Datasets:
vgainullin
/
xciting_data

Dataset card Data Studio Files
xet
 Community
1
paragraph_index
int64
sec
string
p_has_citation
int64
cites
string
citeids
list
pmid
int64
cited_id
string
sentences
string
all_sent_cites
list
sent_len
int64
sentence_batch_index
int64
sent_has_citation
float64
qc_fail
bool
cited_sentence
string
cites_in_sentence
list
cln_sentence
string
is_cap
bool
is_alpha
bool
ends_wp
bool
cit_qc
bool
lgtm
bool
__index_level_0__
int64
12
DISCUSSION
1
29
[ "b29", "b29" ]
17,090,584
pmid-15024409|pmid-15024409
Our results implicate DCL2 in production of 22 nt viral siRNAs.
[ "29", "29" ]
63
9,600
0
false
Our results implicate DCL2 in production of 22 nt viral siRNAs.
[]
Our results implicate DCL2 in production of 22 nt viral siRNAs.
true
true
true
true
true
1,528
12
DISCUSSION
1
29
[ "b29", "b29" ]
17,090,584
pmid-15024409|pmid-15024409
These species accumulate in wt but not dcl2 plants infected with both DNA viruses studied here.
[ "29", "29" ]
95
9,601
0
false
These species accumulate in wt but not dcl2 plants infected with both DNA viruses studied here.
[]
These species accumulate in wt but not dcl2 plants infected with both DNA viruses studied here.
true
true
true
true
true
1,528
12
DISCUSSION
1
29
[ "b29", "b29" ]
17,090,584
pmid-15024409|pmid-15024409
Based on the increased accumulation of DCL2-dependent 22 nt siRNA in dcl3, dcl4 and d3d4, DCL2 appears to gain access to substrates normally processed by others DCLs.
[ "29", "29" ]
166
9,602
0
false
Based on the increased accumulation of DCL2-dependent 22 nt siRNA in dcl3, dcl4 and d3d4, DCL2 appears to gain access to substrates normally processed by others DCLs.
[]
Based on the increased accumulation of DCL2-dependent 22 nt siRNA in dcl3, dcl4 and d3d4, DCL2 appears to gain access to substrates normally processed by others DCLs.
true
true
true
true
true
1,528
12
DISCUSSION
1
29
[ "b29", "b29" ]
17,090,584
pmid-15024409|pmid-15024409
An antiviral role of DCL2 was suggested by Xie et al.
[ "29", "29" ]
53
9,603
0
false
An antiviral role of DCL2 was suggested by Xie et al.
[]
An antiviral role of DCL2 was suggested by Xie et al.
true
true
true
true
true
1,528
12
DISCUSSION
1
29
[ "b29", "b29" ]
17,090,584
pmid-15024409|pmid-15024409
(29) based on increased susceptibility of dcl2 plants to the RNA carmovirus TCV, which correlates with the absence of TCV-derived siRNAs at the early stage of infection.
[ "29", "29" ]
169
9,604
1
false
based on increased susceptibility of dcl2 plants to the RNA carmovirus TCV, which correlates with the absence of TCV-derived siRNAs at the early stage of infection.
[ "29" ]
based on increased susceptibility of dcl2 plants to the RNA carmovirus TCV, which correlates with the absence of TCV-derived siRNAs at the early stage of infection.
false
true
true
true
false
1,528
12
DISCUSSION
1
29
[ "b29", "b29" ]
17,090,584
pmid-15024409|pmid-15024409
Nonetheless, infection with RNA viruses including CMV, TuMV (29) and ORMV (this study) did not result in differences of viral titers or siRNA accumulation in dcl2 or other mutants, except dcl4 (this study).
[ "29", "29" ]
206
9,605
1
false
Nonetheless, infection with RNA viruses including CMV, TuMV and ORMV (this study) did not result in differences of viral titers or siRNA accumulation in dcl2 or other mutants, except dcl4 (this study).
[ "29" ]
Nonetheless, infection with RNA viruses including CMV, TuMV and ORMV (this study) did not result in differences of viral titers or siRNA accumulation in dcl2 or other mutants, except dcl4 (this study).
true
true
true
true
true
1,528
12
DISCUSSION
1
29
[ "b29", "b29" ]
17,090,584
pmid-15024409|pmid-15024409
We did notice, however, that DCL2-dependent 22 nt ORMV siRNAs accumulate in dcl4.
[ "29", "29" ]
81
9,606
0
false
We did notice, however, that DCL2-dependent 22 nt ORMV siRNAs accumulate in dcl4.
[]
We did notice, however, that DCL2-dependent 22 nt ORMV siRNAs accumulate in dcl4.
true
true
true
true
true
1,528
13
DISCUSSION
1
30
[ "b30", "b31" ]
17,090,584
pmid-16741077|pmid-16810317
Based on their analyses of RNA viruses, Deleris et al.
[ "30", "31" ]
54
9,607
0
false
Based on their analyses of RNA viruses, Deleris et al.
[]
Based on their analyses of RNA viruses, Deleris et al.
true
true
true
true
true
1,529
13
DISCUSSION
1
30
[ "b30", "b31" ]
17,090,584
pmid-16741077|pmid-16810317
(30) and Bouche et al.
[ "30", "31" ]
22
9,608
1
false
and Bouche et al.
[ "30" ]
and Bouche et al.
false
true
true
true
false
1,529
13
DISCUSSION
1
31
[ "b30", "b31" ]
17,090,584
pmid-16741077|pmid-16810317
(31) concluded that DCL4 plays a key role in anti-viral defense and RNA-VIGS but, when DCL4 is mutated or inhibited by viral suppression, DCL2 takes over this role.
[ "30", "31" ]
164
9,609
1
false
concluded that DCL4 plays a key role in anti-viral defense and RNA-VIGS but, when DCL4 is mutated or inhibited by viral suppression, DCL2 takes over this role.
[ "31" ]
concluded that DCL4 plays a key role in anti-viral defense and RNA-VIGS but, when DCL4 is mutated or inhibited by viral suppression, DCL2 takes over this role.
false
true
true
true
false
1,529
13
DISCUSSION
1
30
[ "b30", "b31" ]
17,090,584
pmid-16741077|pmid-16810317
Our results for the RNA tobamovirus confirm such a hierarchical action of DCL4 and DCL2 and further show that DCL3 can also limit viral RNA accumulation.
[ "30", "31" ]
153
9,610
0
false
Our results for the RNA tobamovirus confirm such a hierarchical action of DCL4 and DCL2 and further show that DCL3 can also limit viral RNA accumulation.
[]
Our results for the RNA tobamovirus confirm such a hierarchical action of DCL4 and DCL2 and further show that DCL3 can also limit viral RNA accumulation.
true
true
true
true
true
1,529
14
DISCUSSION
1
19
[ "b19", "b35", "b36", "b7" ]
17,090,584
pmid-16421273|pmid-16724105|pmid-16731914|pmid-16081530
RNA viruses might circumvent complex DCL redundancies by suppressing RNA silencing downstream, at the shared HEN1 step.
[ "19", "35", "36", "7" ]
119
9,611
0
false
RNA viruses might circumvent complex DCL redundancies by suppressing RNA silencing downstream, at the shared HEN1 step.
[]
RNA viruses might circumvent complex DCL redundancies by suppressing RNA silencing downstream, at the shared HEN1 step.
true
true
true
true
true
1,530
14
DISCUSSION
1
19
[ "b19", "b35", "b36", "b7" ]
17,090,584
pmid-16421273|pmid-16724105|pmid-16731914|pmid-16081530
We show that ORMV infection interferes with HEN1-mediated methylation of viral siRNAs and endogenous sRNAs, including miRNAs and ta-siRNAs, but not 24 nt ra-siRNAs
[ "19", "35", "36", "7" ]
163
9,612
0
false
We show that ORMV infection interferes with HEN1-mediated methylation of viral siRNAs and endogenous sRNAs, including miRNAs and ta-siRNAs, but not 24 nt ra-siRNAs
[]
We show that ORMV infection interferes with HEN1-mediated methylation of viral siRNAs and endogenous sRNAs, including miRNAs and ta-siRNAs, but not 24 nt ra-siRNAs
true
true
false
true
false
1,530
14
DISCUSSION
1
19
[ "b19", "b35", "b36", "b7" ]
17,090,584
pmid-16421273|pmid-16724105|pmid-16731914|pmid-16081530
[this work and (19)].
[ "19", "35", "36", "7" ]
21
9,613
0
false
.
[ "this work and (19)" ]
.
false
false
true
true
false
1,530
14
DISCUSSION
1
19
[ "b19", "b35", "b36", "b7" ]
17,090,584
pmid-16421273|pmid-16724105|pmid-16731914|pmid-16081530
Furthermore, miRNA* and ta-siRNA* strands over-accumulate during ORMV infection.
[ "19", "35", "36", "7" ]
80
9,614
0
false
Furthermore, miRNA* and ta-siRNA* strands over-accumulate during ORMV infection.
[]
Furthermore, miRNA* and ta-siRNA* strands over-accumulate during ORMV infection.
true
true
true
true
true
1,530
14
DISCUSSION
1
19
[ "b19", "b35", "b36", "b7" ]
17,090,584
pmid-16421273|pmid-16724105|pmid-16731914|pmid-16081530
The tobamovirus factor responsible for interference with HEN1 remains to be identified.
[ "19", "35", "36", "7" ]
87
9,615
0
false
The tobamovirus factor responsible for interference with HEN1 remains to be identified.
[]
The tobamovirus factor responsible for interference with HEN1 remains to be identified.
true
true
true
true
true
1,530
14
DISCUSSION
1
19
[ "b19", "b35", "b36", "b7" ]
17,090,584
pmid-16421273|pmid-16724105|pmid-16731914|pmid-16081530
Mechanistically, one of the viral proteins might bind sRNA duplexes, as was demonstrated for several viral suppressors (35,36), or inactivate HEN1 directly through a protein-protein interaction.
[ "19", "35", "36", "7" ]
194
9,616
0
false
Mechanistically, one of the viral proteins might bind sRNA duplexes, as was demonstrated for several viral suppressors, or inactivate HEN1 directly through a protein-protein interaction.
[ "35,36" ]
Mechanistically, one of the viral proteins might bind sRNA duplexes, as was demonstrated for several viral suppressors, or inactivate HEN1 directly through a protein-protein interaction.
true
true
true
true
true
1,530
14
DISCUSSION
1
19
[ "b19", "b35", "b36", "b7" ]
17,090,584
pmid-16421273|pmid-16724105|pmid-16731914|pmid-16081530
Unmethylated sRNA duplexes appear to undergo partial degradation at their 2 nt overhangs that results in accumulation of shorter-sized sRNAs of both viral and endogenous origin.
[ "19", "35", "36", "7" ]
177
9,617
0
false
Unmethylated sRNA duplexes appear to undergo partial degradation at their 2 nt overhangs that results in accumulation of shorter-sized sRNAs of both viral and endogenous origin.
[]
Unmethylated sRNA duplexes appear to undergo partial degradation at their 2 nt overhangs that results in accumulation of shorter-sized sRNAs of both viral and endogenous origin.
true
true
true
true
true
1,530
14
DISCUSSION
1
19
[ "b19", "b35", "b36", "b7" ]
17,090,584
pmid-16421273|pmid-16724105|pmid-16731914|pmid-16081530
Additionally, they are also subject to 3′-end oligouridylation observed at least for the miR173/miR173* duplex (Figure 6C).
[ "19", "35", "36", "7" ]
123
9,618
0
false
Additionally, they are also subject to 3′-end oligouridylation observed at least for the miR173/miR173* duplex (Figure 6C).
[]
Additionally, they are also subject to 3′-end oligouridylation observed at least for the miR173/miR173* duplex (Figure 6C).
true
true
true
true
true
1,530
14
DISCUSSION
1
19
[ "b19", "b35", "b36", "b7" ]
17,090,584
pmid-16421273|pmid-16724105|pmid-16731914|pmid-16081530
In both cases, assembly of RISC and the spread of silencing might be compromised.
[ "19", "35", "36", "7" ]
81
9,619
0
false
In both cases, assembly of RISC and the spread of silencing might be compromised.
[]
In both cases, assembly of RISC and the spread of silencing might be compromised.
true
true
true
true
true
1,530
14
DISCUSSION
1
7
[ "b19", "b35", "b36", "b7" ]
17,090,584
pmid-16421273|pmid-16724105|pmid-16731914|pmid-16081530
The proposed RISC assembly defect is supported by Baumberger and Baulcombe (7) who found that siRNAs derived from three RNA viruses (including another tobamovirus) are not associated with the RISC slicer component AGO1.
[ "19", "35", "36", "7" ]
219
9,620
1
false
The proposed RISC assembly defect is supported by Baumberger and Baulcombe who found that siRNAs derived from three RNA viruses (including another tobamovirus) are not associated with the RISC slicer component AGO1.
[ "7" ]
The proposed RISC assembly defect is supported by Baumberger and Baulcombe who found that siRNAs derived from three RNA viruses (including another tobamovirus) are not associated with the RISC slicer component AGO1.
true
true
true
true
true
1,530
14
DISCUSSION
1
19
[ "b19", "b35", "b36", "b7" ]
17,090,584
pmid-16421273|pmid-16724105|pmid-16731914|pmid-16081530
It would be interesting to test whether other viruses from the AGO1 study interfere with HEN1.
[ "19", "35", "36", "7" ]
94
9,621
0
false
It would be interesting to test whether other viruses from the AGO1 study interfere with HEN1.
[]
It would be interesting to test whether other viruses from the AGO1 study interfere with HEN1.
true
true
true
true
true
1,530
15
DISCUSSION
1
35
[ "b35", "b38", "b58" ]
17,090,584
pmid-16724105|pmid-15131083|pmid-16678167
When expressed as transgenes in Arabidopsis, silencing suppressors including potyviral HC-Pro, tombusviral p19 and closteroviral p21, known to bind miRNA and siRNA duplexes in vitro (35), increase accumulation of miRNA* strands (38) and prevent miRNA methylation by HEN1 (58).
[ "35", "38", "58" ]
276
9,622
1
false
When expressed as transgenes in Arabidopsis, silencing suppressors including potyviral HC-Pro, tombusviral p19 and closteroviral p21, known to bind miRNA and siRNA duplexes in vitro, increase accumulation of miRNA* strands and prevent miRNA methylation by HEN1.
[ "35", "38", "58" ]
When expressed as transgenes in Arabidopsis, silencing suppressors including potyviral HC-Pro, tombusviral p19 and closteroviral p21, known to bind miRNA and siRNA duplexes in vitro, increase accumulation of miRNA* strands and prevent miRNA methylation by HEN1.
true
true
true
true
true
1,531
15
DISCUSSION
1
35
[ "b35", "b38", "b58" ]
17,090,584
pmid-16724105|pmid-15131083|pmid-16678167
If these suppressors also interfere with HEN1 activity during viral infection, then targeting HEN1 would be a general silencing suppression strategy.
[ "35", "38", "58" ]
149
9,623
0
false
If these suppressors also interfere with HEN1 activity during viral infection, then targeting HEN1 would be a general silencing suppression strategy.
[]
If these suppressors also interfere with HEN1 activity during viral infection, then targeting HEN1 would be a general silencing suppression strategy.
true
true
true
true
true
1,531
16
DISCUSSION
0
null
null
17,090,584
null
Additionally, our results suggest that the pararetrovirus CaMV has evolved a suppressor that stabilizes dsRNA products of RDR6.
null
127
9,624
0
false
null
null
Additionally, our results suggest that the pararetrovirus CaMV has evolved a suppressor that stabilizes dsRNA products of RDR6.
true
true
true
true
true
1,532
16
DISCUSSION
0
null
null
17,090,584
null
Indeed, several abundant long dsRNA precursors of ta-siRNAs accumulate in CaMV-infected plants.
null
95
9,625
0
false
null
null
Indeed, several abundant long dsRNA precursors of ta-siRNAs accumulate in CaMV-infected plants.
true
true
true
true
true
1,532
16
DISCUSSION
0
null
null
17,090,584
null
Potentially, the putative suppressor impairs the processing of these long dsRNAs by DCL4.
null
89
9,626
0
false
null
null
Potentially, the putative suppressor impairs the processing of these long dsRNAs by DCL4.
true
true
true
true
true
1,532
16
DISCUSSION
0
null
null
17,090,584
null
Suppression of DCL4 in CaMV-infected tissues would be consistent with our result that the major fraction of 21 nt CaMV siRNAs depends on DCL1; during CaLCuV and ORMV infection, DCL4 performs this function instead.
null
213
9,627
0
false
null
null
Suppression of DCL4 in CaMV-infected tissues would be consistent with our result that the major fraction of 21 nt CaMV siRNAs depends on DCL1; during CaLCuV and ORMV infection, DCL4 performs this function instead.
true
true
true
true
true
1,532
16
DISCUSSION
0
null
null
17,090,584
null
No silencing suppressor encoded by plant pararetroviruses has been reported so far.
null
83
9,628
0
false
null
null
No silencing suppressor encoded by plant pararetroviruses has been reported so far.
true
true
true
true
true
1,532
16
DISCUSSION
0
null
null
17,090,584
null
Our findings provide the basis for identifying this factor and for using CaMV as a tool to study ta-siRNA biogenesis.
null
117
9,629
0
false
null
null
Our findings provide the basis for identifying this factor and for using CaMV as a tool to study ta-siRNA biogenesis.
true
true
true
true
true
1,532
17
DISCUSSION
1
59
[ "b59", "b60", "b60" ]
17,090,584
pmid-15681452|pmid-16006510|pmid-16006510
The silencing suppression strategies we propose for CaMV and ORMV do not appear to be exploited by CaLCuV.
[ "59", "60", "60" ]
106
9,630
0
false
The silencing suppression strategies we propose for CaMV and ORMV do not appear to be exploited by CaLCuV.
[]
The silencing suppression strategies we propose for CaMV and ORMV do not appear to be exploited by CaLCuV.
true
true
true
true
true
1,533
17
DISCUSSION
1
59
[ "b59", "b60", "b60" ]
17,090,584
pmid-15681452|pmid-16006510|pmid-16006510
DCL4- and HEN1-dependent production of methylated 21 nt viral siRNAs is not impaired in CaLCuV infected Arabidopsis.
[ "59", "60", "60" ]
116
9,631
0
false
DCL4- and HEN1-dependent production of methylated 21 nt viral siRNAs is not impaired in CaLCuV infected Arabidopsis.
[]
DCL4- and HEN1-dependent production of methylated 21 nt viral siRNAs is not impaired in CaLCuV infected Arabidopsis.
true
true
true
true
true
1,533
17
DISCUSSION
1
59
[ "b59", "b60", "b60" ]
17,090,584
pmid-15681452|pmid-16006510|pmid-16006510
Geminiviruses encode at least two types of silencing suppressor proteins, AC2 and AC4 (59,60).
[ "59", "60", "60" ]
94
9,632
0
false
Geminiviruses encode at least two types of silencing suppressor proteins, AC2 and AC4.
[ "59,60" ]
Geminiviruses encode at least two types of silencing suppressor proteins, AC2 and AC4.
true
true
true
true
true
1,533
17
DISCUSSION
1
60
[ "b59", "b60", "b60" ]
17,090,584
pmid-15681452|pmid-16006510|pmid-16006510
The latter specifically binds single-stranded 21 nt sRNA in vitro and miRNA in vivo (60).
[ "59", "60", "60" ]
89
9,633
1
false
The latter specifically binds single-stranded 21 nt sRNA in vitro and miRNA in vivo.
[ "60" ]
The latter specifically binds single-stranded 21 nt sRNA in vitro and miRNA in vivo.
true
true
true
true
true
1,533
17
DISCUSSION
1
59
[ "b59", "b60", "b60" ]
17,090,584
pmid-15681452|pmid-16006510|pmid-16006510
Since VIGS initiated by CaLCuV::Chl spreads efficiently into emerging leaves via the action of DCL4, HEN1 and RDR6, geminivirus suppressors of silencing might act downstream of methylated 21 nt siRNA production.
[ "59", "60", "60" ]
211
9,634
0
false
Since VIGS initiated by CaLCuV::Chl spreads efficiently into emerging leaves via the action of DCL4, HEN1 and RDR6, geminivirus suppressors of silencing might act downstream of methylated 21 nt siRNA production.
[]
Since VIGS initiated by CaLCuV::Chl spreads efficiently into emerging leaves via the action of DCL4, HEN1 and RDR6, geminivirus suppressors of silencing might act downstream of methylated 21 nt siRNA production.
true
true
true
true
true
1,533
0
INTRODUCTION
1
1
[ "b1", "b4", "b5", "b6" ]
16,945,962
pmid-1567678|pmid-11340626|pmid-8710842|pmid-9039264|pmid-11292336|pmid-16862129|pmid-15164066|pmid-16428451
Chromosomal DNA is exposed to various DNA-damaging agents and sustains damage that induces genomic instability.
[ "1", "4", "5", "6" ]
111
9,635
0
false
Chromosomal DNA is exposed to various DNA-damaging agents and sustains damage that induces genomic instability.
[]
Chromosomal DNA is exposed to various DNA-damaging agents and sustains damage that induces genomic instability.
true
true
true
true
true
1,534
0
INTRODUCTION
1
1
[ "b1", "b4", "b5", "b6" ]
16,945,962
pmid-1567678|pmid-11340626|pmid-8710842|pmid-9039264|pmid-11292336|pmid-16862129|pmid-15164066|pmid-16428451
A double-strand break (DSB) is caused by ionizing radiation, cross-linking reagents, oxidative stress and DNA replication failure.
[ "1", "4", "5", "6" ]
130
9,636
0
false
A double-strand break (DSB) is caused by ionizing radiation, cross-linking reagents, oxidative stress and DNA replication failure.
[]
A double-strand break (DSB) is caused by ionizing radiation, cross-linking reagents, oxidative stress and DNA replication failure.
true
true
true
true
true
1,534
0
INTRODUCTION
1
1
[ "b1", "b4", "b5", "b6" ]
16,945,962
pmid-1567678|pmid-11340626|pmid-8710842|pmid-9039264|pmid-11292336|pmid-16862129|pmid-15164066|pmid-16428451
If the DSB is left unrepaired, then cell death occurs (1–4).
[ "1", "4", "5", "6" ]
60
9,637
0
false
If the DSB is left unrepaired, then cell death occurs.
[ "1–4" ]
If the DSB is left unrepaired, then cell death occurs.
true
true
true
true
true
1,534
0
INTRODUCTION
1
1
[ "b1", "b4", "b5", "b6" ]
16,945,962
pmid-1567678|pmid-11340626|pmid-8710842|pmid-9039264|pmid-11292336|pmid-16862129|pmid-15164066|pmid-16428451
Homologous recombination is one of the major DSB repair pathways.
[ "1", "4", "5", "6" ]
65
9,638
0
false
Homologous recombination is one of the major DSB repair pathways.
[]
Homologous recombination is one of the major DSB repair pathways.
true
true
true
true
true
1,534
0
INTRODUCTION
1
1
[ "b1", "b4", "b5", "b6" ]
16,945,962
pmid-1567678|pmid-11340626|pmid-8710842|pmid-9039264|pmid-11292336|pmid-16862129|pmid-15164066|pmid-16428451
This repair pathway is essentially error-free, since a homologous region of the undamaged sister chromatid is used as the template for repair.
[ "1", "4", "5", "6" ]
142
9,639
0
false
This repair pathway is essentially error-free, since a homologous region of the undamaged sister chromatid is used as the template for repair.
[]
This repair pathway is essentially error-free, since a homologous region of the undamaged sister chromatid is used as the template for repair.
true
true
true
true
true
1,534
0
INTRODUCTION
1
1
[ "b1", "b4", "b5", "b6" ]
16,945,962
pmid-1567678|pmid-11340626|pmid-8710842|pmid-9039264|pmid-11292336|pmid-16862129|pmid-15164066|pmid-16428451
In contrast to the mitotic DSB repair pathway, meiotic cell division involves homologous recombination between homologous chromosomes, but not between sister chromatids.
[ "1", "4", "5", "6" ]
169
9,640
0
false
In contrast to the mitotic DSB repair pathway, meiotic cell division involves homologous recombination between homologous chromosomes, but not between sister chromatids.
[]
In contrast to the mitotic DSB repair pathway, meiotic cell division involves homologous recombination between homologous chromosomes, but not between sister chromatids.
true
true
true
true
true
1,534
0
INTRODUCTION
1
1
[ "b1", "b4", "b5", "b6" ]
16,945,962
pmid-1567678|pmid-11340626|pmid-8710842|pmid-9039264|pmid-11292336|pmid-16862129|pmid-15164066|pmid-16428451
This preferential recombination between homologous chromosomes is initiated by the formation of a programmed DSB and ensures correct chromosomal segregation at meiosis I through the formation of chiasmata, which physically connect homologous chromosomes (5,6).
[ "1", "4", "5", "6" ]
260
9,641
0
false
This preferential recombination between homologous chromosomes is initiated by the formation of a programmed DSB and ensures correct chromosomal segregation at meiosis I through the formation of chiasmata, which physically connect homologous chromosomes.
[ "5,6" ]
This preferential recombination between homologous chromosomes is initiated by the formation of a programmed DSB and ensures correct chromosomal segregation at meiosis I through the formation of chiasmata, which physically connect homologous chromosomes.
true
true
true
true
true
1,534
0
INTRODUCTION
1
1
[ "b1", "b4", "b5", "b6" ]
16,945,962
pmid-1567678|pmid-11340626|pmid-8710842|pmid-9039264|pmid-11292336|pmid-16862129|pmid-15164066|pmid-16428451
Thus, homologous recombination is important to maintain the integrity of the chromosome in both mitotic and meiotic cells.
[ "1", "4", "5", "6" ]
122
9,642
0
false
Thus, homologous recombination is important to maintain the integrity of the chromosome in both mitotic and meiotic cells.
[]
Thus, homologous recombination is important to maintain the integrity of the chromosome in both mitotic and meiotic cells.
true
true
true
true
true
1,534
1
INTRODUCTION
1
7
[ "b7", "b12", "b13", "b16", "b17", "b22", "b23", "b24" ]
16,945,962
pmid-156361|pmid-6325943|pmid-1581960|pmid-8602360|pmid-8066464|pmid-15164066|pmid-12456786|pmid-12912992|pmid-15164066|pmid-15917243|pmid-15235592|pmid-11459986|pmid-15899844|pmid-10485886|pmid-15125839
In homologous recombination, a single-stranded DNA (ssDNA) tail, produced at the DSB site, is incorporated into a nucleoprotein complex called the presynaptic filament.
[ "7", "12", "13", "16", "17", "22", "23", "24" ]
168
9,643
0
false
In homologous recombination, a single-stranded DNA (ssDNA) tail, produced at the DSB site, is incorporated into a nucleoprotein complex called the presynaptic filament.
[]
In homologous recombination, a single-stranded DNA (ssDNA) tail, produced at the DSB site, is incorporated into a nucleoprotein complex called the presynaptic filament.
true
true
true
true
true
1,535
1
INTRODUCTION
1
7
[ "b7", "b12", "b13", "b16", "b17", "b22", "b23", "b24" ]
16,945,962
pmid-156361|pmid-6325943|pmid-1581960|pmid-8602360|pmid-8066464|pmid-15164066|pmid-12456786|pmid-12912992|pmid-15164066|pmid-15917243|pmid-15235592|pmid-11459986|pmid-15899844|pmid-10485886|pmid-15125839
This presynaptic filament catalyzes homologous pairing and strand exchange with an intact homologous region of the double-stranded DNA (dsDNA) molecule.
[ "7", "12", "13", "16", "17", "22", "23", "24" ]
152
9,644
0
false
This presynaptic filament catalyzes homologous pairing and strand exchange with an intact homologous region of the double-stranded DNA (dsDNA) molecule.
[]
This presynaptic filament catalyzes homologous pairing and strand exchange with an intact homologous region of the double-stranded DNA (dsDNA) molecule.
true
true
true
true
true
1,535
1
INTRODUCTION
1
7
[ "b7", "b12", "b13", "b16", "b17", "b22", "b23", "b24" ]
16,945,962
pmid-156361|pmid-6325943|pmid-1581960|pmid-8602360|pmid-8066464|pmid-15164066|pmid-12456786|pmid-12912992|pmid-15164066|pmid-15917243|pmid-15235592|pmid-11459986|pmid-15899844|pmid-10485886|pmid-15125839
The bacterial RecA protein is known to form helical presynaptic filaments and to play central roles in homologous recombination (7–12).
[ "7", "12", "13", "16", "17", "22", "23", "24" ]
135
9,645
0
false
The bacterial RecA protein is known to form helical presynaptic filaments and to play central roles in homologous recombination.
[ "7–12" ]
The bacterial RecA protein is known to form helical presynaptic filaments and to play central roles in homologous recombination.
true
true
true
true
true
1,535
1
INTRODUCTION
1
7
[ "b7", "b12", "b13", "b16", "b17", "b22", "b23", "b24" ]
16,945,962
pmid-156361|pmid-6325943|pmid-1581960|pmid-8602360|pmid-8066464|pmid-15164066|pmid-12456786|pmid-12912992|pmid-15164066|pmid-15917243|pmid-15235592|pmid-11459986|pmid-15899844|pmid-10485886|pmid-15125839
In eukaryotes, two homologs of RecA, the Rad51 and Dmc1 proteins, which are conserved from yeast to human, are assumed to fulfill this role.
[ "7", "12", "13", "16", "17", "22", "23", "24" ]
140
9,646
0
false
In eukaryotes, two homologs of RecA, the Rad51 and Dmc1 proteins, which are conserved from yeast to human, are assumed to fulfill this role.
[]
In eukaryotes, two homologs of RecA, the Rad51 and Dmc1 proteins, which are conserved from yeast to human, are assumed to fulfill this role.
true
true
true
true
true
1,535
1
INTRODUCTION
1
7
[ "b7", "b12", "b13", "b16", "b17", "b22", "b23", "b24" ]
16,945,962
pmid-156361|pmid-6325943|pmid-1581960|pmid-8602360|pmid-8066464|pmid-15164066|pmid-12456786|pmid-12912992|pmid-15164066|pmid-15917243|pmid-15235592|pmid-11459986|pmid-15899844|pmid-10485886|pmid-15125839
Rad51 is expressed in both meiotic and mitotic cells, whereas the expression of Dmc1 is restricted to meiotic cells (13–16).
[ "7", "12", "13", "16", "17", "22", "23", "24" ]
124
9,647
0
false
Rad51 is expressed in both meiotic and mitotic cells, whereas the expression of Dmc1 is restricted to meiotic cells.
[ "13–16" ]
Rad51 is expressed in both meiotic and mitotic cells, whereas the expression of Dmc1 is restricted to meiotic cells.
true
true
true
true
true
1,535
1
INTRODUCTION
1
7
[ "b7", "b12", "b13", "b16", "b17", "b22", "b23", "b24" ]
16,945,962
pmid-156361|pmid-6325943|pmid-1581960|pmid-8602360|pmid-8066464|pmid-15164066|pmid-12456786|pmid-12912992|pmid-15164066|pmid-15917243|pmid-15235592|pmid-11459986|pmid-15899844|pmid-10485886|pmid-15125839
Although previous biochemical studies demonstrated that Rad51 and Dmc1 have recombinational activities similar to those of RecA (17–22), other studies have also revealed that many ancillary factors, such as replication protein A (RPA), Rad52 and Rad54, significantly affect the activities of Rad51 and Dmc1 (23,24).
[ "7", "12", "13", "16", "17", "22", "23", "24" ]
315
9,648
0
false
Although previous biochemical studies demonstrated that Rad51 and Dmc1 have recombinational activities similar to those of RecA, other studies have also revealed that many ancillary factors, such as replication protein A (RPA), Rad52 and Rad54, significantly affect the activities of Rad51 and Dmc1.
[ "17–22", "23,24" ]
Although previous biochemical studies demonstrated that Rad51 and Dmc1 have recombinational activities similar to those of RecA, other studies have also revealed that many ancillary factors, such as replication protein A (RPA), Rad52 and Rad54, significantly affect the activities of Rad51 and Dmc1.
true
true
true
true
true
1,535
2
INTRODUCTION
1
25
[ "b25", "b31", "b32", "b33", "b34", "b35", "b37" ]
16,945,962
pmid-7651832|pmid-15105430|pmid-9108475|pmid-10209103|pmid-11030336|pmid-9590697|pmid-12453424|pmid-16862129|pmid-16818238
Rad54 is a member of the SWI2/SNF2 family of proteins, which have DNA-dependent ATPase activities and are involved in chromatin remodeling (25–31).
[ "25", "31", "32", "33", "34", "35", "37" ]
147
9,649
0
false
Rad54 is a member of the SWI2/SNF2 family of proteins, which have DNA-dependent ATPase activities and are involved in chromatin remodeling.
[ "25–31" ]
Rad54 is a member of the SWI2/SNF2 family of proteins, which have DNA-dependent ATPase activities and are involved in chromatin remodeling.
true
true
true
true
true
1,536
2
INTRODUCTION
1
32
[ "b25", "b31", "b32", "b33", "b34", "b35", "b37" ]
16,945,962
pmid-7651832|pmid-15105430|pmid-9108475|pmid-10209103|pmid-11030336|pmid-9590697|pmid-12453424|pmid-16862129|pmid-16818238
Genetic studies revealed that Rad54-deficient cells are sensitive to DNA-damaging agents, such as ionizing radiation, methyl methanesulfonate (MMS) and mitomycin C (32).
[ "25", "31", "32", "33", "34", "35", "37" ]
169
9,650
1
false
Genetic studies revealed that Rad54-deficient cells are sensitive to DNA-damaging agents, such as ionizing radiation, methyl methanesulfonate (MMS) and mitomycin C.
[ "32" ]
Genetic studies revealed that Rad54-deficient cells are sensitive to DNA-damaging agents, such as ionizing radiation, methyl methanesulfonate (MMS) and mitomycin C.
true
true
true
true
true
1,536
2
INTRODUCTION
1
25
[ "b25", "b31", "b32", "b33", "b34", "b35", "b37" ]
16,945,962
pmid-7651832|pmid-15105430|pmid-9108475|pmid-10209103|pmid-11030336|pmid-9590697|pmid-12453424|pmid-16862129|pmid-16818238
Rad54 utilizes the free energy from ATP hydrolysis to generate superhelical torsion into dsDNA by translocating on the DNA (33,34).
[ "25", "31", "32", "33", "34", "35", "37" ]
131
9,651
0
false
Rad54 utilizes the free energy from ATP hydrolysis to generate superhelical torsion into dsDNA by translocating on the DNA.
[ "33,34" ]
Rad54 utilizes the free energy from ATP hydrolysis to generate superhelical torsion into dsDNA by translocating on the DNA.
true
true
true
true
true
1,536
2
INTRODUCTION
1
25
[ "b25", "b31", "b32", "b33", "b34", "b35", "b37" ]
16,945,962
pmid-7651832|pmid-15105430|pmid-9108475|pmid-10209103|pmid-11030336|pmid-9590697|pmid-12453424|pmid-16862129|pmid-16818238
Furthermore, yeast Rad54 promotes the assembly and disassembly of the Rad51 nucleoprotein filament, and both yeast and human Rad54 stimulate the Rad51-mediated homologous pairing activity by directly binding to Rad51 (35–37).
[ "25", "31", "32", "33", "34", "35", "37" ]
225
9,652
0
false
Furthermore, yeast Rad54 promotes the assembly and disassembly of the Rad51 nucleoprotein filament, and both yeast and human Rad54 stimulate the Rad51-mediated homologous pairing activity by directly binding to Rad51.
[ "35–37" ]
Furthermore, yeast Rad54 promotes the assembly and disassembly of the Rad51 nucleoprotein filament, and both yeast and human Rad54 stimulate the Rad51-mediated homologous pairing activity by directly binding to Rad51.
true
true
true
true
true
1,536
3
INTRODUCTION
1
22
[ "b22", "b38", "b39", "b40", "b41", "b41", "b41" ]
16,945,962
pmid-15164066|pmid-16428451|pmid-11884632|pmid-10362364|pmid-11782437|pmid-11782437|pmid-11782437
Recent studies showed that the human Rad54B protein, a homolog of Rad54, interacts with the human Rad51and Dmc1 proteins, and stimulates the homologous pairing activity mediated by these proteins (22,38).
[ "22", "38", "39", "40", "41", "41", "41" ]
204
9,653
0
false
Recent studies showed that the human Rad54B protein, a homolog of Rad54, interacts with the human Rad51and Dmc1 proteins, and stimulates the homologous pairing activity mediated by these proteins.
[ "22,38" ]
Recent studies showed that the human Rad54B protein, a homolog of Rad54, interacts with the human Rad51and Dmc1 proteins, and stimulates the homologous pairing activity mediated by these proteins.
true
true
true
true
true
1,537
3
INTRODUCTION
1
39
[ "b22", "b38", "b39", "b40", "b41", "b41", "b41" ]
16,945,962
pmid-15164066|pmid-16428451|pmid-11884632|pmid-10362364|pmid-11782437|pmid-11782437|pmid-11782437
Similar to Rad54, human Rad54B is a DNA-dependent ATPase (39) and is expressed in both mitotic and meiotic cells (40).
[ "22", "38", "39", "40", "41", "41", "41" ]
118
9,654
1
false
Similar to Rad54, human Rad54B is a DNA-dependent ATPase and is expressed in both mitotic and meiotic cells.
[ "39", "40" ]
Similar to Rad54, human Rad54B is a DNA-dependent ATPase and is expressed in both mitotic and meiotic cells.
true
true
true
true
true
1,537
3
INTRODUCTION
1
41
[ "b22", "b38", "b39", "b40", "b41", "b41", "b41" ]
16,945,962
pmid-15164066|pmid-16428451|pmid-11884632|pmid-10362364|pmid-11782437|pmid-11782437|pmid-11782437
However, genetic studies revealed that human Rad54B-deficient cells are not overly sensitive to ionizing radiation, MMS and cisplatin (41).
[ "22", "38", "39", "40", "41", "41", "41" ]
139
9,655
1
false
However, genetic studies revealed that human Rad54B-deficient cells are not overly sensitive to ionizing radiation, MMS and cisplatin.
[ "41" ]
However, genetic studies revealed that human Rad54B-deficient cells are not overly sensitive to ionizing radiation, MMS and cisplatin.
true
true
true
true
true
1,537
3
INTRODUCTION
1
41
[ "b22", "b38", "b39", "b40", "b41", "b41", "b41" ]
16,945,962
pmid-15164066|pmid-16428451|pmid-11884632|pmid-10362364|pmid-11782437|pmid-11782437|pmid-11782437
Furthermore, the human Rad54B-deficient cells are also proficient in mitotic sister chromatid exchange (41).
[ "22", "38", "39", "40", "41", "41", "41" ]
108
9,656
1
false
Furthermore, the human Rad54B-deficient cells are also proficient in mitotic sister chromatid exchange.
[ "41" ]
Furthermore, the human Rad54B-deficient cells are also proficient in mitotic sister chromatid exchange.
true
true
true
true
true
1,537
3
INTRODUCTION
1
41
[ "b22", "b38", "b39", "b40", "b41", "b41", "b41" ]
16,945,962
pmid-15164066|pmid-16428451|pmid-11884632|pmid-10362364|pmid-11782437|pmid-11782437|pmid-11782437
On the other hand, a severe reduction in targeted integration frequency was detected in the Rad54B-deficient cells (41).
[ "22", "38", "39", "40", "41", "41", "41" ]
120
9,657
1
false
On the other hand, a severe reduction in targeted integration frequency was detected in the Rad54B-deficient cells.
[ "41" ]
On the other hand, a severe reduction in targeted integration frequency was detected in the Rad54B-deficient cells.
true
true
true
true
true
1,537
3
INTRODUCTION
1
22
[ "b22", "b38", "b39", "b40", "b41", "b41", "b41" ]
16,945,962
pmid-15164066|pmid-16428451|pmid-11884632|pmid-10362364|pmid-11782437|pmid-11782437|pmid-11782437
These characteristics are different from those of Rad54, indicating that Rad54B may have a unique role in homologous recombination.
[ "22", "38", "39", "40", "41", "41", "41" ]
131
9,658
0
false
These characteristics are different from those of Rad54, indicating that Rad54B may have a unique role in homologous recombination.
[]
These characteristics are different from those of Rad54, indicating that Rad54B may have a unique role in homologous recombination.
true
true
true
true
true
1,537
4
INTRODUCTION
0
null
null
16,945,962
null
To understand the function of Rad54B in homologous recombination, in the present study, we purified the human Rad54B protein, which was overexpressed in insect cells and biochemically characterized it.
null
201
9,659
0
false
null
null
To understand the function of Rad54B in homologous recombination, in the present study, we purified the human Rad54B protein, which was overexpressed in insect cells and biochemically characterized it.
true
true
true
true
true
1,538
4
INTRODUCTION
0
null
null
16,945,962
null
The purified Rad54B protein bound to the ATPase domain of Dmc1.
null
63
9,660
0
false
null
null
The purified Rad54B protein bound to the ATPase domain of Dmc1.
true
true
true
true
true
1,538
4
INTRODUCTION
0
null
null
16,945,962
null
Furthermore, Rad54B stimulated the DNA strand exchange mediated by Dmc1 and stabilized the Dmc1–ssDNA complex.
null
110
9,661
0
false
null
null
Furthermore, Rad54B stimulated the DNA strand exchange mediated by Dmc1 and stabilized the Dmc1–ssDNA complex.
true
true
true
true
true
1,538
4
INTRODUCTION
0
null
null
16,945,962
null
Therefore, Rad54B may stimulate the Dmc1-mediated strand exchange by stabilizing the Dmc1–ssDNA nucleoprotein filament during homologous recombination.
null
151
9,662
0
false
null
null
Therefore, Rad54B may stimulate the Dmc1-mediated strand exchange by stabilizing the Dmc1–ssDNA nucleoprotein filament during homologous recombination.
true
true
true
true
true
1,538
0
DISCUSSION
1
54
[ "b54", "b55", "b22", "b38" ]
16,945,962
pmid-1567678|pmid-11340626|pmid-8710842|pmid-9039264|pmid-11292336|pmid-16862129|pmid-15164066|pmid-16428451
The yeast and human Rad54 proteins stimulate strand exchange by Rad51 (54,55), but, thus far, the activation of Dmc1-mediated strand exchange by the Rad54 homologs has not been reported.
[ "54", "55", "22", "38" ]
186
9,663
0
false
The yeast and human Rad54 proteins stimulate strand exchange by Rad51, but, thus far, the activation of Dmc1-mediated strand exchange by the Rad54 homologs has not been reported.
[ "54,55" ]
The yeast and human Rad54 proteins stimulate strand exchange by Rad51, but, thus far, the activation of Dmc1-mediated strand exchange by the Rad54 homologs has not been reported.
true
true
true
true
true
1,539
0
DISCUSSION
1
54
[ "b54", "b55", "b22", "b38" ]
16,945,962
pmid-1567678|pmid-11340626|pmid-8710842|pmid-9039264|pmid-11292336|pmid-16862129|pmid-15164066|pmid-16428451
The present findings suggest that the human Rad54B protein stimulates the Dmc1-mediated strand exchange, probably through the stabilization of the presynaptic filament formed by ssDNA and Dmc1.
[ "54", "55", "22", "38" ]
193
9,664
0
false
The present findings suggest that the human Rad54B protein stimulates the Dmc1-mediated strand exchange, probably through the stabilization of the presynaptic filament formed by ssDNA and Dmc1.
[]
The present findings suggest that the human Rad54B protein stimulates the Dmc1-mediated strand exchange, probably through the stabilization of the presynaptic filament formed by ssDNA and Dmc1.
true
true
true
true
true
1,539
0
DISCUSSION
1
54
[ "b54", "b55", "b22", "b38" ]
16,945,962
pmid-1567678|pmid-11340626|pmid-8710842|pmid-9039264|pmid-11292336|pmid-16862129|pmid-15164066|pmid-16428451
Recent studies have shown that Rad54B enhances D-loop formation by Dmc1 and Rad51 (22,38).
[ "54", "55", "22", "38" ]
90
9,665
0
false
Recent studies have shown that Rad54B enhances D-loop formation by Dmc1 and Rad51.
[ "22,38" ]
Recent studies have shown that Rad54B enhances D-loop formation by Dmc1 and Rad51.
true
true
true
true
true
1,539
0
DISCUSSION
1
54
[ "b54", "b55", "b22", "b38" ]
16,945,962
pmid-1567678|pmid-11340626|pmid-8710842|pmid-9039264|pmid-11292336|pmid-16862129|pmid-15164066|pmid-16428451
Taken together, Rad54B assists Dmc1 in the initial strand invasion step (homologous pairing), as well as in the extension of the heteroduplex region (strand exchange).
[ "54", "55", "22", "38" ]
167
9,666
0
false
Taken together, Rad54B assists Dmc1 in the initial strand invasion step (homologous pairing), as well as in the extension of the heteroduplex region (strand exchange).
[]
Taken together, Rad54B assists Dmc1 in the initial strand invasion step (homologous pairing), as well as in the extension of the heteroduplex region (strand exchange).
true
true
true
true
true
1,539
0
DISCUSSION
1
54
[ "b54", "b55", "b22", "b38" ]
16,945,962
pmid-1567678|pmid-11340626|pmid-8710842|pmid-9039264|pmid-11292336|pmid-16862129|pmid-15164066|pmid-16428451
To stabilize the Dmc1–ssDNA complex, catalytic amounts of Rad54B were sufficient.
[ "54", "55", "22", "38" ]
81
9,667
0
false
To stabilize the Dmc1–ssDNA complex, catalytic amounts of Rad54B were sufficient.
[]
To stabilize the Dmc1–ssDNA complex, catalytic amounts of Rad54B were sufficient.
true
true
true
true
true
1,539
0
DISCUSSION
1
54
[ "b54", "b55", "b22", "b38" ]
16,945,962
pmid-1567678|pmid-11340626|pmid-8710842|pmid-9039264|pmid-11292336|pmid-16862129|pmid-15164066|pmid-16428451
Consistent with this result, we observed that Rad54B associated with the termini of the Dmc1–ssDNA filament, by an electron microscopic analysis.
[ "54", "55", "22", "38" ]
145
9,668
0
false
Consistent with this result, we observed that Rad54B associated with the termini of the Dmc1–ssDNA filament, by an electron microscopic analysis.
[]
Consistent with this result, we observed that Rad54B associated with the termini of the Dmc1–ssDNA filament, by an electron microscopic analysis.
true
true
true
true
true
1,539
0
DISCUSSION
1
54
[ "b54", "b55", "b22", "b38" ]
16,945,962
pmid-1567678|pmid-11340626|pmid-8710842|pmid-9039264|pmid-11292336|pmid-16862129|pmid-15164066|pmid-16428451
These observations suggest that Rad54B may stabilize the Dmc1–ssDNA complex by interacting with the terminal region of the Dmc1–ssDNA complex.
[ "54", "55", "22", "38" ]
142
9,669
0
false
These observations suggest that Rad54B may stabilize the Dmc1–ssDNA complex by interacting with the terminal region of the Dmc1–ssDNA complex.
[]
These observations suggest that Rad54B may stabilize the Dmc1–ssDNA complex by interacting with the terminal region of the Dmc1–ssDNA complex.
true
true
true
true
true
1,539
1
DISCUSSION
1
22
[ "b22", "b45", "b48", "b56", "b58", "b59", "b43" ]
16,945,962
pmid-156361|pmid-6325943|pmid-1581960|pmid-8602360|pmid-8066464|pmid-15164066|pmid-12456786|pmid-12912992|pmid-15164066|pmid-15917243|pmid-15235592|pmid-11459986|pmid-15899844|pmid-10485886|pmid-15125839
How could Rad54B stabilize the Dmc1–ssDNA complexes?
[ "22", "45", "48", "56", "58", "59", "43" ]
52
9,670
0
false
How could Rad54B stabilize the Dmc1–ssDNA complexes?
[]
How could Rad54B stabilize the Dmc1–ssDNA complexes?
true
true
true
true
true
1,540
1
DISCUSSION
1
22
[ "b22", "b45", "b48", "b56", "b58", "b59", "b43" ]
16,945,962
pmid-156361|pmid-6325943|pmid-1581960|pmid-8602360|pmid-8066464|pmid-15164066|pmid-12456786|pmid-12912992|pmid-15164066|pmid-15917243|pmid-15235592|pmid-11459986|pmid-15899844|pmid-10485886|pmid-15125839
One possibility is that Rad54B could prevent the Dmc1–ssDNA nucleoprotein filament from disassembling by binding to one end of the filament.
[ "22", "45", "48", "56", "58", "59", "43" ]
140
9,671
0
false
One possibility is that Rad54B could prevent the Dmc1–ssDNA nucleoprotein filament from disassembling by binding to one end of the filament.
[]
One possibility is that Rad54B could prevent the Dmc1–ssDNA nucleoprotein filament from disassembling by binding to one end of the filament.
true
true
true
true
true
1,540
1
DISCUSSION
1
22
[ "b22", "b45", "b48", "b56", "b58", "b59", "b43" ]
16,945,962
pmid-156361|pmid-6325943|pmid-1581960|pmid-8602360|pmid-8066464|pmid-15164066|pmid-12456786|pmid-12912992|pmid-15164066|pmid-15917243|pmid-15235592|pmid-11459986|pmid-15899844|pmid-10485886|pmid-15125839
This may lead to the unidirectional assembly of the Dmc1–ssDNA nucleoprotein filament at the DSB site.
[ "22", "45", "48", "56", "58", "59", "43" ]
102
9,672
0
false
This may lead to the unidirectional assembly of the Dmc1–ssDNA nucleoprotein filament at the DSB site.
[]
This may lead to the unidirectional assembly of the Dmc1–ssDNA nucleoprotein filament at the DSB site.
true
true
true
true
true
1,540
1
DISCUSSION
1
22
[ "b22", "b45", "b48", "b56", "b58", "b59", "b43" ]
16,945,962
pmid-156361|pmid-6325943|pmid-1581960|pmid-8602360|pmid-8066464|pmid-15164066|pmid-12456786|pmid-12912992|pmid-15164066|pmid-15917243|pmid-15235592|pmid-11459986|pmid-15899844|pmid-10485886|pmid-15125839
The second possibility is that by physically interacting with Dmc1, Rad54B could alter the conformation of the Dmc1–ssDNA nucleoprotein filament from an inactive form to an active form.
[ "22", "45", "48", "56", "58", "59", "43" ]
185
9,673
0
false
The second possibility is that by physically interacting with Dmc1, Rad54B could alter the conformation of the Dmc1–ssDNA nucleoprotein filament from an inactive form to an active form.
[]
The second possibility is that by physically interacting with Dmc1, Rad54B could alter the conformation of the Dmc1–ssDNA nucleoprotein filament from an inactive form to an active form.
true
true
true
true
true
1,540
1
DISCUSSION
1
22
[ "b22", "b45", "b48", "b56", "b58", "b59", "b43" ]
16,945,962
pmid-156361|pmid-6325943|pmid-1581960|pmid-8602360|pmid-8066464|pmid-15164066|pmid-12456786|pmid-12912992|pmid-15164066|pmid-15917243|pmid-15235592|pmid-11459986|pmid-15899844|pmid-10485886|pmid-15125839
Multiple studies have indicated that the fundamental mechanism of Dmc1-mediated recombination is the same as that of the RecA homologs, suggesting that Dmc1 forms helical filaments when performing the strand exchange reaction (22,45,48,56–58).
[ "22", "45", "48", "56", "58", "59", "43" ]
243
9,674
0
false
Multiple studies have indicated that the fundamental mechanism of Dmc1-mediated recombination is the same as that of the RecA homologs, suggesting that Dmc1 forms helical filaments when performing the strand exchange reaction.
[ "22,45,48,56–58" ]
Multiple studies have indicated that the fundamental mechanism of Dmc1-mediated recombination is the same as that of the RecA homologs, suggesting that Dmc1 forms helical filaments when performing the strand exchange reaction.
true
true
true
true
true
1,540
1
DISCUSSION
1
59
[ "b22", "b45", "b48", "b56", "b58", "b59", "b43" ]
16,945,962
pmid-156361|pmid-6325943|pmid-1581960|pmid-8602360|pmid-8066464|pmid-15164066|pmid-12456786|pmid-12912992|pmid-15164066|pmid-15917243|pmid-15235592|pmid-11459986|pmid-15899844|pmid-10485886|pmid-15125839
However, Dmc1 forms octameric rings alone and on DNA (59), and the conversion from rings to filaments is probably essential for the proper function of Dmc1.
[ "22", "45", "48", "56", "58", "59", "43" ]
156
9,675
1
false
However, Dmc1 forms octameric rings alone and on DNA, and the conversion from rings to filaments is probably essential for the proper function of Dmc1.
[ "59" ]
However, Dmc1 forms octameric rings alone and on DNA, and the conversion from rings to filaments is probably essential for the proper function of Dmc1.
true
true
true
true
true
1,540
1
DISCUSSION
1
43
[ "b22", "b45", "b48", "b56", "b58", "b59", "b43" ]
16,945,962
pmid-156361|pmid-6325943|pmid-1581960|pmid-8602360|pmid-8066464|pmid-15164066|pmid-12456786|pmid-12912992|pmid-15164066|pmid-15917243|pmid-15235592|pmid-11459986|pmid-15899844|pmid-10485886|pmid-15125839
A recent study indicated that ATP binding may act as a trigger in the conversion of the Dmc1 octameric ring form to the helical filament form (43).
[ "22", "45", "48", "56", "58", "59", "43" ]
147
9,676
1
false
A recent study indicated that ATP binding may act as a trigger in the conversion of the Dmc1 octameric ring form to the helical filament form.
[ "43" ]
A recent study indicated that ATP binding may act as a trigger in the conversion of the Dmc1 octameric ring form to the helical filament form.
true
true
true
true
true
1,540
1
DISCUSSION
1
22
[ "b22", "b45", "b48", "b56", "b58", "b59", "b43" ]
16,945,962
pmid-156361|pmid-6325943|pmid-1581960|pmid-8602360|pmid-8066464|pmid-15164066|pmid-12456786|pmid-12912992|pmid-15164066|pmid-15917243|pmid-15235592|pmid-11459986|pmid-15899844|pmid-10485886|pmid-15125839
We found that Rad54B bound to the isolated ATPase domain of Dmc1, and this interaction may assist in changing in the conformation of the Dmc1 monomer to favor the formation of the helical filament, thus stabilizing the complex.
[ "22", "45", "48", "56", "58", "59", "43" ]
227
9,677
0
false
We found that Rad54B bound to the isolated ATPase domain of Dmc1, and this interaction may assist in changing in the conformation of the Dmc1 monomer to favor the formation of the helical filament, thus stabilizing the complex.
[]
We found that Rad54B bound to the isolated ATPase domain of Dmc1, and this interaction may assist in changing in the conformation of the Dmc1 monomer to favor the formation of the helical filament, thus stabilizing the complex.
true
true
true
true
true
1,540
1
DISCUSSION
1
22
[ "b22", "b45", "b48", "b56", "b58", "b59", "b43" ]
16,945,962
pmid-156361|pmid-6325943|pmid-1581960|pmid-8602360|pmid-8066464|pmid-15164066|pmid-12456786|pmid-12912992|pmid-15164066|pmid-15917243|pmid-15235592|pmid-11459986|pmid-15899844|pmid-10485886|pmid-15125839
Based on these possibilities, we propose the following model (Figure 6), which explains the mechanism of DNA strand exchange promoted by Rad54B and Dmc1.
[ "22", "45", "48", "56", "58", "59", "43" ]
153
9,678
0
false
Based on these possibilities, we propose the following model (Figure 6), which explains the mechanism of DNA strand exchange promoted by Rad54B and Dmc1.
[]
Based on these possibilities, we propose the following model (Figure 6), which explains the mechanism of DNA strand exchange promoted by Rad54B and Dmc1.
true
true
true
true
true
1,540
1
DISCUSSION
1
22
[ "b22", "b45", "b48", "b56", "b58", "b59", "b43" ]
16,945,962
pmid-156361|pmid-6325943|pmid-1581960|pmid-8602360|pmid-8066464|pmid-15164066|pmid-12456786|pmid-12912992|pmid-15164066|pmid-15917243|pmid-15235592|pmid-11459986|pmid-15899844|pmid-10485886|pmid-15125839
First, Rad54B associates with the terminus of the stacked rings, and binds to the ATPase domain of Dmc1.
[ "22", "45", "48", "56", "58", "59", "43" ]
104
9,679
0
false
First, Rad54B associates with the terminus of the stacked rings, and binds to the ATPase domain of Dmc1.
[]
First, Rad54B associates with the terminus of the stacked rings, and binds to the ATPase domain of Dmc1.
true
true
true
true
true
1,540
1
DISCUSSION
1
22
[ "b22", "b45", "b48", "b56", "b58", "b59", "b43" ]
16,945,962
pmid-156361|pmid-6325943|pmid-1581960|pmid-8602360|pmid-8066464|pmid-15164066|pmid-12456786|pmid-12912992|pmid-15164066|pmid-15917243|pmid-15235592|pmid-11459986|pmid-15899844|pmid-10485886|pmid-15125839
This process may catalytically prevent the Dmc1–ssDNA filament from disassembling or promote the conversion of the Dmc1–DNA complex from stacked octameric rings to helical filaments.
[ "22", "45", "48", "56", "58", "59", "43" ]
182
9,680
0
false
This process may catalytically prevent the Dmc1–ssDNA filament from disassembling or promote the conversion of the Dmc1–DNA complex from stacked octameric rings to helical filaments.
[]
This process may catalytically prevent the Dmc1–ssDNA filament from disassembling or promote the conversion of the Dmc1–DNA complex from stacked octameric rings to helical filaments.
true
true
true
true
true
1,540
1
DISCUSSION
1
22
[ "b22", "b45", "b48", "b56", "b58", "b59", "b43" ]
16,945,962
pmid-156361|pmid-6325943|pmid-1581960|pmid-8602360|pmid-8066464|pmid-15164066|pmid-12456786|pmid-12912992|pmid-15164066|pmid-15917243|pmid-15235592|pmid-11459986|pmid-15899844|pmid-10485886|pmid-15125839
The Dmc1–ssDNA nucleoprotein filament, which is probably the active form for the strand exchange reaction, then invades the homologous duplex DNA, forming a heteroduplex DNA intermediate.
[ "22", "45", "48", "56", "58", "59", "43" ]
187
9,681
0
false
The Dmc1–ssDNA nucleoprotein filament, which is probably the active form for the strand exchange reaction, then invades the homologous duplex DNA, forming a heteroduplex DNA intermediate.
[]
The Dmc1–ssDNA nucleoprotein filament, which is probably the active form for the strand exchange reaction, then invades the homologous duplex DNA, forming a heteroduplex DNA intermediate.
true
true
true
true
true
1,540
2
DISCUSSION
1
55
[ "b55", "b60" ]
16,945,962
pmid-7651832|pmid-15105430|pmid-9108475|pmid-10209103|pmid-11030336|pmid-9590697|pmid-12453424|pmid-16862129|pmid-16818238
Recent studies have shown that Rad54 has a potent translocase activity and stimulates the branch migration activity of Rad51 (55,60).
[ "55", "60" ]
133
9,682
0
false
Recent studies have shown that Rad54 has a potent translocase activity and stimulates the branch migration activity of Rad51.
[ "55,60" ]
Recent studies have shown that Rad54 has a potent translocase activity and stimulates the branch migration activity of Rad51.
true
true
true
true
true
1,541
2
DISCUSSION
1
55
[ "b55", "b60" ]
16,945,962
pmid-7651832|pmid-15105430|pmid-9108475|pmid-10209103|pmid-11030336|pmid-9590697|pmid-12453424|pmid-16862129|pmid-16818238
These activities suggest that Rad54 is involved in the post-synaptic phase of recombination.
[ "55", "60" ]
92
9,683
0
false
These activities suggest that Rad54 is involved in the post-synaptic phase of recombination.
[]
These activities suggest that Rad54 is involved in the post-synaptic phase of recombination.
true
true
true
true
true
1,541
2
DISCUSSION
1
55
[ "b55", "b60" ]
16,945,962
pmid-7651832|pmid-15105430|pmid-9108475|pmid-10209103|pmid-11030336|pmid-9590697|pmid-12453424|pmid-16862129|pmid-16818238
Although the previous and present Rad54B results have suggested its involvement in the presynaptic phase of recombination, it is easy to imagine that Rad54B functions in the post-synaptic phase of recombination, such as Rad54.
[ "55", "60" ]
226
9,684
0
false
Although the previous and present Rad54B results have suggested its involvement in the presynaptic phase of recombination, it is easy to imagine that Rad54B functions in the post-synaptic phase of recombination, such as Rad54.
[]
Although the previous and present Rad54B results have suggested its involvement in the presynaptic phase of recombination, it is easy to imagine that Rad54B functions in the post-synaptic phase of recombination, such as Rad54.
true
true
true
true
true
1,541
2
DISCUSSION
1
55
[ "b55", "b60" ]
16,945,962
pmid-7651832|pmid-15105430|pmid-9108475|pmid-10209103|pmid-11030336|pmid-9590697|pmid-12453424|pmid-16862129|pmid-16818238
Further analyses of the effects of Rad54B on Dmc1 complexed with various DNA structures representing recombination intermediates may provide clues toward understanding the precise mechanism of the Rad54B-stimulated homologous recombination.
[ "55", "60" ]
240
9,685
0
false
Further analyses of the effects of Rad54B on Dmc1 complexed with various DNA structures representing recombination intermediates may provide clues toward understanding the precise mechanism of the Rad54B-stimulated homologous recombination.
[]
Further analyses of the effects of Rad54B on Dmc1 complexed with various DNA structures representing recombination intermediates may provide clues toward understanding the precise mechanism of the Rad54B-stimulated homologous recombination.
true
true
true
true
true
1,541
0
INTRODUCTION
1
1
[ "B1", "B2", "B3 B4 B5 B6", "B7", "B8", "B9", "B6" ]
17,526,518
pmid-12483510|pmid-15568983|pmid-7819187|pmid-10074426|pmid-10499592|pmid-11554300|pmid-9016624|pmid-10393198|pmid-15084312|pmid-11554300|pmid-15084312|pmid-15084312
Uracil (U) arises in DNA either by erroneous incorporation of dUMP opposite adenine (A) during DNA synthesis or by deamination of cytosine (C), which generates a U mispaired with guanine (G).
[ "1", "2", "3–6", "7", "8", "9", "6" ]
191
9,686
0
false
Uracil (U) arises in DNA either by erroneous incorporation of dUMP opposite adenine (A) during DNA synthesis or by deamination of cytosine (C), which generates a U mispaired with guanine (G).
[]
Uracil (U) arises in DNA either by erroneous incorporation of dUMP opposite adenine (A) during DNA synthesis or by deamination of cytosine (C), which generates a U mispaired with guanine (G).
true
true
true
true
true
1,542
0
INTRODUCTION
1
1
[ "B1", "B2", "B3 B4 B5 B6", "B7", "B8", "B9", "B6" ]
17,526,518
pmid-12483510|pmid-15568983|pmid-7819187|pmid-10074426|pmid-10499592|pmid-11554300|pmid-9016624|pmid-10393198|pmid-15084312|pmid-11554300|pmid-15084312|pmid-15084312
To what extent A•U base pairs affect the function of DNA is unclear; G•U mispairs, however, give rise to C → T mutations if a DNA polymerase replicates across.
[ "1", "2", "3–6", "7", "8", "9", "6" ]
159
9,687
0
false
To what extent A•U base pairs affect the function of DNA is unclear; G•U mispairs, however, give rise to C → T mutations if a DNA polymerase replicates across.
[]
To what extent A•U base pairs affect the function of DNA is unclear; G•U mispairs, however, give rise to C → T mutations if a DNA polymerase replicates across.
true
true
true
true
true
1,542
0
INTRODUCTION
1
1
[ "B1", "B2", "B3 B4 B5 B6", "B7", "B8", "B9", "B6" ]
17,526,518
pmid-12483510|pmid-15568983|pmid-7819187|pmid-10074426|pmid-10499592|pmid-11554300|pmid-9016624|pmid-10393198|pmid-15084312|pmid-11554300|pmid-15084312|pmid-15084312
Uracil DNA glycosylases (UDGs) (1) have evolved to eliminate this irregular base from the DNA.
[ "1", "2", "3–6", "7", "8", "9", "6" ]
94
9,688
1
false
Uracil DNA glycosylases (UDGs) have evolved to eliminate this irregular base from the DNA.
[ "1" ]
Uracil DNA glycosylases (UDGs) have evolved to eliminate this irregular base from the DNA.
true
true
true
true
true
1,542
0
INTRODUCTION
1
2
[ "B1", "B2", "B3 B4 B5 B6", "B7", "B8", "B9", "B6" ]
17,526,518
pmid-12483510|pmid-15568983|pmid-7819187|pmid-10074426|pmid-10499592|pmid-11554300|pmid-9016624|pmid-10393198|pmid-15084312|pmid-11554300|pmid-15084312|pmid-15084312
They hydrolyze the N-glycosidic bond linking the U to the sugar moiety of the nucleotide, thereby initiating a base excision repair (BER) process (2) that restores the canonical Watson–Crick base pair.
[ "1", "2", "3–6", "7", "8", "9", "6" ]
201
9,689
1
false
They hydrolyze the N-glycosidic bond linking the U to the sugar moiety of the nucleotide, thereby initiating a base excision repair (BER) process that restores the canonical Watson–Crick base pair.
[ "2" ]
They hydrolyze the N-glycosidic bond linking the U to the sugar moiety of the nucleotide, thereby initiating a base excision repair (BER) process that restores the canonical Watson–Crick base pair.
true
true
true
true
true
1,542
0
INTRODUCTION
1
3–6
[ "B1", "B2", "B3 B4 B5 B6", "B7", "B8", "B9", "B6" ]
17,526,518
pmid-12483510|pmid-15568983|pmid-7819187|pmid-10074426|pmid-10499592|pmid-11554300|pmid-9016624|pmid-10393198|pmid-15084312|pmid-11554300|pmid-15084312|pmid-15084312
Mammalian cells posses at least four enzymes with UDG activity, namely UNG, TDG, SMUG1 and MBD4 (3–6), and the successful co-evolution of these enzymes implies that each of them fulfils specific non-redundant biological functions.
[ "1", "2", "3–6", "7", "8", "9", "6" ]
230
9,690
1
false
Mammalian cells posses at least four enzymes with UDG activity, namely UNG, TDG, SMUG1 and MBD4, and the successful co-evolution of these enzymes implies that each of them fulfils specific non-redundant biological functions.
[ "3–6" ]
Mammalian cells posses at least four enzymes with UDG activity, namely UNG, TDG, SMUG1 and MBD4, and the successful co-evolution of these enzymes implies that each of them fulfils specific non-redundant biological functions.
true
true
true
true
true
1,542
0
INTRODUCTION
1
1
[ "B1", "B2", "B3 B4 B5 B6", "B7", "B8", "B9", "B6" ]
17,526,518
pmid-12483510|pmid-15568983|pmid-7819187|pmid-10074426|pmid-10499592|pmid-11554300|pmid-9016624|pmid-10393198|pmid-15084312|pmid-11554300|pmid-15084312|pmid-15084312
The question then is how cells achieve the functional separation of these enzymatically redundant activities.
[ "1", "2", "3–6", "7", "8", "9", "6" ]
109
9,691
0
false
The question then is how cells achieve the functional separation of these enzymatically redundant activities.
[]
The question then is how cells achieve the functional separation of these enzymatically redundant activities.
true
true
true
true
true
1,542
0
INTRODUCTION
1
1
[ "B1", "B2", "B3 B4 B5 B6", "B7", "B8", "B9", "B6" ]
17,526,518
pmid-12483510|pmid-15568983|pmid-7819187|pmid-10074426|pmid-10499592|pmid-11554300|pmid-9016624|pmid-10393198|pmid-15084312|pmid-11554300|pmid-15084312|pmid-15084312
One way would be to control their spatial and temporal distribution as exemplified by the UNG proteins.
[ "1", "2", "3–6", "7", "8", "9", "6" ]
103
9,692
0
false
One way would be to control their spatial and temporal distribution as exemplified by the UNG proteins.
[]
One way would be to control their spatial and temporal distribution as exemplified by the UNG proteins.
true
true
true
true
true
1,542
0
INTRODUCTION
1
7
[ "B1", "B2", "B3 B4 B5 B6", "B7", "B8", "B9", "B6" ]
17,526,518
pmid-12483510|pmid-15568983|pmid-7819187|pmid-10074426|pmid-10499592|pmid-11554300|pmid-9016624|pmid-10393198|pmid-15084312|pmid-11554300|pmid-15084312|pmid-15084312
Differential expression of the human UNG gene from two alternative promoters generates two isoforms, UNG1 and UNG2, that localize to mitochondria and to nuclei, respectively (7).
[ "1", "2", "3–6", "7", "8", "9", "6" ]
178
9,693
1
false
Differential expression of the human UNG gene from two alternative promoters generates two isoforms, UNG1 and UNG2, that localize to mitochondria and to nuclei, respectively.
[ "7" ]
Differential expression of the human UNG gene from two alternative promoters generates two isoforms, UNG1 and UNG2, that localize to mitochondria and to nuclei, respectively.
true
true
true
true
true
1,542
0
INTRODUCTION
1
1
[ "B1", "B2", "B3 B4 B5 B6", "B7", "B8", "B9", "B6" ]
17,526,518
pmid-12483510|pmid-15568983|pmid-7819187|pmid-10074426|pmid-10499592|pmid-11554300|pmid-9016624|pmid-10393198|pmid-15084312|pmid-11554300|pmid-15084312|pmid-15084312
Moreover, UNG2 expression is up-regulated during S-phase of the cell cycle where the protein associates with PCNA and RPA at replication foci, implicating a role for this UDG in the removal of misincorporated U during DNA replication (8,9).
[ "1", "2", "3–6", "7", "8", "9", "6" ]
240
9,694
0
false
Moreover, UNG2 expression is up-regulated during S-phase of the cell cycle where the protein associates with PCNA and RPA at replication foci, implicating a role for this UDG in the removal of misincorporated U during DNA replication.
[ "8,9" ]
Moreover, UNG2 expression is up-regulated during S-phase of the cell cycle where the protein associates with PCNA and RPA at replication foci, implicating a role for this UDG in the removal of misincorporated U during DNA replication.
true
true
true
true
true
1,542
0
INTRODUCTION
1
1
[ "B1", "B2", "B3 B4 B5 B6", "B7", "B8", "B9", "B6" ]
17,526,518
pmid-12483510|pmid-15568983|pmid-7819187|pmid-10074426|pmid-10499592|pmid-11554300|pmid-9016624|pmid-10393198|pmid-15084312|pmid-11554300|pmid-15084312|pmid-15084312
Whether similar forms of regulation apply to other UDGs and, thus, could provide a cellular mechanism for functional coordination of uracil repair is not known.
[ "1", "2", "3–6", "7", "8", "9", "6" ]
160
9,695
0
false
Whether similar forms of regulation apply to other UDGs and, thus, could provide a cellular mechanism for functional coordination of uracil repair is not known.
[]
Whether similar forms of regulation apply to other UDGs and, thus, could provide a cellular mechanism for functional coordination of uracil repair is not known.
true
true
true
true
true
1,542
0
INTRODUCTION
1
1
[ "B1", "B2", "B3 B4 B5 B6", "B7", "B8", "B9", "B6" ]
17,526,518
pmid-12483510|pmid-15568983|pmid-7819187|pmid-10074426|pmid-10499592|pmid-11554300|pmid-9016624|pmid-10393198|pmid-15084312|pmid-11554300|pmid-15084312|pmid-15084312
Here, we report that Thymine-DNA Glycosylase (TDG), a mismatch-specific UDG, underlies strict cell cycle regulation.
[ "1", "2", "3–6", "7", "8", "9", "6" ]
116
9,696
0
false
Here, we report that Thymine-DNA Glycosylase (TDG), a mismatch-specific UDG, underlies strict cell cycle regulation.
[]
Here, we report that Thymine-DNA Glycosylase (TDG), a mismatch-specific UDG, underlies strict cell cycle regulation.
true
true
true
true
true
1,542
0
INTRODUCTION
1
1
[ "B1", "B2", "B3 B4 B5 B6", "B7", "B8", "B9", "B6" ]
17,526,518
pmid-12483510|pmid-15568983|pmid-7819187|pmid-10074426|pmid-10499592|pmid-11554300|pmid-9016624|pmid-10393198|pmid-15084312|pmid-11554300|pmid-15084312|pmid-15084312
TDG has a comparably broad substrate spectrum including the deamination product of 5-methylcytosine, i.e.
[ "1", "2", "3–6", "7", "8", "9", "6" ]
105
9,697
0
false
TDG has a comparably broad substrate spectrum including the deamination product of 5-methylcytosine, i.e.
[]
TDG has a comparably broad substrate spectrum including the deamination product of 5-methylcytosine, i.e.
true
true
true
true
true
1,542
0
INTRODUCTION
1
6
[ "B1", "B2", "B3 B4 B5 B6", "B7", "B8", "B9", "B6" ]
17,526,518
pmid-12483510|pmid-15568983|pmid-7819187|pmid-10074426|pmid-10499592|pmid-11554300|pmid-9016624|pmid-10393198|pmid-15084312|pmid-11554300|pmid-15084312|pmid-15084312
a T mispaired with a G, but its most efficiently processed physiological substrate is a G•U mispair (6).
[ "1", "2", "3–6", "7", "8", "9", "6" ]
104
9,698
1
false
a T mispaired with a G, but its most efficiently processed physiological substrate is a G•U mispair.
[ "6" ]
a T mispaired with a G, but its most efficiently processed physiological substrate is a G•U mispair.
false
true
true
true
false
1,542
0
INTRODUCTION
1
1
[ "B1", "B2", "B3 B4 B5 B6", "B7", "B8", "B9", "B6" ]
17,526,518
pmid-12483510|pmid-15568983|pmid-7819187|pmid-10074426|pmid-10499592|pmid-11554300|pmid-9016624|pmid-10393198|pmid-15084312|pmid-11554300|pmid-15084312|pmid-15084312
Cells entering S-phase eliminate this glycosylase through the ubiquitin–proteasome pathway and maintain a TDG free state until DNA replication is completed.
[ "1", "2", "3–6", "7", "8", "9", "6" ]
156
9,699
0
false
Cells entering S-phase eliminate this glycosylase through the ubiquitin–proteasome pathway and maintain a TDG free state until DNA replication is completed.
[]
Cells entering S-phase eliminate this glycosylase through the ubiquitin–proteasome pathway and maintain a TDG free state until DNA replication is completed.
true
true
true
true
true
1,542