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_:vb391550043 _:vb391550044 _:vb391550045 _:vb391550046 _:vb391550047 _:vb391550032 _:vb391550033 _:vb391550034 _:vb391550035 _:vb391550036 _:vb391550037 _:vb391550038 _:vb391550039 _:vb391550024 _:vb391550025 _:vb391550026 _:vb391550027 _:vb391550028 _:vb391550029 _:vb391550030 _:vb391550031 _:vb391550016 _:vb391550017 _:vb391550018 _:vb391550019 _:vb391550020 _:vb391550021 _:vb391550022 _:vb391550023 _:vb391550072 _:vb391550073 _:vb391550074 _:vb391550075 _:vb391550076 _:vb391550077 _:vb391550078 _:vb391550079 _:vb391550064 _:vb391550065 _:vb391550066 _:vb391550067 _:vb391550068 _:vb391550069 _:vb391550070 _:vb391550071 _:vb391550056 _:vb391550057 _:vb391550058 _:vb391550059 _:vb391550060 _:vb391550061 _:vb391550062 _:vb391550063 _:vb391550048 _:vb391550049 _:vb391550050 _:vb391550051 _:vb391550052 _:vb391550053 _:vb391550054 _:vb391550055 _:vb391550104 _:vb391550105 _:vb391550106 _:vb391550107 _:vb391550108 _:vb391550109 _:vb391550110 _:vb391550111 _:vb391550096 _:vb391550097 _:vb391550098 _:vb391550099 _:vb391550100 _:vb391550101 _:vb391550102 _:vb391550103 _:vb391550088 _:vb391550089 _:vb391550090 _:vb391550091 _:vb391550092 _:vb391550093 _:vb391550094 _:vb391550095 _:vb391550080 _:vb391550081 _:vb391550082 _:vb391550083 _:vb391550084 _:vb391550085 _:vb391550086 _:vb391550087 _:vb391550136 _:vb391550137 _:vb391550138 _:vb391550139 _:vb391550140 _:vb391550141 _:vb391550142 _:vb391550143 _:vb391550128 _:vb391550129 _:vb391550130 _:vb391550131 _:vb391550132 _:vb391550133 _:vb391550134 _:vb391550135 _:vb391550120 _:vb391550121 _:vb391550122 _:vb391550123 _:vb391550124 _:vb391550125 _:vb391550126 _:vb391550127 _:vb391550112 _:vb391550113 _:vb391550114 _:vb391550115 _:vb391550116 _:vb391550117 _:vb391550118 _:vb391550119 _:vb391550168 _:vb391550169 _:vb391550170 _:vb391550171 _:vb391550172 _:vb391550173 _:vb391550174 _:vb391550175 _:vb391550160 _:vb391550161 _:vb391550162 _:vb391550163 _:vb391550164 _:vb391550165 _:vb391550166 _:vb391550167 _:vb391550152 _:vb391550153 _:vb391550154 _:vb391550155 _:vb391550156 _:vb391550157 _:vb391550158 _:vb391550159 _:vb391550144 _:vb391550145 _:vb391550146 _:vb391550147 _:vb391550148 _:vb391550149 _:vb391550150 _:vb391550151 _:vb391550200 _:vb391550201 _:vb391550202 _:vb391550203 _:vb391550204 _:vb391550205 _:vb391550206 _:vb391550207 _:vb391550192 _:vb391550193 _:vb391550194 _:vb391550195 _:vb391550196 _:vb391550197 _:vb391550198 _:vb391550199 _:vb391550184 _:vb391550185 _:vb391550186 _:vb391550187 _:vb391550188 _:vb391550189 _:vb391550190 _:vb391550191 _:vb391550176 _:vb391550177 _:vb391550178 _:vb391550179 _:vb391550180 _:vb391550181 _:vb391550182 _:vb391550183
n2:pmcid: PMC0
bibo:doi: 10.1093%2Fnar%2Fgkn937
n5:contains: _:vb4399425 _:vb4399446 _:vb4399463 _:vb4399380 _:vb4399404 _:vb4399326 _:vb4399344 _:vb4399244 _:vb4399270 _:vb4399183 _:vb4399191 _:vb4399205

Subject Item: _:vb4399183
rdf:type: n5:Section
dc:title: introduction
n5:contains: _:vb4399184 _:vb4399185 _:vb4399186 _:vb4399187 _:vb4399188 _:vb4399189 _:vb4399190

Subject Item: _:vb4399184
rdf:type: n2:Context
rdf:value: For example, while the cell requires DNA polymerases to copy the genetic material, these enzymes insert an incorrect base approximately every 107 nt (>>1<<). Consequently, in the absence of mismatch repair pathways, human DNA polymerases would generate several hundred mutations every round of cell division. Furthermore, while DNA glycosylases initiate base-excision repair pathways, these
n2:mentions: n3:18626473

Subject Item: _:vb4399185
rdf:type: n2:Context
rdf:value: Furthermore, while DNA glycosylases initiate base-excision repair pathways, these enzymes can convert innocuous lesions to abasic sites with far greater mutagenic potential (>>2<<). Finally, while cytochrome P450 enzymes play critical roles in detoxification pathways, they sometimes convert inert xenobiotic chemicals to compounds with mutagenic properties (3).
n2:mentions: n3:18166975

Subject Item: _:vb4399186
rdf:type: n2:Context
rdf:value: Finally, while cytochrome P450 enzymes play critical roles in detoxification pathways, they sometimes convert inert xenobiotic chemicals to compounds with mutagenic properties (>>3<<).
n2:mentions: n3:16584116

Subject Item: _:vb4399187
rdf:type: n2:Context
rdf:value: Of all the enzymes required to sustain cellular growth, topoisomerase II is one of the most dangerous (4–>>8<<). As discussed below, this enzyme unwinds, unknots and untangles the genetic material by generating transient double-stranded breaks in DNA (8–12).
n2:mentions: n3:11340607 n3:10697411 n3:9748584 n3:16857431 n3:17681352

Subject Item: _:vb4399188
rdf:type: n2:Context
rdf:value: As discussed below, this enzyme unwinds, unknots and untangles the genetic material by generating transient double-stranded breaks in DNA (8–>>12<<). Although the cell cannot survive without topoisomerase II, the strand breaks that the enzyme generates have the potential to trigger cell death pathways or chromosomal translocations (8,13).
n2:mentions: n3:12042765 n3:9748506 n3:8811192 n3:17681352

Subject Item: _:vb4399189
rdf:type: n2:Context
rdf:value: Although the cell cannot survive without topoisomerase II, the strand breaks that the enzyme generates have the potential to trigger cell death pathways or chromosomal translocations (>>8<<,13).
n2:mentions: n3:17681352

Subject Item: _:vb4399190
rdf:type: n2:Context
rdf:value: Although the cell cannot survive without topoisomerase II, the strand breaks that the enzyme generates have the potential to trigger cell death pathways or chromosomal translocations (8,>>13<<).
n2:mentions: n3:9748575

Subject Item: _:vb4399191
rdf:type: n5:Section
dc:title: dna topology
n5:contains: _:vb4399200 _:vb4399201 _:vb4399202 _:vb4399203 _:vb4399204 _:vb4399192 _:vb4399193 _:vb4399194 _:vb4399195 _:vb4399196 _:vb4399197 _:vb4399198 _:vb4399199

Subject Item: _:vb4399192
rdf:type: n2:Context
rdf:value: Because the genetic material is anchored to the chromosome scaffold and the two strands of the double helix are plectonemically coiled, accessing the genome is a complex topological challenge (>>11<<,1216–18).
n2:mentions: n3:8811192

Subject Item: _:vb4399193
rdf:type: n2:Context
rdf:value: Because the genetic material is anchored to the chromosome scaffold and the two strands of the double helix are plectonemically coiled, accessing the genome is a complex topological challenge (11,1216–>>18<<).
n2:mentions: n3:17268506 n3:17622799 n3:15130115

Subject Item: _:vb4399194
rdf:type: n2:Context
rdf:value: In all living systems, from bacteria to humans, DNA is globally underwound (i.e. negatively supercoiled) by ∼6% (12,19–>>21<<). This is important because duplex DNA is merely the storage form for the genetic information. In order to replicate or express this information, the two strands of DNA must be separated. Since global underwinding of the genome imparts
n2:mentions: n3:7919794 n3:6587352 n3:6256851

Subject Item: _:vb4399195
rdf:type: n2:Context
rdf:value: Since global underwinding of the genome imparts increased single-stranded character to the double helix, negative supercoiling greatly facilitates strand separation (12,16–>>18<<).
n2:mentions: n3:17268506 n3:17622799 n3:15130115

Subject Item: _:vb4399196
rdf:type: n2:Context
rdf:value: The linear movement of tracking enzymes, such as helicases and polymerases, compresses the turns of the double helix into a shorter region (Figure 1) (12,19–>>21<<). Consequently, the double helix becomes increasingly overwound ahead of tracking systems. The positive supercoiling that results makes it more difficult to open the two strands of the double helix and ultimately blocks essential nucleic
n2:mentions: n3:7919794 n3:6587352 n3:6256851

Subject Item: _:vb4399197
rdf:type: n2:Context
rdf:value: The positive supercoiling that results makes it more difficult to open the two strands of the double helix and ultimately blocks essential nucleic acid processes (>>10<<, 12, 16–18).
n2:mentions: n3:12042765

Subject Item: _:vb4399198
rdf:type: n2:Context
rdf:value: The positive supercoiling that results makes it more difficult to open the two strands of the double helix and ultimately blocks essential nucleic acid processes (10, 12, 16–>>18<<). Figure 1.
n2:mentions: n3:17268506 n3:17622799 n3:15130115

Subject Item: _:vb4399199
rdf:type: n2:Context
rdf:value: Intramolecular knots (formed within the same DNA molecule) are generated during recombination, and intermolecular tangles (formed between daughter DNA molecules) are produced during replication (Figure 1) (>>8<<,10,12,17).
n2:mentions: n3:17681352

Subject Item: _:vb4399200
rdf:type: n2:Context
rdf:value: Intramolecular knots (formed within the same DNA molecule) are generated during recombination, and intermolecular tangles (formed between daughter DNA molecules) are produced during replication (Figure 1) (8,>>10<<,12,17). DNA knots block essential nucleic acid processes because they make it impossible to separate the two strands of the double helix. Moreover, tangled DNA molecules cannot be segregated during mitosis or meiosis (8,10,12,17).
n2:mentions: n3:12042765

Subject Item: _:vb4399201
rdf:type: n2:Context
rdf:value: Intramolecular knots (formed within the same DNA molecule) are generated during recombination, and intermolecular tangles (formed between daughter DNA molecules) are produced during replication (Figure 1) (8,10,12,>>17<<). DNA knots block essential nucleic acid processes because they make it impossible to separate the two strands of the double helix. Moreover, tangled DNA molecules cannot be segregated during mitosis or meiosis (8,10,12,17). Consequently,
n2:mentions: n3:17622799

Subject Item: _:vb4399202
rdf:type: n2:Context
rdf:value: Moreover, tangled DNA molecules cannot be segregated during mitosis or meiosis (>>8<<,10,12,17).
n2:mentions: n3:17681352

Subject Item: _:vb4399203
rdf:type: n2:Context
rdf:value: Moreover, tangled DNA molecules cannot be segregated during mitosis or meiosis (8,>>10<<,12,17). Consequently, DNA knots and tangles can be lethal to cells if they are not resolved.
n2:mentions: n3:12042765

Subject Item: _:vb4399204
rdf:type: n2:Context
rdf:value: Moreover, tangled DNA molecules cannot be segregated during mitosis or meiosis (8,10,12,>>17<<). Consequently, DNA knots and tangles can be lethal to cells if they are not resolved.
n2:mentions: n3:17622799

Subject Item: _:vb4399205
rdf:type: n5:Section
dc:title: dna topoisomerases
n5:contains: _:vb4399216 _:vb4399217 _:vb4399218 _:vb4399219 _:vb4399220 _:vb4399221 _:vb4399222 _:vb4399223 _:vb4399224 _:vb4399225 _:vb4399226 _:vb4399227 _:vb4399228 _:vb4399229 _:vb4399230 _:vb4399231 _:vb4399206 _:vb4399207 _:vb4399208 _:vb4399209 _:vb4399210 _:vb4399211 _:vb4399212 _:vb4399213 _:vb4399214 _:vb4399215 _:vb4399232 _:vb4399233 _:vb4399234 _:vb4399235 _:vb4399236 _:vb4399237 _:vb4399238 _:vb4399239 _:vb4399240 _:vb4399241 _:vb4399242 _:vb4399243

Subject Item: _:vb4399206
rdf:type: n2:Context
rdf:value: The topological state of the genetic material is regulated by enzymes known as topoisomerases (>>8<<,10,11,22,23). Topoisomerases are required for the survival of all organisms and alter DNA topology by generating transient breaks in the double helix (8,10,11,22,23).
n2:mentions: n3:17681352

Subject Item: _:vb4399207
rdf:type: n2:Context
rdf:value: The topological state of the genetic material is regulated by enzymes known as topoisomerases (8,>>10<<,11,22,23). Topoisomerases are required for the survival of all organisms and alter DNA topology by generating transient breaks in the double helix (8,10,11,22,23).
n2:mentions: n3:12042765

Subject Item: _:vb4399208
rdf:type: n2:Context
rdf:value: The topological state of the genetic material is regulated by enzymes known as topoisomerases (8,10,>>11<<,22,23). Topoisomerases are required for the survival of all organisms and alter DNA topology by generating transient breaks in the double helix (8,10,11,22,23).
n2:mentions: n3:8811192

Subject Item: _:vb4399209
rdf:type: n2:Context
rdf:value: The topological state of the genetic material is regulated by enzymes known as topoisomerases (8,10,11,>>22<<,23). Topoisomerases are required for the survival of all organisms and alter DNA topology by generating transient breaks in the double helix (8,10,11,22,23).
n2:mentions: n3:11395412

Subject Item: _:vb4399210
rdf:type: n2:Context
rdf:value: The topological state of the genetic material is regulated by enzymes known as topoisomerases (8,10,11,22,>>23<<). Topoisomerases are required for the survival of all organisms and alter DNA topology by generating transient breaks in the double helix (8,10,11,22,23).
n2:mentions: n3:16246147

Subject Item: _:vb4399211
rdf:type: n2:Context
rdf:value: Topoisomerases are required for the survival of all organisms and alter DNA topology by generating transient breaks in the double helix (>>8<<,10,11,22,23).
n2:mentions: n3:17681352

Subject Item: _:vb4399212
rdf:type: n2:Context
rdf:value: Topoisomerases are required for the survival of all organisms and alter DNA topology by generating transient breaks in the double helix (8,>>10<<,11,22,23).
n2:mentions: n3:12042765

Subject Item: _:vb4399213
rdf:type: n2:Context
rdf:value: Topoisomerases are required for the survival of all organisms and alter DNA topology by generating transient breaks in the double helix (8,10,>>11<<,22,23). There are two major classes of topoisomerases, type I and type II, that are distinguished by the number of DNA strands that they cleave and the mechanism by which they alter the topological properties of the genetic material
n2:mentions: n3:8811192

Subject Item: _:vb4399214
rdf:type: n2:Context
rdf:value: Topoisomerases are required for the survival of all organisms and alter DNA topology by generating transient breaks in the double helix (8,10,11,>>22<<,23). There are two major classes of topoisomerases, type I and type II, that are distinguished by the number of DNA strands that they cleave and the mechanism by which they alter the topological properties of the genetic material
n2:mentions: n3:11395412

Subject Item: _:vb4399215
rdf:type: n2:Context
rdf:value: Topoisomerases are required for the survival of all organisms and alter DNA topology by generating transient breaks in the double helix (8,10,11,22,>>23<<). There are two major classes of topoisomerases, type I and type II, that are distinguished by the number of DNA strands that they cleave and the mechanism by which they alter the topological properties of the genetic material
n2:mentions: n3:16246147

Subject Item: _:vb4399216
rdf:type: n2:Context
rdf:value: There are two major classes of topoisomerases, type I and type II, that are distinguished by the number of DNA strands that they cleave and the mechanism by which they alter the topological properties of the genetic material (>>8<<,10,11,22,23).
n2:mentions: n3:17681352

Subject Item: _:vb4399217
rdf:type: n2:Context
rdf:value: There are two major classes of topoisomerases, type I and type II, that are distinguished by the number of DNA strands that they cleave and the mechanism by which they alter the topological properties of the genetic material (8,>>10<<,11,22,23).
n2:mentions: n3:12042765

Subject Item: _:vb4399218
rdf:type: n2:Context
rdf:value: There are two major classes of topoisomerases, type I and type II, that are distinguished by the number of DNA strands that they cleave and the mechanism by which they alter the topological properties of the genetic material (8,10,>>11<<,22,23).
n2:mentions: n3:8811192

Subject Item: _:vb4399219
rdf:type: n2:Context
rdf:value: There are two major classes of topoisomerases, type I and type II, that are distinguished by the number of DNA strands that they cleave and the mechanism by which they alter the topological properties of the genetic material (8,10,11,>>22<<,23).
n2:mentions: n3:11395412

Subject Item: _:vb4399220
rdf:type: n2:Context
rdf:value: There are two major classes of topoisomerases, type I and type II, that are distinguished by the number of DNA strands that they cleave and the mechanism by which they alter the topological properties of the genetic material (8,10,11,22,>>23<<).
n2:mentions: n3:16246147

Subject Item: _:vb4399221
rdf:type: n2:Context
rdf:value: Eukaryotic type I topoisomerases are monomeric enzymes that require no high-energy cofactor (>>11<<,22,24). Type I enzymes are organized into two subclasses: type IA and type IB.
n2:mentions: n3:8811192

Subject Item: _:vb4399222
rdf:type: n2:Context
rdf:value: Eukaryotic type I topoisomerases are monomeric enzymes that require no high-energy cofactor (11,>>22<<,24). Type I enzymes are organized into two subclasses: type IA and type IB.
n2:mentions: n3:11395412

Subject Item: _:vb4399223
rdf:type: n2:Context
rdf:value: Eukaryotic type I topoisomerases are monomeric enzymes that require no high-energy cofactor (11,22,>>24<<). Type I enzymes are organized into two subclasses: type IA and type IB.
n2:mentions: n3:15830206

Subject Item: _:vb4399224
rdf:type: n2:Context
rdf:value: These enzymes alter topology by creating transient single-stranded breaks in the DNA, followed by passage of the opposite intact strand through the break (type IA) or by controlled rotation of the helix around the break (type IB) (>>11<<,22,24). Type IA topoisomerases need divalent metal ions for DNA scission and attach covalently to the 5′-terminal phosphate of the DNA (11,22,24). In contrast, type IB enzymes do not require divalent metal ions and covalently link to the
n2:mentions: n3:8811192

Subject Item: _:vb4399225
rdf:type: n2:Context
rdf:value: These enzymes alter topology by creating transient single-stranded breaks in the DNA, followed by passage of the opposite intact strand through the break (type IA) or by controlled rotation of the helix around the break (type IB) (11,>>22<<,24). Type IA topoisomerases need divalent metal ions for DNA scission and attach covalently to the 5′-terminal phosphate of the DNA (11,22,24).
n2:mentions: n3:11395412

Subject Item: _:vb4399226
rdf:type: n2:Context
rdf:value: These enzymes alter topology by creating transient single-stranded breaks in the DNA, followed by passage of the opposite intact strand through the break (type IA) or by controlled rotation of the helix around the break (type IB) (11,22,>>24<<). Type IA topoisomerases need divalent metal ions for DNA scission and attach covalently to the 5′-terminal phosphate of the DNA (11,22,24).
n2:mentions: n3:15830206

Subject Item: _:vb4399227
rdf:type: n2:Context
rdf:value: Type IA topoisomerases need divalent metal ions for DNA scission and attach covalently to the 5′-terminal phosphate of the DNA (>>11<<,22,24). In contrast, type IB enzymes do not require divalent metal ions and covalently link to the 3′-terminal phosphate (11,22,24). As a result of their reaction mechanism, type I topoisomerases can modulate DNA under- and overwinding,
n2:mentions: n3:8811192

Subject Item: _:vb4399228
rdf:type: n2:Context
rdf:value: Type IA topoisomerases need divalent metal ions for DNA scission and attach covalently to the 5′-terminal phosphate of the DNA (11,>>22<<,24). In contrast, type IB enzymes do not require divalent metal ions and covalently link to the 3′-terminal phosphate (11,22,24). As a result of their reaction mechanism, type I topoisomerases can modulate DNA under- and overwinding, but
n2:mentions: n3:11395412

Subject Item: _:vb4399229
rdf:type: n2:Context
rdf:value: Type IA topoisomerases need divalent metal ions for DNA scission and attach covalently to the 5′-terminal phosphate of the DNA (11,22,>>24<<). In contrast, type IB enzymes do not require divalent metal ions and covalently link to the 3′-terminal phosphate (11,22,24). As a result of their reaction mechanism, type I topoisomerases can modulate DNA under- and overwinding, but
n2:mentions: n3:15830206

Subject Item: _:vb4399230
rdf:type: n2:Context
rdf:value: In contrast, type IB enzymes do not require divalent metal ions and covalently link to the 3′-terminal phosphate (>>11<<,22,24). As a result of their reaction mechanism, type I topoisomerases can modulate DNA under- and overwinding, but cannot remove knots or tangles from duplex DNA. A number of excellent review articles on type I topoisomerases have
n2:mentions: n3:8811192

Subject Item: _:vb4399231
rdf:type: n2:Context
rdf:value: In contrast, type IB enzymes do not require divalent metal ions and covalently link to the 3′-terminal phosphate (11,>>22<<,24). As a result of their reaction mechanism, type I topoisomerases can modulate DNA under- and overwinding, but cannot remove knots or tangles from duplex DNA. A number of excellent review articles on type I topoisomerases have appeared
n2:mentions: n3:11395412

Subject Item: _:vb4399232
rdf:type: n2:Context
rdf:value: In contrast, type IB enzymes do not require divalent metal ions and covalently link to the 3′-terminal phosphate (11,22,>>24<<). As a result of their reaction mechanism, type I topoisomerases can modulate DNA under- and overwinding, but cannot remove knots or tangles from duplex DNA. A number of excellent review articles on type I topoisomerases have appeared
n2:mentions: n3:15830206

Subject Item: _:vb4399233
rdf:type: n2:Context
rdf:value: A number of excellent review articles on type I topoisomerases have appeared recently (>>22<<,24,25). Consequently, these enzymes will not be discussed further in this article.
n2:mentions: n3:11395412

Subject Item: _:vb4399234
rdf:type: n2:Context
rdf:value: A number of excellent review articles on type I topoisomerases have appeared recently (22,>>24<<,25). Consequently, these enzymes will not be discussed further in this article.
n2:mentions: n3:15830206

Subject Item: _:vb4399235
rdf:type: n2:Context
rdf:value: A number of excellent review articles on type I topoisomerases have appeared recently (22,24,>>25<<). Consequently, these enzymes will not be discussed further in this article.
n2:mentions: n3:16990856

Subject Item: _:vb4399236
rdf:type: n2:Context
rdf:value: Eukaryotic type II topoisomerases function as homodimers and require divalent metal ions and ATP for complete catalytic activity (>>5<<,8,26–28). These enzymes interconvert different topological forms of DNA by a ‘double-stranded DNA passage reaction’ that can be separated into a number of discrete steps (5,8,26–28).
n2:mentions: n3:10697411

Subject Item: _:vb4399237
rdf:type: n2:Context
rdf:value: Eukaryotic type II topoisomerases function as homodimers and require divalent metal ions and ATP for complete catalytic activity (5,>>8<<,26–28). These enzymes interconvert different topological forms of DNA by a ‘double-stranded DNA passage reaction’ that can be separated into a number of discrete steps (5,8,26–28).
n2:mentions: n3:17681352

Subject Item: _:vb4399238
rdf:type: n2:Context
rdf:value: Eukaryotic type II topoisomerases function as homodimers and require divalent metal ions and ATP for complete catalytic activity (5,8,26–>>28<<). These enzymes interconvert different topological forms of DNA by a ‘double-stranded DNA passage reaction’ that can be separated into a number of discrete steps (5,8,26–28).
n2:mentions: n3:8538787

Subject Item: _:vb4399239
rdf:type: n2:Context
rdf:value: These enzymes interconvert different topological forms of DNA by a ‘double-stranded DNA passage reaction’ that can be separated into a number of discrete steps (>>5<<,8,26–28). Briefly, type II topoisomerases (i) bind two separate segments of DNA, (ii) create a double-stranded break in one of the segments, (iii) translocate the second DNA segment through the cleaved nucleic acid ‘gate’, (iv) rejoin (i.
n2:mentions: n3:10697411

Subject Item: _:vb4399240
rdf:type: n2:Context
rdf:value: These enzymes interconvert different topological forms of DNA by a ‘double-stranded DNA passage reaction’ that can be separated into a number of discrete steps (5,>>8<<,26–28). Briefly, type II topoisomerases (i) bind two separate segments of DNA, (ii) create a double-stranded break in one of the segments, (iii) translocate the second DNA segment through the cleaved nucleic acid ‘gate’, (iv) rejoin (i.e.
n2:mentions: n3:17681352

Subject Item: _:vb4399241
rdf:type: n2:Context
rdf:value: These enzymes interconvert different topological forms of DNA by a ‘double-stranded DNA passage reaction’ that can be separated into a number of discrete steps (5,8,26–>>28<<). Briefly, type II topoisomerases (i) bind two separate segments of DNA, (ii) create a double-stranded break in one of the segments, (iii) translocate the second DNA segment through the cleaved nucleic acid ‘gate’, (iv) rejoin (i.e.
n2:mentions: n3:8538787

Subject Item: _:vb4399242
rdf:type: n2:Context
rdf:value: the cleaved nucleic acid ‘gate’, (iv) rejoin (i.e. ligate) the cleaved DNA, (v) release the translocated segment through a gate in the protein and (vi) close the protein gate and regain the ability to start a new round of catalysis (>>5<<,26–34). Because of their double-stranded DNA passage mechanism, type II topoisomerases can modulate DNA supercoiling and also can remove DNA knots and tangles.
n2:mentions: n3:10697411

Subject Item: _:vb4399243
rdf:type: n2:Context
rdf:value: cleaved nucleic acid ‘gate’, (iv) rejoin (i.e. ligate) the cleaved DNA, (v) release the translocated segment through a gate in the protein and (vi) close the protein gate and regain the ability to start a new round of catalysis (5,26–>>34<<). Because of their double-stranded DNA passage mechanism, type II topoisomerases can modulate DNA supercoiling and also can remove DNA knots and tangles.
n2:mentions: n3:8385137 n3:18653531 n3:8538787 n3:2827726 n3:3015913 n3:11359787 n3:1330327

Subject Item: _:vb4399244
rdf:type: n5:Section
dc:title: topoisomerase ii
n5:contains: _:vb4399252 _:vb4399253 _:vb4399254 _:vb4399255 _:vb4399248 _:vb4399249 _:vb4399250 _:vb4399251 _:vb4399260 _:vb4399261 _:vb4399262 _:vb4399263 _:vb4399256 _:vb4399257 _:vb4399258 _:vb4399259 _:vb4399245 _:vb4399246 _:vb4399247 _:vb4399268 _:vb4399269 _:vb4399264 _:vb4399265 _:vb4399266 _:vb4399267

Subject Item: _:vb4399245
rdf:type: n2:Context
rdf:value: Lower eukaryotes and invertebrates encode only a single type II topoisomerase, topoisomerase II (35–>>38<<). In contrast, vertebrate species encode two closely related isoforms of the enzyme, topoisomerase IIα and topoisomerase IIβ.
n2:mentions: n3:6088500 n3:6279616 n3:3012525 n3:6323017

Subject Item: _:vb4399246
rdf:type: n2:Context
rdf:value: These isoforms differ in their protomer molecular masses (170 versus 180 kDa, respectively) and are encoded by separate genes (>>8<<,10,22,28,39–46).
n2:mentions: n3:17681352

Subject Item: _:vb4399247
rdf:type: n2:Context
rdf:value: These isoforms differ in their protomer molecular masses (170 versus 180 kDa, respectively) and are encoded by separate genes (8,>>10<<,22,28,39–46).
n2:mentions: n3:12042765

Subject Item: _:vb4399248
rdf:type: n2:Context
rdf:value: These isoforms differ in their protomer molecular masses (170 versus 180 kDa, respectively) and are encoded by separate genes (8,10,>>22<<,28,39–46).
n2:mentions: n3:11395412

Subject Item: _:vb4399249
rdf:type: n2:Context
rdf:value: These isoforms differ in their protomer molecular masses (170 versus 180 kDa, respectively) and are encoded by separate genes (8,10,22,28,39–>>46<<). Topoisomerase IIα and topoisomerase IIβ display a high degree (∼70%) of amino acid sequence identity and similar enzymological characteristics. One notable difference between the two isoforms is that topoisomerase IIα relaxes (i.e.
n2:mentions: n3:1333583 n3:2557897 n3:12570766 n3:2556712 n3:2824504 n3:2845399 n3:1309226 n3:2163884

Subject Item: _:vb4399250
rdf:type: n2:Context
rdf:value: isoforms is that topoisomerase IIα relaxes (i.e. removes) positive superhelical twists ∼10 times faster than it does negative in vitro, while the β isoform is unable to distinguish the geometry of DNA supercoils during DNA relaxation (>>47<<).
n2:mentions: n3:16188892

Subject Item: _:vb4399251
rdf:type: n2:Context
rdf:value: Topoisomerase IIα is essential for the survival of proliferating cells, and protein levels rise dramatically during periods of cell growth (48–>>51<<). The enzyme is further regulated over the cell cycle, with protein concentrations peaking in G2/M (50,52,53). Topoisomerase IIα is associated with replication forks and remains tightly bound to chromosomes during mitosis (9,51,54–56).
n2:mentions: n3:1651102 n3:2835157 n3:9837951 n3:3025219

Subject Item: _:vb4399252
rdf:type: n2:Context
rdf:value: The enzyme is further regulated over the cell cycle, with protein concentrations peaking in G2/M (>>50<<,52,53). Topoisomerase IIα is associated with replication forks and remains tightly bound to chromosomes during mitosis (9,51,54–56). Thus, it is believed to be the isoform that functions in growth-related processes, such as DNA
n2:mentions: n3:1651102

Subject Item: _:vb4399253
rdf:type: n2:Context
rdf:value: The enzyme is further regulated over the cell cycle, with protein concentrations peaking in G2/M (50,>>52<<,53). Topoisomerase IIα is associated with replication forks and remains tightly bound to chromosomes during mitosis (9,51,54–56). Thus, it is believed to be the isoform that functions in growth-related processes, such as DNA replication
n2:mentions: n3:2829215

Subject Item: _:vb4399254
rdf:type: n2:Context
rdf:value: The enzyme is further regulated over the cell cycle, with protein concentrations peaking in G2/M (50,52,>>53<<). Topoisomerase IIα is associated with replication forks and remains tightly bound to chromosomes during mitosis (9,51,54–56). Thus, it is believed to be the isoform that functions in growth-related processes, such as DNA replication and
n2:mentions: n3:8288578

Subject Item: _:vb4399255
rdf:type: n2:Context
rdf:value: Topoisomerase IIα is associated with replication forks and remains tightly bound to chromosomes during mitosis (>>9<<,51,54–56).
n2:mentions: n3:9748506

Subject Item: _:vb4399256
rdf:type: n2:Context
rdf:value: Topoisomerase IIα is associated with replication forks and remains tightly bound to chromosomes during mitosis (9,>>51<<,54–56). Thus, it is believed to be the isoform that functions in growth-related processes, such as DNA replication and chromosome segregation (10,51).
n2:mentions: n3:9837951

Subject Item: _:vb4399257
rdf:type: n2:Context
rdf:value: Topoisomerase IIα is associated with replication forks and remains tightly bound to chromosomes during mitosis (9,51,54–>>56<<). Thus, it is believed to be the isoform that functions in growth-related processes, such as DNA replication and chromosome segregation (10,51).
n2:mentions: n3:17526531 n3:9071722 n3:11927602

Subject Item: _:vb4399258
rdf:type: n2:Context
rdf:value: Thus, it is believed to be the isoform that functions in growth-related processes, such as DNA replication and chromosome segregation (>>10<<,51).
n2:mentions: n3:12042765

Subject Item: _:vb4399259
rdf:type: n2:Context
rdf:value: Thus, it is believed to be the isoform that functions in growth-related processes, such as DNA replication and chromosome segregation (10,>>51<<).
n2:mentions: n3:9837951

Subject Item: _:vb4399260
rdf:type: n2:Context
rdf:value: Topoisomerase IIβ is dispensable at the cellular level but appears to be required for proper neural development (57–>>59<<). Expression of topoisomerase IIβ is independent of proliferative status and cell cycle, and the enzyme dissociates from chromosomes during mitosis (54,60,61).
n2:mentions: n3:10615047 n3:7579726 n3:9331091

Subject Item: _:vb4399261
rdf:type: n2:Context
rdf:value: Expression of topoisomerase IIβ is independent of proliferative status and cell cycle, and the enzyme dissociates from chromosomes during mitosis (>>54<<,60,61). Topoisomerase IIβ cannot compensate for the loss of topoisomerase IIα in mammalian cells, suggesting that these two isoforms do not play redundant roles in replicative processes (51,60,62,63). Although the physiological functions
n2:mentions: n3:17526531

Subject Item: _:vb4399262
rdf:type: n2:Context
rdf:value: Expression of topoisomerase IIβ is independent of proliferative status and cell cycle, and the enzyme dissociates from chromosomes during mitosis (54,>>60<<,61). Topoisomerase IIβ cannot compensate for the loss of topoisomerase IIα in mammalian cells, suggesting that these two isoforms do not play redundant roles in replicative processes (51,60,62,63). Although the physiological functions of
n2:mentions: n3:9631649

Subject Item: _:vb4399263
rdf:type: n2:Context
rdf:value: Expression of topoisomerase IIβ is independent of proliferative status and cell cycle, and the enzyme dissociates from chromosomes during mitosis (54,60,>>61<<). Topoisomerase IIβ cannot compensate for the loss of topoisomerase IIα in mammalian cells, suggesting that these two isoforms do not play redundant roles in replicative processes (51,60,62,63). Although the physiological functions of
n2:mentions: n3:9748535

Subject Item: _:vb4399264
rdf:type: n2:Context
rdf:value: Topoisomerase IIβ cannot compensate for the loss of topoisomerase IIα in mammalian cells, suggesting that these two isoforms do not play redundant roles in replicative processes (>>51<<,60,62,63).
n2:mentions: n3:9837951

Subject Item: _:vb4399265
rdf:type: n2:Context
rdf:value: Topoisomerase IIβ cannot compensate for the loss of topoisomerase IIα in mammalian cells, suggesting that these two isoforms do not play redundant roles in replicative processes (51,>>60<<,62,63). Although the physiological functions of topoisomerase IIβ have yet to be defined, recent evidence indicates involvement in the transcription of hormonally or developmentally regulated genes (63,64).
n2:mentions: n3:9631649

Subject Item: _:vb4399266
rdf:type: n2:Context
rdf:value: Topoisomerase IIβ cannot compensate for the loss of topoisomerase IIα in mammalian cells, suggesting that these two isoforms do not play redundant roles in replicative processes (51,60,>>62<<,63). Although the physiological functions of topoisomerase IIβ have yet to be defined, recent evidence indicates involvement in the transcription of hormonally or developmentally regulated genes (63,64).
n2:mentions: n3:14996935

Subject Item: _:vb4399267
rdf:type: n2:Context
rdf:value: Topoisomerase IIβ cannot compensate for the loss of topoisomerase IIα in mammalian cells, suggesting that these two isoforms do not play redundant roles in replicative processes (51,60,62,>>63<<). Although the physiological functions of topoisomerase IIβ have yet to be defined, recent evidence indicates involvement in the transcription of hormonally or developmentally regulated genes (63,64).
n2:mentions: n3:16794079

Subject Item: _:vb4399268
rdf:type: n2:Context
rdf:value: Although the physiological functions of topoisomerase IIβ have yet to be defined, recent evidence indicates involvement in the transcription of hormonally or developmentally regulated genes (>>63<<,64).
n2:mentions: n3:16794079

Subject Item: _:vb4399269
rdf:type: n2:Context
rdf:value: Although the physiological functions of topoisomerase IIβ have yet to be defined, recent evidence indicates involvement in the transcription of hormonally or developmentally regulated genes (63,>>64<<).
n2:mentions: n3:16794066

Subject Item: _:vb4399270
rdf:type: n5:Section
dc:title: topoisomerase ii-mediated dna cleavage and ligation
n5:contains: _:vb4399324 _:vb4399325 _:vb4399320 _:vb4399321 _:vb4399322 _:vb4399323 _:vb4399316 _:vb4399317 _:vb4399318 _:vb4399319 _:vb4399312 _:vb4399313 _:vb4399314 _:vb4399315 _:vb4399308 _:vb4399309 _:vb4399310 _:vb4399311 _:vb4399304 _:vb4399305 _:vb4399306 _:vb4399307 _:vb4399300 _:vb4399301 _:vb4399302 _:vb4399303 _:vb4399296 _:vb4399297 _:vb4399298 _:vb4399299 _:vb4399292 _:vb4399293 _:vb4399294 _:vb4399295 _:vb4399288 _:vb4399289 _:vb4399290 _:vb4399291 _:vb4399284 _:vb4399285 _:vb4399286 _:vb4399287 _:vb4399280 _:vb4399281 _:vb4399282 _:vb4399283 _:vb4399276 _:vb4399277 _:vb4399278 _:vb4399279 _:vb4399272 _:vb4399273 _:vb4399274 _:vb4399275 _:vb4399271

Subject Item: _:vb4399271
rdf:type: n2:Context
rdf:value: The ability of topoisomerase II to cleave and ligate DNA is central to all of its catalytic functions (>>5<<,8,11,27). All topoisomerases utilize active site tyrosyl residues to mediate DNA cleavage and ligation.
n2:mentions: n3:10697411

Subject Item: _:vb4399272
rdf:type: n2:Context
rdf:value: The ability of topoisomerase II to cleave and ligate DNA is central to all of its catalytic functions (5,>>8<<,11,27). All topoisomerases utilize active site tyrosyl residues to mediate DNA cleavage and ligation.
n2:mentions: n3:17681352

Subject Item: _:vb4399273
rdf:type: n2:Context
rdf:value: The ability of topoisomerase II to cleave and ligate DNA is central to all of its catalytic functions (5,8,>>11<<,27). All topoisomerases utilize active site tyrosyl residues to mediate DNA cleavage and ligation.
n2:mentions: n3:8811192

Subject Item: _:vb4399274
rdf:type: n2:Context
rdf:value: The ability of topoisomerase II to cleave and ligate DNA is central to all of its catalytic functions (5,8,11,>>27<<). All topoisomerases utilize active site tyrosyl residues to mediate DNA cleavage and ligation.
n2:mentions: n3:8538787

Subject Item: _:vb4399275
rdf:type: n2:Context
rdf:value: Topoisomerase II initiates DNA cleavage by the nucleophilic attack of the active site tyrosine on the phosphate of the nucleic acid backbone (Figure 2) (>>11<<,23,26,27). The resulting transesterification reaction results in the formation of a covalent phosphotyrosyl bond that links the protein to the newly generated 5′-terminus of the DNA chain.
n2:mentions: n3:8811192

Subject Item: _:vb4399276
rdf:type: n2:Context
rdf:value: Topoisomerase II initiates DNA cleavage by the nucleophilic attack of the active site tyrosine on the phosphate of the nucleic acid backbone (Figure 2) (11,>>23<<,26,27). The resulting transesterification reaction results in the formation of a covalent phosphotyrosyl bond that links the protein to the newly generated 5′-terminus of the DNA chain.
n2:mentions: n3:16246147

Subject Item: _:vb4399277
rdf:type: n2:Context
rdf:value: Topoisomerase II initiates DNA cleavage by the nucleophilic attack of the active site tyrosine on the phosphate of the nucleic acid backbone (Figure 2) (11,23,26,>>27<<). The resulting transesterification reaction results in the formation of a covalent phosphotyrosyl bond that links the protein to the newly generated 5′-terminus of the DNA chain.
n2:mentions: n3:8538787

Subject Item: _:vb4399278
rdf:type: n2:Context
rdf:value: Thus, topoisomerase II generates cleaved DNA molecules with four-base 5′-single-stranded cohesive ends, each of which is covalently linked to a separate protomer subunit of the enzyme (65–>>67<<). Figure 2.
n2:mentions: n3:6317692 n3:6305984 n3:2551367

Subject Item: _:vb4399279
rdf:type: n2:Context
rdf:value: Second, because it does not allow the cleaved DNA chain to dissociate from the enzyme, the protein–DNA linkage maintains the integrity of the genetic material during the cleavage event (>>11<<,23,26,27).
n2:mentions: n3:8811192

Subject Item: _:vb4399280
rdf:type: n2:Context
rdf:value: Second, because it does not allow the cleaved DNA chain to dissociate from the enzyme, the protein–DNA linkage maintains the integrity of the genetic material during the cleavage event (11,>>23<<,26,27). The covalent topoisomerase II-cleaved DNA reaction intermediate is referred to as the ‘cleavage complex’ and is critical for the pharmacological activities of the enzyme, which are discussed later in this article.
n2:mentions: n3:16246147

Subject Item: _:vb4399281
rdf:type: n2:Context
rdf:value: Second, because it does not allow the cleaved DNA chain to dissociate from the enzyme, the protein–DNA linkage maintains the integrity of the genetic material during the cleavage event (11,23,26,>>27<<). The covalent topoisomerase II-cleaved DNA reaction intermediate is referred to as the ‘cleavage complex’ and is critical for the pharmacological activities of the enzyme, which are discussed later in this article.
n2:mentions: n3:8538787

Subject Item: _:vb4399282
rdf:type: n2:Context
rdf:value: Although topoisomerase II acts globally, it cleaves DNA at preferred sites (>>68<<). The consensus sequence for cleavage is weak, and many sites of action do not conform to it (68).
n2:mentions: n3:9748568

Subject Item: _:vb4399283
rdf:type: n2:Context
rdf:value: The consensus sequence for cleavage is weak, and many sites of action do not conform to it (>>68<<). Ultimately, the mechanism by which topoisomerase II selects DNA sites is not apparent, and it is nearly impossible to predict de novo whether a given DNA sequence will support scission. Most likely, the specificity of topoisomerase
n2:mentions: n3:9748568

Subject Item: _:vb4399284
rdf:type: n2:Context
rdf:value: specificity of topoisomerase II-mediated cleavage is determined by the local structure, flexibility, or malleability of the DNA that accompanies the sequence, as opposed to a direct recognition of the bases that comprise that sequence (>>69<<).
n2:mentions: n3:15751973

Subject Item: _:vb4399285
rdf:type: n2:Context
rdf:value: information regarding the roles of specific amino acid residues comes from structural studies on the catalytic core of yeast topoisomerase II generated in the absence of DNA or in a noncovalent complex with its nucleic acid substrate (>>27<<,70). For consistency, all amino acid assignments discussed below are for the homologous positions in human topoisomerase IIα.
n2:mentions: n3:8538787

Subject Item: _:vb4399286
rdf:type: n2:Context
rdf:value: regarding the roles of specific amino acid residues comes from structural studies on the catalytic core of yeast topoisomerase II generated in the absence of DNA or in a noncovalent complex with its nucleic acid substrate (27,>>70<<). For consistency, all amino acid assignments discussed below are for the homologous positions in human topoisomerase IIα.
n2:mentions: n3:18097402

Subject Item: _:vb4399287
rdf:type: n2:Context
rdf:value: The type II enzyme utilizes a two-metal ion mechanism similar to that utilized by primases and polymerases (>>34<<,70,71,74–77,155,156).
n2:mentions: n3:18653531

Subject Item: _:vb4399288
rdf:type: n2:Context
rdf:value: The type II enzyme utilizes a two-metal ion mechanism similar to that utilized by primases and polymerases (34,>>70<<,71,74–77,155,156).
n2:mentions: n3:18097402

Subject Item: _:vb4399289
rdf:type: n2:Context
rdf:value: The type II enzyme utilizes a two-metal ion mechanism similar to that utilized by primases and polymerases (34,70,>>71<<,74–77,155,156).
n2:mentions: n3:9722641

Subject Item: _:vb4399290
rdf:type: n2:Context
rdf:value: The type II enzyme utilizes a two-metal ion mechanism similar to that utilized by primases and polymerases (34,70,71,74–>>77<<,155,156). Amino acids that are postulated to interact with the metal ions in the active site of topoisomerase IIα and topoisomerase IIβ are indicated. One of the metal ions (shown at left) makes a critical interaction with the 3′-bridging
n2:mentions: n3:10684600 n3:16239602 n3:18403371

Subject Item: _:vb4399291
rdf:type: n2:Context
rdf:value: The type II enzyme utilizes a two-metal ion mechanism similar to that utilized by primases and polymerases (34,70,71,74–77,>>155<<,156). Amino acids that are postulated to interact with the metal ions in the active site of topoisomerase IIα and topoisomerase IIβ are indicated. One of the metal ions (shown at left) makes a critical interaction with the 3′-bridging
n2:mentions: n3:8260491

Subject Item: _:vb4399292
rdf:type: n2:Context
rdf:value: The acid may be a water molecule or an unidentified amino acid in the active site of topoisomerase II. Figure adapted from Noble and Maxwell (>>73<<).
n2:mentions: n3:12051843

Subject Item: _:vb4399293
rdf:type: n2:Context
rdf:value: The DNA cleavage reaction requires a divalent metal ion (>>5<<,30,34,71,72). Mg2+ appears to fulfill this function in vivo (5).
n2:mentions: n3:10697411

Subject Item: _:vb4399294
rdf:type: n2:Context
rdf:value: The DNA cleavage reaction requires a divalent metal ion (5,>>30<<,34,71,72). Mg2+ appears to fulfill this function in vivo (5).
n2:mentions: n3:2827726

Subject Item: _:vb4399295
rdf:type: n2:Context
rdf:value: The DNA cleavage reaction requires a divalent metal ion (5,30,>>34<<,71,72). Mg2+ appears to fulfill this function in vivo (5).
n2:mentions: n3:18653531

Subject Item: _:vb4399296
rdf:type: n2:Context
rdf:value: The DNA cleavage reaction requires a divalent metal ion (5,30,34,>>71<<,72). Mg2+ appears to fulfill this function in vivo (5).
n2:mentions: n3:9722641

Subject Item: _:vb4399297
rdf:type: n2:Context
rdf:value: The DNA cleavage reaction requires a divalent metal ion (5,30,34,71,>>72<<). Mg2+ appears to fulfill this function in vivo (5).
n2:mentions: n3:9653108

Subject Item: _:vb4399298
rdf:type: n2:Context
rdf:value: Mg2+ appears to fulfill this function in vivo (>>5<<). Recent evidence indicates that human topoisomerase IIα utilizes a ‘two-metal-ion’ mechanism, in which one of the metal ions interacts with the bridging 5′-oxygen of the scissile bond (34).
n2:mentions: n3:10697411

Subject Item: _:vb4399299
rdf:type: n2:Context
rdf:value: Recent evidence indicates that human topoisomerase IIα utilizes a ‘two-metal-ion’ mechanism, in which one of the metal ions interacts with the bridging 5′-oxygen of the scissile bond (>>34<<). This interaction greatly accelerates rates of enzyme-mediated DNA cleavage and most likely is needed to stabilize the leaving 3′-oxygen. The role of the second metal ion is not known. However, it is believed to make critical contacts
n2:mentions: n3:18653531

Subject Item: _:vb4399300
rdf:type: n2:Context
rdf:value: However, it is believed to make critical contacts with the active site tyrosine and may stabilize the DNA transition state and/or help deprotonate the active site tyrosine (>>34<<,73). It has been postulated that the divalent metal ions are coordinated by Glu461, Asp541, Asp543 and Asp545 in human topoisomerase IIα and corresponding residues in the β isoform (Figure 3) (34,70,74,75). A two-metal-ion mechanism for
n2:mentions: n3:18653531

Subject Item: _:vb4399301
rdf:type: n2:Context
rdf:value: However, it is believed to make critical contacts with the active site tyrosine and may stabilize the DNA transition state and/or help deprotonate the active site tyrosine (34,>>73<<). It has been postulated that the divalent metal ions are coordinated by Glu461, Asp541, Asp543 and Asp545 in human topoisomerase IIα and corresponding residues in the β isoform (Figure 3) (34,70,74,75). A two-metal-ion mechanism for DNA
n2:mentions: n3:12051843

Subject Item: _:vb4399302
rdf:type: n2:Context
rdf:value: It has been postulated that the divalent metal ions are coordinated by Glu461, Asp541, Asp543 and Asp545 in human topoisomerase IIα and corresponding residues in the β isoform (Figure 3) (>>34<<,70,74,75).
n2:mentions: n3:18653531

Subject Item: _:vb4399303
rdf:type: n2:Context
rdf:value: It has been postulated that the divalent metal ions are coordinated by Glu461, Asp541, Asp543 and Asp545 in human topoisomerase IIα and corresponding residues in the β isoform (Figure 3) (34,>>70<<,74,75). A two-metal-ion mechanism for DNA cleavage mediated by the bacterial type II topoisomerase, DNA gyrase, also has been proposed (73).
n2:mentions: n3:18097402

Subject Item: _:vb4399304
rdf:type: n2:Context
rdf:value: It has been postulated that the divalent metal ions are coordinated by Glu461, Asp541, Asp543 and Asp545 in human topoisomerase IIα and corresponding residues in the β isoform (Figure 3) (34,70,>>74<<,75). A two-metal-ion mechanism for DNA cleavage mediated by the bacterial type II topoisomerase, DNA gyrase, also has been proposed (73).
n2:mentions: n3:10684600

Subject Item: _:vb4399305
rdf:type: n2:Context
rdf:value: It has been postulated that the divalent metal ions are coordinated by Glu461, Asp541, Asp543 and Asp545 in human topoisomerase IIα and corresponding residues in the β isoform (Figure 3) (34,70,74,>>75<<). A two-metal-ion mechanism for DNA cleavage mediated by the bacterial type II topoisomerase, DNA gyrase, also has been proposed (73).
n2:mentions: n3:16239602

Subject Item: _:vb4399306
rdf:type: n2:Context
rdf:value: A two-metal-ion mechanism for DNA cleavage mediated by the bacterial type II topoisomerase, DNA gyrase, also has been proposed (>>73<<).
n2:mentions: n3:12051843

Subject Item: _:vb4399307
rdf:type: n2:Context
rdf:value: Topoisomerase II–DNA cleavage complexes normally are short-lived and readily reversible (>>5<<,8,76), and the DNA cleavage/ligation equilibrium of the enzyme greatly favors ligation (5,8,11,23,26,27,77,78).
n2:mentions: n3:10697411

Subject Item: _:vb4399308
rdf:type: n2:Context
rdf:value: Topoisomerase II–DNA cleavage complexes normally are short-lived and readily reversible (5,>>8<<,76), and the DNA cleavage/ligation equilibrium of the enzyme greatly favors ligation (5,8,11,23,26,27,77,78).
n2:mentions: n3:17681352

Subject Item: _:vb4399309
rdf:type: n2:Context
rdf:value: Topoisomerase II–DNA cleavage complexes normally are short-lived and readily reversible (5,8,76), and the DNA cleavage/ligation equilibrium of the enzyme greatly favors ligation (>>5<<,8,11,23,26,27,77,78). Under equilibrium conditions, ∼0.5–1% of topoisomerase II in a DNA scission reaction mixture exists as a cleavage complex (65–67,78,79).
n2:mentions: n3:10697411

Subject Item: _:vb4399310
rdf:type: n2:Context
rdf:value: Topoisomerase II–DNA cleavage complexes normally are short-lived and readily reversible (5,8,76), and the DNA cleavage/ligation equilibrium of the enzyme greatly favors ligation (5,>>8<<,11,23,26,27,77,78). Under equilibrium conditions, ∼0.5–1% of topoisomerase II in a DNA scission reaction mixture exists as a cleavage complex (65–67,78,79).
n2:mentions: n3:17681352

Subject Item: _:vb4399311
rdf:type: n2:Context
rdf:value: Topoisomerase II–DNA cleavage complexes normally are short-lived and readily reversible (5,8,76), and the DNA cleavage/ligation equilibrium of the enzyme greatly favors ligation (5,8,>>11<<,23,26,27,77,78). Under equilibrium conditions, ∼0.5–1% of topoisomerase II in a DNA scission reaction mixture exists as a cleavage complex (65–67,78,79).
n2:mentions: n3:8811192

Subject Item: _:vb4399312
rdf:type: n2:Context
rdf:value: Topoisomerase II–DNA cleavage complexes normally are short-lived and readily reversible (5,8,76), and the DNA cleavage/ligation equilibrium of the enzyme greatly favors ligation (5,8,11,>>23<<,26,27,77,78). Under equilibrium conditions, ∼0.5–1% of topoisomerase II in a DNA scission reaction mixture exists as a cleavage complex (65–67,78,79).
n2:mentions: n3:16246147

Subject Item: _:vb4399313
rdf:type: n2:Context
rdf:value: Topoisomerase II–DNA cleavage complexes normally are short-lived and readily reversible (5,8,76), and the DNA cleavage/ligation equilibrium of the enzyme greatly favors ligation (5,8,11,23,26,>>27<<,77,78). Under equilibrium conditions, ∼0.5–1% of topoisomerase II in a DNA scission reaction mixture exists as a cleavage complex (65–67,78,79).
n2:mentions: n3:8538787

Subject Item: _:vb4399314
rdf:type: n2:Context
rdf:value: Topoisomerase II–DNA cleavage complexes normally are short-lived and readily reversible (5,8,76), and the DNA cleavage/ligation equilibrium of the enzyme greatly favors ligation (5,8,11,23,26,27,>>77<<,78). Under equilibrium conditions, ∼0.5–1% of topoisomerase II in a DNA scission reaction mixture exists as a cleavage complex (65–67,78,79).
n2:mentions: n3:18403371

Subject Item: _:vb4399315
rdf:type: n2:Context
rdf:value: Topoisomerase II–DNA cleavage complexes normally are short-lived and readily reversible (5,8,76), and the DNA cleavage/ligation equilibrium of the enzyme greatly favors ligation (5,8,11,23,26,27,77,>>78<<). Under equilibrium conditions, ∼0.5–1% of topoisomerase II in a DNA scission reaction mixture exists as a cleavage complex (65–67,78,79).
n2:mentions: n3:2551368

Subject Item: _:vb4399316
rdf:type: n2:Context
rdf:value: Under equilibrium conditions, ∼0.5–1% of topoisomerase II in a DNA scission reaction mixture exists as a cleavage complex (65–>>67<<,78,79). Furthermore, when Mg2+ is utilized as the divalent metal ion, ∼1/2–3/4 of the complexes contain double-stranded breaks with the remainder containing single-stranded DNA breaks. The fact that a significant proportion of cleavage
n2:mentions: n3:6317692 n3:6305984 n3:2551367

Subject Item: _:vb4399317
rdf:type: n2:Context
rdf:value: Under equilibrium conditions, ∼0.5–1% of topoisomerase II in a DNA scission reaction mixture exists as a cleavage complex (65–67,>>78<<,79). Furthermore, when Mg2+ is utilized as the divalent metal ion, ∼1/2–3/4 of the complexes contain double-stranded breaks with the remainder containing single-stranded DNA breaks. The fact that a significant proportion of cleavage
n2:mentions: n3:18318502

Subject Item: _:vb4399318
rdf:type: n2:Context
rdf:value: Under equilibrium conditions, ∼0.5–1% of topoisomerase II in a DNA scission reaction mixture exists as a cleavage complex (65–67,78,>>79<<). Furthermore, when Mg2+ is utilized as the divalent metal ion, ∼1/2–3/4 of the complexes contain double-stranded breaks with the remainder containing single-stranded DNA breaks. The fact that a significant proportion of cleavage
n2:mentions: n3:2551368

Subject Item: _:vb4399319
rdf:type: n2:Context
rdf:value: The fact that a significant proportion of cleavage complexes contain single-stranded breaks was initially taken as an indication for poor coordination between the two protomer subunits of topoisomerase II (>>80<<). However, with hindsight, if the protomers cut the two strands of the double helix in a completely noncoordinated fashion, virtually no double-stranded DNA breaks would be generated (1% × 1% ≈ 0.01% cleavage complexes). These findings
n2:mentions: n3:12473657

Subject Item: _:vb4399320
rdf:type: n2:Context
rdf:value: These findings suggest that there must be a relatively high degree of coordination between the two protomer active sites of the enzyme, even if they do not act in complete concert with one another (>>78<<). To this point, once topoisomerase II cleaves the first strand, it is estimated that the enzyme cuts the second strand ∼20-fold faster (77,78).
n2:mentions: n3:18318502

Subject Item: _:vb4399321
rdf:type: n2:Context
rdf:value: To this point, once topoisomerase II cleaves the first strand, it is estimated that the enzyme cuts the second strand ∼20-fold faster (>>77<<,78).
n2:mentions: n3:18403371

Subject Item: _:vb4399322
rdf:type: n2:Context
rdf:value: To this point, once topoisomerase II cleaves the first strand, it is estimated that the enzyme cuts the second strand ∼20-fold faster (77,>>78<<).
n2:mentions: n3:18318502

Subject Item: _:vb4399323
rdf:type: n2:Context
rdf:value: The conversion of the terminal hydroxyl moiety to an oxyanion induces a nucleophilic attack on the phosphotyrosyl bond (>>11<<,23,26,27).
n2:mentions: n3:8811192

Subject Item: _:vb4399324
rdf:type: n2:Context
rdf:value: The conversion of the terminal hydroxyl moiety to an oxyanion induces a nucleophilic attack on the phosphotyrosyl bond (11,>>23<<,26,27). This action represents the reverse of the cleavage event and regenerates an intact DNA chain as well as the active site of topoisomerase II.
n2:mentions: n3:16246147

Subject Item: _:vb4399325
rdf:type: n2:Context
rdf:value: The conversion of the terminal hydroxyl moiety to an oxyanion induces a nucleophilic attack on the phosphotyrosyl bond (11,23,26,>>27<<). This action represents the reverse of the cleavage event and regenerates an intact DNA chain as well as the active site of topoisomerase II.
n2:mentions: n3:8538787

Subject Item: _:vb4399326
rdf:type: n5:Section
dc:title: topoisomerase ii as a cellular toxin
n5:contains: _:vb4399327 _:vb4399340 _:vb4399341 _:vb4399342 _:vb4399343 _:vb4399336 _:vb4399337 _:vb4399338 _:vb4399339 _:vb4399332 _:vb4399333 _:vb4399334 _:vb4399335 _:vb4399328 _:vb4399329 _:vb4399330 _:vb4399331

Subject Item: _:vb4399327
rdf:type: n2:Context
rdf:value: Proliferating cells cannot exist without type II topoisomerases (>>5<<,8,10). However, since these enzymes generate obligatory double-stranded DNA breaks as part of their reaction mechanism, they are intrinsically dangerous proteins.
n2:mentions: n3:10697411

Subject Item: _:vb4399328
rdf:type: n2:Context
rdf:value: Proliferating cells cannot exist without type II topoisomerases (5,>>8<<,10). However, since these enzymes generate obligatory double-stranded DNA breaks as part of their reaction mechanism, they are intrinsically dangerous proteins.
n2:mentions: n3:17681352

Subject Item: _:vb4399329
rdf:type: n2:Context
rdf:value: Proliferating cells cannot exist without type II topoisomerases (5,8,>>10<<). However, since these enzymes generate obligatory double-stranded DNA breaks as part of their reaction mechanism, they are intrinsically dangerous proteins.
n2:mentions: n3:12042765

Subject Item: _:vb4399330
rdf:type: n2:Context
rdf:value: Because of this dual persona, levels of cleavage complexes are maintained in a critical balance (>>5<<,8). When levels drop below threshold concentrations, daughter chromosomes remain entangled following replication. As a result, chromosomes cannot segregate properly during mitosis and cells die as a result of catastrophic mitotic failure
n2:mentions: n3:10697411

Subject Item: _:vb4399331
rdf:type: n2:Context
rdf:value: Because of this dual persona, levels of cleavage complexes are maintained in a critical balance (5,>>8<<). When levels drop below threshold concentrations, daughter chromosomes remain entangled following replication. As a result, chromosomes cannot segregate properly during mitosis and cells die as a result of catastrophic mitotic failure
n2:mentions: n3:17681352

Subject Item: _:vb4399332
rdf:type: n2:Context
rdf:value: intermediates are converted to permanent strand breaks when replication forks, transcription complexes or DNA tracking enzymes such as helicases attempt to traverse the covalently bound protein ‘roadblock’ in the genetic material (>>5<<,8,76,81). The resulting collision disrupts cleavage complexes and ultimately converts transient topoisomerase II-associated DNA breaks to permanent double-stranded breaks that are no longer tethered by proteinaceous bridges (5,8,76,81).
n2:mentions: n3:10697411

Subject Item: _:vb4399333
rdf:type: n2:Context
rdf:value: intermediates are converted to permanent strand breaks when replication forks, transcription complexes or DNA tracking enzymes such as helicases attempt to traverse the covalently bound protein ‘roadblock’ in the genetic material (5,>>8<<,76,81). The resulting collision disrupts cleavage complexes and ultimately converts transient topoisomerase II-associated DNA breaks to permanent double-stranded breaks that are no longer tethered by proteinaceous bridges (5,8,76,81).
n2:mentions: n3:17681352

Subject Item: _:vb4399334
rdf:type: n2:Context
rdf:value: are converted to permanent strand breaks when replication forks, transcription complexes or DNA tracking enzymes such as helicases attempt to traverse the covalently bound protein ‘roadblock’ in the genetic material (5,8,76,>>81<<). The resulting collision disrupts cleavage complexes and ultimately converts transient topoisomerase II-associated DNA breaks to permanent double-stranded breaks that are no longer tethered by proteinaceous bridges (5,8,76,81).
n2:mentions: n3:1698546

Subject Item: _:vb4399335
rdf:type: n2:Context
rdf:value: The resulting collision disrupts cleavage complexes and ultimately converts transient topoisomerase II-associated DNA breaks to permanent double-stranded breaks that are no longer tethered by proteinaceous bridges (>>5<<,8,76,81). The resulting damage and induction of recombination/repair pathways can trigger mutations, chromosomal translocations and other aberrations. When these permanent DNA breaks are present in sufficient numbers, they can overwhelm
n2:mentions: n3:10697411

Subject Item: _:vb4399336
rdf:type: n2:Context
rdf:value: The resulting collision disrupts cleavage complexes and ultimately converts transient topoisomerase II-associated DNA breaks to permanent double-stranded breaks that are no longer tethered by proteinaceous bridges (5,>>8<<,76,81). The resulting damage and induction of recombination/repair pathways can trigger mutations, chromosomal translocations and other aberrations. When these permanent DNA breaks are present in sufficient numbers, they can overwhelm the
n2:mentions: n3:17681352

Subject Item: _:vb4399337
rdf:type: n2:Context
rdf:value: The resulting collision disrupts cleavage complexes and ultimately converts transient topoisomerase II-associated DNA breaks to permanent double-stranded breaks that are no longer tethered by proteinaceous bridges (5,8,76,>>81<<). The resulting damage and induction of recombination/repair pathways can trigger mutations, chromosomal translocations and other aberrations. When these permanent DNA breaks are present in sufficient numbers, they can overwhelm the cell
n2:mentions: n3:1698546

Subject Item: _:vb4399338
rdf:type: n2:Context
rdf:value: When these permanent DNA breaks are present in sufficient numbers, they can overwhelm the cell and initiate death pathways in eukaryotes (>>4<<,5,7,8,13,76,81).
n2:mentions: n3:9748584

Subject Item: _:vb4399339
rdf:type: n2:Context
rdf:value: When these permanent DNA breaks are present in sufficient numbers, they can overwhelm the cell and initiate death pathways in eukaryotes (4,>>5<<,7,8,13,76,81).
n2:mentions: n3:10697411

Subject Item: _:vb4399340
rdf:type: n2:Context
rdf:value: When these permanent DNA breaks are present in sufficient numbers, they can overwhelm the cell and initiate death pathways in eukaryotes (4,5,>>7<<,8,13,76,81).
n2:mentions: n3:16857431

Subject Item: _:vb4399341
rdf:type: n2:Context
rdf:value: When these permanent DNA breaks are present in sufficient numbers, they can overwhelm the cell and initiate death pathways in eukaryotes (4,5,7,>>8<<,13,76,81).
n2:mentions: n3:17681352

Subject Item: _:vb4399342
rdf:type: n2:Context
rdf:value: When these permanent DNA breaks are present in sufficient numbers, they can overwhelm the cell and initiate death pathways in eukaryotes (4,5,7,8,>>13<<,76,81).
n2:mentions: n3:9748575

Subject Item: _:vb4399343
rdf:type: n2:Context
rdf:value: When these permanent DNA breaks are present in sufficient numbers, they can overwhelm the cell and initiate death pathways in eukaryotes (4,5,7,8,13,76,>>81<<).
n2:mentions: n3:1698546

Subject Item: _:vb4399344
rdf:type: n5:Section
dc:title: topoisomerase ii poisons
n5:contains: _:vb4399364 _:vb4399365 _:vb4399366 _:vb4399367 _:vb4399360 _:vb4399361 _:vb4399362 _:vb4399363 _:vb4399372 _:vb4399373 _:vb4399374 _:vb4399375 _:vb4399368 _:vb4399369 _:vb4399370 _:vb4399371 _:vb4399376 _:vb4399377 _:vb4399378 _:vb4399379 _:vb4399348 _:vb4399349 _:vb4399350 _:vb4399351 _:vb4399345 _:vb4399346 _:vb4399347 _:vb4399356 _:vb4399357 _:vb4399358 _:vb4399359 _:vb4399352 _:vb4399353 _:vb4399354 _:vb4399355

Subject Item: _:vb4399345
rdf:type: n2:Context
rdf:value: Chemicals in the first category decrease the overall activity of the enzyme and are known as catalytic inhibitors (>>5<<,8,76). Chemicals in the second category increase levels of topoisomerase II–DNA cleavage complexes. These latter compounds are said to ‘poison’ the type II enzyme and convert it to a cellular toxin that initiates the mutagenic and lethal
n2:mentions: n3:10697411

Subject Item: _:vb4399346
rdf:type: n2:Context
rdf:value: Chemicals in the first category decrease the overall activity of the enzyme and are known as catalytic inhibitors (5,>>8<<,76). Chemicals in the second category increase levels of topoisomerase II–DNA cleavage complexes. These latter compounds are said to ‘poison’ the type II enzyme and convert it to a cellular toxin that initiates the mutagenic and lethal
n2:mentions: n3:17681352

Subject Item: _:vb4399347
rdf:type: n2:Context
rdf:value: These latter compounds are said to ‘poison’ the type II enzyme and convert it to a cellular toxin that initiates the mutagenic and lethal consequences described above (>>5<<,8,76). Because of their actions, these compounds are referred to as ‘topoisomerase II poisons’ to distinguish them from inhibitors that do not affect enzyme-mediated DNA cleavage/ligation (5,8,76). Although some topoisomerase II poisons
n2:mentions: n3:10697411

Subject Item: _:vb4399348
rdf:type: n2:Context
rdf:value: These latter compounds are said to ‘poison’ the type II enzyme and convert it to a cellular toxin that initiates the mutagenic and lethal consequences described above (5,>>8<<,76). Because of their actions, these compounds are referred to as ‘topoisomerase II poisons’ to distinguish them from inhibitors that do not affect enzyme-mediated DNA cleavage/ligation (5,8,76). Although some topoisomerase II poisons
n2:mentions: n3:17681352

Subject Item: _:vb4399349
rdf:type: n2:Context
rdf:value: Because of their actions, these compounds are referred to as ‘topoisomerase II poisons’ to distinguish them from inhibitors that do not affect enzyme-mediated DNA cleavage/ligation (>>5<<,8,76). Although some topoisomerase II poisons also inhibit overall activity, the ‘gain of function’ induced by these compounds in the cell (i.e. increased levels of cleavage complexes) is a dominant phenotype (8,76).
n2:mentions: n3:10697411

Subject Item: _:vb4399350
rdf:type: n2:Context
rdf:value: Because of their actions, these compounds are referred to as ‘topoisomerase II poisons’ to distinguish them from inhibitors that do not affect enzyme-mediated DNA cleavage/ligation (5,>>8<<,76). Although some topoisomerase II poisons also inhibit overall activity, the ‘gain of function’ induced by these compounds in the cell (i.e. increased levels of cleavage complexes) is a dominant phenotype (8,76).
n2:mentions: n3:17681352

Subject Item: _:vb4399351
rdf:type: n2:Context
rdf:value: Although some topoisomerase II poisons also inhibit overall activity, the ‘gain of function’ induced by these compounds in the cell (i.e. increased levels of cleavage complexes) is a dominant phenotype (>>8<<,76).
n2:mentions: n3:17681352

Subject Item: _:vb4399352
rdf:type: n2:Context
rdf:value: Some compounds, such as the anticancer drug etoposide (see below), act by inhibiting the ability of the enzyme to ligate cleaved DNA molecules (>>5<<,8,76,78). Other poisons, such as abasic sites and other forms of DNA damage (see below) work primarily by enhancing the forward rate of scission (8,76,78). Because of the manner in which they act, abasic sites poison topoisomerase II
n2:mentions: n3:10697411

Subject Item: _:vb4399353
rdf:type: n2:Context
rdf:value: Some compounds, such as the anticancer drug etoposide (see below), act by inhibiting the ability of the enzyme to ligate cleaved DNA molecules (5,>>8<<,76,78). Other poisons, such as abasic sites and other forms of DNA damage (see below) work primarily by enhancing the forward rate of scission (8,76,78). Because of the manner in which they act, abasic sites poison topoisomerase II
n2:mentions: n3:17681352

Subject Item: _:vb4399354
rdf:type: n2:Context
rdf:value: Some compounds, such as the anticancer drug etoposide (see below), act by inhibiting the ability of the enzyme to ligate cleaved DNA molecules (5,8,76,>>78<<). Other poisons, such as abasic sites and other forms of DNA damage (see below) work primarily by enhancing the forward rate of scission (8,76,78). Because of the manner in which they act, abasic sites poison topoisomerase II without
n2:mentions: n3:18318502

Subject Item: _:vb4399355
rdf:type: n2:Context
rdf:value: Other poisons, such as abasic sites and other forms of DNA damage (see below) work primarily by enhancing the forward rate of scission (>>8<<,76,78). Because of the manner in which they act, abasic sites poison topoisomerase II without inhibiting overall catalytic activity.
n2:mentions: n3:17681352

Subject Item: _:vb4399356
rdf:type: n2:Context
rdf:value: Other poisons, such as abasic sites and other forms of DNA damage (see below) work primarily by enhancing the forward rate of scission (8,76,>>78<<). Because of the manner in which they act, abasic sites poison topoisomerase II without inhibiting overall catalytic activity.
n2:mentions: n3:18318502

Subject Item: _:vb4399357
rdf:type: n2:Context
rdf:value: Compounds in the first group are referred to as traditional, noncovalent, interfacial or redox-independent topoisomerase II poisons (>>8<<,46,76,82).
n2:mentions: n3:17681352

Subject Item: _:vb4399358
rdf:type: n2:Context
rdf:value: Compounds in the first group are referred to as traditional, noncovalent, interfacial or redox-independent topoisomerase II poisons (8,>>46<<,76,82). These chemicals form noncovalent interactions with topoisomerase II at the protein–DNA interface in the vicinity of the active site tyrosine (8,46,84–87). Because these compounds also interact with DNA within the ternary
n2:mentions: n3:12570766

Subject Item: _:vb4399359
rdf:type: n2:Context
rdf:value: Compounds in the first group are referred to as traditional, noncovalent, interfacial or redox-independent topoisomerase II poisons (8,46,76,>>82<<). These chemicals form noncovalent interactions with topoisomerase II at the protein–DNA interface in the vicinity of the active site tyrosine (8,46,84–87). Because these compounds also interact with DNA within the ternary
n2:mentions: n3:16101492

Subject Item: _:vb4399360
rdf:type: n2:Context
rdf:value: These chemicals form noncovalent interactions with topoisomerase II at the protein–DNA interface in the vicinity of the active site tyrosine (>>8<<,46,84–87).
n2:mentions: n3:17681352

Subject Item: _:vb4399361
rdf:type: n2:Context
rdf:value: These chemicals form noncovalent interactions with topoisomerase II at the protein–DNA interface in the vicinity of the active site tyrosine (8,>>46<<,84–87). Because these compounds also interact with DNA within the ternary enzyme–DNA–poison complex, they generally alter the DNA cleavage site specificity of the enzyme (88). Finally, their actions against topoisomerase II are not
n2:mentions: n3:12570766

Subject Item: _:vb4399362
rdf:type: n2:Context
rdf:value: These chemicals form noncovalent interactions with topoisomerase II at the protein–DNA interface in the vicinity of the active site tyrosine (8,46,84–>>87<<). Because these compounds also interact with DNA within the ternary enzyme–DNA–poison complex, they generally alter the DNA cleavage site specificity of the enzyme (88). Finally, their actions against topoisomerase II are not affected by
n2:mentions: n3:11264450 n3:11327821 n3:12094551 n3:10090731

Subject Item: _:vb4399363
rdf:type: n2:Context
rdf:value: Because these compounds also interact with DNA within the ternary enzyme–DNA–poison complex, they generally alter the DNA cleavage site specificity of the enzyme (>>88<<). Finally, their actions against topoisomerase II are not affected by reducing agents, such as dithiothreitol, and these compounds induce similar levels of enzyme-mediated DNA cleavage whether they are added to the binary topoisomerase
n2:mentions: n3:9582297

Subject Item: _:vb4399364
rdf:type: n2:Context
rdf:value: and these compounds induce similar levels of enzyme-mediated DNA cleavage whether they are added to the binary topoisomerase II–DNA complex or are incubated with the enzyme prior to the addition of nucleic acid substrates (>>8<<,82,83,89).
n2:mentions: n3:17681352

Subject Item: _:vb4399365
rdf:type: n2:Context
rdf:value: and these compounds induce similar levels of enzyme-mediated DNA cleavage whether they are added to the binary topoisomerase II–DNA complex or are incubated with the enzyme prior to the addition of nucleic acid substrates (8,>>82<<,83,89).
n2:mentions: n3:16101492

Subject Item: _:vb4399366
rdf:type: n2:Context
rdf:value: and these compounds induce similar levels of enzyme-mediated DNA cleavage whether they are added to the binary topoisomerase II–DNA complex or are incubated with the enzyme prior to the addition of nucleic acid substrates (8,82,>>83<<,89).
n2:mentions: n3:8910583

Subject Item: _:vb4399367
rdf:type: n2:Context
rdf:value: and these compounds induce similar levels of enzyme-mediated DNA cleavage whether they are added to the binary topoisomerase II–DNA complex or are incubated with the enzyme prior to the addition of nucleic acid substrates (8,82,83,>>89<<).
n2:mentions: n3:15182198

Subject Item: _:vb4399368
rdf:type: n2:Context
rdf:value: The redox-dependent poisons covalently adduct to the enzyme at amino acid residues outside of the active site (>>8<<,76,89–96) and generally enhance DNA cleavage at sites that are intrinsically cut by the enzyme (89,94).
n2:mentions: n3:17681352

Subject Item: _:vb4399369
rdf:type: n2:Context
rdf:value: The redox-dependent poisons covalently adduct to the enzyme at amino acid residues outside of the active site (8,76,89–>>96<<) and generally enhance DNA cleavage at sites that are intrinsically cut by the enzyme (89,94).
n2:mentions: n3:11258951 n3:17516663 n3:18293940 n3:17298034 n3:15035644 n3:16906772 n3:15833037 n3:15182198

Subject Item: _:vb4399370
rdf:type: n2:Context
rdf:value: The redox-dependent poisons covalently adduct to the enzyme at amino acid residues outside of the active site (8,76,89–96) and generally enhance DNA cleavage at sites that are intrinsically cut by the enzyme (>>89<<,94). Moreover, because these compounds require redox chemistry for activation, their ability to poison topoisomerase II is abrogated by reducing agents (89,91,94,97–99). Finally, compounds within this group enhance DNA cleavage when added
n2:mentions: n3:15182198

Subject Item: _:vb4399371
rdf:type: n2:Context
rdf:value: The redox-dependent poisons covalently adduct to the enzyme at amino acid residues outside of the active site (8,76,89–96) and generally enhance DNA cleavage at sites that are intrinsically cut by the enzyme (89,>>94<<). Moreover, because these compounds require redox chemistry for activation, their ability to poison topoisomerase II is abrogated by reducing agents (89,91,94,97–99). Finally, compounds within this group enhance DNA cleavage when added to
n2:mentions: n3:16906772

Subject Item: _:vb4399372
rdf:type: n2:Context
rdf:value: Moreover, because these compounds require redox chemistry for activation, their ability to poison topoisomerase II is abrogated by reducing agents (>>89<<,91,94,97–99).
n2:mentions: n3:15182198

Subject Item: _:vb4399373
rdf:type: n2:Context
rdf:value: Moreover, because these compounds require redox chemistry for activation, their ability to poison topoisomerase II is abrogated by reducing agents (89,>>91<<,94,97–99).
n2:mentions: n3:11258951

Subject Item: _:vb4399374
rdf:type: n2:Context
rdf:value: Moreover, because these compounds require redox chemistry for activation, their ability to poison topoisomerase II is abrogated by reducing agents (89,91,>>94<<,97–99). Finally, compounds within this group enhance DNA cleavage when added to the protein–DNA complex, but display the distinguishing feature of inhibiting topoisomerase II activity when incubated with the enzyme prior to the addition
n2:mentions: n3:16906772

Subject Item: _:vb4399375
rdf:type: n2:Context
rdf:value: Moreover, because these compounds require redox chemistry for activation, their ability to poison topoisomerase II is abrogated by reducing agents (89,91,94,97–>>99<<). Finally, compounds within this group enhance DNA cleavage when added to the protein–DNA complex, but display the distinguishing feature of inhibiting topoisomerase II activity when incubated with the enzyme prior to the addition of DNA
n2:mentions: n3:9044837 n3:9118913 n3:11468185

Subject Item: _:vb4399376
rdf:type: n2:Context
rdf:value: Finally, compounds within this group enhance DNA cleavage when added to the protein–DNA complex, but display the distinguishing feature of inhibiting topoisomerase II activity when incubated with the enzyme prior to the addition of DNA (>>89<<,91,94,97–99).
n2:mentions: n3:15182198

Subject Item: _:vb4399377
rdf:type: n2:Context
rdf:value: compounds within this group enhance DNA cleavage when added to the protein–DNA complex, but display the distinguishing feature of inhibiting topoisomerase II activity when incubated with the enzyme prior to the addition of DNA (89,>>91<<,94,97–99).
n2:mentions: n3:11258951

Subject Item: _:vb4399378
rdf:type: n2:Context
rdf:value: compounds within this group enhance DNA cleavage when added to the protein–DNA complex, but display the distinguishing feature of inhibiting topoisomerase II activity when incubated with the enzyme prior to the addition of DNA (89,91,>>94<<,97–99).
n2:mentions: n3:16906772

Subject Item: _:vb4399379
rdf:type: n2:Context
rdf:value: within this group enhance DNA cleavage when added to the protein–DNA complex, but display the distinguishing feature of inhibiting topoisomerase II activity when incubated with the enzyme prior to the addition of DNA (89,91,94,97–>>99<<).
n2:mentions: n3:9044837 n3:9118913 n3:11468185

Subject Item: _:vb4399380
rdf:type: n5:Section
dc:title: topoisomerase ii as a target for anticancer drugs
n5:contains: _:vb4399396 _:vb4399397 _:vb4399398 _:vb4399399 _:vb4399392 _:vb4399393 _:vb4399394 _:vb4399395 _:vb4399400 _:vb4399401 _:vb4399402 _:vb4399403 _:vb4399381 _:vb4399382 _:vb4399383 _:vb4399388 _:vb4399389 _:vb4399390 _:vb4399391 _:vb4399384 _:vb4399385 _:vb4399386 _:vb4399387

Subject Item: _:vb4399381
rdf:type: n2:Context
rdf:value: These drugs encompass a diverse group of natural and synthetic compounds that are commonly used to treat a variety of human malignancies (>>5<<,8,76,82,100,101).
n2:mentions: n3:10697411

Subject Item: _:vb4399382
rdf:type: n2:Context
rdf:value: These drugs encompass a diverse group of natural and synthetic compounds that are commonly used to treat a variety of human malignancies (5,>>8<<,76,82,100,101).
n2:mentions: n3:17681352

Subject Item: _:vb4399383
rdf:type: n2:Context
rdf:value: These drugs encompass a diverse group of natural and synthetic compounds that are commonly used to treat a variety of human malignancies (5,8,76,>>82<<,100,101). At the present time, six topoisomerase II-targeted anticancer agents are approved for use in the United States, and additional drugs are prescribed elsewhere in the world (101). These agents all act as traditional topoisomerase
n2:mentions: n3:16101492

Subject Item: _:vb4399384
rdf:type: n2:Context
rdf:value: These drugs encompass a diverse group of natural and synthetic compounds that are commonly used to treat a variety of human malignancies (5,8,76,82,>>100<<,101). At the present time, six topoisomerase II-targeted anticancer agents are approved for use in the United States, and additional drugs are prescribed elsewhere in the world (101). These agents all act as traditional topoisomerase II
n2:mentions: n3:16101488

Subject Item: _:vb4399385
rdf:type: n2:Context
rdf:value: These drugs encompass a diverse group of natural and synthetic compounds that are commonly used to treat a variety of human malignancies (5,8,76,82,100,>>101<<). At the present time, six topoisomerase II-targeted anticancer agents are approved for use in the United States, and additional drugs are prescribed elsewhere in the world (101). These agents all act as traditional topoisomerase II
n2:mentions: n3:16110609

Subject Item: _:vb4399386
rdf:type: n2:Context
rdf:value: At the present time, six topoisomerase II-targeted anticancer agents are approved for use in the United States, and additional drugs are prescribed elsewhere in the world (>>101<<). These agents all act as traditional topoisomerase II poisons and function primarily by inhibiting enzyme-mediated DNA ligation. Figure 5.
n2:mentions: n3:16110609

Subject Item: _:vb4399387
rdf:type: n2:Context
rdf:value: One of the first topoisomerase II-targeted agents to be discovered was etoposide, which is derived from podophyllotoxin (>>100<<,102). This natural product is found in Podophyllum peltatum, more commonly known as the mayapple or mandrake plant (100,102).
n2:mentions: n3:16101488

Subject Item: _:vb4399388
rdf:type: n2:Context
rdf:value: One of the first topoisomerase II-targeted agents to be discovered was etoposide, which is derived from podophyllotoxin (100,>>102<<). This natural product is found in Podophyllum peltatum, more commonly known as the mayapple or mandrake plant (100,102).
n2:mentions: n3:9893622

Subject Item: _:vb4399389
rdf:type: n2:Context
rdf:value: This natural product is found in Podophyllum peltatum, more commonly known as the mayapple or mandrake plant (>>100<<,102). Podophyllotoxin has been used as a folk remedy for over a 1000 years (100,102). The clinical use of this compound as an antineoplastic agent was prevented by high toxicity, but two synthetic analogs, etoposide and teniposide,
n2:mentions: n3:16101488

Subject Item: _:vb4399390
rdf:type: n2:Context
rdf:value: This natural product is found in Podophyllum peltatum, more commonly known as the mayapple or mandrake plant (100,>>102<<). Podophyllotoxin has been used as a folk remedy for over a 1000 years (100,102). The clinical use of this compound as an antineoplastic agent was prevented by high toxicity, but two synthetic analogs, etoposide and teniposide, displayed
n2:mentions: n3:9893622

Subject Item: _:vb4399391
rdf:type: n2:Context
rdf:value: Podophyllotoxin has been used as a folk remedy for over a 1000 years (>>100<<,102). The clinical use of this compound as an antineoplastic agent was prevented by high toxicity, but two synthetic analogs, etoposide and teniposide, displayed increased antineoplastic activity and decreased toxicity (100,102).
n2:mentions: n3:16101488

Subject Item: _:vb4399392
rdf:type: n2:Context
rdf:value: Podophyllotoxin has been used as a folk remedy for over a 1000 years (100,>>102<<). The clinical use of this compound as an antineoplastic agent was prevented by high toxicity, but two synthetic analogs, etoposide and teniposide, displayed increased antineoplastic activity and decreased toxicity (100,102).
n2:mentions: n3:9893622

Subject Item: _:vb4399393
rdf:type: n2:Context
rdf:value: The clinical use of this compound as an antineoplastic agent was prevented by high toxicity, but two synthetic analogs, etoposide and teniposide, displayed increased antineoplastic activity and decreased toxicity (>>100<<,102). Etoposide was approved for clinical use against cancer in the mid-1980s and for several years was the most widely prescribed anticancer drug in the world (100,102).
n2:mentions: n3:16101488

Subject Item: _:vb4399394
rdf:type: n2:Context
rdf:value: The clinical use of this compound as an antineoplastic agent was prevented by high toxicity, but two synthetic analogs, etoposide and teniposide, displayed increased antineoplastic activity and decreased toxicity (100,>>102<<). Etoposide was approved for clinical use against cancer in the mid-1980s and for several years was the most widely prescribed anticancer drug in the world (100,102).
n2:mentions: n3:9893622

Subject Item: _:vb4399395
rdf:type: n2:Context
rdf:value: Etoposide was approved for clinical use against cancer in the mid-1980s and for several years was the most widely prescribed anticancer drug in the world (>>100<<,102).
n2:mentions: n3:16101488

Subject Item: _:vb4399396
rdf:type: n2:Context
rdf:value: Etoposide was approved for clinical use against cancer in the mid-1980s and for several years was the most widely prescribed anticancer drug in the world (100,>>102<<).
n2:mentions: n3:9893622

Subject Item: _:vb4399397
rdf:type: n2:Context
rdf:value: Etoposide and other drugs such as doxorubicin (and its derivatives) are front-line therapy for a variety of systemic cancers and solid tumors, including leukemias, lymphomas, sarcomas and breast, lung and germline cancers (100–>>102<<). Mitoxantrone is used to treat breast cancer, and both it and amsacrine are used to treat relapsed acute myeloid leukemia (103,104).
n2:mentions: n3:16101488 n3:9893622 n3:16110609

Subject Item: _:vb4399398
rdf:type: n2:Context
rdf:value: Mitoxantrone is used to treat breast cancer, and both it and amsacrine are used to treat relapsed acute myeloid leukemia (>>103<<,104). Every form of cancer that is considered to be curable by chemotherapy utilizes treatment regimens that include topoisomerase II-targeted drugs (100–102,105). In addition to the use of mitoxantrone in anticancer regimens, it is used
n2:mentions: n3:18473961

Subject Item: _:vb4399399
rdf:type: n2:Context
rdf:value: Mitoxantrone is used to treat breast cancer, and both it and amsacrine are used to treat relapsed acute myeloid leukemia (103,>>104<<). Every form of cancer that is considered to be curable by chemotherapy utilizes treatment regimens that include topoisomerase II-targeted drugs (100–102,105). In addition to the use of mitoxantrone in anticancer regimens, it is used as a
n2:mentions: n3:18367336

Subject Item: _:vb4399400
rdf:type: n2:Context
rdf:value: Every form of cancer that is considered to be curable by chemotherapy utilizes treatment regimens that include topoisomerase II-targeted drugs (100–>>102<<,105). In addition to the use of mitoxantrone in anticancer regimens, it is used as a treatment for autoimmune diseases, such as multiple sclerosis (106).
n2:mentions: n3:16101488 n3:9893622 n3:16110609

Subject Item: _:vb4399401
rdf:type: n2:Context
rdf:value: Every form of cancer that is considered to be curable by chemotherapy utilizes treatment regimens that include topoisomerase II-targeted drugs (100–102,>>105<<). In addition to the use of mitoxantrone in anticancer regimens, it is used as a treatment for autoimmune diseases, such as multiple sclerosis (106).
n2:mentions: n3:9748545

Subject Item: _:vb4399402
rdf:type: n2:Context
rdf:value: In addition to the use of mitoxantrone in anticancer regimens, it is used as a treatment for autoimmune diseases, such as multiple sclerosis (>>106<<).
n2:mentions: n3:18317677

Subject Item: _:vb4399403
rdf:type: n2:Context
rdf:value: appreciably in quiescent cells, the actions of topoisomerase II-targeted agents against the β isoform in differentiated tissues, such as cardiac cells, most likely are responsible for much of the off-target toxicity of these drugs (107–>>109<<). Alternatively, since topoisomerase IIα and topoisomerase IIβ are involved in different cellular processes, it may be that cleavage complexes formed with one or the other isoform are more likely to be converted to permanent DNA strand
n2:mentions: n3:8394080 n3:16923961 n3:17578914

Subject Item: _:vb4399404
rdf:type: n5:Section
dc:title: dietary topoisomerase ii poisons
n5:contains: _:vb4399424 _:vb4399412 _:vb4399413 _:vb4399414 _:vb4399415 _:vb4399408 _:vb4399409 _:vb4399410 _:vb4399411 _:vb4399420 _:vb4399421 _:vb4399422 _:vb4399423 _:vb4399416 _:vb4399417 _:vb4399418 _:vb4399419 _:vb4399405 _:vb4399406 _:vb4399407

Subject Item: _:vb4399405
rdf:type: n2:Context
rdf:value: The most prominent natural products with activity against the mammalian type II enzymes are the bioflavonoids (i.e. phytoestrogens) (110–>>113<<). Bioflavonoids represent a broad group of polyphenolic compounds (including flavones, flavonols, isoflavones and catechins) that are components of many fruits, vegetables and plant leaves (114–117). These compounds affect human cells
n2:mentions: n3:10758153 n3:7769390 n3:11030085 n3:15223063

Subject Item: _:vb4399406
rdf:type: n2:Context
rdf:value: Bioflavonoids represent a broad group of polyphenolic compounds (including flavones, flavonols, isoflavones and catechins) that are components of many fruits, vegetables and plant leaves (114–>>117<<). These compounds affect human cells through a variety of pathways; they are strong antioxidants and efficient inhibitors of growth factor receptor tyrosine kinases (114–117). In addition, many bioflavonoids, especially genistein, are
n2:mentions: n3:16613577 n3:16425281 n3:7901532 n3:10837323

Subject Item: _:vb4399407
rdf:type: n2:Context
rdf:value: These compounds affect human cells through a variety of pathways; they are strong antioxidants and efficient inhibitors of growth factor receptor tyrosine kinases (114–>>117<<). In addition, many bioflavonoids, especially genistein, are potent topoisomerase II poisons (90,110–113,118–122). Figure 6.
n2:mentions: n3:16613577 n3:16425281 n3:7901532 n3:10837323

Subject Item: _:vb4399408
rdf:type: n2:Context
rdf:value: In addition, many bioflavonoids, especially genistein, are potent topoisomerase II poisons (>>90<<,110–113,118–122).
n2:mentions: n3:18293940

Subject Item: _:vb4399409
rdf:type: n2:Context
rdf:value: In addition, many bioflavonoids, especially genistein, are potent topoisomerase II poisons (90,110–>>113<<,118–122). Figure 6.
n2:mentions: n3:10758153 n3:7769390 n3:11030085 n3:15223063

Subject Item: _:vb4399410
rdf:type: n2:Context
rdf:value: In addition, many bioflavonoids, especially genistein, are potent topoisomerase II poisons (90,110–113,118–>>122<<). Figure 6.
n2:mentions: n3:2548712 n3:17458941 n3:7632161 n3:1313232 n3:18461976

Subject Item: _:vb4399411
rdf:type: n2:Context
rdf:value: Abbreviations used are epigallocatechin gallate (EGCG), N-acetyl-p-benzoquinone imine (NAPQI) and 2-(4-chloro-phenyl)-[>>1<<,4]benzoquinone (4′Cl-2,5pQ).
n2:mentions: n3:18626473

Subject Item: _:vb4399412
rdf:type: n2:Context
rdf:value: Abbreviations used are epigallocatechin gallate (EGCG), N-acetyl-p-benzoquinone imine (NAPQI) and 2-(4-chloro-phenyl)-[1,>>4<<]benzoquinone (4′Cl-2,5pQ).
n2:mentions: n3:9748584

Subject Item: _:vb4399413
rdf:type: n2:Context
rdf:value: Genistein, which is prominent in soy, is believed to be a chemopreventative agent in adults that contributes to the low incidence of breast and colorectal cancers in the Pacific Rim (Figure 6) (>>116<<,117). However, as discussed below, there also is evidence associating genistein consumption during pregnancy with the development of infant leukemias (111,123–126).
n2:mentions: n3:16425281

Subject Item: _:vb4399414
rdf:type: n2:Context
rdf:value: Genistein, which is prominent in soy, is believed to be a chemopreventative agent in adults that contributes to the low incidence of breast and colorectal cancers in the Pacific Rim (Figure 6) (116,>>117<<). However, as discussed below, there also is evidence associating genistein consumption during pregnancy with the development of infant leukemias (111,123–126).
n2:mentions: n3:16613577

Subject Item: _:vb4399415
rdf:type: n2:Context
rdf:value: However, as discussed below, there also is evidence associating genistein consumption during pregnancy with the development of infant leukemias (>>111<<,123–126). In addition, (–)-epigallocatechin gallate (EGCG), the most abundant and biologically active polyphenol in green tea, is a topoisomerase II poison (Figure 6) (90,116,121). Many of the therapeutic benefits of green tea have been
n2:mentions: n3:10758153

Subject Item: _:vb4399416
rdf:type: n2:Context
rdf:value: However, as discussed below, there also is evidence associating genistein consumption during pregnancy with the development of infant leukemias (111,123–>>126<<). In addition, (–)-epigallocatechin gallate (EGCG), the most abundant and biologically active polyphenol in green tea, is a topoisomerase II poison (Figure 6) (90,116,121). Many of the therapeutic benefits of green tea have been
n2:mentions: n3:10781030 n3:7966394 n3:8932918 n3:15767345

Subject Item: _:vb4399417
rdf:type: n2:Context
rdf:value: In addition, (–)-epigallocatechin gallate (EGCG), the most abundant and biologically active polyphenol in green tea, is a topoisomerase II poison (Figure 6) (>>90<<,116,121). Many of the therapeutic benefits of green tea have been attributed to this compound.
n2:mentions: n3:18293940

Subject Item: _:vb4399418
rdf:type: n2:Context
rdf:value: In addition, (–)-epigallocatechin gallate (EGCG), the most abundant and biologically active polyphenol in green tea, is a topoisomerase II poison (Figure 6) (90,>>116<<,121). Many of the therapeutic benefits of green tea have been attributed to this compound.
n2:mentions: n3:16425281

Subject Item: _:vb4399419
rdf:type: n2:Context
rdf:value: In addition, (–)-epigallocatechin gallate (EGCG), the most abundant and biologically active polyphenol in green tea, is a topoisomerase II poison (Figure 6) (90,116,>>121<<). Many of the therapeutic benefits of green tea have been attributed to this compound.
n2:mentions: n3:18461976

Subject Item: _:vb4399420
rdf:type: n2:Context
rdf:value: The ring structure of genistein is remarkably similar to that of quinolones (>>122<<). These latter compounds, which target the prokaryotic type II topoisomerases DNA gyrase and topoisomerase IV, represent the most active and broad-spectrum antibacterials currently in clinical use (127–129).
n2:mentions: n3:17458941

Subject Item: _:vb4399421
rdf:type: n2:Context
rdf:value: These latter compounds, which target the prokaryotic type II topoisomerases DNA gyrase and topoisomerase IV, represent the most active and broad-spectrum antibacterials currently in clinical use (127–>>129<<). Like the quinolones and the anticancer drugs discussed above, genistein increases levels of topoisomerase II–DNA cleavage complexes as a traditional topoisomerase II poison (122). In contrast, since many bioflavonoids undergo redox
n2:mentions: n3:12570763 n3:9748489 n3:11254893

Subject Item: _:vb4399422
rdf:type: n2:Context
rdf:value: Like the quinolones and the anticancer drugs discussed above, genistein increases levels of topoisomerase II–DNA cleavage complexes as a traditional topoisomerase II poison (>>122<<). In contrast, since many bioflavonoids undergo redox chemistry, several members of the class act as redox-dependent topoisomerase II points. EGCG and some related catechins poison topoisomerase II by this latter mechanism (90,121).
n2:mentions: n3:17458941

Subject Item: _:vb4399423
rdf:type: n2:Context
rdf:value: EGCG and some related catechins poison topoisomerase II by this latter mechanism (>>90<<,121).
n2:mentions: n3:18293940

Subject Item: _:vb4399424
rdf:type: n2:Context
rdf:value: EGCG and some related catechins poison topoisomerase II by this latter mechanism (90,>>121<<).
n2:mentions: n3:18461976

Subject Item: _:vb4399425
rdf:type: n5:Section
dc:title: environmental topoisomerase ii poisons
n5:contains: _:vb4399426 _:vb4399427 _:vb4399428 _:vb4399429 _:vb4399430 _:vb4399431 _:vb4399432 _:vb4399433 _:vb4399434 _:vb4399435 _:vb4399436 _:vb4399437 _:vb4399438 _:vb4399439 _:vb4399440 _:vb4399441 _:vb4399442 _:vb4399443 _:vb4399444 _:vb4399445

Subject Item: _:vb4399426
rdf:type: n2:Context
rdf:value: The toxic metabolites of some drugs and industrial chemicals are topoisomerase II poisons (Figure 6) (>>92<<,93,95,130,131). In all cases described to date, these chemicals include quinones (aromatic rings that feature ketone groups) as part of their structures (132–135).
n2:mentions: n3:17516663

Subject Item: _:vb4399427
rdf:type: n2:Context
rdf:value: The toxic metabolites of some drugs and industrial chemicals are topoisomerase II poisons (Figure 6) (92,>>93<<,95,130,131). In all cases described to date, these chemicals include quinones (aromatic rings that feature ketone groups) as part of their structures (132–135).
n2:mentions: n3:17298034

Subject Item: _:vb4399428
rdf:type: n2:Context
rdf:value: The toxic metabolites of some drugs and industrial chemicals are topoisomerase II poisons (Figure 6) (92,93,>>95<<,130,131). In all cases described to date, these chemicals include quinones (aromatic rings that feature ketone groups) as part of their structures (132–135).
n2:mentions: n3:15833037

Subject Item: _:vb4399429
rdf:type: n2:Context
rdf:value: The toxic metabolites of some drugs and industrial chemicals are topoisomerase II poisons (Figure 6) (92,93,95,>>130<<,131). In all cases described to date, these chemicals include quinones (aromatic rings that feature ketone groups) as part of their structures (132–135).
n2:mentions: n3:11086940

Subject Item: _:vb4399430
rdf:type: n2:Context
rdf:value: The toxic metabolites of some drugs and industrial chemicals are topoisomerase II poisons (Figure 6) (92,93,95,130,>>131<<). In all cases described to date, these chemicals include quinones (aromatic rings that feature ketone groups) as part of their structures (132–135).
n2:mentions: n3:15935817

Subject Item: _:vb4399431
rdf:type: n2:Context
rdf:value: In all cases described to date, these chemicals include quinones (aromatic rings that feature ketone groups) as part of their structures (132–>>135<<). Quinones commonly are produced in the body as a result of detoxification or metabolism pathways (132–135). These compounds are highly reactive and often damage cells by generating oxidative radicals and by covalently modifying proteins
n2:mentions: n3:8735467 n3:10220568 n3:11405442 n3:11888901

Subject Item: _:vb4399432
rdf:type: n2:Context
rdf:value: Quinones commonly are produced in the body as a result of detoxification or metabolism pathways (132–>>135<<). These compounds are highly reactive and often damage cells by generating oxidative radicals and by covalently modifying proteins and (to a lesser extent) nucleic acids (132–135).
n2:mentions: n3:8735467 n3:10220568 n3:11405442 n3:11888901

Subject Item: _:vb4399433
rdf:type: n2:Context
rdf:value: These compounds are highly reactive and often damage cells by generating oxidative radicals and by covalently modifying proteins and (to a lesser extent) nucleic acids (132–>>135<<).
n2:mentions: n3:8735467 n3:10220568 n3:11405442 n3:11888901

Subject Item: _:vb4399434
rdf:type: n2:Context
rdf:value: acetaminophen is the most widely utilized analgesic in the world, the second most prevalent cause of toxic drug admissions to emergency departments in the United States is overdosage (both accidental and intentional) of this drug (>>136<<). The toxic metabolite of acetaminophen, N-acetyl p-benzoquinone imine (NAPQI), is a potent topoisomerase II poison that produces liver failure (96).
n2:mentions: n3:11319582

Subject Item: _:vb4399435
rdf:type: n2:Context
rdf:value: The toxic metabolite of acetaminophen, N-acetyl p-benzoquinone imine (NAPQI), is a potent topoisomerase II poison that produces liver failure (>>96<<). Benzene is an industrial solvent that is associated with the development of human leukemias (130,132–135). One of the most prevalent metabolites of benzene, 1,4-benzoquinone, is a highly reactive topoisomerase II poison
n2:mentions: n3:15035644

Subject Item: _:vb4399436
rdf:type: n2:Context
rdf:value: Benzene is an industrial solvent that is associated with the development of human leukemias (>>130<<,132–135). One of the most prevalent metabolites of benzene, 1,4-benzoquinone, is a highly reactive topoisomerase II poison (92,93,95,130,131). Finally, polychlorinated biphenyls (PCBs), which have multiple industrial uses, have been
n2:mentions: n3:11086940

Subject Item: _:vb4399437
rdf:type: n2:Context
rdf:value: Benzene is an industrial solvent that is associated with the development of human leukemias (130,132–>>135<<). One of the most prevalent metabolites of benzene, 1,4-benzoquinone, is a highly reactive topoisomerase II poison (92,93,95,130,131). Finally, polychlorinated biphenyls (PCBs), which have multiple industrial uses, have been linked to a
n2:mentions: n3:8735467 n3:10220568 n3:11405442 n3:11888901

Subject Item: _:vb4399438
rdf:type: n2:Context
rdf:value: One of the most prevalent metabolites of benzene, 1,4-benzoquinone, is a highly reactive topoisomerase II poison (>>92<<,93,95,130,131).
n2:mentions: n3:17516663

Subject Item: _:vb4399439
rdf:type: n2:Context
rdf:value: One of the most prevalent metabolites of benzene, 1,4-benzoquinone, is a highly reactive topoisomerase II poison (92,>>93<<,95,130,131).
n2:mentions: n3:17298034

Subject Item: _:vb4399440
rdf:type: n2:Context
rdf:value: One of the most prevalent metabolites of benzene, 1,4-benzoquinone, is a highly reactive topoisomerase II poison (92,93,>>95<<,130,131). Finally, polychlorinated biphenyls (PCBs), which have multiple industrial uses, have been linked to a variety of human health issues (94). The quinone metabolites of these compounds display activity against human type II
n2:mentions: n3:15833037

Subject Item: _:vb4399441
rdf:type: n2:Context
rdf:value: One of the most prevalent metabolites of benzene, 1,4-benzoquinone, is a highly reactive topoisomerase II poison (92,93,95,>>130<<,131). Finally, polychlorinated biphenyls (PCBs), which have multiple industrial uses, have been linked to a variety of human health issues (94). The quinone metabolites of these compounds display activity against human type II
n2:mentions: n3:11086940

Subject Item: _:vb4399442
rdf:type: n2:Context
rdf:value: One of the most prevalent metabolites of benzene, 1,4-benzoquinone, is a highly reactive topoisomerase II poison (92,93,95,130,>>131<<). Finally, polychlorinated biphenyls (PCBs), which have multiple industrial uses, have been linked to a variety of human health issues (94). The quinone metabolites of these compounds display activity against human type II topoisomerases.
n2:mentions: n3:15935817

Subject Item: _:vb4399443
rdf:type: n2:Context
rdf:value: Finally, polychlorinated biphenyls (PCBs), which have multiple industrial uses, have been linked to a variety of human health issues (>>94<<). The quinone metabolites of these compounds display activity against human type II topoisomerases. Consistent with their highly active redox chemistry, all quinone-based topoisomerase II poisons act in a redox-dependent manner that
n2:mentions: n3:16906772

Subject Item: _:vb4399444
rdf:type: n2:Context
rdf:value: Consistent with their highly active redox chemistry, all quinone-based topoisomerase II poisons act in a redox-dependent manner that involves covalent attachment to the enzyme (91–>>93<<,97).
n2:mentions: n3:17516663 n3:17298034 n3:11258951

Subject Item: _:vb4399445
rdf:type: n2:Context
rdf:value: Consistent with their highly active redox chemistry, all quinone-based topoisomerase II poisons act in a redox-dependent manner that involves covalent attachment to the enzyme (91–93,>>97<<).
n2:mentions: n3:9044837

Subject Item: _:vb4399446
rdf:type: n5:Section
dc:title: dna damage as topoisomerase ii poisons
n5:contains: _:vb4399460 _:vb4399461 _:vb4399462 _:vb4399456 _:vb4399457 _:vb4399458 _:vb4399459 _:vb4399452 _:vb4399453 _:vb4399454 _:vb4399455 _:vb4399448 _:vb4399449 _:vb4399450 _:vb4399451 _:vb4399447

Subject Item: _:vb4399447
rdf:type: n2:Context
rdf:value: Several forms of nucleic acid damage enhance topoisomerase II-mediated DNA cleavage (Figure 6) (>>69<<,78,137–144). The type II enzymes are particularly sensitive to abasic sites, alkylated bases that contain exocyclic rings, and other lesions that distort the double helix.
n2:mentions: n3:15751973

Subject Item: _:vb4399448
rdf:type: n2:Context
rdf:value: Several forms of nucleic acid damage enhance topoisomerase II-mediated DNA cleavage (Figure 6) (69,>>78<<,137–144). The type II enzymes are particularly sensitive to abasic sites, alkylated bases that contain exocyclic rings, and other lesions that distort the double helix.
n2:mentions: n3:18318502

Subject Item: _:vb4399449
rdf:type: n2:Context
rdf:value: Several forms of nucleic acid damage enhance topoisomerase II-mediated DNA cleavage (Figure 6) (69,78,137–>>144<<). The type II enzymes are particularly sensitive to abasic sites, alkylated bases that contain exocyclic rings, and other lesions that distort the double helix.
n2:mentions: n3:10514448 n3:10756196 n3:14523238 n3:9748592 n3:9054451 n3:9166762 n3:10569932 n3:8995415

Subject Item: _:vb4399450
rdf:type: n2:Context
rdf:value: DNA damage increases cleavage at naturally occurring sites of topoisomerase II action (>>69<<,78,137–144). In order to enhance cleavage, lesions must be located within the four-base stagger that separates the two scissile bonds (69,78,137–144).
n2:mentions: n3:15751973

Subject Item: _:vb4399451
rdf:type: n2:Context
rdf:value: DNA damage increases cleavage at naturally occurring sites of topoisomerase II action (69,>>78<<,137–144). In order to enhance cleavage, lesions must be located within the four-base stagger that separates the two scissile bonds (69,78,137–144).
n2:mentions: n3:18318502

Subject Item: _:vb4399452
rdf:type: n2:Context
rdf:value: DNA damage increases cleavage at naturally occurring sites of topoisomerase II action (69,78,137–>>144<<). In order to enhance cleavage, lesions must be located within the four-base stagger that separates the two scissile bonds (69,78,137–144).
n2:mentions: n3:10514448 n3:10756196 n3:14523238 n3:9748592 n3:9054451 n3:9166762 n3:10569932 n3:8995415

Subject Item: _:vb4399453
rdf:type: n2:Context
rdf:value: In order to enhance cleavage, lesions must be located within the four-base stagger that separates the two scissile bonds (>>69<<,78,137–144).
n2:mentions: n3:15751973

Subject Item: _:vb4399454
rdf:type: n2:Context
rdf:value: In order to enhance cleavage, lesions must be located within the four-base stagger that separates the two scissile bonds (69,>>78<<,137–144). Unlike the traditional and redox-dependent topoisomerase II poisons discussed above, DNA damage has no obvious effect on rates of topoisomerase II-mediated ligation and appears to act primarily by enhancing the forward rate of
n2:mentions: n3:18318502

Subject Item: _:vb4399455
rdf:type: n2:Context
rdf:value: In order to enhance cleavage, lesions must be located within the four-base stagger that separates the two scissile bonds (69,78,137–>>144<<). Unlike the traditional and redox-dependent topoisomerase II poisons discussed above, DNA damage has no obvious effect on rates of topoisomerase II-mediated ligation and appears to act primarily by enhancing the forward rate of scission
n2:mentions: n3:10514448 n3:10756196 n3:14523238 n3:9748592 n3:9054451 n3:9166762 n3:10569932 n3:8995415

Subject Item: _:vb4399456
rdf:type: n2:Context
rdf:value: Unlike the traditional and redox-dependent topoisomerase II poisons discussed above, DNA damage has no obvious effect on rates of topoisomerase II-mediated ligation and appears to act primarily by enhancing the forward rate of scission (>>69<<,78,137–144).
n2:mentions: n3:15751973

Subject Item: _:vb4399457
rdf:type: n2:Context
rdf:value: the traditional and redox-dependent topoisomerase II poisons discussed above, DNA damage has no obvious effect on rates of topoisomerase II-mediated ligation and appears to act primarily by enhancing the forward rate of scission (69,>>78<<,137–144).
n2:mentions: n3:18318502

Subject Item: _:vb4399458
rdf:type: n2:Context
rdf:value: traditional and redox-dependent topoisomerase II poisons discussed above, DNA damage has no obvious effect on rates of topoisomerase II-mediated ligation and appears to act primarily by enhancing the forward rate of scission (69,78,137–>>144<<).
n2:mentions: n3:10514448 n3:10756196 n3:14523238 n3:9054451 n3:9748592 n3:9166762 n3:10569932 n3:8995415

Subject Item: _:vb4399459
rdf:type: n2:Context
rdf:value: However, human topoisomerase IIα and topoisomerase IIβ both appear to play roles in fragmenting genomic DNA and releasing chromosomal loops during apoptosis (>>145<<,146). It has been suggested that the apoptotic activities of topoisomerase II are enhanced (or perhaps triggered) by DNA lesions that are generated following the release of oxidative radicals from permeable mitochondria in apoptotic cells
n2:mentions: n3:11940566

Subject Item: _:vb4399460
rdf:type: n2:Context
rdf:value: However, human topoisomerase IIα and topoisomerase IIβ both appear to play roles in fragmenting genomic DNA and releasing chromosomal loops during apoptosis (145,>>146<<). It has been suggested that the apoptotic activities of topoisomerase II are enhanced (or perhaps triggered) by DNA lesions that are generated following the release of oxidative radicals from permeable mitochondria in apoptotic cells
n2:mentions: n3:16304768

Subject Item: _:vb4399461
rdf:type: n2:Context
rdf:value: It has been suggested that the apoptotic activities of topoisomerase II are enhanced (or perhaps triggered) by DNA lesions that are generated following the release of oxidative radicals from permeable mitochondria in apoptotic cells (>>145<<,146).
n2:mentions: n3:11940566

Subject Item: _:vb4399462
rdf:type: n2:Context
rdf:value: has been suggested that the apoptotic activities of topoisomerase II are enhanced (or perhaps triggered) by DNA lesions that are generated following the release of oxidative radicals from permeable mitochondria in apoptotic cells (145,>>146<<).
n2:mentions: n3:16304768

Subject Item: _:vb4399463
rdf:type: n5:Section
dc:title: topoisomerase ii and leukemia
n5:contains: _:vb4399480 _:vb4399481 _:vb4399482 _:vb4399483 _:vb4399484 _:vb4399485 _:vb4399486 _:vb4399487 _:vb4399472 _:vb4399473 _:vb4399474 _:vb4399475 _:vb4399476 _:vb4399477 _:vb4399478 _:vb4399479 _:vb4399464 _:vb4399465 _:vb4399466 _:vb4399467 _:vb4399468 _:vb4399469 _:vb4399470 _:vb4399471 _:vb4399488 _:vb4399489 _:vb4399490 _:vb4399491

Subject Item: _:vb4399464
rdf:type: n2:Context
rdf:value: Despite the importance of topoisomerase II in cancer chemotherapy, evidence suggests that DNA cleavage mediated by the enzyme can trigger chromosomal translocations that lead to specific types of leukemia (Figure 4) (5–>>8<<,76,147,148). To this point, 2–3% of patients who receive regimens that include etoposide or other topoisomerase II-targeted drugs eventually develop acute myeloid leukemias (AMLs).
n2:mentions: n3:10697411 n3:16857431 n3:17681352 n3:11340607

Subject Item: _:vb4399465
rdf:type: n2:Context
rdf:value: Despite the importance of topoisomerase II in cancer chemotherapy, evidence suggests that DNA cleavage mediated by the enzyme can trigger chromosomal translocations that lead to specific types of leukemia (Figure 4) (5–8,76,>>147<<,148). To this point, 2–3% of patients who receive regimens that include etoposide or other topoisomerase II-targeted drugs eventually develop acute myeloid leukemias (AMLs).
n2:mentions: n3:7756657

Subject Item: _:vb4399466
rdf:type: n2:Context
rdf:value: Despite the importance of topoisomerase II in cancer chemotherapy, evidence suggests that DNA cleavage mediated by the enzyme can trigger chromosomal translocations that lead to specific types of leukemia (Figure 4) (5–8,76,147,>>148<<). To this point, 2–3% of patients who receive regimens that include etoposide or other topoisomerase II-targeted drugs eventually develop acute myeloid leukemias (AMLs).
n2:mentions: n3:9748598

Subject Item: _:vb4399467
rdf:type: n2:Context
rdf:value: Most of these leukemias are accompanied by translocations with breakpoints in the MLL (mixed lineage leukemia) gene at chromosomal band 11q23 (>>6<<,7,76). The MLL protein is a histone methyltransferase that regulates the Hox genes, which control proliferation in hematopoietic cells (6,7,76). Several breakpoints in MLL have been identified and are located in close proximity to
n2:mentions: n3:11340607

Subject Item: _:vb4399468
rdf:type: n2:Context
rdf:value: Most of these leukemias are accompanied by translocations with breakpoints in the MLL (mixed lineage leukemia) gene at chromosomal band 11q23 (6,>>7<<,76). The MLL protein is a histone methyltransferase that regulates the Hox genes, which control proliferation in hematopoietic cells (6,7,76). Several breakpoints in MLL have been identified and are located in close proximity to
n2:mentions: n3:16857431

Subject Item: _:vb4399469
rdf:type: n2:Context
rdf:value: The MLL protein is a histone methyltransferase that regulates the Hox genes, which control proliferation in hematopoietic cells (>>6<<,7,76). Several breakpoints in MLL have been identified and are located in close proximity to topoisomerase II–DNA cleavage sites (6,7,76).
n2:mentions: n3:11340607

Subject Item: _:vb4399470
rdf:type: n2:Context
rdf:value: The MLL protein is a histone methyltransferase that regulates the Hox genes, which control proliferation in hematopoietic cells (6,>>7<<,76). Several breakpoints in MLL have been identified and are located in close proximity to topoisomerase II–DNA cleavage sites (6,7,76).
n2:mentions: n3:16857431

Subject Item: _:vb4399471
rdf:type: n2:Context
rdf:value: Several breakpoints in MLL have been identified and are located in close proximity to topoisomerase II–DNA cleavage sites (>>6<<,7,76).
n2:mentions: n3:11340607

Subject Item: _:vb4399472
rdf:type: n2:Context
rdf:value: Several breakpoints in MLL have been identified and are located in close proximity to topoisomerase II–DNA cleavage sites (6,>>7<<,76).
n2:mentions: n3:16857431

Subject Item: _:vb4399473
rdf:type: n2:Context
rdf:value: Patients with these leukemias display translocations between the PML (promyelocytic leukemia) gene on chromosome 15 and the RARA (retinoic acid receptor α) gene on chromosome 17 (>>149<<,150).
n2:mentions: n3:18650449

Subject Item: _:vb4399474
rdf:type: n2:Context
rdf:value: Patients with these leukemias display translocations between the PML (promyelocytic leukemia) gene on chromosome 15 and the RARA (retinoic acid receptor α) gene on chromosome 17 (149,>>150<<).
n2:mentions: n3:15829534

Subject Item: _:vb4399475
rdf:type: n2:Context
rdf:value: In addition to treatment-related leukmias, ∼80% of infants with AML or acute lymphoblastic leukemia (ALL) display translocations that involve the MLL gene (>>6<<,7,111,123–125,147,148,151). The chromosomal translocations associated with these cancers have been observed in utero, indicating that infant leukemias are initiated during pregnancy.
n2:mentions: n3:11340607

Subject Item: _:vb4399476
rdf:type: n2:Context
rdf:value: In addition to treatment-related leukmias, ∼80% of infants with AML or acute lymphoblastic leukemia (ALL) display translocations that involve the MLL gene (6,>>7<<,111,123–125,147,148,151). The chromosomal translocations associated with these cancers have been observed in utero, indicating that infant leukemias are initiated during pregnancy.
n2:mentions: n3:16857431

Subject Item: _:vb4399477
rdf:type: n2:Context
rdf:value: In addition to treatment-related leukmias, ∼80% of infants with AML or acute lymphoblastic leukemia (ALL) display translocations that involve the MLL gene (6,7,>>111<<,123–125,147,148,151). The chromosomal translocations associated with these cancers have been observed in utero, indicating that infant leukemias are initiated during pregnancy.
n2:mentions: n3:10758153

Subject Item: _:vb4399478
rdf:type: n2:Context
rdf:value: In addition to treatment-related leukmias, ∼80% of infants with AML or acute lymphoblastic leukemia (ALL) display translocations that involve the MLL gene (6,7,111,123–>>125<<,147,148,151). The chromosomal translocations associated with these cancers have been observed in utero, indicating that infant leukemias are initiated during pregnancy.
n2:mentions: n3:10781030 n3:7966394 n3:8932918

Subject Item: _:vb4399479
rdf:type: n2:Context
rdf:value: In addition to treatment-related leukmias, ∼80% of infants with AML or acute lymphoblastic leukemia (ALL) display translocations that involve the MLL gene (6,7,111,123–125,>>147<<,148,151). The chromosomal translocations associated with these cancers have been observed in utero, indicating that infant leukemias are initiated during pregnancy.
n2:mentions: n3:7756657

Subject Item: _:vb4399480
rdf:type: n2:Context
rdf:value: In addition to treatment-related leukmias, ∼80% of infants with AML or acute lymphoblastic leukemia (ALL) display translocations that involve the MLL gene (6,7,111,123–125,147,>>148<<,151). The chromosomal translocations associated with these cancers have been observed in utero, indicating that infant leukemias are initiated during pregnancy.
n2:mentions: n3:9748598

Subject Item: _:vb4399481
rdf:type: n2:Context
rdf:value: studies indicate that the risk of developing these infant leukemias is increased >3-fold by the maternal consumption of foods that are high in naturally occurring topoisomerase II poisons such as genistein or other bioflavonoids (>>111<<,123–126).
n2:mentions: n3:10758153

Subject Item: _:vb4399482
rdf:type: n2:Context
rdf:value: indicate that the risk of developing these infant leukemias is increased >3-fold by the maternal consumption of foods that are high in naturally occurring topoisomerase II poisons such as genistein or other bioflavonoids (111,123–>>126<<).
n2:mentions: n3:15767345 n3:10781030 n3:7966394 n3:8932918

Subject Item: _:vb4399483
rdf:type: n2:Context
rdf:value: If the concentration of enzyme-associated DNA breaks is sufficient, DNA recombination/repair pathways can be overwhelmed and cells will die (>>5<<,8,76). However, if the levels of breaks are not adequate to induce death, pathways that promote cell survival can lead to the formation of stable chromosomal translocations that ultimately lead to cancerous growth (Figure 4) (5,8,76).
n2:mentions: n3:10697411

Subject Item: _:vb4399484
rdf:type: n2:Context
rdf:value: If the concentration of enzyme-associated DNA breaks is sufficient, DNA recombination/repair pathways can be overwhelmed and cells will die (5,>>8<<,76). However, if the levels of breaks are not adequate to induce death, pathways that promote cell survival can lead to the formation of stable chromosomal translocations that ultimately lead to cancerous growth (Figure 4) (5,8,76).
n2:mentions: n3:17681352

Subject Item: _:vb4399485
rdf:type: n2:Context
rdf:value: However, if the levels of breaks are not adequate to induce death, pathways that promote cell survival can lead to the formation of stable chromosomal translocations that ultimately lead to cancerous growth (Figure 4) (>>5<<,8,76).
n2:mentions: n3:10697411

Subject Item: _:vb4399486
rdf:type: n2:Context
rdf:value: However, if the levels of breaks are not adequate to induce death, pathways that promote cell survival can lead to the formation of stable chromosomal translocations that ultimately lead to cancerous growth (Figure 4) (5,>>8<<,76).
n2:mentions: n3:17681352

Subject Item: _:vb4399487
rdf:type: n2:Context
rdf:value: However, evidence suggests that (with at least some drugs) topoisomerase IIα plays a more important role in cytotoxicity (>>107<<,152), while topoisomerase IIβ may play a greater role in triggering drug-induced cancers (107).
n2:mentions: n3:17578914

Subject Item: _:vb4399488
rdf:type: n2:Context
rdf:value: However, evidence suggests that (with at least some drugs) topoisomerase IIα plays a more important role in cytotoxicity (107,>>152<<), while topoisomerase IIβ may play a greater role in triggering drug-induced cancers (107).
n2:mentions: n3:10570059

Subject Item: _:vb4399489
rdf:type: n2:Context
rdf:value: However, evidence suggests that (with at least some drugs) topoisomerase IIα plays a more important role in cytotoxicity (107,152), while topoisomerase IIβ may play a greater role in triggering drug-induced cancers (>>107<<). Although no isoform-specific topoisomerase II-targeted drugs are available at the present time, it may be possible to preferentially target topoisomerase IIα by scheduling. In this regard, topoisomerase IIα–DNA cleavage complexes
n2:mentions: n3:17578914

Subject Item: _:vb4399490
rdf:type: n2:Context
rdf:value: In this regard, topoisomerase IIα–DNA cleavage complexes induced by etoposide persist approximately three to four times longer than those formed with topoisomerase IIβ (153,>>154<<). Therefore, it has been suggested that the use of pulsed chemotherapeutic regimens, in which patients receive cycles of drug treatment followed by recovery, may maintain higher levels of topoisomerase IIα as compared to topoisomerase IIβ
n2:mentions: n3:18922022

Subject Item: _:vb4399491
rdf:type: n2:Context
rdf:value: pulsed chemotherapeutic regimens, in which patients receive cycles of drug treatment followed by recovery, may maintain higher levels of topoisomerase IIα as compared to topoisomerase IIβ cleavage complexes over the course of therapy (>>154<<).
n2:mentions: n3:18922022

Subject Item: _:vb391549725
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 37
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rdf:type: n2:RelevantBibliographicResource
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Subject Item: _:vb391549727
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 25
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Subject Item: _:vb391549728
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 22
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Subject Item: _:vb391549729
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 22
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rdf:type: n2:RelevantBibliographicResource
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rdf:type: n2:RelevantBibliographicResource
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rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 13
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Subject Item: _:vb391549733
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 13
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Subject Item: _:vb391549734
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 13
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Subject Item: _:vb391549735
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 12
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Subject Item: _:vb391549736
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 12
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rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 12
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Subject Item: _:vb391549738
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 11
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Subject Item: _:vb391549739
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 11
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Subject Item: _:vb391549740
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 10
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Subject Item: _:vb391549741
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 10
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Subject Item: _:vb391549742
rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 10
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rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 10
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rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 10
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n2:RelevantScore: 9
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n2:RelevantScore: 9
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rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 9
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rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 9
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rdf:type: n2:RelevantBibliographicResource
n2:RelevantScore: 9
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n2:RelevantScore: 9
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n2:RelevantScore: 9
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n2:RelevantScore: 9
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n2:RelevantScore: 9
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n2:RelevantScore: 8
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