled DNA: implications for enzyme action ahead of replication forks
J. Biol. Chem.
280
39337-39345
2005
Homo sapiens
Manually annotated by BRENDA team
Sakaguchi, A.; Kikuchi, A.
Functional compatibility between isoform alpha and beta of type II DNA topoisomerase
J. Cell Sci.
117
1047-1054
2004
Homo sapiens
Manually annotated by BRENDA team
Christmann-Franck, S.; Bertrand, H.O.; Goupil-Lamy, A.; der Garabedian, P.A.; Mauffret, O.; Hoffmann, R.; Fermandjian, S.
Structure-based virtual screening: an application to human topoisomerase II alpha
J. Med. Chem.
47
6840-6853
2004
Homo sapiens (P11388), Homo sapiens
Manually annotated by BRENDA team
Walker, J.; Saravia, N.G.
Inhibition of Leishmania donovani promastigote DNA topoisomerase I and human monocyte DNA topoisomerases I and II by antimonial drugs and classical antitopoisomerase agents
J. Parasitol.
90
1155-1162
2004
Homo sapiens
Manually annotated by BRENDA team
Carpenter, A.J.; Porter, A.C.
Construction, characterization, and complementation of a conditional-lethal DNA topoisomerase IIalpha mutant human cell line
Mol. Biol. Cell
15
5700-5711
2004
Homo sapiens
Manually annotated by BRENDA team
Zhou, Z.; Guan, H.; Kleinerman, E.S.
E1A specifically enhances sensitivity to topoisomerase IIa targeting anticancer drug by up-regulating the promoter activity
Mol. Cancer Res.
3
271-275
2005
Homo sapiens
Manually annotated by BRENDA team
Fellows, I.M.; Schwaebe, M.; Dexheimer, T.S.; Vankayalapati, H.; Gleason-Guzman, M.; Whitten, J.P.; Hurley, L.H.
Determination of the importance of the stereochemistry of psorospermin in topoisomerase II-induced alkylation of DNA and in vitro and in vivo biological activity
Mol. Cancer Ther.
4
1729-1739
2005
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Skladanowski, A.; Come, M.G.; Sabisz, M.; Escargueil, A.E.; Larsen, A.K.
Down-regulation of DNA topoisomerase IIalpha leads to prolonged cell cycle transit in G2 and early M phases and increased survival to microtubule-interacting agents
Mol. Pharmacol.
68
625-634
2005
Homo sapiens
Manually annotated by BRENDA team
Potter, A.J.; Rabinovitch, P.S.
The cell cycle phases of DNA damage and repair initiated by topoisomerase II-targeting chemotherapeutic drugs
Mutat. Res.
572
27-44
2005
Homo sapiens
Manually annotated by BRENDA team
Suda, N.; Ito, Y.; Imai, T.; Kikumori, T.; Kikuchi, A.; Nishiyama, Y.; Yoshida, S.; Suzuki, M.
The alpha4 residues of human DNA topoisomerase IIalpha function in enzymatic activity and anticancer drug sensitivity
Nucleic Acids Res.
32
1767-1773
2004
Homo sapiens
Manually annotated by BRENDA team
Montaner, B.; Castillo-Avila, W.; Martinell, M.; Ollinger, R.; Aymami, J.; Giralt, E.; Perez-Tomas, R.
DNA interaction and dual topoisomerase I and II inhibition properties of the anti-tumor drug prodigiosin
Toxicol. Sci.
85
870-879
2005
Homo sapiens
Manually annotated by BRENDA team
Kondapi, A.K.; Satyanarayana, N.; Saikrishna, A.D.
A study of the topoisomerase II activity in HIV-1 replication using the ferrocene derivatives as probes
Arch. Biochem. Biophys.
450
123-132
2006
Homo sapiens
Manually annotated by BRENDA team
Mandraju, R.K.; Kannapiran, P.; Kondapi, A.K.
Distinct roles of Topoisomerase II isoforms: DNA damage accelerating alpha, double strand break repair promoting beta
Arch. Biochem. Biophys.
470
27-34
2008
Homo sapiens
Manually annotated by BRENDA team
Vispe, S.; Vandenberghe, I.; Robin, M.; Annereau, J.P.; Creancier, L.; Pique, V.; Galy, J.P.; Kruczynski, A.; Barret, J.M.; Bailly, C.
Novel tetra-acridine derivatives as dual inhibitors of topoisomerase II and the human proteasome
Biochem. Pharmacol.
73
1863-1872
2007
Homo sapiens
Manually annotated by BRENDA team
Bender, R.P.; Lehmler, H.J.; Robertson, L.W.; Ludewig, G.; Osheroff, N.
Polychlorinated biphenyl quinone metabolites poison human topoisomerase IIalpha: altering enzyme function by blocking the N-terminal protein gate
Biochemistry
45
10140-10152
2006
Homo sapiens
Manually annotated by BRENDA team
Bender, R.P.; Ham, A.J.; Osheroff, N.
Quinone-induced enhancement of DNA cleavage by human topoisomerase IIalpha: adduction of cysteine residues 392 and 405
Biochemistry
46
2856-2864
2007
Homo sapiens
Manually annotated by BRENDA team
Bandele, O.J.; Osheroff, N.
Bioflavonoids as poisons of human topoisomerase II alpha and II beta
Biochemistry
46
6097-6108
2007
Homo sapiens
Manually annotated by BRENDA team
Wilstermann, A.M.; Bender, R.P.; Godfrey, M.; Choi, S.; Anklin, C.; Berkowitz, D.B.; Osheroff, N.; Graves, D.E.
Topoisomerase II - drug interaction domains: identification of substituents on etoposide that interact with the enzyme
Biochemistry
46
8217-8225
2007
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Morant-Lhomel, A.; Rene, B.; Zargarian, L.; Troalen, F.; Mauffret, O.; Fermandjian, S.
Self-association and DNA binding properties of the human topoisomerase IIA alpha 2HTH module
Biochimie
88
253-263
2006
Homo sapiens
Manually annotated by BRENDA team
Yamada, M.; Hayashi, K.; Ikeda, S.; Tsutsui, K.; Tsutsui, K.; Ito, T.; Iinuma, M.; Nozaki, H.
Inhibitory activity of plant stilbene oligomers against DNA topoisomerase II
Biol. Pharm. Bull.
29
1504-1507
2006
Homo sapiens
Manually annotated by BRENDA team
Rhee, H.K.; Park, H.J.; Lee, S.K.; Lee, C.O.; Choo, H.Y.
Synthesis, cytotoxicity, and DNA topoisomerase II inhibitory activity of benzofuroquinolinediones
Bioorg. Med. Chem.
15
1651-1658
2007
Homo sapiens
Manually annotated by BRENDA team
Basnet, A.; Thapa, P.; Karki, R.; Na, Y.; Jahng, Y.; Jeong, B.S.; Jeong, T.C.; Lee, C.S.; Lee, E.S.
2,4,6-Trisubstituted pyridines: Synthesis, topoisomerase I and II inhibitory activity, cytotoxicity, and structure-activity relationship
Bioorg. Med. Chem.
15
4351-4359
2007
Homo sapiens
Manually annotated by BRENDA team
Bender, R.P.; Osheroff, N.
Mutation of cysteine residue 455 to alanine in human topoisomerase IIalpha confers hypersensitivity to quinones: enhancing DNA scission by closing the N-terminal protein gate
Chem. Res. Toxicol.
20
975-981
2007
Homo sapiens
Manually annotated by BRENDA team
Cortazar, T.M.; Coombs, G.H.; Walker, J.
Leishmania panamensis: comparative inhibition of nuclear DNA topoisomerase II enzymes from promastigotes and human macrophages reveals anti-parasite selectivity of fluoroquinolones, flavonoids and pentamidine
Exp. Parasitol.
116
475-482
2007
Homo sapiens, Leishmania panamensis
Manually annotated by BRENDA team
Jo, J.Y.; Gonzalez de Mejia, E.; Lila, M.A.
Catalytic inhibition of human DNA topoisomerase II by interactions of grape cell culture polyphenols
J. Agric. Food Chem.
54
2083-2087
2006
Homo sapiens
Manually annotated by BRENDA team
Yoshida, K.; Yamaguchi, T.; Shinagawa, H.; Taira, N.; Nakayama, K.I.; Miki, Y.
Protein kinase C delta activates topoisomerase IIalpha to induce apoptotic cell death in response to DNA damage
Mol. Cell. Biol.
26
3414-3431
2006
Homo sapiens
Manually annotated by BRENDA team
Leontiou, C.; Lakey, J.H.; Lightowlers, R.; Turnbull, R.M.; Austin, C.A.
Mutation P732L in human DNA topoisomerase IIbeta abolishes DNA cleavage in the presence of calcium and confers drug resistance
Mol. Pharmacol.
69
130-139
2006
Homo sapiens (Q02880), Homo sapiens
Manually annotated by BRENDA team
Hu, C.X.; Zuo, Z.L.; Xiong, B.; Ma, J.G.; Geng, M.Y.; Lin, L.P.; Jiang, H.L.; Ding, J.
Salvicine functions as novel topoisomerase II poison by binding to ATP pocket
Mol. Pharmacol.
70
1593-1601
2006
Homo sapiens (P11388), Homo sapiens
Manually annotated by BRENDA team
Duca, M.; Guianvarch, D.; Oussedik, K.; Halby, L.; Garbesi, A.; Dauzonne, D.; Monneret, C.; Osheroff, N.; Giovannangeli, C.; Arimondo, P.B.
Molecular basis of the targeting of topoisomerase II-mediated DNA cleavage by VP16 derivatives conjugated to triplex-forming oligonucleotides
Nucleic Acids Res.
34
1900-1911
2006
Homo sapiens
Manually annotated by BRENDA team
Linka, R.M.; Porter, A.C.; Volkov, A.; Mielke, C.; Boege, F.; Christensen, M.O.
C-terminal regions of topoisomerase IIalpha and IIbeta determine isoform-specific functioning of the enzymes in vivo
Nucleic Acids Res.
35
3810-3822
2007
Homo sapiens
Manually annotated by BRENDA team
Stros, M.; Bacikova, A.; Polanska, E.; Stokrova, J.; Strauss, F.
HMGB1 interacts with human topoisomerase IIalpha and stimulates its catalytic activity
Nucleic Acids Res.
35
5001-5013
2007
Homo sapiens
Manually annotated by BRENDA team
Choi, J.Y.; Seo, C.S.; Zheng, M.S.; Lee, C.S.; Son, J.K.
Topoisomerase I and II inhibitory constituents from the bark of Tilia amurensis
Arch. Pharm. Res.
31
1413-1418
2008
Homo sapiens
Manually annotated by BRENDA team
Kim, J.S.; Rhee, H.K.; Park, H.J.; Lee, S.K.; Lee, C.O.; Park Choo, H.Y.
Synthesis of 1-/2-substituted-[1,2,3]triazolo[4,5-g]phthalazine-4,9-diones and evaluation of their cytotoxicity and topoisomerase II inhibition
Bioorg. Med. Chem.
16
4545-4550
2008
Homo sapiens
Manually annotated by BRENDA team
Filosa, R.; Peduto, A.; Micco, S.D.; Caprariis, P.; Festa, M.; Petrella, A.; Capranico, G.; Bifulco, G.
Molecular modelling studies, synthesis and biological activity of a series of novel bisnaphthalimides and their development as new DNA topoisomerase II inhibitors
Bioorg. Med. Chem.
17
13-24
2009
Homo sapiens
Manually annotated by BRENDA team
Chene, P.; Rudloff, J.; Schoepfer, J.; Furet, P.; Meier, P.; Qian, Z.; Schlaeppi, J.M.; Schmitz, R.; Radimerski, T.
Catalytic inhibition of topoisomerase II by a novel rationally designed ATP-competitive purine analogue
BMC Chem. Biol.
9
1-16
2009
Homo sapiens
Manually annotated by BRENDA team
Reymann, S.; Borlak, J.
Topoisomerase II inhibition involves characteristic chromosomal expression patterns
BMC Genomics
9
324
2008
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Terry, S.Y.; Riches, A.C.; Bryant, P.E.
A role for topoisomerase II alpha in the formation of radiation-induced chromatid breaks
Br. J. Cancer
99
670-674
2008
Homo sapiens
Manually annotated by BRENDA team
Woo, S.; Kang, D.; Kim, J.; Lee, C.; Lee, E.; Jahng, Y.; Kwon, Y.; Na, Y.
Synthesis, cytotoxicity and topoisomerase II inhibition study of new thioxanthone analogues
Bull. Korean Chem. Soc.
29
471-474
2008
Homo sapiens
-
Manually annotated by BRENDA team
Agostinho, M.; Santos, V.; Ferreira, F.; Costa, R.; Cardoso, J.; Pinheiro, I.; Rino, J.; Jaffray, E.; Hay, R.T.; Ferreira, J.
Conjugation of human topoisomerase 2 alpha with small ubiquitin-like modifiers 2/3 in response to topoisomerase inhibitors: cell cycle stage and chromosome domain specificity
Cancer Res.
68
2409-2418
2008
Homo sapiens
Manually annotated by BRENDA team
Bandele, O.J.; Clawson, S.J.; Osheroff, N.
Dietary polyphenols as topoisomerase II poisons: B ring and C ring substituents determine the mechanism of enzyme-mediated DNA cleavage enhancement
Chem. Res. Toxicol.
21
1253-1260
2008
Homo sapiens
Manually annotated by BRENDA team
Bandele, O.J.; Osheroff, N.
(-)-Epigallocatechin gallate, a major constituent of green tea, poisons human type II topoisomerases
Chem. Res. Toxicol.
21
936-943
2008
Homo sapiens
Manually annotated by BRENDA team
Quan, Z.W.; Yue, J.N.; Li, J.Y.; Qin, Y.Y.; Guo, R.S.; Li, S.G.
Somatostatin elevates topoisomerase II alpha and enhances the cytotoxic effect of doxorubicin on gallbladder cancer cells
Chemotherapy
54
431-437
2008
Homo sapiens
Manually annotated by BRENDA team
Di Leo, A.; Biganzoli, L.; Claudino, W.; Licitra, S.; Pestrin, M.; Larsimont, D.
Topoisomerase II alpha as a marker predicting anthracyclines activity in early breast cancer patients: ready for the primetime?
Eur. J. Cancer
44
2791-2798
2008
Homo sapiens
Manually annotated by BRENDA team
Lopez-Lazaro, M.; Willmore, E.; Elliott, S.L.; Austin, C.A.
Selenite induces topoisomerase I and II-DNA complexes in K562 leukemia cells
Int. J. Cancer
123
2217-2221
2008
Homo sapiens
Manually annotated by BRENDA team
Wang, W.; Rupasinghe, S.G.; Schuler, M.A.; Gonzalez de Mejia, E.
Identification and characterization of topoisomerase II inhibitory peptides from soy protein hydrolysates
J. Agric. Food Chem.
56
6267-6277
2008
Homo sapiens
Manually annotated by BRENDA team
Pritchard, K.I.; Messersmith, H.; Elavathil, L.; Trudeau, M.; OMalley, F.; Dhesy-Thind, B.
HER-2 and topoisomerase II as predictors of response to chemotherapy
J. Clin. Oncol.
26
736-744
2008
Homo sapiens
Manually annotated by BRENDA team
Goodell, J.R.; Ougolkov, A.V.; Hiasa, H.; Kaur, H.; Remmel, R.; Billadeau, D.D.; Ferguson, D.M.
Acridine-based agents with topoisomerase II activity inhibit pancreatic cancer cell proliferation and induce apoptosis
J. Med. Chem.
51
179-182
2008
Homo sapiens
Manually annotated by BRENDA team
Ryckebusch, A.; Garcin, D.; Lansiaux, A.; Goossens, J.F.; Baldeyrou, B.; Houssin, R.; Bailly, C.; Henichart, J.P.
Synthesis, cytotoxicity, DNA interaction, and topoisomerase II inhibition properties of novel indeno[2,1-c]quinolin-7-one and indeno[1,2-c]isoquinolin-5,11-dione derivatives
J. Med. Chem.
51
3617-3629
2008
Homo sapiens
Manually annotated by BRENDA team
Jimenez-Alonso, S.; Orellana, H.C.; Estevez-Braun, A.; Ravelo, A.G.; Perez-Sacau, E.; Machin, F.
Design and synthesis of a novel series of pyranonaphthoquinones as topoisomerase II catalytic inhibitors
J. Med. Chem.
51
6761-6772
2008
Homo sapiens (P11388), Homo sapiens
Manually annotated by BRENDA team
Stuchinskaya, T.; Mitchenall, L.A.; Schoeffler, A.J.; Corbett, K.D.; Berger, J.M.; Bates, A.D.; Maxwell, A.
How do type II topoisomerases use ATP hydrolysis to simplify DNA topology beyond equilibrium? Investigating the relaxation reaction of nonsupercoiling type II topoisomerases
J. Mol. Biol.
385
1397-1408
2008
Saccharomyces cerevisiae, Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Lin, Y.C.; Li, J.; Irwin, C.R.; Jenkins, H.; DeLange, L.; Evans, D.H.
Vaccinia virus DNA ligase recruits cellular topoisomerase II to sites of viral replication and assembly
J. Virol.
82
5922-5932
2008
Homo sapiens
Manually annotated by BRENDA team
Park, S.W.; Parrott, A.M.; Fritz, D.T.; Park, Y.; Mathews, M.B.; Lee, C.G.
Regulation of the catalytic function of topoisomerase II alpha through association with RNA
Nucleic Acids Res.
36
6080-6090
2008
Homo sapiens (P11388)
Manually annotated by BRENDA team
Meczes, E.L.; Gilroy, K.L.; West, K.L.; Austin, C.A.
The impact of the human DNA topoisomerase II C-terminal domain on activity
PLoS ONE
3
e1754
2008
Homo sapiens
Manually annotated by BRENDA team
Huang, C.P.; Fang, W.H.; Lin, L.I.; Chiou, R.Y.; Kan, L.S.; Chi, N.H.; Chen, Y.R.; Lin, T.Y.; Lin, S.B.
Anticancer activity of botanical alkyl hydroquinones attributed to topoisomerase II poisoning
Toxicol. Appl. Pharmacol.
227
331-338
2008
Homo sapiens
Manually annotated by BRENDA team
Kik, K.; Studzian, K.; Wasowska-Lukawska, M.; Oszczapowicz, I.; Szmigiero, L.
Cytotoxicity and inhibitory properties against topoisomerase II of doxorubicin and its formamidine derivatives
Acta Biochim. Pol.
56
135-142
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Pham, M.H.; Kondapalli, N.; Reckord, C.L.; Foglesong, P.D.
Interleukin-2 induces the activities of DNA topoisomerase I and DNA topoisomerase II in HuT 78 cells
Biochem. Biophys. Res. Commun.
390
577-580
2009
Homo sapiens
Manually annotated by BRENDA team
Deweese, J.E.; Osheroff, N.
Coordinating the two protomer active sites of human topoisomerase IIalpha: nicks as topoisomerase II poisons
Biochemistry
48
1439-1441
2009
Homo sapiens
Manually annotated by BRENDA team
Furet, P.; Schoepfer, J.; Radimerski, T.; Chene, P.
Discovery of a new class of catalytic topoisomerase II inhibitors targeting the ATP-binding site by structure based design. Part I
Bioorg. Med. Chem. Lett.
19
4014-4017
2009
Homo sapiens
Manually annotated by BRENDA team
Galvez-Peralta, M.; Hackbarth, J.S.; Flatten, K.S.; Kaufmann, S.H.; Hiasa, H.; Xing, C.; Ferguson, D.M.
On the role of topoisomerase I in mediating the cytotoxicity of 9-aminoacridine-based anticancer agents
Bioorg. Med. Chem. Lett.
19
4459-4462
2009
Homo sapiens
Manually annotated by BRENDA team
Cho, H.J.; Jung, M.J.; Kwon, Y.; Na, Y.
Oxiranylmethyloxy or thiiranylmethyloxy-azaxanthones and -acridone analogues as potential topoisomerase I inhibitors
Bioorg. Med. Chem. Lett.
19
6766-6769
2009
Homo sapiens
Manually annotated by BRENDA team
Wang, P.; Ownby, S.; Zhang, Z.; Yuan, W.; Li, S.
Cytotoxicity and inhibition of DNA topoisomerase I of polyhydroxylated triterpenoids and triterpenoid glycosides
Bioorg. Med. Chem. Lett.
20
2790-2796
2010
Homo sapiens
Manually annotated by BRENDA team
Sperry, J.; Lorenzo-Castrillejo, I.; Brimble, M.A.; Machin, F.
Pyranonaphthoquinone derivatives of eleutherin, ventiloquinone L, thysanone and nanaomycin A possessing a diverse topoisomerase II inhibition and cytotoxicity spectrum
Bioorg. Med. Chem.
17
7131-7137
2009
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Thapa, P.; Karki, R.; Thapa, U.; Jahng, Y.; Jung, M.J.; Nam, J.M.; Na, Y.; Kwon, Y.; Lee, E.S.
2-Thienyl-4-furyl-6-aryl pyridine derivatives: synthesis, topoisomerase I and II inhibitory activity, cytotoxicity, and structure-activity relationship study
Bioorg. Med. Chem.
18
377-386
2010
Homo sapiens
Manually annotated by BRENDA team
Leone, S.; Cornetta, T.; Basso, E.; Cozzi, R.
Resveratrol induces DNA double-strand breaks through human topoisomerase II interaction
Cancer Lett.
295
167-172
2010
Homo sapiens
Manually annotated by BRENDA team
Shuai, L.; Wang, S.; Zhang, L.; Fu, B.; Zhou, X.
Cationic porphyrins and analogues as new DNA topoisomerase I and II inhibitors
Chem. Biodivers.
6
827-837
2009
Homo sapiens
Manually annotated by BRENDA team
Mondrala, S.; Eastmond, D.A.
Topoisomerase II inhibition by the bioactivated benzene metabolite hydroquinone involves multiple mechanisms
Chem. Biol. Interact.
184
259-268
2010
Homo sapiens
Manually annotated by BRENDA team
Chen, Z.; Liang, X.; Zhang, H.; Xie, H.; Liu, J.; Xu, Y.; Zhu, W.; Wang, Y.; Wang, X.; Tan, S.; Kuang, D.; Qian, X.
A new class of naphthalimide-based antitumor agents that inhibit topoisomerase II and induce lysosomal membrane permeabilization and apoptosis
J. Med. Chem.
53
2589-2600
2010
Homo sapiens
Manually annotated by BRENDA team
Hu, C.; Xu, D.; Du, W.; Qian, S.; Wang, L.; Lou, J.; He, Q.; Yang, B.; Hu, Y.
Novel 4 beta-anilino-podophyllotoxin derivatives: design synthesis and biological evaluation as potent DNA-topoisomerase II poisons and anti-MDR agents
Mol. Biosyst.
6
410-420
2010
Homo sapiens
Manually annotated by BRENDA team
Nitiss, J.L.
DNA topoisomerase II and its growing repertoire of biological functions
Nat. Rev. Cancer
9
327-337
2009
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Collins, T.R.; Hammes, G.G.; Hsieh, T.S.
Analysis of the eukaryotic topoisomerase II DNA gate: a single-molecule FRET and structural perspective
Nucleic Acids Res.
37
712-720
2009
Homo sapiens, Saccharomyces cerevisiae (P06786)
Manually annotated by BRENDA team
Pitts, S.L.; Jablonksy, M.J.; Duca, M.; Dauzonne, D.; Monneret, C.; Arimondo, P.B.; Anklin, C.; Graves, D.E.; Osheroff, N.
Contributions of the D-ring to the activity of etoposide against human topoisomerase IIalpha: potential interactions with DNA in the ternary enzyme-drug-DNA complex
Biochemistry
50
5058-5066
2011
Homo sapiens
Manually annotated by BRENDA team
Na, Y.; Nam, J.M.
Synthesis and topoisomerase II inhibitory and cytotoxic activity of oxiranylmethoxy- and thiiranylmethoxy-chalcone derivatives
Bioorg. Med. Chem. Lett.
21
211-214
2011
Homo sapiens
Manually annotated by BRENDA team
Ahn, G.; Schifano-Faux, N.; Goossens, J.F.; Baldeyrou, B.; Couture, A.; Grandclaudon, P.; Lansiaux, A.; Ryckebusch, A.
Synthesis, cytotoxicity and topoisomerase inhibition properties of multifarious aminoalkylated indeno[1,2-c]isoquinolin-5,11-diones
Bioorg. Med. Chem. Lett.
21
2259-2263
2011
Homo sapiens
Manually annotated by BRENDA team
Karki, R.; Thapa, P.; Kang, M.J.; Jeong, T.C.; Nam, J.M.; Kim, H.L.; Na, Y.; Cho, W.J.; Kwon, Y.; Lee, E.S.
Synthesis, topoisomerase I and II inhibitory activity, cytotoxicity, and structure-activity relationship study of hydroxylated 2,4-diphenyl-6-aryl pyridines
Bioorg. Med. Chem.
18
3066-3077
2010
Homo sapiens
Manually annotated by BRENDA team
Shi, W.; Marcus, S.L.; Lowary, T.L.
Cytotoxicity and topoisomerase I/II inhibition of glycosylated 2-phenyl-indoles, 2-phenyl-benzo[b]thiophenes and 2-phenyl-benzo[b]furans
Bioorg. Med. Chem.
19
603-612
2011
Homo sapiens
Manually annotated by BRENDA team
Kundukad, B.; van der Maarel, J.R.
Control of the flow properties of DNA by topoisomerase II and its targeting inhibitor
Biophys. J.
99
1906-1915
2010
Homo sapiens
Manually annotated by BRENDA team
Jeong, B.; Choi, H.; Thapa, P.; Karki, R.; Lee, E.; Nam, J.; Na, Y.; Ha, E.; Kwon, Y.; Lee, E.
Synthesis, topoisomerase I and II inhibitory activity, cytotoxicity, and structure-activity relationship study of rigid analogues of 2,4,6-trisubstituted pyridine containing 5,6-dihydrobenzo[h]quinoline moiety
Bull. Korean Chem. Soc.
32
303-306
2011
Homo sapiens
-
Manually annotated by BRENDA team
Wang, G.; Huang, H.; Gao, J.; Chen, P.; You, W.; Wu, B.; Wang, M.
Tissue microarray analysis of topoisomerase IIalpha protein in gastric adenocarcinomas: histogenetic and prognostic implications
Cancer Genomics Proteomics
8
127-133
2011
Homo sapiens
Manually annotated by BRENDA team
Xie, P.
Dynamics of strand passage catalyzed by topoisomerase II
Eur. Biophys. J.
39
1251-1259
2010
Homo sapiens
Manually annotated by BRENDA team
Hajbi, Y.; Neagoie, C.; Biannic, B.; Chilloux, A.; Vedrenne, E.; Baldeyrou, B.; Bailly, C.; Merour, J.Y.; Rosca, S.; Routier, S.; Lansiaux, A.
Synthesis and biological activities of new furo[3,4-b]carbazoles: potential topoisomerase II inhibitors
Eur. J. Med. Chem.
45
5428-5437
2010
Homo sapiens
Manually annotated by BRENDA team
Jun, K.Y.; Lee, E.Y.; Jung, M.J.; Lee, O.H.; Lee, E.S.; Park Choo, H.Y.; Na, Y.; Kwon, Y.
Synthesis, biological evaluation, and molecular docking study of 3-(3-heteroatom substituted-2-hydroxy-1-propyloxy) xanthone analogues as novel topoisomerase IIalpha catalytic inhibitor
Eur. J. Med. Chem.
46
1964-1971
2011
Homo sapiens
Manually annotated by BRENDA team
Thapa, U.; Thapa, P.; Karki, R.; Yun, M.; Choi, J.H.; Jahng, Y.; Lee, E.; Jeon, K.H.; Na, Y.; Ha, E.M.; Cho, W.J.; Kwon, Y.; Lee, E.S.
Synthesis of 2,4-diaryl chromenopyridines and evaluation of their topoisomerase I and II inhibitory activity, cytotoxicity, and structure-activity relationship
Eur. J. Med. Chem.
46
3201-3209
2011
Homo sapiens
Manually annotated by BRENDA team
Huang, H.; Chen, Q.; Ku, X.; Meng, L.; Lin, L.; Wang, X.; Zhu, C.; Wang, Y.; Chen, Z.; Li, M.; Jiang, H.; Chen, K.; Ding, J.; Liu, H.
A series of alpha-heterocyclic carboxaldehyde thiosemicarbazones inhibit topoisomerase IIalpha catalytic activity
J. Med. Chem.
53
3048-3064
2010
Homo sapiens
Manually annotated by BRENDA team
Baviskar, A.T.; Madaan, C.; Preet, R.; Mohapatra, P.; Jain, V.; Agarwal, A.; Guchhait, S.K.; Kundu, C.N.; Banerjee, U.C.; Bharatam, P.V.
N-fused imidazoles as novel anticancer agents that inhibit catalytic activity of topoisomerase IIalpha and induce apoptosis in G1/S phase
J. Med. Chem.
54
5013-5030
2011
Homo sapiens (P11388), Homo sapiens
Manually annotated by BRENDA team
Arjmand, F.; Muddassir, M.
Design and synthesis of heterobimetallic topoisomerase I and II inhibitor complexes: In vitro DNA binding, interaction with 5'-GMP and 5'-TMP and cleavage studies
J. Photochem. Photobiol. B
101
37-46
2010
Homo sapiens
Manually annotated by BRENDA team
Heng, X.; Le, W.D.
The function of DNA topoisomerase IIbeta in neuronal development
Neurosci. Bull.
26
411-416
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Cowell, I.G.; Papageorgiou, N.; Padget, K.; Watters, G.P.; Austin, C.A.
Histone deacetylase inhibition redistributes topoisomerase IIbeta from heterochromatin to euchromatin
Nucleus
2
61-71
2011
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Gilroy, K.L.; Austin, C.A.
The impact of the C-terminal domain on the interaction of human DNA topoisomerase II alpha and beta with DNA
PLoS ONE
6
e14693
2011
Homo sapiens
Manually annotated by BRENDA team
Singh, P.K.; Chan, P.F.; Hibbs, M.J.; Vazquez, M.J.; Segura, D.C.; Thomas, D.A.; Theobald, A.J.; Gallagher, K.T.; Hassan, N.J.
High-yield production and characterization of biologically active GST-tagged human topoisomerase IIalpha protein in insect cells for the development of a high-throughput assay
Protein Expr. Purif.
76
165-172
2011
Homo sapiens (P11388), Homo sapiens
Manually annotated by BRENDA team
Grozav, A.G.; Willard, B.B.; Kozuki, T.; Chikamori, K.; Micluta, M.A.; Petrescu, A.J.; Kinter, M.; Ganapathi, R.; Ganapathi, M.K.
Tyrosine 656 in topoisomerase IIbeta is important for the catalytic activity of the enzyme: identification based on artifactual +80-Da modification at this site
Proteomics
11
829-842
2011
Homo sapiens
Manually annotated by BRENDA team
Ju, B.
A topoisomerase beta-mediated dsDNA break required for regulated transcription
Science
332
1798-1802
2011
Homo sapiens
-
Manually annotated by BRENDA team
Midura-Nowaczek, K.; Purwin, M.; Markowska, A.; Drozdowska, D.; Bruzgo, M.
Effect of short peptides containing lysine and epsilon-aminocaproic acid on fibrinolytic activity of plasmin and topoisomerase II action on supercoiled DNA
Acta Pol. Pharm.
70
431-434
2013
Homo sapiens
Manually annotated by BRENDA team
Sangthong, S.; Krusong, K.; Ngamrojanavanich, N.; Vilaivan, T.; Puthong, S.; Chandchawan, S.; Muangsin, N.
Synthesis of rotenoid derivatives with cytotoxic and topoisomerase II inhibitory activities
Bioorg. Med. Chem. Lett.
21
4813-4818
2011
Homo sapiens
Manually annotated by BRENDA team
Zhao, W.; Chen, L.; Li, H.M.; Wang, D.J.; Li, D.S.; Chen, T.; Yuan, Z.P.; Tang, Y.J.
A rational design strategy of the novel topoisomerase II inhibitors for the synthesis of the 4-O-(2-pyrazinecarboxylic)-4-demethylepipodophyllotoxin with antitumor activity by diminishing the relaxation reaction of topoisomerase II-DNA decatenation
Bioorg. Med. Chem.
22
2998-3007
2014
Homo sapiens
Manually annotated by BRENDA team
Senarisoy, M.; Canturk, P.; Zencir, S.; Baran, Y.; Topcu, Z.
Gossypol interferes with both type I and type II topoisomerase activities without generating strand breaks
Cell Biochem. Biophys.
66
199-204
2013
Homo sapiens
Manually annotated by BRENDA team
Lin, T.Y.; Huang, C.P.; Au, L.C.; Chang, Y.W.; Hu, C.Y.; Lin, S.B.
A cysteine-reactive alkyl hydroquinone modifies topoisomerase IIalpha, enhances DNA breakage, and induces apoptosis in cancer cells
Chem. Res. Toxicol.
25
2340-2351
2012
Homo sapiens
Manually annotated by BRENDA team
Alam, S.; Khan, F.
QSAR and docking studies on xanthone derivatives for anticancer activity targeting DNA topoisomerase IIalpha
Drug Des. Devel. Ther.
8
183-195
2014
Homo sapiens
Manually annotated by BRENDA team
Qi, X.; Hou, S.; Lepp, A.; Li, R.; Basir, Z.; Lou, Z.; Chen, G.
Phosphorylation and stabilization of topoisomerase IIalpha protein by p38gamma mitogen-activated protein kinase sensitize breast cancer cells to its poisons
J. Biol. Chem.
286
35883-35890
2011
Homo sapiens
Manually annotated by BRENDA team
Ponder, J.; Yoo, B.H.; Abraham, A.D.; Li, Q.; Ashley, A.K.; Amerin, C.L.; Zhou, Q.; Reid, B.G.; Reigan, P.; Hromas, R.; Nickoloff, J.A.; LaBarbera, D.V.
Neoamphimedine circumvents metnase-enhanced DNA topoisomerase IIalpha activity through ATP-competitive inhibition
Mar. Drugs
9
2397-2408
2011
Homo sapiens
Manually annotated by BRENDA team
Esteves-Souza, A.; Rodrigues-Santos, C.E.; Del Cistia, C.d.e..N.; Silva, D.R.; Santanna, C.M.; Echevarria, A.
Solvent-free synthesis, DNA-topoisomerase II activity and molecular docking study of new asymmetrically N,N-substituted ureas
Molecules
17
12882-12894
2012
Homo sapiens
Manually annotated by BRENDA team
Tian, Q.T.; Ding, C.Y.; Song, S.S.; Wang, Y.Q.; Zhang, A.; Miao, Z.H.
New tanshinone I derivatives S222 and S439 similarly inhibit topoisomerase I/II but reveal different p53-dependency in inducing G2/M arrest and apoptosis
Biochem. Pharmacol.
154
255-264
2018
Homo sapiens
Manually annotated by BRENDA team
Pogorelcnik, B.; Janezic, M.; Sosic, I.; Gobec, S.; Solmajer, T.; Perdih, A.
4,6-Substituted-1,3,5-triazin-2(1H)-ones as monocyclic catalytic inhibitors of human DNA topoisomerase IIalpha targeting the ATP binding site
Bioorg. Med. Chem.
23
4218-4229
2015
Homo sapiens
Manually annotated by BRENDA team
de Oliveira Figueiredo, P.; Perdomo, R.T.; Garcez, F.R.; de Fatima Cepa Matos, M.; de Carvalho, J.E.; Garcez, W.S.
Further constituents of Galianthe thalictroides (Rubiaceae) and inhibition of DNA topoisomerases I and IIalpha by its cytotoxic beta-carboline alkaloids
Bioorg. Med. Chem. Lett.
24
1358-1361
2014
Homo sapiens (P11388)
Manually annotated by BRENDA team
Pogorelcnik, B.; Brvar, M.; Zajc, I.; Filipic, M.; Solmajer, T.; Perdih, A.
Monocyclic 4-amino-6-(phenylamino)-1,3,5-triazines as inhibitors of human DNA topoisomerase IIalpha
Bioorg. Med. Chem. Lett.
24
5762-5768
2014
Homo sapiens (P11388)
Manually annotated by BRENDA team
Vann, K.R.; Erguen, Y.; Zencir, S.; Oncuoglu, S.; Osheroff, N.; Topcu, Z.
Inhibition of human DNA topoisomerase IIalpha by two novel ellipticine derivatives
Bioorg. Med. Chem. Lett.
26
1809-1812
2016
Homo sapiens (P11388), Homo sapiens
Manually annotated by BRENDA team
Chen, W.; Shen, Y.; Li, Z.; Zhang, M.; Lu, C.; Shen, Y.
Design and synthesis of 2-phenylnaphthalenoids as inhibitors of DNA topoisomeraseIIalpha and antitumor agents
Eur. J. Med. Chem.
86
782-796
2014
Homo sapiens (P11388)
Manually annotated by BRENDA team
Kumar, A.; Bora, U.
Molecular docking studies of curcumin natural derivatives with DNA topoisomerase I and II-DNA complexes
Interdiscip. Sci. Comput. Life Sci.
6
285-291
2014
Homo sapiens (Q02880)
Manually annotated by BRENDA team
Plech, T.; Kapro?, B.; Paneth, A.; Wujec, M.; Czarnomysy, R.; Bielawska, A.; Bielawski, K.; Trotsko, N.; Ku?mierz, E.; Paneth, P.
Search for human DNA topoisomerase II poisons in the group of 2,5-disubstituted-1,3,4-thiadiazoles
J. Enzyme Inhib. Med. Chem.
30
1021-1026
2015
Homo sapiens
Manually annotated by BRENDA team
Li, H.; Xie, N.; Gleave, M.E.; Dong, X.
Catalytic inhibitors of DNA topoisomerase II suppress the androgen receptor signaling and prostate cancer progression
Oncotarget
6
20474-20484
2015
Homo sapiens
Manually annotated by BRENDA team
Bollimpelli, V.S.; Dholaniya, P.S.; Kondapi, A.K.
Topoisomerase IIbeta and its role in different biological contexts
Arch. Biochem. Biophys.
633
78-84
2017
Homo sapiens
Manually annotated by BRENDA team
Gibson, E.G.; King, M.M.; Mercer, S.L.; Deweese, J.E.
Two-mechanism model for the interaction of etoposide quinone with topoisomerase IIalpha
Chem. Res. Toxicol.
29
1541-1548
2016
Homo sapiens
Manually annotated by BRENDA team
Janezic, M.; Pogorelcnik, B.; Brvar, M.; Solmajer, T.; Perdih, A.
3-substituted-1H-indazoles as catalytic inhibitors of the human DNA topoisomerase IIalpha
ChemistrySelect
2
480-488
2017
Homo sapiens
-
Manually annotated by BRENDA team
Yao, B.L.; Mai, Y.W.; Chen, S.B.; Xie, H.T.; Yao, P.F.; Ou, T.M.; Tan, J.H.; Wang, H.G.; Li, D.; Huang, S.L.; Gu, L.Q.; Huang, Z.S.
Design, synthesis and biological evaluation of novel 7-alkylamino substituted benzo[a]phenazin derivatives as dual topoisomerase I/II inhibitors
Eur. J. Med. Chem.
92
540-553
2015
Homo sapiens (P11388), Homo sapiens
Manually annotated by BRENDA team
Mahalapbutr, P.; Chusuth, P.; Kungwan, N.; Chavasiri, W.; Wolschann, P.; Rungrotmongkol, T.
Molecular recognition of naphthoquinone-containing compounds against human DNA topoisomerase IIalpha ATPase domain A molecular modeling study
J. Mol. Liq.
247
374-385
2017
Homo sapiens (P11388)
-
Manually annotated by BRENDA team
Manohar, M.; Choi, H.W.; Manosalva, P.; Austin, C.A.; Peters, J.E.; Klessig, D.F.
Plant and human MORC proteins have DNA-modifying activities similar to type II topoisomerases, but require one or more additional factors for full activity
Mol. Plant Microbe Interact.
30
87-100
2017
Homo sapiens, Solanum lycopersicum
Manually annotated by BRENDA team
Ziraldo, R.; Hanke, A.; Levene, S.D.
Kinetic pathways of topology simplification by type-II topoisomerases in knotted supercoiled DNA
Nucleic Acids Res.
47
69-84
2019
Homo sapiens
Manually annotated by BRENDA team
Bedez, C.; Lotz, C.; Batisse, C.; Broeck, A.; Stote, R.; Howard, E.; Pradeau-Aubreton, K.; Ruff, M.; Lamour, V.
Post-translational modifications in DNA topoisomerase 2alpha highlight the role of a eukaryote-specific residue in the ATPase domain
Sci. Rep.
8
9272
2018
Homo sapiens (P11388)
-
Manually annotated by BRENDA team