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_:vb350803682 _:vb350803683 _:vb350803684 _:vb350803685 _:vb350803686 _:vb350803687 _:vb350803688 _:vb350803689 _:vb350803690 _:vb350803691 _:vb350803692 _:vb350803693 _:vb350803694 _:vb350803695 _:vb350803696 _:vb350803697 _:vb350803698 _:vb350803699 _:vb350803700 _:vb350803701 _:vb350803702 _:vb350803703 _:vb350803704 _:vb350803705 _:vb350803706 _:vb350803707 _:vb350803708 _:vb350803709 _:vb350803710 _:vb350803711 _:vb350803648 _:vb350803649 _:vb350803650 _:vb350803651 _:vb350803652 _:vb350803653 _:vb350803654 _:vb350803655 _:vb350803656 _:vb350803657 _:vb350803658 _:vb350803659 _:vb350803660 _:vb350803661 _:vb350803662 _:vb350803663 _:vb350803664 _:vb350803665 _:vb350803666 _:vb350803667 _:vb350803668 _:vb350803669 _:vb350803670 _:vb350803671 _:vb350803672 _:vb350803673 _:vb350803674 _:vb350803675 _:vb350803676 _:vb350803677 _:vb350803678 _:vb350803679 _:vb350804384 _:vb350804385 _:vb350804386 _:vb350804387 _:vb350804388 _:vb350804389 _:vb350804390 _:vb350804391 _:vb350804392 _:vb350804393 _:vb350804394 _:vb350804395 _:vb350804396 _:vb350804397 _:vb350804398 _:vb350804399 _:vb350804400 _:vb350804401 _:vb350804402 _:vb350804403 _:vb350804404 _:vb350804405 _:vb350804406 _:vb350804407 _:vb350804408 _:vb350804409 _:vb350804410 _:vb350804411 _:vb350804412 _:vb350804413 _:vb350804414 _:vb350804415 _:vb350804352 _:vb350804353 _:vb350804354 _:vb350804355 _:vb350804356 _:vb350804357 _:vb350804358 _:vb350804359 _:vb350804360 _:vb350804361 _:vb350804362 _:vb350804363 _:vb350804364 _:vb350804365 _:vb350804366 _:vb350804367 _:vb350804368 _:vb350804369 _:vb350804370 _:vb350804371 _:vb350804372 _:vb350804373 _:vb350804374 _:vb350804375 _:vb350804376 _:vb350804377 _:vb350804378 _:vb350804379 _:vb350804380 _:vb350804381 _:vb350804382 _:vb350804383 _:vb350804416 _:vb350804417 _:vb350804418 _:vb350804419 _:vb350804420 _:vb350804421 _:vb350804422 _:vb350804423 _:vb350804424 _:vb350804425 _:vb350804426 _:vb350804427 _:vb350804428 _:vb350804429 _:vb350804430 _:vb350804431 _:vb350804256 _:vb350804257 _:vb350804258 _:vb350804259 _:vb350804260 _:vb350804261 _:vb350804262 _:vb350804263 _:vb350804264 _:vb350804265 _:vb350804266 _:vb350804267 _:vb350804268 _:vb350804269 _:vb350804270 _:vb350804271 _:vb350804272 _:vb350804273 _:vb350804274 _:vb350804275 _:vb350804276 _:vb350804277 _:vb350804278 _:vb350804279 _:vb350804280 _:vb350804281 _:vb350804282 _:vb350804283 _:vb350804284 _:vb350804285 _:vb350804286 _:vb350804287 _:vb350804224 _:vb350804225 _:vb350804226 _:vb350804227 _:vb350804228 _:vb350804229 _:vb350804230 _:vb350804231 _:vb350804232 _:vb350804233 _:vb350804234 _:vb350804235 _:vb350804236 _:vb350804237 _:vb350804238 _:vb350804239 _:vb350804240 _:vb350804241 _:vb350804242 _:vb350804243 _:vb350804244 _:vb350804245 _:vb350804246 _:vb350804247 _:vb350804248 _:vb350804249 _:vb350804250 _:vb350804251 _:vb350804252 _:vb350804253 _:vb350804254 _:vb350804255 _:vb350804320 _:vb350804321 _:vb350804322 _:vb350804323 _:vb350804324 _:vb350804325 _:vb350804326 _:vb350804327 _:vb350804328 _:vb350804329 _:vb350804330 _:vb350804331 _:vb350804332 _:vb350804333 _:vb350804334 _:vb350804335 _:vb350804336 _:vb350804337 _:vb350804338 _:vb350804339 _:vb350804340 _:vb350804341 _:vb350804342 _:vb350804343 _:vb350804344 _:vb350804345 _:vb350804346 _:vb350804347 _:vb350804348 _:vb350804349 _:vb350804350 _:vb350804351 _:vb350804288 _:vb350804289 _:vb350804290 _:vb350804291 _:vb350804292 _:vb350804293 _:vb350804294 _:vb350804295 _:vb350804296 _:vb350804297 _:vb350804298 _:vb350804299 _:vb350804300 _:vb350804301 _:vb350804302 _:vb350804303 _:vb350804304 _:vb350804305 _:vb350804306 _:vb350804307 _:vb350804308 _:vb350804309 _:vb350804310 _:vb350804311 _:vb350804312 _:vb350804313 _:vb350804314 _:vb350804315 _:vb350804316 _:vb350804317 _:vb350804318 _:vb350804319 _:vb350804128 _:vb350804129 _:vb350804130 _:vb350804131 _:vb350804132 _:vb350804133 _:vb350804134 _:vb350804135 _:vb350804136 _:vb350804137 _:vb350804138 _:vb350804139 _:vb350804140 _:vb350804141 _:vb350804142 _:vb350804143 _:vb350804144 _:vb350804145 _:vb350804146 _:vb350804147 _:vb350804148 _:vb350804149 _:vb350804150 _:vb350804151 _:vb350804152 _:vb350804153 _:vb350804154 _:vb350804155 _:vb350804156 _:vb350804157 _:vb350804158 _:vb350804159 _:vb350804096 _:vb350804097 _:vb350804098 _:vb350804099 _:vb350804100 _:vb350804101 _:vb350804102 _:vb350804103 _:vb350804104 _:vb350804105 _:vb350804106 _:vb350804107 _:vb350804108 _:vb350804109 _:vb350804110 _:vb350804111 _:vb350804112 _:vb350804113 _:vb350804114 _:vb350804115 _:vb350804116 _:vb350804117 _:vb350804118 _:vb350804119 _:vb350804120 _:vb350804121 _:vb350804122 _:vb350804123 _:vb350804124 _:vb350804125 _:vb350804126 _:vb350804127 _:vb350804192 _:vb350804193 _:vb350804194 _:vb350804195 _:vb350804196 _:vb350804197 _:vb350804198 _:vb350804199 _:vb350804200 _:vb350804201 _:vb350804202 _:vb350804203 _:vb350804204 _:vb350804205 _:vb350804206 _:vb350804207 _:vb350804208 _:vb350804209 _:vb350804210 _:vb350804211 _:vb350804212 _:vb350804213 _:vb350804214 _:vb350804215 _:vb350804216 _:vb350804217 _:vb350804218 _:vb350804219 _:vb350804220 _:vb350804221 _:vb350804222 _:vb350804223 _:vb350804160 _:vb350804161 _:vb350804162 _:vb350804163 _:vb350804164 _:vb350804165 _:vb350804166 _:vb350804167 _:vb350804168 _:vb350804169 _:vb350804170 _:vb350804171 _:vb350804172 _:vb350804173 _:vb350804174 _:vb350804175 _:vb350804176 _:vb350804177 _:vb350804178 _:vb350804179 _:vb350804180 _:vb350804181 _:vb350804182 _:vb350804183 _:vb350804184 _:vb350804185 _:vb350804186 _:vb350804187 _:vb350804188 _:vb350804189 _:vb350804190 _:vb350804191 _:vb350804000 _:vb350804001 _:vb350804002 _:vb350804003 _:vb350804004 _:vb350804005 _:vb350804006 _:vb350804007 _:vb350804008 _:vb350804009 _:vb350804010 _:vb350804011 _:vb350804012 _:vb350804013 _:vb350804014 _:vb350804015 _:vb350804016 _:vb350804017 _:vb350804018 _:vb350804019 _:vb350804020 _:vb350804021 _:vb350804022 _:vb350804023 _:vb350804024 _:vb350804025 _:vb350804026 _:vb350804027 _:vb350804028 _:vb350804029 _:vb350804030 _:vb350804031 _:vb350803968 _:vb350803969 _:vb350803970 _:vb350803971 _:vb350803972 _:vb350803973 _:vb350803974 _:vb350803975 _:vb350803976 _:vb350803977 _:vb350803978 _:vb350803979 _:vb350803980 _:vb350803981 _:vb350803982 _:vb350803983 _:vb350803984 _:vb350803985 _:vb350803986 _:vb350803987 _:vb350803988 _:vb350803989 _:vb350803990 _:vb350803991 _:vb350803992 _:vb350803993 _:vb350803994 _:vb350803995 _:vb350803996 _:vb350803997 _:vb350803998 _:vb350803999 _:vb350804064 _:vb350804065 _:vb350804066 _:vb350804067 _:vb350804068 _:vb350804069 _:vb350804070 _:vb350804071 _:vb350804072 _:vb350804073 _:vb350804074 _:vb350804075 _:vb350804076 _:vb350804077 _:vb350804078 _:vb350804079 _:vb350804080 _:vb350804081 _:vb350804082 _:vb350804083 _:vb350804084 _:vb350804085 _:vb350804086 _:vb350804087 _:vb350804088 _:vb350804089 _:vb350804090 _:vb350804091 _:vb350804092 _:vb350804093 _:vb350804094 _:vb350804095 _:vb350804032 _:vb350804033 _:vb350804034 _:vb350804035 _:vb350804036 _:vb350804037 _:vb350804038 _:vb350804039 _:vb350804040 _:vb350804041 _:vb350804042 _:vb350804043 _:vb350804044 _:vb350804045 _:vb350804046 _:vb350804047 _:vb350804048 _:vb350804049 _:vb350804050 _:vb350804051 _:vb350804052 _:vb350804053 _:vb350804054 _:vb350804055 _:vb350804056 _:vb350804057 _:vb350804058 _:vb350804059 _:vb350804060 _:vb350804061 _:vb350804062 _:vb350804063
n3:pmcid: PMC0
bibo:doi: 10.1083%2Fjcb.200608077
n9:contains: _:vb2303221 _:vb2303194 _:vb2303178 _:vb2303148

Subject Item: _:vb2303148
rdf:type: n9:Section
dc:title: introduction
n9:contains: _:vb2303172 _:vb2303173 _:vb2303174 _:vb2303175 _:vb2303168 _:vb2303169 _:vb2303170 _:vb2303171 _:vb2303176 _:vb2303177 _:vb2303156 _:vb2303157 _:vb2303158 _:vb2303159 _:vb2303152 _:vb2303153 _:vb2303154 _:vb2303155 _:vb2303164 _:vb2303165 _:vb2303166 _:vb2303167 _:vb2303160 _:vb2303161 _:vb2303162 _:vb2303163 _:vb2303149 _:vb2303150 _:vb2303151

Subject Item: _:vb2303149
rdf:type: n3:Context
rdf:value: At least two distinct pathways have evolved that mediate the repair of DSBs: homologous recombination (HR) and nonhomologous end-joining (NHEJ; Critchlow and Jackson, >>1998<<; Kanaar et al., 1998; van Gent et al., 2001; Lieber et al., 2003).
n3:mentions: n2:9810228

Subject Item: _:vb2303150
rdf:type: n3:Context
rdf:value: At least two distinct pathways have evolved that mediate the repair of DSBs: homologous recombination (HR) and nonhomologous end-joining (NHEJ; Critchlow and Jackson, 1998; Kanaar et al., >>1998<<; van Gent et al., 2001; Lieber et al., 2003).
n3:mentions: n2:9861670

Subject Item: _:vb2303151
rdf:type: n3:Context
rdf:value: At least two distinct pathways have evolved that mediate the repair of DSBs: homologous recombination (HR) and nonhomologous end-joining (NHEJ; Critchlow and Jackson, 1998; Kanaar et al., 1998; van Gent et al., >>2001<<; Lieber et al., 2003). NHEJ is considered to be the prevailing pathway during the G0 and G1 phases of the cell cycle in mammalian cells because this repair pathway does not require the presence of an intact DNA template.
n3:mentions: n2:11256071

Subject Item: _:vb2303152
rdf:type: n3:Context
rdf:value: At least two distinct pathways have evolved that mediate the repair of DSBs: homologous recombination (HR) and nonhomologous end-joining (NHEJ; Critchlow and Jackson, 1998; Kanaar et al., 1998; van Gent et al., 2001; Lieber et al., >>2003<<). NHEJ is considered to be the prevailing pathway during the G0 and G1 phases of the cell cycle in mammalian cells because this repair pathway does not require the presence of an intact DNA template.
n3:mentions: n2:14506474

Subject Item: _:vb2303153
rdf:type: n3:Context
rdf:value: Two protein complexes make up the catalytic core of the NHEJ process: the DNA-dependent protein kinase holoenzyme (DNA-PK) and the DNA ligase IV–XRCC4 complex (Lees-Miller and Meek, >>2003<<; Weterings and van Gent, 2004). Ligase IV–XRCC4 mediates ligation of the juxtaposed DNA ends in the final NHEJ step.
n3:mentions: n2:14726021

Subject Item: _:vb2303154
rdf:type: n3:Context
rdf:value: Two protein complexes make up the catalytic core of the NHEJ process: the DNA-dependent protein kinase holoenzyme (DNA-PK) and the DNA ligase IV–XRCC4 complex (Lees-Miller and Meek, 2003; Weterings and van Gent, >>2004<<). Ligase IV–XRCC4 mediates ligation of the juxtaposed DNA ends in the final NHEJ step.
n3:mentions: n2:15380098

Subject Item: _:vb2303155
rdf:type: n3:Context
rdf:value: The formation of a kinase-competent DNA-PK complex by Ku70/80 and DNA-PKCS requires simultaneous binding of these enzymes to a DNA terminus (Lees-Miller and Meek, >>2003<<; Weterings and van Gent, 2004). Because Ku70/80 has much higher affinity for DNA ends than DNA-PKCS, this heterodimer most likely binds to DNA termini first and subsequently attracts DNA-PKCS toward the DSB.
n3:mentions: n2:14726021

Subject Item: _:vb2303156
rdf:type: n3:Context
rdf:value: The formation of a kinase-competent DNA-PK complex by Ku70/80 and DNA-PKCS requires simultaneous binding of these enzymes to a DNA terminus (Lees-Miller and Meek, 2003; Weterings and van Gent, >>2004<<). Because Ku70/80 has much higher affinity for DNA ends than DNA-PKCS, this heterodimer most likely binds to DNA termini first and subsequently attracts DNA-PKCS toward the DSB.
n3:mentions: n2:15380098

Subject Item: _:vb2303157
rdf:type: n3:Context
rdf:value: It is, however, well established that DNA-PKCS has the ability to autophosphorylate itself at a cluster of 6 phosphorylation sites between the Thr2609 and Thr2647 amino acid residues (Douglas et al., >>2002<<), as well as at an additional site outside this cluster, the Ser2056 residue (Chen et al., 2005).
n3:mentions: n2:12186630

Subject Item: _:vb2303158
rdf:type: n3:Context
rdf:value: to autophosphorylate itself at a cluster of 6 phosphorylation sites between the Thr2609 and Thr2647 amino acid residues (Douglas et al., 2002), as well as at an additional site outside this cluster, the Ser2056 residue (Chen et al., >>2005<<). This activity possibly leads to alteration of the protein's affinity for DNA and to inactivation of its kinase activity.
n3:mentions: n2:15677476

Subject Item: _:vb2303159
rdf:type: n3:Context
rdf:value: Such phosphorylation-induced alterations are important during DSB repair in vivo because mutations in the phosphorylation cluster cause severely increased radiation sensitivity and decreased DNA repair (Chan et al., >>2002<<; Ding et al., 2003; Soubeyrand et al., 2003).
n3:mentions: n2:12231622

Subject Item: _:vb2303160
rdf:type: n3:Context
rdf:value: Such phosphorylation-induced alterations are important during DSB repair in vivo because mutations in the phosphorylation cluster cause severely increased radiation sensitivity and decreased DNA repair (Chan et al., 2002; Ding et al., >>2003<<; Soubeyrand et al., 2003).
n3:mentions: n2:12897153

Subject Item: _:vb2303161
rdf:type: n3:Context
rdf:value: alterations are important during DSB repair in vivo because mutations in the phosphorylation cluster cause severely increased radiation sensitivity and decreased DNA repair (Chan et al., 2002; Ding et al., 2003; Soubeyrand et al., >>2003<<).
n3:mentions: n2:12649176

Subject Item: _:vb2303162
rdf:type: n3:Context
rdf:value: Several studies have shown that the presence of DNA-PKCS at DNA ends interferes with efficient ligation, most likely caused by the large dimensions of the protein molecule (Calsou et al., >>1999<<; Weterings et al., 2003; Block et al., 2004; Cui et al., 2005).
n3:mentions: n2:10075677

Subject Item: _:vb2303163
rdf:type: n3:Context
rdf:value: Several studies have shown that the presence of DNA-PKCS at DNA ends interferes with efficient ligation, most likely caused by the large dimensions of the protein molecule (Calsou et al., 1999; Weterings et al., >>2003<<; Block et al., 2004; Cui et al., 2005).
n3:mentions: n2:14654699

Subject Item: _:vb2303164
rdf:type: n3:Context
rdf:value: Several studies have shown that the presence of DNA-PKCS at DNA ends interferes with efficient ligation, most likely caused by the large dimensions of the protein molecule (Calsou et al., 1999; Weterings et al., 2003; Block et al., >>2004<<; Cui et al., 2005).
n3:mentions: n2:15314205

Subject Item: _:vb2303165
rdf:type: n3:Context
rdf:value: have shown that the presence of DNA-PKCS at DNA ends interferes with efficient ligation, most likely caused by the large dimensions of the protein molecule (Calsou et al., 1999; Weterings et al., 2003; Block et al., 2004; Cui et al., >>2005<<). This inhibition of ligation can be relieved by DNA-PKCS autophosphorylation, indicating that autophosphorylation induces a conformational change in the DNA-PKCS molecule that liberates DNA ends (Weterings et al., 2003; Block et al.,
n3:mentions: n2:16314509

Subject Item: _:vb2303166
rdf:type: n3:Context
rdf:value: This inhibition of ligation can be relieved by DNA-PKCS autophosphorylation, indicating that autophosphorylation induces a conformational change in the DNA-PKCS molecule that liberates DNA ends (Weterings et al., >>2003<<; Block et al., 2004; Reddy et al., 2004; Cui et al., 2005).
n3:mentions: n2:14654699

Subject Item: _:vb2303167
rdf:type: n3:Context
rdf:value: This inhibition of ligation can be relieved by DNA-PKCS autophosphorylation, indicating that autophosphorylation induces a conformational change in the DNA-PKCS molecule that liberates DNA ends (Weterings et al., 2003; Block et al., >>2004<<; Reddy et al., 2004; Cui et al., 2005).
n3:mentions: n2:15314205

Subject Item: _:vb2303168
rdf:type: n3:Context
rdf:value: ligation can be relieved by DNA-PKCS autophosphorylation, indicating that autophosphorylation induces a conformational change in the DNA-PKCS molecule that liberates DNA ends (Weterings et al., 2003; Block et al., 2004; Reddy et al., >>2004<<; Cui et al., 2005).
n3:mentions: n2:15258142

Subject Item: _:vb2303169
rdf:type: n3:Context
rdf:value: by DNA-PKCS autophosphorylation, indicating that autophosphorylation induces a conformational change in the DNA-PKCS molecule that liberates DNA ends (Weterings et al., 2003; Block et al., 2004; Reddy et al., 2004; Cui et al., >>2005<<). These findings gave rise to the current notion that DNA-PKCS functions as a “gatekeeper,” which protects DNA ends from premature processing and ligation, until the two DNA ends are properly juxtaposed and DNA-PKCS autophosphorylation
n3:mentions: n2:16314509

Subject Item: _:vb2303170
rdf:type: n3:Context
rdf:value: notion that DNA-PKCS functions as a “gatekeeper,” which protects DNA ends from premature processing and ligation, until the two DNA ends are properly juxtaposed and DNA-PKCS autophosphorylation can take place (Weterings and van Gent, >>2004<<).
n3:mentions: n2:15380098

Subject Item: _:vb2303171
rdf:type: n3:Context
rdf:value: the use of microscope-coupled lasers to introduce DNA damage in specified regions of the cell nucleus to address questions concerning the sequential recruitment of different DSB repair enzymes to those damage sites (Kim et al., >>2005<<; Bekker-Jensen et al., 2006).
n3:mentions: n2:16061690

Subject Item: _:vb2303172
rdf:type: n3:Context
rdf:value: A recent study examined the in vivo recruitment of NHEJ core enzymes to DSBs after the introduction of DNA damage by the use of a pulsed, near-infrared laser (Mari et al., >>2006<<), and it showed that the binding of Ku70/80 to DNA ends is a highly dynamic equilibrium of association and dissociation.
n3:mentions: n2:17124166

Subject Item: _:vb2303173
rdf:type: n3:Context
rdf:value: These mutations are known to interfere with efficient DSB repair (Kurimasa et al., >>1999<<; Kienker et al., 2000; Chan et al., 2002; Ding et al., 2003; Soubeyrand et al., 2003).
n3:mentions: n2:10207111

Subject Item: _:vb2303174
rdf:type: n3:Context
rdf:value: These mutations are known to interfere with efficient DSB repair (Kurimasa et al., 1999; Kienker et al., >>2000<<; Chan et al., 2002; Ding et al., 2003; Soubeyrand et al., 2003).
n3:mentions: n2:10908332

Subject Item: _:vb2303175
rdf:type: n3:Context
rdf:value: These mutations are known to interfere with efficient DSB repair (Kurimasa et al., 1999; Kienker et al., 2000; Chan et al., >>2002<<; Ding et al., 2003; Soubeyrand et al., 2003).
n3:mentions: n2:12231622

Subject Item: _:vb2303176
rdf:type: n3:Context
rdf:value: These mutations are known to interfere with efficient DSB repair (Kurimasa et al., 1999; Kienker et al., 2000; Chan et al., 2002; Ding et al., >>2003<<; Soubeyrand et al., 2003).
n3:mentions: n2:12897153

Subject Item: _:vb2303177
rdf:type: n3:Context
rdf:value: These mutations are known to interfere with efficient DSB repair (Kurimasa et al., 1999; Kienker et al., 2000; Chan et al., 2002; Ding et al., 2003; Soubeyrand et al., >>2003<<).
n3:mentions: n2:12649176

Subject Item: _:vb2303178
rdf:type: n9:Section
dc:title: materials and methods
n9:contains: _:vb2303180 _:vb2303181 _:vb2303182 _:vb2303183 _:vb2303179 _:vb2303192 _:vb2303193 _:vb2303188 _:vb2303189 _:vb2303190 _:vb2303191 _:vb2303184 _:vb2303185 _:vb2303186 _:vb2303187

Subject Item: _:vb2303179
rdf:type: n3:Context
rdf:value: CHO cell lines AA8 (WT), V3 cells (defective in DNA-PKcs expression; Whitmore et al., >>1989<<), and Xrs6 cells (defective in Ku80 expression; Denekamp et al., 1989) were maintained at 37°C in α-minimum Eagle's medium with 10% FCS, 100 units/ml penicillin, and 100 μg/ml streptomycin (HyClone).
n3:mentions: n2:2573661

Subject Item: _:vb2303180
rdf:type: n3:Context
rdf:value: CHO cell lines AA8 (WT), V3 cells (defective in DNA-PKcs expression; Whitmore et al., 1989), and Xrs6 cells (defective in Ku80 expression; Denekamp et al., >>1989<<) were maintained at 37°C in α-minimum Eagle's medium with 10% FCS, 100 units/ml penicillin, and 100 μg/ml streptomycin (HyClone).
n3:mentions: n2:2564870

Subject Item: _:vb2303181
rdf:type: n3:Context
rdf:value: Fluorescent immunostaining was performed as previously described (Chen et al., >>2005<<). In brief, the irradiated cells were fixed with cold methanol for 20 min on ice and permeabilized for 10 min in PBS containing 0.5% Triton X-100.
n3:mentions: n2:15677476

Subject Item: _:vb2303182
rdf:type: n3:Context
rdf:value: Anti-pS2056 and -pT2647 polyclonal antibodies and anti-pT2609 and -γH2AX monoclonal antibodies were generated as described previously (Chan et al., >>2002<<; Chen et al., 2005; Yajima et al., 2006).
n3:mentions: n2:12231622

Subject Item: _:vb2303183
rdf:type: n3:Context
rdf:value: Anti-pS2056 and -pT2647 polyclonal antibodies and anti-pT2609 and -γH2AX monoclonal antibodies were generated as described previously (Chan et al., 2002; Chen et al., >>2005<<; Yajima et al., 2006).
n3:mentions: n2:15677476

Subject Item: _:vb2303184
rdf:type: n3:Context
rdf:value: Anti-pS2056 and -pT2647 polyclonal antibodies and anti-pT2609 and -γH2AX monoclonal antibodies were generated as described previously (Chan et al., 2002; Chen et al., 2005; Yajima et al., >>2006<<). Anti-γH2AX polyclonal antibody was purchased from Cell Signaling Technology. Secondary antibodies (anti–mouse or–rabbit conjugated with Alexa Fluor 488/350 or rhodamine) were purchased from Invitrogen. DNA ends in irradiated cells were
n3:mentions: n2:16908529

Subject Item: _:vb2303185
rdf:type: n3:Context
rdf:value: DSBs were introduced in the nuclei of cultured cells by microirradiation with a pulsed nitrogen laser (Spectra-Physics; 365 nm, 10 Hz pulse) as previously described (Lan et al., >>2004<<, 2005). The laser system was directly coupled (Micropoint Ablation Laser System; Photonic Instruments, Inc.
n3:mentions: n2:15365186

Subject Item: _:vb2303186
rdf:type: n3:Context
rdf:value: DSBs were introduced in the nuclei of cultured cells by microirradiation with a pulsed nitrogen laser (Spectra-Physics; 365 nm, 10 Hz pulse) as previously described (Lan et al., 2004, >>2005<<). The laser system was directly coupled (Micropoint Ablation Laser System; Photonic Instruments, Inc.
n3:mentions: n2:16141234

Subject Item: _:vb2303187
rdf:type: n3:Context
rdf:value: the number of DSBs that were induced by microirradiation, we compared the DNA-PKCS accumulation that was caused by our 365-nm laser system with the DNA-PKCS accumulation that was caused by a previously calibrated system (Mari et al., >>2006<<). Mari et al. (2006) used an 800-nm multiphoton laser to induce DNA damage.
n3:mentions: n2:17124166

Subject Item: _:vb2303188
rdf:type: n3:Context
rdf:value: Mari et al. (>>2006<<) used an 800-nm multiphoton laser to induce DNA damage.
n3:mentions: n2:17124166

Subject Item: _:vb2303189
rdf:type: n3:Context
rdf:value: We microirradiated several YFP-DNA-PKCS–expressing V3 cells with either our 365-nm laser system or with the microirradiation system used by Mari et al. (>>2006<<; both systems are based on LSM 510 confocal microscopes, set to provide comparable background and fluorescence intensity levels).
n3:mentions: n2:17124166

Subject Item: _:vb2303190
rdf:type: n3:Context
rdf:value: Using the same microirradiation system that was used by Mari et al. (>>2006<<; facility of the Erasmus Medical Center, Rotterdam, Netherlands) and following the same protocol, a small disk within the nucleus was irradiated with a pulsed 800-nm laser.
n3:mentions: n2:17124166

Subject Item: _:vb2303191
rdf:type: n3:Context
rdf:value: expressing YFP-tagged DNA-PKCS, were irradiated with uranium particles with an initial energy of 11.4 MeV/nucleon (energy on the target cells, 3.8 MeV/nucleon) at the UNILAC facility at GSI, as previously described (Jakob et al., >>2000<<). Cells were cultured in a Petri dish on 40-μm-thick polycarbonate sheets. Duration of irradiation was <5 ms per sample.
n3:mentions: n2:11023603

Subject Item: _:vb2303192
rdf:type: n3:Context
rdf:value: Kinetic measurements of the recruitment of YFP-DNA-PKCS at sites of ion traversals were performed using a beamline microscope (Jakob et al., >>2005<<) equipped with a 7190–53 EBCCD-camera (Hamamatsu).
n3:mentions: n2:15913400

Subject Item: _:vb2303193
rdf:type: n3:Context
rdf:value: Uranium ion tracks were visualized by etching polycarbonate, as described previously (Jakob et al., >>2005<<).
n3:mentions: n2:15913400

Subject Item: _:vb2303194
rdf:type: n9:Section
dc:title: results
n9:contains: _:vb2303196 _:vb2303197 _:vb2303198 _:vb2303199 _:vb2303195 _:vb2303212 _:vb2303213 _:vb2303214 _:vb2303215 _:vb2303208 _:vb2303209 _:vb2303210 _:vb2303211 _:vb2303204 _:vb2303205 _:vb2303206 _:vb2303207 _:vb2303200 _:vb2303201 _:vb2303202 _:vb2303203 _:vb2303220 _:vb2303216 _:vb2303217 _:vb2303218 _:vb2303219

Subject Item: _:vb2303195
rdf:type: n3:Context
rdf:value: of DSBs that was produced during microirradiation, we compared the DNA-PKCS accumulation that was caused by our laser-system with the DNA-PKCS accumulation that was caused by an already calibrated microirradiation system (Mari et al., >>2006<<). In brief, we treated YFP-DNA-PKCS–expressing cells with either our 365-nm laser system or with the 800-nm multiphoton laser system used by Mari et al. (2006), which is known to introduce between 1,000 and 1,500 DSBs.
n3:mentions: n2:17124166

Subject Item: _:vb2303196
rdf:type: n3:Context
rdf:value: In brief, we treated YFP-DNA-PKCS–expressing cells with either our 365-nm laser system or with the 800-nm multiphoton laser system used by Mari et al. (>>2006<<), which is known to introduce between 1,000 and 1,500 DSBs.
n3:mentions: n2:17124166

Subject Item: _:vb2303197
rdf:type: n3:Context
rdf:value: We have previously shown that IR induces phosphorylation/autophosphorylation of the Ser2056 and Thr2609 amino acid residues of DNA-PKCS (Chan et al., >>2002<<; Chen et al., 2005).
n3:mentions: n2:12231622

Subject Item: _:vb2303198
rdf:type: n3:Context
rdf:value: We have previously shown that IR induces phosphorylation/autophosphorylation of the Ser2056 and Thr2609 amino acid residues of DNA-PKCS (Chan et al., 2002; Chen et al., >>2005<<). Immunostaining with phosphospecific antibodies revealed that both the Ser-2056 and Thr-2609 residues were phosphorylated in the microirradiated region (Fig. 1 E), indicating that the laser-induced DNA lesions are capable of inducing a
n3:mentions: n2:15677476

Subject Item: _:vb2303199
rdf:type: n3:Context
rdf:value: Many in vitro studies have shown that the Ku70/80 heterodimer directs DNA-PKCS to DNA ends and stabilizes the DNA–DNA-PKCS interaction (Smith and Jackson, >>1999<<). To investigate whether the recruitment of DNA-PKCS to DSB sites is dependent on the Ku protein in vivo, we generated a Ku80-deficient Xrs6 cell line that stably expressed YFP-DNA-PKCS.
n3:mentions: n2:10215620

Subject Item: _:vb2303200
rdf:type: n3:Context
rdf:value: From these data and the previously reported notion that the phosphorylation of Thr2609 does not take place in Ku-deficient cells (Falck et al., >>2005<<), we conclude that phosphorylation/autophosphorylation of DNA-PKCS is a Ku-dependent process.
n3:mentions: n2:15758953

Subject Item: _:vb2303201
rdf:type: n3:Context
rdf:value: It has previously been shown that the kinase activity of DNA-PKCS is essential during NHEJ-mediated DSB repair in mammalian cells (Kurimasa et al., >>1999<<; Kienker et al., 2000).
n3:mentions: n2:10207111

Subject Item: _:vb2303202
rdf:type: n3:Context
rdf:value: It has previously been shown that the kinase activity of DNA-PKCS is essential during NHEJ-mediated DSB repair in mammalian cells (Kurimasa et al., 1999; Kienker et al., >>2000<<). Because mutation of DNA-PKCS phosphorylation sites is also known to interfere with DSB repair, clustered phosphorylation of DNA-PKCS is likely to play an important role during NHEJ (Chan et al., 2002; Ding et al., 2003; Chen et al.,
n3:mentions: n2:10908332

Subject Item: _:vb2303203
rdf:type: n3:Context
rdf:value: Because mutation of DNA-PKCS phosphorylation sites is also known to interfere with DSB repair, clustered phosphorylation of DNA-PKCS is likely to play an important role during NHEJ (Chan et al., >>2002<<; Ding et al., 2003; Chen et al., 2005; Cui et al., 2005).
n3:mentions: n2:12231622

Subject Item: _:vb2303204
rdf:type: n3:Context
rdf:value: Because mutation of DNA-PKCS phosphorylation sites is also known to interfere with DSB repair, clustered phosphorylation of DNA-PKCS is likely to play an important role during NHEJ (Chan et al., 2002; Ding et al., >>2003<<; Chen et al., 2005; Cui et al., 2005).
n3:mentions: n2:12897153

Subject Item: _:vb2303205
rdf:type: n3:Context
rdf:value: Because mutation of DNA-PKCS phosphorylation sites is also known to interfere with DSB repair, clustered phosphorylation of DNA-PKCS is likely to play an important role during NHEJ (Chan et al., 2002; Ding et al., 2003; Chen et al., >>2005<<; Cui et al., 2005). To test whether kinase activity and clustered phosphorylation of DNA-PKCS are important for its recruitment to DSB sites, we generated two V3 cell lines that stably expressed YFP-tagged mutant forms of DNA-PKCS.
n3:mentions: n2:15677476

Subject Item: _:vb2303206
rdf:type: n3:Context
rdf:value: of DNA-PKCS phosphorylation sites is also known to interfere with DSB repair, clustered phosphorylation of DNA-PKCS is likely to play an important role during NHEJ (Chan et al., 2002; Ding et al., 2003; Chen et al., 2005; Cui et al., >>2005<<). To test whether kinase activity and clustered phosphorylation of DNA-PKCS are important for its recruitment to DSB sites, we generated two V3 cell lines that stably expressed YFP-tagged mutant forms of DNA-PKCS.
n3:mentions: n2:16314509

Subject Item: _:vb2303207
rdf:type: n3:Context
rdf:value: In one mutant form (KD), we impaired the kinase ability (Kurimasa et al., >>1999<<). In the other mutant (7A), we substituted all of the 7 major phosphorylation sites (Thr2609-Thr2647 and Ser2056) with alanine residues, impairing phosphorylation of these sites (Fig. 3 A). Cellular expression of both mutant proteins was
n3:mentions: n2:10207111

Subject Item: _:vb2303208
rdf:type: n3:Context
rdf:value: This is consistent with our previous finding that Ser2056 is an autophosphorylation site and that phosphorylation of this residue therefore requires the DNA-PKCS kinase activity (Chen et al., >>2005<<). The Thr2609 and Thr2647 residues, which were previously reported to be autophosphorylation sites (Chan et al., 2002; Ding et al., 2003), apparently do not require the DNA-PKCS kinase to be phosphorylated. It has recently been shown that
n3:mentions: n2:15677476

Subject Item: _:vb2303209
rdf:type: n3:Context
rdf:value: The Thr2609 and Thr2647 residues, which were previously reported to be autophosphorylation sites (Chan et al., >>2002<<; Ding et al., 2003), apparently do not require the DNA-PKCS kinase to be phosphorylated.
n3:mentions: n2:12231622

Subject Item: _:vb2303210
rdf:type: n3:Context
rdf:value: The Thr2609 and Thr2647 residues, which were previously reported to be autophosphorylation sites (Chan et al., 2002; Ding et al., >>2003<<), apparently do not require the DNA-PKCS kinase to be phosphorylated.
n3:mentions: n2:12897153

Subject Item: _:vb2303211
rdf:type: n3:Context
rdf:value: intensity of the accumulation area in mutant cells most likely reflects the inability of these cells to quickly repair the introduced DSBs because it is known that 7A and KD mutants display deficient DSB repair (Kurimasa et al., >>1999<<; Kienker et al., 2000; Chan et al., 2002; Ding et al., 2003; Soubeyrand et al., 2003).
n3:mentions: n2:10207111

Subject Item: _:vb2303212
rdf:type: n3:Context
rdf:value: accumulation area in mutant cells most likely reflects the inability of these cells to quickly repair the introduced DSBs because it is known that 7A and KD mutants display deficient DSB repair (Kurimasa et al., 1999; Kienker et al., >>2000<<; Chan et al., 2002; Ding et al., 2003; Soubeyrand et al., 2003). To verify this, we generated an XRCC4-deficient (XR1) cell line that expressed YFP-tagged WT DNA-PKCS.
n3:mentions: n2:10908332

Subject Item: _:vb2303213
rdf:type: n3:Context
rdf:value: in mutant cells most likely reflects the inability of these cells to quickly repair the introduced DSBs because it is known that 7A and KD mutants display deficient DSB repair (Kurimasa et al., 1999; Kienker et al., 2000; Chan et al., >>2002<<; Ding et al., 2003; Soubeyrand et al., 2003). To verify this, we generated an XRCC4-deficient (XR1) cell line that expressed YFP-tagged WT DNA-PKCS.
n3:mentions: n2:12231622

Subject Item: _:vb2303214
rdf:type: n3:Context
rdf:value: likely reflects the inability of these cells to quickly repair the introduced DSBs because it is known that 7A and KD mutants display deficient DSB repair (Kurimasa et al., 1999; Kienker et al., 2000; Chan et al., 2002; Ding et al., >>2003<<; Soubeyrand et al., 2003). To verify this, we generated an XRCC4-deficient (XR1) cell line that expressed YFP-tagged WT DNA-PKCS.
n3:mentions: n2:12897153

Subject Item: _:vb2303215
rdf:type: n3:Context
rdf:value: of these cells to quickly repair the introduced DSBs because it is known that 7A and KD mutants display deficient DSB repair (Kurimasa et al., 1999; Kienker et al., 2000; Chan et al., 2002; Ding et al., 2003; Soubeyrand et al., >>2003<<). To verify this, we generated an XRCC4-deficient (XR1) cell line that expressed YFP-tagged WT DNA-PKCS.
n3:mentions: n2:12649176

Subject Item: _:vb2303216
rdf:type: n3:Context
rdf:value: Because XR1 cells are unable to efficiently repair DSBs (Li et al., >>1995<<), we expected the presence of DNA-PKCS to be maintained at the DSB site.
n3:mentions: n2:8548796

Subject Item: _:vb2303217
rdf:type: n3:Context
rdf:value: Because phosphorylation of both Thr2609 and Ser2056 is thought to be important for DSB repair via the NHEJ pathway (Chan et al., >>2002<<; Ding et al., 2003; Chen et al., 2005; Cui et al., 2005), we generated V3 cell lines that stably expressed YFP-tagged mutant forms of DNA-PKCS that could not be phosphorylated at those sites (Fig.
n3:mentions: n2:12231622

Subject Item: _:vb2303218
rdf:type: n3:Context
rdf:value: Because phosphorylation of both Thr2609 and Ser2056 is thought to be important for DSB repair via the NHEJ pathway (Chan et al., 2002; Ding et al., >>2003<<; Chen et al., 2005; Cui et al., 2005), we generated V3 cell lines that stably expressed YFP-tagged mutant forms of DNA-PKCS that could not be phosphorylated at those sites (Fig.
n3:mentions: n2:12897153

Subject Item: _:vb2303219
rdf:type: n3:Context
rdf:value: Because phosphorylation of both Thr2609 and Ser2056 is thought to be important for DSB repair via the NHEJ pathway (Chan et al., 2002; Ding et al., 2003; Chen et al., >>2005<<; Cui et al., 2005), we generated V3 cell lines that stably expressed YFP-tagged mutant forms of DNA-PKCS that could not be phosphorylated at those sites (Fig.
n3:mentions: n2:15677476

Subject Item: _:vb2303220
rdf:type: n3:Context
rdf:value: Because phosphorylation of both Thr2609 and Ser2056 is thought to be important for DSB repair via the NHEJ pathway (Chan et al., 2002; Ding et al., 2003; Chen et al., 2005; Cui et al., >>2005<<), we generated V3 cell lines that stably expressed YFP-tagged mutant forms of DNA-PKCS that could not be phosphorylated at those sites (Fig.
n3:mentions: n2:16314509

Subject Item: _:vb2303221
rdf:type: n9:Section
dc:title: discussion
n9:contains: _:vb2303232 _:vb2303233 _:vb2303234 _:vb2303235 _:vb2303222 _:vb2303223 _:vb2303224 _:vb2303225 _:vb2303226 _:vb2303227 _:vb2303228 _:vb2303229 _:vb2303230 _:vb2303231

Subject Item: _:vb2303222
rdf:type: n3:Context
rdf:value: We chose to use a 365-nm laser system, which is known for its ability to generate DNA damage in a controlled fashion (Lan et al., >>2004<<, 2005). The type and amount of DNA damage that is introduced by this laser can be controlled by adjusting the laser output intensity and the pulse frequency (Lan et al., 2005). A previous study has demonstrated the recruitment of DSB
n3:mentions: n2:15365186

Subject Item: _:vb2303223
rdf:type: n3:Context
rdf:value: We chose to use a 365-nm laser system, which is known for its ability to generate DNA damage in a controlled fashion (Lan et al., 2004, >>2005<<). The type and amount of DNA damage that is introduced by this laser can be controlled by adjusting the laser output intensity and the pulse frequency (Lan et al., 2005). A previous study has demonstrated the recruitment of DSB repair
n3:mentions: n2:16141234

Subject Item: _:vb2303224
rdf:type: n3:Context
rdf:value: The type and amount of DNA damage that is introduced by this laser can be controlled by adjusting the laser output intensity and the pulse frequency (Lan et al., >>2005<<). A previous study has demonstrated the recruitment of DSB repair proteins (NBS1, BRCA1, RAD52, and WRN) toward regions of the cell nucleus that were treated with this laser system, indicating that the system is capable of generating DSBs
n3:mentions: n2:16141234

Subject Item: _:vb2303225
rdf:type: n3:Context
rdf:value: has demonstrated the recruitment of DSB repair proteins (NBS1, BRCA1, RAD52, and WRN) toward regions of the cell nucleus that were treated with this laser system, indicating that the system is capable of generating DSBs (Lan et al., >>2005<<). In addition, we show that the laser system generates DNA ends and that microirradiated areas colocalize with γH2AX, thereby demonstrating the formation of DSBs.
n3:mentions: n2:16141234

Subject Item: _:vb2303226
rdf:type: n3:Context
rdf:value: A recent study, in which cells were exposed to a comparable number of DSBs, showed conclusively that these cells were still able to complete cell division (Mari et al., >>2006<<). In addition, we would like to stipulate that the recruitment of DNA-PKCS in our system fully depends on the presence of Ku, ruling out the possibility of artificial, aspecific aggregation.
n3:mentions: n2:17124166

Subject Item: _:vb2303227
rdf:type: n3:Context
rdf:value: It is generally assumed that the Ku70/80 heterodimer is the first NHEJ factor to bind to a broken DNA strand and that DNA-PKCS is subsequently attracted to the DSB sites (Chen et al., 1996; Singleton et al., >>1999<<). Recent studies have demonstrated that conserved C-terminal sequence motifs in Ku80 have the ability to interact with DNA-PKCS (Falck et al., 2005).
n3:mentions: n2:10207052

Subject Item: _:vb2303228
rdf:type: n3:Context
rdf:value: Recent studies have demonstrated that conserved C-terminal sequence motifs in Ku80 have the ability to interact with DNA-PKCS (Falck et al., >>2005<<). However, these in vitro studies do not form direct evidence for Ku80's ability to recruit DNA-PKCS to DSB sites. Some experiments have even suggested that DNA-PKCS is able to bind to DNA ends in the absence of Ku70/80 (Hammarsten and
n3:mentions: n2:15758953

Subject Item: _:vb2303229
rdf:type: n3:Context
rdf:value: Some experiments have even suggested that DNA-PKCS is able to bind to DNA ends in the absence of Ku70/80 (Hammarsten and Chu, >>1998<<; Merkle et al., 2002).
n3:mentions: n2:9435225

Subject Item: _:vb2303230
rdf:type: n3:Context
rdf:value: Some experiments have even suggested that DNA-PKCS is able to bind to DNA ends in the absence of Ku70/80 (Hammarsten and Chu, 1998; Merkle et al., >>2002<<). We directly demonstrate that DNA-PKCS does not visibly accumulate at induced DSB sites in Ku80-deficient cells. Complementing these cells with Ku80 restores the ability of DNA-PKCS to accumulate. Collectively, our findings indicate that
n3:mentions: n2:12379113

Subject Item: _:vb2303231
rdf:type: n3:Context
rdf:value: These findings are in agreement with recent observations of the in vivo behavior of Ku80 at DSB sites (Mari et al., >>2006<<). The 7A and KD mutations cause a dramatic decrease in the exchange rate of bound and free molecules. In other words, these mutant DNA-PKCS molecules are more stably bound to DNA ends than WT molecules. Obviously, there is still exchange
n3:mentions: n2:17124166

Subject Item: _:vb2303232
rdf:type: n3:Context
rdf:value: Biochemical experiments have demonstrated that unphosphorylated DNA-PKCS blocks DNA ends, and thereby inhibits efficient ligation (Weterings et al., >>2003<<; Block et al., 2004). This ligation block can be relieved by DNA-PKCS autophosphorylation, which induces a conformational change in the DNA–protein complex that liberates the DNA ends.
n3:mentions: n2:14654699

Subject Item: _:vb2303233
rdf:type: n3:Context
rdf:value: Biochemical experiments have demonstrated that unphosphorylated DNA-PKCS blocks DNA ends, and thereby inhibits efficient ligation (Weterings et al., 2003; Block et al., >>2004<<). This ligation block can be relieved by DNA-PKCS autophosphorylation, which induces a conformational change in the DNA–protein complex that liberates the DNA ends.
n3:mentions: n2:15314205

Subject Item: _:vb2303234
rdf:type: n3:Context
rdf:value: Subsequently, when the DNA ends are correctly juxtaposed (Cui et al., >>2005<<), the DNA-PKCS molecules will autophosphorylate each other.
n3:mentions: n2:16314509

Subject Item: _:vb2303235
rdf:type: n3:Context
rdf:value: For example, we did not mutate the Ser3205 residue that has previously been identified as an autophosphorylation site (Douglas et al., >>2002<<). This site can still be phosphorylated in the 7A mutant, but not in the KD mutant.
n3:mentions: n2:12186630

Subject Item: _:vb350803625
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 20
n3:hasRelevantPaperId: n2:16314509

Subject Item: _:vb350803626
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 19
n3:hasRelevantPaperId: n2:20192759

Subject Item: _:vb350803627
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 19
n3:hasRelevantPaperId: n2:12897153

Subject Item: _:vb350803628
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 19
n3:hasRelevantPaperId: n2:15677476

Subject Item: _:vb350803629
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 18
n3:hasRelevantPaperId: n2:11493912

Subject Item: _:vb350803630
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 16
n3:hasRelevantPaperId: n2:17124166

Subject Item: _:vb350803631
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 15
n3:hasRelevantPaperId: n2:17189255

Subject Item: _:vb350803632
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 14
n3:hasRelevantPaperId: n2:18064046

Subject Item: _:vb350803633
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 14
n3:hasRelevantPaperId: n2:17353268

Subject Item: _:vb350803634
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 14
n3:hasRelevantPaperId: n2:8422676

Subject Item: _:vb350803635
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 13
n3:hasRelevantPaperId: n2:17158925

Subject Item: _:vb350803636
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 13
n3:hasRelevantPaperId: n2:25818648

Subject Item: _:vb350803637
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 13
n3:hasRelevantPaperId: n2:20965415

Subject Item: _:vb350803638
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 13
n3:hasRelevantPaperId: n2:12231622

Subject Item: _:vb350803639
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 12
n3:hasRelevantPaperId: n2:19117531

Subject Item: _:vb350803640
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 11
n3:hasRelevantPaperId: n2:16618811

Subject Item: _:vb350803641
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 11
n3:hasRelevantPaperId: n2:24680878

Subject Item: _:vb350803642
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 11
n3:hasRelevantPaperId: n2:23897892

Subject Item: _:vb350803643
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 11
n3:hasRelevantPaperId: n2:19847258

Subject Item: _:vb350803644
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 10
n3:hasRelevantPaperId: n2:15059890

Subject Item: _:vb350803645
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 10
n3:hasRelevantPaperId: n2:12897142

Subject Item: _:vb350803646
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 10
n3:hasRelevantPaperId: n2:25550082

Subject Item: _:vb350803647
rdf:type: n3:RelevantBibliographicResource
n3:RelevantScore: 10
n3:hasRelevantPaperId: n2:21030321

Subject Item: _:vb350803648
rdf:type: n3:RelevantBibliographicResource
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