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
2
INTRODUCTION
1
11
[ "b11" ]
17,065,465
NA
The Influenza Virus Database (IVDB) contains both BIG's data and published IV sequences after expert curation to ensure a high standard of accuracy and completeness.
[ "11" ]
165
4,100
0
false
The Influenza Virus Database (IVDB) contains both BIG's data and published IV sequences after expert curation to ensure a high standard of accuracy and completeness.
[]
The Influenza Virus Database (IVDB) contains both BIG's data and published IV sequences after expert curation to ensure a high standard of accuracy and completeness.
true
true
true
true
true
697
2
INTRODUCTION
1
11
[ "b11" ]
17,065,465
NA
We have further developed tools and viewers to analyze and browse our data that include information concerning genomes, genes, polymorphisms, and phylogenetic relationships.
[ "11" ]
173
4,101
0
false
We have further developed tools and viewers to analyze and browse our data that include information concerning genomes, genes, polymorphisms, and phylogenetic relationships.
[]
We have further developed tools and viewers to analyze and browse our data that include information concerning genomes, genes, polymorphisms, and phylogenetic relationships.
true
true
true
true
true
697
2
INTRODUCTION
1
11
[ "b11" ]
17,065,465
NA
IVDB aims to be a powerful information resource and an analysis workbench for scientists working on IV genetics, evolution, diagnostics, vaccine development and drug design.
[ "11" ]
173
4,102
0
false
IVDB aims to be a powerful information resource and an analysis workbench for scientists working on IV genetics, evolution, diagnostics, vaccine development and drug design.
[]
IVDB aims to be a powerful information resource and an analysis workbench for scientists working on IV genetics, evolution, diagnostics, vaccine development and drug design.
true
true
true
true
true
697
0
INTRODUCTION
1
1
[ "b1", "b2", "b3", "b4", "b5", "b6", "b7" ]
16,998,185
pmid-9759486|pmid-1377982|pmid-1623519|pmid-8602511|pmid-7515008|pmid-14729943|pmid-11207361
The ribonucleoprotein enzyme RNase P (ribonuclease P) is an endonuclease that processes tRNA precursors to generate the mature 5′ end.
[ "1", "2", "3", "4", "5", "6", "7" ]
134
4,103
0
false
The ribonucleoprotein enzyme RNase P (ribonuclease P) is an endonuclease that processes tRNA precursors to generate the mature 5′ end.
[]
The ribonucleoprotein enzyme RNase P (ribonuclease P) is an endonuclease that processes tRNA precursors to generate the mature 5′ end.
true
true
true
true
true
698
0
INTRODUCTION
1
1
[ "b1", "b2", "b3", "b4", "b5", "b6", "b7" ]
16,998,185
pmid-9759486|pmid-1377982|pmid-1623519|pmid-8602511|pmid-7515008|pmid-14729943|pmid-11207361
It is a nearly ubiquitous enzyme present in Archaea, Bacteria and Eukarya as well as in mitochondria and chloroplasts (1).
[ "1", "2", "3", "4", "5", "6", "7" ]
122
4,104
1
false
It is a nearly ubiquitous enzyme present in Archaea, Bacteria and Eukarya as well as in mitochondria and chloroplasts.
[ "1" ]
It is a nearly ubiquitous enzyme present in Archaea, Bacteria and Eukarya as well as in mitochondria and chloroplasts.
true
true
true
true
true
698
0
INTRODUCTION
1
1
[ "b1", "b2", "b3", "b4", "b5", "b6", "b7" ]
16,998,185
pmid-9759486|pmid-1377982|pmid-1623519|pmid-8602511|pmid-7515008|pmid-14729943|pmid-11207361
A structurally and evolutionary related RNP, the RNase MRP (2,3), is found only in Eukarya.
[ "1", "2", "3", "4", "5", "6", "7" ]
91
4,105
0
false
A structurally and evolutionary related RNP, the RNase MRP, is found only in Eukarya.
[ "2,3" ]
A structurally and evolutionary related RNP, the RNase MRP, is found only in Eukarya.
true
true
true
true
true
698
0
INTRODUCTION
1
1
[ "b1", "b2", "b3", "b4", "b5", "b6", "b7" ]
16,998,185
pmid-9759486|pmid-1377982|pmid-1623519|pmid-8602511|pmid-7515008|pmid-14729943|pmid-11207361
RNase MRP processes ribosomal RNA precursors at the A3 site allowing formation of the 5.8S pre-rRNA (4,5).
[ "1", "2", "3", "4", "5", "6", "7" ]
106
4,106
0
false
RNase MRP processes ribosomal RNA precursors at the A3 site allowing formation of the 5.8S pre-rRNA.
[ "4,5" ]
RNase MRP processes ribosomal RNA precursors at the A3 site allowing formation of the 5.8S pre-rRNA.
true
true
true
true
true
698
0
INTRODUCTION
1
6
[ "b1", "b2", "b3", "b4", "b5", "b6", "b7" ]
16,998,185
pmid-9759486|pmid-1377982|pmid-1623519|pmid-8602511|pmid-7515008|pmid-14729943|pmid-11207361
RNase MRP is also known to have a role in the degradation of specific mRNAs involved in cell-cycle regulation (6) and it is affected in the autosomal recessive disease cartilage hair hypoplasia (7).
[ "1", "2", "3", "4", "5", "6", "7" ]
198
4,107
1
false
RNase MRP is also known to have a role in the degradation of specific mRNAs involved in cell-cycle regulation and it is affected in the autosomal recessive disease cartilage hair hypoplasia.
[ "6", "7" ]
RNase MRP is also known to have a role in the degradation of specific mRNAs involved in cell-cycle regulation and it is affected in the autosomal recessive disease cartilage hair hypoplasia.
true
true
true
true
true
698
1
INTRODUCTION
1
8
[ "b8", "b9", "b10", "b11", "b12" ]
16,998,185
pmid-16595295|pmid-1696176|pmid-16087735|pmid-9620854|pmid-8876159
The RNases P and MRP both have an RNA molecule and one or several protein subunits (8).
[ "8", "9", "10", "11", "12" ]
87
4,108
1
false
The RNases P and MRP both have an RNA molecule and one or several protein subunits.
[ "8" ]
The RNases P and MRP both have an RNA molecule and one or several protein subunits.
true
true
true
true
true
699
1
INTRODUCTION
1
8
[ "b8", "b9", "b10", "b11", "b12" ]
16,998,185
pmid-16595295|pmid-1696176|pmid-16087735|pmid-9620854|pmid-8876159
The RNA molecules of P and MRP are related with respect to sequence and structure (9,10).
[ "8", "9", "10", "11", "12" ]
89
4,109
0
false
The RNA molecules of P and MRP are related with respect to sequence and structure.
[ "9,10" ]
The RNA molecules of P and MRP are related with respect to sequence and structure.
true
true
true
true
true
699
1
INTRODUCTION
1
8
[ "b8", "b9", "b10", "b11", "b12" ]
16,998,185
pmid-16595295|pmid-1696176|pmid-16087735|pmid-9620854|pmid-8876159
The bacterial RNase P has a single protein subunit, but archaeal RNase P and eukaryotic nuclear RNase P/MRP enzymes contain multiple protein subunits.
[ "8", "9", "10", "11", "12" ]
150
4,110
0
false
The bacterial RNase P has a single protein subunit, but archaeal RNase P and eukaryotic nuclear RNase P/MRP enzymes contain multiple protein subunits.
[]
The bacterial RNase P has a single protein subunit, but archaeal RNase P and eukaryotic nuclear RNase P/MRP enzymes contain multiple protein subunits.
true
true
true
true
true
699
1
INTRODUCTION
1
8
[ "b8", "b9", "b10", "b11", "b12" ]
16,998,185
pmid-16595295|pmid-1696176|pmid-16087735|pmid-9620854|pmid-8876159
In eukaryotes most of the protein subunits are shared between P and MRP (11,12).
[ "8", "9", "10", "11", "12" ]
80
4,111
0
false
In eukaryotes most of the protein subunits are shared between P and MRP.
[ "11,12" ]
In eukaryotes most of the protein subunits are shared between P and MRP.
true
true
true
true
true
699
2
INTRODUCTION
1
13
[ "b13", "b14", "b15" ]
16,998,185
pmid-6197186|pmid-10393902|pmid-7916700
The RNA molecule in the bacterial RNase P can function as a ribozyme in vitro, although the cleavage rate of pre-tRNA is enhanced 20-fold by the protein moiety (13).
[ "13", "14", "15" ]
165
4,112
1
false
The RNA molecule in the bacterial RNase P can function as a ribozyme in vitro, although the cleavage rate of pre-tRNA is enhanced 20-fold by the protein moiety.
[ "13" ]
The RNA molecule in the bacterial RNase P can function as a ribozyme in vitro, although the cleavage rate of pre-tRNA is enhanced 20-fold by the protein moiety.
true
true
true
true
true
700
2
INTRODUCTION
1
14
[ "b13", "b14", "b15" ]
16,998,185
pmid-6197186|pmid-10393902|pmid-7916700
While some archaeal RNase P RNAs show enzymatic activity under high salt conditions (14), the catalytic activity of the eukaryotic RNA subunit of RNase P requires the presence of protein subunits (15).
[ "13", "14", "15" ]
201
4,113
1
false
While some archaeal RNase P RNAs show enzymatic activity under high salt conditions, the catalytic activity of the eukaryotic RNA subunit of RNase P requires the presence of protein subunits.
[ "14", "15" ]
While some archaeal RNase P RNAs show enzymatic activity under high salt conditions, the catalytic activity of the eukaryotic RNA subunit of RNase P requires the presence of protein subunits.
true
true
true
true
true
700
3
INTRODUCTION
1
16
[ "b16", "b11", "b17", "b18", "b19", "b20", "b21", "b22", "b23", "b24" ]
16,998,185
pmid-11880623|pmid-9620854|pmid-7958920|pmid-15637077|pmid-11158571|pmid-15096576|pmid-16723659|pmid-12045094|pmid-12003490|pmid-14550630
At least nine protein subunits are part of the nuclear RNase P of Saccharomyces cerevisiae; Pop1, Pop3, Pop4, Pop5, Pop6, Pop7, Pop8, Rpr2 and Rpp1 (16).
[ "16", "11", "17", "18", "19", "20", "21", "22", "23", "24" ]
153
4,114
1
false
At least nine protein subunits are part of the nuclear RNase P of Saccharomyces cerevisiae; Pop1, Pop3, Pop4, Pop5, Pop6, Pop7, Pop8, Rpr2 and Rpp1.
[ "16" ]
At least nine protein subunits are part of the nuclear RNase P of Saccharomyces cerevisiae; Pop1, Pop3, Pop4, Pop5, Pop6, Pop7, Pop8, Rpr2 and Rpp1.
true
true
true
true
true
701
3
INTRODUCTION
1
11
[ "b16", "b11", "b17", "b18", "b19", "b20", "b21", "b22", "b23", "b24" ]
16,998,185
pmid-11880623|pmid-9620854|pmid-7958920|pmid-15637077|pmid-11158571|pmid-15096576|pmid-16723659|pmid-12045094|pmid-12003490|pmid-14550630
Many of these subunits seem to be present also in the RNase MRP, with the exception of Rpr2 (Rpp21) which is unique to RNase P (11).
[ "16", "11", "17", "18", "19", "20", "21", "22", "23", "24" ]
132
4,115
1
false
Many of these subunits seem to be present also in the RNase MRP, with the exception of Rpr2 which is unique to RNase P.
[ "Rpp21", "11" ]
Many of these subunits seem to be present also in the RNase MRP, with the exception of Rpr2 which is unique to RNase P.
true
true
true
true
true
701
3
INTRODUCTION
1
17
[ "b16", "b11", "b17", "b18", "b19", "b20", "b21", "b22", "b23", "b24" ]
16,998,185
pmid-11880623|pmid-9620854|pmid-7958920|pmid-15637077|pmid-11158571|pmid-15096576|pmid-16723659|pmid-12045094|pmid-12003490|pmid-14550630
MRP also contains Snm1 (17) and Rmp1 (18).
[ "16", "11", "17", "18", "19", "20", "21", "22", "23", "24" ]
42
4,116
1
false
MRP also contains Snm1 and Rmp1.
[ "17", "18" ]
MRP also contains Snm1 and Rmp1.
true
true
true
true
true
701
3
INTRODUCTION
1
21
[ "b16", "b11", "b17", "b18", "b19", "b20", "b21", "b22", "b23", "b24" ]
16,998,185
pmid-11880623|pmid-9620854|pmid-7958920|pmid-15637077|pmid-11158571|pmid-15096576|pmid-16723659|pmid-12045094|pmid-12003490|pmid-14550630
Human nuclear RNase P and MRP appears to contain at least 10 protein subunits, Rpp14, Rpp20, Rpp21, Rpp25, Rpp29, Rpp30, Rpp38, Rpp40, hPop1 and hPop5 (19,20), although there is recent evidence that not all of these subunits are shared between P and MRP (21).
[ "16", "11", "17", "18", "19", "20", "21", "22", "23", "24" ]
259
4,117
1
false
Human nuclear RNase P and MRP appears to contain at least 10 protein subunits, Rpp14, Rpp20, Rpp21, Rpp25, Rpp29, Rpp30, Rpp38, Rpp40, hPop1 and hPop5, although there is recent evidence that not all of these subunits are shared between P and MRP.
[ "19,20", "21" ]
Human nuclear RNase P and MRP appears to contain at least 10 protein subunits, Rpp14, Rpp20, Rpp21, Rpp25, Rpp29, Rpp30, Rpp38, Rpp40, hPop1 and hPop5, although there is recent evidence that not all of these subunits are shared between P and MRP.
true
true
true
true
true
701
3
INTRODUCTION
1
22
[ "b16", "b11", "b17", "b18", "b19", "b20", "b21", "b22", "b23", "b24" ]
16,998,185
pmid-11880623|pmid-9620854|pmid-7958920|pmid-15637077|pmid-11158571|pmid-15096576|pmid-16723659|pmid-12045094|pmid-12003490|pmid-14550630
At least six of the P/MRP subunits appear to be homologous to the subunits identified in S.cerevisiae (22).
[ "16", "11", "17", "18", "19", "20", "21", "22", "23", "24" ]
107
4,118
1
false
At least six of the P/MRP subunits appear to be homologous to the subunits identified in S.cerevisiae.
[ "22" ]
At least six of the P/MRP subunits appear to be homologous to the subunits identified in S.cerevisiae.
true
true
true
true
true
701
3
INTRODUCTION
1
16
[ "b16", "b11", "b17", "b18", "b19", "b20", "b21", "b22", "b23", "b24" ]
16,998,185
pmid-11880623|pmid-9620854|pmid-7958920|pmid-15637077|pmid-11158571|pmid-15096576|pmid-16723659|pmid-12045094|pmid-12003490|pmid-14550630
Comparative studies show that archaeal RNase P has at least four protein subunits homologous to eukaryotic RNase P/MRP proteins (23,24).
[ "16", "11", "17", "18", "19", "20", "21", "22", "23", "24" ]
136
4,119
0
false
Comparative studies show that archaeal RNase P has at least four protein subunits homologous to eukaryotic RNase P/MRP proteins.
[ "23,24" ]
Comparative studies show that archaeal RNase P has at least four protein subunits homologous to eukaryotic RNase P/MRP proteins.
true
true
true
true
true
701
4
INTRODUCTION
1
16
[ "b16", "b19", "b20", "b25", "b27", "b28", "b20", "b29", "b16" ]
16,998,185
pmid-11880623|pmid-11158571|pmid-15096576|pmid-15973057|pmid-15810434|pmid-11455963|pmid-15096576|pmid-10199568|pmid-11880623
Models for the protein–protein and RNA–protein interactions in eukaryal RNases P and MRP have been proposed for human and yeast (16,19,20).
[ "16", "19", "20", "25", "27", "28", "20", "29", "16" ]
139
4,120
0
false
Models for the protein–protein and RNA–protein interactions in eukaryal RNases P and MRP have been proposed for human and yeast.
[ "16,19,20" ]
Models for the protein–protein and RNA–protein interactions in eukaryal RNases P and MRP have been proposed for human and yeast.
true
true
true
true
true
702
4
INTRODUCTION
1
16
[ "b16", "b19", "b20", "b25", "b27", "b28", "b20", "b29", "b16" ]
16,998,185
pmid-11880623|pmid-11158571|pmid-15096576|pmid-15973057|pmid-15810434|pmid-11455963|pmid-15096576|pmid-10199568|pmid-11880623
Many of these interactions have also been found in Archaea (25–27).
[ "16", "19", "20", "25", "27", "28", "20", "29", "16" ]
67
4,121
0
false
Many of these interactions have also been found in Archaea.
[ "25–27" ]
Many of these interactions have also been found in Archaea.
true
true
true
true
true
702
4
INTRODUCTION
1
28
[ "b16", "b19", "b20", "b25", "b27", "b28", "b20", "b29", "b16" ]
16,998,185
pmid-11880623|pmid-11158571|pmid-15096576|pmid-15973057|pmid-15810434|pmid-11455963|pmid-15096576|pmid-10199568|pmid-11880623
In the human RNase P the RNA molecule has been shown to interact with Rpp29, Rpp30, Rpp21 and Rpp38 (28).
[ "16", "19", "20", "25", "27", "28", "20", "29", "16" ]
105
4,122
1
false
In the human RNase P the RNA molecule has been shown to interact with Rpp29, Rpp30, Rpp21 and Rpp38.
[ "28" ]
In the human RNase P the RNA molecule has been shown to interact with Rpp29, Rpp30, Rpp21 and Rpp38.
true
true
true
true
true
702
4
INTRODUCTION
1
16
[ "b16", "b19", "b20", "b25", "b27", "b28", "b20", "b29", "b16" ]
16,998,185
pmid-11880623|pmid-11158571|pmid-15096576|pmid-15973057|pmid-15810434|pmid-11455963|pmid-15096576|pmid-10199568|pmid-11880623
The RNA molecule in the human RNase MRP has been shown to interact with the protein subunits Pop1, Rpp29, Rpp20, Rpp25 and Rpp38 (20,29) and for the yeast MRP there is evidence that RNA interacts with the protein subunits Pop1 and Pop4 (16).
[ "16", "19", "20", "25", "27", "28", "20", "29", "16" ]
241
4,123
1
false
The RNA molecule in the human RNase MRP has been shown to interact with the protein subunits Pop1, Rpp29, Rpp20, Rpp25 and Rpp38 and for the yeast MRP there is evidence that RNA interacts with the protein subunits Pop1 and Pop4.
[ "20,29", "16" ]
The RNA molecule in the human RNase MRP has been shown to interact with the protein subunits Pop1, Rpp29, Rpp20, Rpp25 and Rpp38 and for the yeast MRP there is evidence that RNA interacts with the protein subunits Pop1 and Pop4.
true
true
true
true
true
702
5
INTRODUCTION
1
10
[ "b10", "b10", "b30", "b24" ]
16,998,185
pmid-16087735|pmid-16087735|pmid-16540690|pmid-14550630
We have recently carried out an inventory of eukaryotic P and MRP RNAs and reported more than 100 novel sequences (10).
[ "10", "10", "30", "24" ]
119
4,124
1
false
We have recently carried out an inventory of eukaryotic P and MRP RNAs and reported more than 100 novel sequences.
[ "10" ]
We have recently carried out an inventory of eukaryotic P and MRP RNAs and reported more than 100 novel sequences.
true
true
true
true
true
703
5
INTRODUCTION
1
10
[ "b10", "b10", "b30", "b24" ]
16,998,185
pmid-16087735|pmid-16087735|pmid-16540690|pmid-14550630
Analysis of these sequences provided further evidence of a structural similarity between the two RNAs (10,30).
[ "10", "10", "30", "24" ]
110
4,125
0
false
Analysis of these sequences provided further evidence of a structural similarity between the two RNAs.
[ "10,30" ]
Analysis of these sequences provided further evidence of a structural similarity between the two RNAs.
true
true
true
true
true
703
5
INTRODUCTION
1
10
[ "b10", "b10", "b30", "b24" ]
16,998,185
pmid-16087735|pmid-16087735|pmid-16540690|pmid-14550630
The similarity between P and MRP RNA should be reflected in the set of protein subunits that are part of the RNP complexes.
[ "10", "10", "30", "24" ]
123
4,126
0
false
The similarity between P and MRP RNA should be reflected in the set of protein subunits that are part of the RNP complexes.
[]
The similarity between P and MRP RNA should be reflected in the set of protein subunits that are part of the RNP complexes.
true
true
true
true
true
703
5
INTRODUCTION
1
10
[ "b10", "b10", "b30", "b24" ]
16,998,185
pmid-16087735|pmid-16087735|pmid-16540690|pmid-14550630
In order to better understand the relationship between protein and RNA subunits, RNA–protein interactions and evolution of the protein subunits in general we have systematically analyzed gene and protein sequences related to the RNase P and MRP protein subunits in all eukaryotic species where genome and protein sequenc...
[ "10", "10", "30", "24" ]
337
4,127
0
false
In order to better understand the relationship between protein and RNA subunits, RNA–protein interactions and evolution of the protein subunits in general we have systematically analyzed gene and protein sequences related to the RNase P and MRP protein subunits in all eukaryotic species where genome and protein sequenc...
[]
In order to better understand the relationship between protein and RNA subunits, RNA–protein interactions and evolution of the protein subunits in general we have systematically analyzed gene and protein sequences related to the RNase P and MRP protein subunits in all eukaryotic species where genome and protein sequenc...
true
true
true
true
true
703
5
INTRODUCTION
1
24
[ "b10", "b10", "b30", "b24" ]
16,998,185
pmid-16087735|pmid-16087735|pmid-16540690|pmid-14550630
Using profile-based searches we have identified several homologues that were not previously reported (24).
[ "10", "10", "30", "24" ]
106
4,128
1
false
Using profile-based searches we have identified several homologues that were not previously reported.
[ "24" ]
Using profile-based searches we have identified several homologues that were not previously reported.
true
true
true
true
true
703
5
INTRODUCTION
1
10
[ "b10", "b10", "b30", "b24" ]
16,998,185
pmid-16087735|pmid-16087735|pmid-16540690|pmid-14550630
Through a phylogenetic analysis of the protein sequences we were able to improve on classification, clarify evolutionary relationships and imply novel protein family relationships.
[ "10", "10", "30", "24" ]
180
4,129
0
false
Through a phylogenetic analysis of the protein sequences we were able to improve on classification, clarify evolutionary relationships and imply novel protein family relationships.
[]
Through a phylogenetic analysis of the protein sequences we were able to improve on classification, clarify evolutionary relationships and imply novel protein family relationships.
true
true
true
true
true
703
0
INTRODUCTION
1
1
[ "b1", "b2", "b3", "b4", "b5", "b1", "b3", "b6", "b7", "b8", "b1", "b8", "b11" ]
17,003,056
pmid-11700277|pmid-10373362|pmid-16387650|pmid-12612652|pmid-15935756|pmid-11700277|pmid-16387650|pmid-14643434|pmid-16452972|pmid-1255724|pmid-11700277|pmid-1255724|pmid-12142537|pmid-11884624|pmid-11884624|pmid-12226657|pmid-14643434|pmid-12724426
The progression of DNA replication forks is frequently impaired by DNA damage, particularly if the blocking lesion is located on the leading-strand template (1).
[ "1", "2", "3", "4", "5", "1", "3", "6", "7", "8", "1", "8", "11" ]
161
4,130
1
false
The progression of DNA replication forks is frequently impaired by DNA damage, particularly if the blocking lesion is located on the leading-strand template.
[ "1" ]
The progression of DNA replication forks is frequently impaired by DNA damage, particularly if the blocking lesion is located on the leading-strand template.
true
true
true
true
true
704
0
INTRODUCTION
1
1
[ "b1", "b2", "b3", "b4", "b5", "b1", "b3", "b6", "b7", "b8", "b1", "b8", "b11" ]
17,003,056
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In this case, synthesis of the leading strand is halted at the lesion, while the lagging-strand synthesis continues beyond the lesion site, resulting in a fork structure with an extensive gap in the leading strand (2,3).
[ "1", "2", "3", "4", "5", "1", "3", "6", "7", "8", "1", "8", "11" ]
220
4,131
0
false
In this case, synthesis of the leading strand is halted at the lesion, while the lagging-strand synthesis continues beyond the lesion site, resulting in a fork structure with an extensive gap in the leading strand.
[ "2,3" ]
In this case, synthesis of the leading strand is halted at the lesion, while the lagging-strand synthesis continues beyond the lesion site, resulting in a fork structure with an extensive gap in the leading strand.
true
true
true
true
true
704
0
INTRODUCTION
1
1
[ "b1", "b2", "b3", "b4", "b5", "b1", "b3", "b6", "b7", "b8", "b1", "b8", "b11" ]
17,003,056
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Replication fork stalling poses a serious threat to genomic stability because it can trigger unscheduled DNA recombination events and hence lead to gross chromosomal re-arrangements that can induce tumorigenesis (4,5).
[ "1", "2", "3", "4", "5", "1", "3", "6", "7", "8", "1", "8", "11" ]
218
4,132
0
false
Replication fork stalling poses a serious threat to genomic stability because it can trigger unscheduled DNA recombination events and hence lead to gross chromosomal re-arrangements that can induce tumorigenesis.
[ "4,5" ]
Replication fork stalling poses a serious threat to genomic stability because it can trigger unscheduled DNA recombination events and hence lead to gross chromosomal re-arrangements that can induce tumorigenesis.
true
true
true
true
true
704
0
INTRODUCTION
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1
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To avoid these detrimental consequences of DNA replication arrest, cells can switch to different DNA damage bypass modes that permit replication across the lesion (1,3,6,7).
[ "1", "2", "3", "4", "5", "1", "3", "6", "7", "8", "1", "8", "11" ]
173
4,133
0
false
To avoid these detrimental consequences of DNA replication arrest, cells can switch to different DNA damage bypass modes that permit replication across the lesion.
[ "1,3,6,7" ]
To avoid these detrimental consequences of DNA replication arrest, cells can switch to different DNA damage bypass modes that permit replication across the lesion.
true
true
true
true
true
704
0
INTRODUCTION
1
8
[ "b1", "b2", "b3", "b4", "b5", "b1", "b3", "b6", "b7", "b8", "b1", "b8", "b11" ]
17,003,056
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One of these mechanisms is proposed to involve a transient template switch to the undamaged sister chromatid, allowing the replicative polymerase to synthesize the sequence complementary to the blocking lesion in an error-free manner (8).
[ "1", "2", "3", "4", "5", "1", "3", "6", "7", "8", "1", "8", "11" ]
238
4,134
1
false
One of these mechanisms is proposed to involve a transient template switch to the undamaged sister chromatid, allowing the replicative polymerase to synthesize the sequence complementary to the blocking lesion in an error-free manner.
[ "8" ]
One of these mechanisms is proposed to involve a transient template switch to the undamaged sister chromatid, allowing the replicative polymerase to synthesize the sequence complementary to the blocking lesion in an error-free manner.
true
true
true
true
true
704
0
INTRODUCTION
1
1
[ "b1", "b2", "b3", "b4", "b5", "b1", "b3", "b6", "b7", "b8", "b1", "b8", "b11" ]
17,003,056
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It is believed that such template-switching is achieved by a movement of the fork backward so as to re-anneal the original template strands and displace the newly synthesized strands which themselves anneal to generate a Holliday junction structure with a short arm (1).
[ "1", "2", "3", "4", "5", "1", "3", "6", "7", "8", "1", "8", "11" ]
270
4,135
1
false
It is believed that such template-switching is achieved by a movement of the fork backward so as to re-anneal the original template strands and displace the newly synthesized strands which themselves anneal to generate a Holliday junction structure with a short arm.
[ "1" ]
It is believed that such template-switching is achieved by a movement of the fork backward so as to re-anneal the original template strands and displace the newly synthesized strands which themselves anneal to generate a Holliday junction structure with a short arm.
true
true
true
true
true
704
0
INTRODUCTION
1
1
[ "b1", "b2", "b3", "b4", "b5", "b1", "b3", "b6", "b7", "b8", "b1", "b8", "b11" ]
17,003,056
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Indeed, such structures have been observed to accumulate upon replication arrest both in prokaryotic and in eukaryotic cells (8–11).
[ "1", "2", "3", "4", "5", "1", "3", "6", "7", "8", "1", "8", "11" ]
132
4,136
0
false
Indeed, such structures have been observed to accumulate upon replication arrest both in prokaryotic and in eukaryotic cells.
[ "8–11" ]
Indeed, such structures have been observed to accumulate upon replication arrest both in prokaryotic and in eukaryotic cells.
true
true
true
true
true
704
0
INTRODUCTION
1
1
[ "b1", "b2", "b3", "b4", "b5", "b1", "b3", "b6", "b7", "b8", "b1", "b8", "b11" ]
17,003,056
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However, it is not clear whether the formation of these structures is promoted enzymatically or occurs spontaneously.
[ "1", "2", "3", "4", "5", "1", "3", "6", "7", "8", "1", "8", "11" ]
117
4,137
0
false
However, it is not clear whether the formation of these structures is promoted enzymatically or occurs spontaneously.
[]
However, it is not clear whether the formation of these structures is promoted enzymatically or occurs spontaneously.
true
true
true
true
true
704
1
INTRODUCTION
1
12
[ "b12", "b12", "b13", "b14", "b15", "b16" ]
17,003,056
pmid-12803543|pmid-12803543|pmid-14685245|pmid-15591207|pmid-15200954|pmid-15960976|pmid-15831450|pmid-14745833|pmid-12748644|pmid-15565170
Proteins belonging to the RecQ family of 3′–5′ DNA helicases are implicated in the processing of aberrant DNA structures arising during DNA replication and repair (12).
[ "12", "12", "13", "14", "15", "16" ]
168
4,138
1
false
Proteins belonging to the RecQ family of 3′–5′ DNA helicases are implicated in the processing of aberrant DNA structures arising during DNA replication and repair.
[ "12" ]
Proteins belonging to the RecQ family of 3′–5′ DNA helicases are implicated in the processing of aberrant DNA structures arising during DNA replication and repair.
true
true
true
true
true
705
1
INTRODUCTION
1
12
[ "b12", "b12", "b13", "b14", "b15", "b16" ]
17,003,056
pmid-12803543|pmid-12803543|pmid-14685245|pmid-15591207|pmid-15200954|pmid-15960976|pmid-15831450|pmid-14745833|pmid-12748644|pmid-15565170
Defects in three of the five known human RecQ homologues have been found to be associated with different autosomal recessive disorders characterized by genomic instability and cancer predisposition—mutations in BLM, WRN and RECQ4 give rise to Bloom syndrome, Werner syndrome and Rothmund–Thomson syndrome, respectively (...
[ "12", "12", "13", "14", "15", "16" ]
324
4,139
1
false
Defects in three of the five known human RecQ homologues have been found to be associated with different autosomal recessive disorders characterized by genomic instability and cancer predisposition—mutations in BLM, WRN and RECQ4 give rise to Bloom syndrome, Werner syndrome and Rothmund–Thomson syndrome, respectively.
[ "12" ]
Defects in three of the five known human RecQ homologues have been found to be associated with different autosomal recessive disorders characterized by genomic instability and cancer predisposition—mutations in BLM, WRN and RECQ4 give rise to Bloom syndrome, Werner syndrome and Rothmund–Thomson syndrome, respectively.
true
true
true
true
true
705
1
INTRODUCTION
1
13
[ "b12", "b12", "b13", "b14", "b15", "b16" ]
17,003,056
pmid-12803543|pmid-12803543|pmid-14685245|pmid-15591207|pmid-15200954|pmid-15960976|pmid-15831450|pmid-14745833|pmid-12748644|pmid-15565170
BLM is known to suppress crossovers during homologous recombination (HR) presumably through its unique ability to act in conjunction with DNA topoisomerase IIIα to decatenate recombination intermediates containing double Holliday junctions (13).
[ "12", "12", "13", "14", "15", "16" ]
245
4,140
1
false
BLM is known to suppress crossovers during homologous recombination (HR) presumably through its unique ability to act in conjunction with DNA topoisomerase IIIα to decatenate recombination intermediates containing double Holliday junctions.
[ "13" ]
BLM is known to suppress crossovers during homologous recombination (HR) presumably through its unique ability to act in conjunction with DNA topoisomerase IIIα to decatenate recombination intermediates containing double Holliday junctions.
true
true
true
true
true
705
1
INTRODUCTION
1
12
[ "b12", "b12", "b13", "b14", "b15", "b16" ]
17,003,056
pmid-12803543|pmid-12803543|pmid-14685245|pmid-15591207|pmid-15200954|pmid-15960976|pmid-15831450|pmid-14745833|pmid-12748644|pmid-15565170
WRN promotes lagging-strand replication of G-rich telomeric regions and resolves telomeric D-loops in a manner regulated by the TRF1 and TRF2 proteins (14,15).
[ "12", "12", "13", "14", "15", "16" ]
159
4,141
0
false
WRN promotes lagging-strand replication of G-rich telomeric regions and resolves telomeric D-loops in a manner regulated by the TRF1 and TRF2 proteins.
[ "14,15" ]
WRN promotes lagging-strand replication of G-rich telomeric regions and resolves telomeric D-loops in a manner regulated by the TRF1 and TRF2 proteins.
true
true
true
true
true
705
1
INTRODUCTION
1
16
[ "b12", "b12", "b13", "b14", "b15", "b16" ]
17,003,056
pmid-12803543|pmid-12803543|pmid-14685245|pmid-15591207|pmid-15200954|pmid-15960976|pmid-15831450|pmid-14745833|pmid-12748644|pmid-15565170
RECQ4 is proposed to be important for the initiation of DNA replication by promoting the loading of replication protein A on unwound origins (16).
[ "12", "12", "13", "14", "15", "16" ]
146
4,142
1
false
RECQ4 is proposed to be important for the initiation of DNA replication by promoting the loading of replication protein A on unwound origins.
[ "16" ]
RECQ4 is proposed to be important for the initiation of DNA replication by promoting the loading of replication protein A on unwound origins.
true
true
true
true
true
705
2
INTRODUCTION
1
17
[ "b17", "b17", "b18", "b19" ]
17,003,056
pmid-15831450|pmid-15831450|pmid-10710432|pmid-15241474|pmid-11459957|pmid-11595187
The role of the human RECQ5 protein in the maintenance of genomic stability remains to be elucidated.
[ "17", "17", "18", "19" ]
101
4,143
0
false
The role of the human RECQ5 protein in the maintenance of genomic stability remains to be elucidated.
[]
The role of the human RECQ5 protein in the maintenance of genomic stability remains to be elucidated.
true
true
true
true
true
706
2
INTRODUCTION
1
17
[ "b17", "b17", "b18", "b19" ]
17,003,056
pmid-15831450|pmid-15831450|pmid-10710432|pmid-15241474|pmid-11459957|pmid-11595187
The inactivation of the Recq5 gene in mouse embryonic stem cells results in a significant increase in the frequency of sister chromatid exchanges (SCEs) comparable to that caused by Blm gene inactivation (17).
[ "17", "17", "18", "19" ]
209
4,144
1
false
The inactivation of the Recq5 gene in mouse embryonic stem cells results in a significant increase in the frequency of sister chromatid exchanges (SCEs) comparable to that caused by Blm gene inactivation.
[ "17" ]
The inactivation of the Recq5 gene in mouse embryonic stem cells results in a significant increase in the frequency of sister chromatid exchanges (SCEs) comparable to that caused by Blm gene inactivation.
true
true
true
true
true
706
2
INTRODUCTION
1
17
[ "b17", "b17", "b18", "b19" ]
17,003,056
pmid-15831450|pmid-15831450|pmid-10710432|pmid-15241474|pmid-11459957|pmid-11595187
Deletion of both Recq5 and Blm genes leads to an even higher frequency of SCEs compared to the single mutants, suggesting that BLM and RECQ5 operate in different pathways that suppress mitotic recombination (17).
[ "17", "17", "18", "19" ]
212
4,145
1
false
Deletion of both Recq5 and Blm genes leads to an even higher frequency of SCEs compared to the single mutants, suggesting that BLM and RECQ5 operate in different pathways that suppress mitotic recombination.
[ "17" ]
Deletion of both Recq5 and Blm genes leads to an even higher frequency of SCEs compared to the single mutants, suggesting that BLM and RECQ5 operate in different pathways that suppress mitotic recombination.
true
true
true
true
true
706
2
INTRODUCTION
1
18
[ "b17", "b17", "b18", "b19" ]
17,003,056
pmid-15831450|pmid-15831450|pmid-10710432|pmid-15241474|pmid-11459957|pmid-11595187
In contrast to the other human RecQ homologues, RECQ5 exists in at least three different isoforms resulting from alternative mRNA splicing (18).
[ "17", "17", "18", "19" ]
144
4,146
1
false
In contrast to the other human RecQ homologues, RECQ5 exists in at least three different isoforms resulting from alternative mRNA splicing.
[ "18" ]
In contrast to the other human RecQ homologues, RECQ5 exists in at least three different isoforms resulting from alternative mRNA splicing.
true
true
true
true
true
706
2
INTRODUCTION
1
19
[ "b17", "b17", "b18", "b19" ]
17,003,056
pmid-15831450|pmid-15831450|pmid-10710432|pmid-15241474|pmid-11459957|pmid-11595187
The largest splice variant, RECQ5β functions not only as a 3′–5′ DNA helicase, but also possesses an intrinsic DNA strand-annealing activity residing in the unique C-terminal half of the protein (19).
[ "17", "17", "18", "19" ]
200
4,147
1
false
The largest splice variant, RECQ5β functions not only as a 3′–5′ DNA helicase, but also possesses an intrinsic DNA strand-annealing activity residing in the unique C-terminal half of the protein.
[ "19" ]
The largest splice variant, RECQ5β functions not only as a 3′–5′ DNA helicase, but also possesses an intrinsic DNA strand-annealing activity residing in the unique C-terminal half of the protein.
true
true
true
true
true
706
2
INTRODUCTION
1
17
[ "b17", "b17", "b18", "b19" ]
17,003,056
pmid-15831450|pmid-15831450|pmid-10710432|pmid-15241474|pmid-11459957|pmid-11595187
This strand-annealing activity is suppressed if the helicase is in its ATP-bound state, suggesting that RECQ5β may mediate DNA transactions that require a coordinated action of helicase and strand-annealing activities, such as replication fork regression.
[ "17", "17", "18", "19" ]
255
4,148
0
false
This strand-annealing activity is suppressed if the helicase is in its ATP-bound state, suggesting that RECQ5β may mediate DNA transactions that require a coordinated action of helicase and strand-annealing activities, such as replication fork regression.
[]
This strand-annealing activity is suppressed if the helicase is in its ATP-bound state, suggesting that RECQ5β may mediate DNA transactions that require a coordinated action of helicase and strand-annealing activities, such as replication fork regression.
true
true
true
true
true
706
3
INTRODUCTION
0
null
null
17,003,056
pmid-15845538|pmid-16766518|pmid-12791985|pmid-10825162|pmid-10373438|pmid-15289460
Here we show that the RECQ5β helicase has the ability to promote strand exchange between arms of synthetic forked DNA structures that resemble a stalled replication fork in a reaction stimulated by the human replication protein A (hRPA).
null
237
4,149
0
false
null
null
Here we show that the RECQ5β helicase has the ability to promote strand exchange between arms of synthetic forked DNA structures that resemble a stalled replication fork in a reaction stimulated by the human replication protein A (hRPA).
true
true
true
true
true
707
3
INTRODUCTION
0
null
null
17,003,056
pmid-15845538|pmid-16766518|pmid-12791985|pmid-10825162|pmid-10373438|pmid-15289460
In contrast, hRPA is found to block strand exchange by BLM and WRN by driving these helicases to mediate unwinding of the parental duplex.
null
138
4,150
0
false
null
null
In contrast, hRPA is found to block strand exchange by BLM and WRN by driving these helicases to mediate unwinding of the parental duplex.
true
true
true
true
true
707
3
INTRODUCTION
0
null
null
17,003,056
pmid-15845538|pmid-16766518|pmid-12791985|pmid-10825162|pmid-10373438|pmid-15289460
On forked DNA structures with heterologous arms, RECQ5β preferentially unwinds the lagging-strand duplex, whereas BLM and WRN show a strong preference for unwinding of the parental duplex even in the absence of hRPA.
null
216
4,151
0
false
null
null
On forked DNA structures with heterologous arms, RECQ5β preferentially unwinds the lagging-strand duplex, whereas BLM and WRN show a strong preference for unwinding of the parental duplex even in the absence of hRPA.
true
true
true
true
true
707
3
INTRODUCTION
0
null
null
17,003,056
pmid-15845538|pmid-16766518|pmid-12791985|pmid-10825162|pmid-10373438|pmid-15289460
The ability of RECQ5β to catalyze the lagging-strand unwinding and strand exchange on hRPA-coated forked structures is dependent on a short region located within the non-conserved portion of RECQ5β.
null
198
4,152
0
false
null
null
The ability of RECQ5β to catalyze the lagging-strand unwinding and strand exchange on hRPA-coated forked structures is dependent on a short region located within the non-conserved portion of RECQ5β.
true
true
true
true
true
707
3
INTRODUCTION
0
null
null
17,003,056
pmid-15845538|pmid-16766518|pmid-12791985|pmid-10825162|pmid-10373438|pmid-15289460
In addition, we show by immunofluorescence microscopy that RECQ5β localizes to DNA replication factories in S phase nuclei and persists at the sites of stalled replication forks.
null
178
4,153
0
false
null
null
In addition, we show by immunofluorescence microscopy that RECQ5β localizes to DNA replication factories in S phase nuclei and persists at the sites of stalled replication forks.
true
true
true
true
true
707
3
INTRODUCTION
0
null
null
17,003,056
pmid-15845538|pmid-16766518|pmid-12791985|pmid-10825162|pmid-10373438|pmid-15289460
Moreover, we have found that RECQ5β physically interacts with the polymerase processivity factor proliferating cell nuclear antigen (PCNA) in vivo and in vitro.
null
160
4,154
0
false
null
null
Moreover, we have found that RECQ5β physically interacts with the polymerase processivity factor proliferating cell nuclear antigen (PCNA) in vivo and in vitro.
true
true
true
true
true
707
3
INTRODUCTION
0
null
null
17,003,056
pmid-15845538|pmid-16766518|pmid-12791985|pmid-10825162|pmid-10373438|pmid-15289460
Based on these findings, we propose that RECQ5β could mediate regression of stalled replication forks to facilitate DNA damage bypass by template-switching.
null
156
4,155
0
false
null
null
Based on these findings, we propose that RECQ5β could mediate regression of stalled replication forks to facilitate DNA damage bypass by template-switching.
true
true
true
true
true
707
0
DISCUSSION
1
33
[ "b33", "b33", "b34", "b6", "b35" ]
17,003,056
pmid-11700277|pmid-10373362|pmid-16387650|pmid-12612652|pmid-15935756|pmid-11700277|pmid-16387650|pmid-14643434|pmid-16452972|pmid-1255724|pmid-11700277|pmid-1255724|pmid-12142537|pmid-11884624|pmid-11884624|pmid-12226657|pmid-14643434|pmid-12724426
There is growing evidence suggesting that RecQ DNA helicases operate in various DNA repair processes induced by DNA replication defects.
[ "33", "33", "34", "6", "35" ]
136
4,156
0
false
There is growing evidence suggesting that RecQ DNA helicases operate in various DNA repair processes induced by DNA replication defects.
[]
There is growing evidence suggesting that RecQ DNA helicases operate in various DNA repair processes induced by DNA replication defects.
true
true
true
true
true
708
0
DISCUSSION
1
33
[ "b33", "b33", "b34", "b6", "b35" ]
17,003,056
pmid-11700277|pmid-10373362|pmid-16387650|pmid-12612652|pmid-15935756|pmid-11700277|pmid-16387650|pmid-14643434|pmid-16452972|pmid-1255724|pmid-11700277|pmid-1255724|pmid-12142537|pmid-11884624|pmid-11884624|pmid-12226657|pmid-14643434|pmid-12724426
However, the DNA transactions mediated by these proteins at damaged replication forks still remain elusive.
[ "33", "33", "34", "6", "35" ]
107
4,157
0
false
However, the DNA transactions mediated by these proteins at damaged replication forks still remain elusive.
[]
However, the DNA transactions mediated by these proteins at damaged replication forks still remain elusive.
true
true
true
true
true
708
0
DISCUSSION
1
33
[ "b33", "b33", "b34", "b6", "b35" ]
17,003,056
pmid-11700277|pmid-10373362|pmid-16387650|pmid-12612652|pmid-15935756|pmid-11700277|pmid-16387650|pmid-14643434|pmid-16452972|pmid-1255724|pmid-11700277|pmid-1255724|pmid-12142537|pmid-11884624|pmid-11884624|pmid-12226657|pmid-14643434|pmid-12724426
Here we show that the human RECQ5β helicase possesses the ability to promote strand exchange on synthetic forked DNA structures that mimic a stalled replication fork.
[ "33", "33", "34", "6", "35" ]
166
4,158
0
false
Here we show that the human RECQ5β helicase possesses the ability to promote strand exchange on synthetic forked DNA structures that mimic a stalled replication fork.
[]
Here we show that the human RECQ5β helicase possesses the ability to promote strand exchange on synthetic forked DNA structures that mimic a stalled replication fork.
true
true
true
true
true
708
0
DISCUSSION
1
33
[ "b33", "b33", "b34", "b6", "b35" ]
17,003,056
pmid-11700277|pmid-10373362|pmid-16387650|pmid-12612652|pmid-15935756|pmid-11700277|pmid-16387650|pmid-14643434|pmid-16452972|pmid-1255724|pmid-11700277|pmid-1255724|pmid-12142537|pmid-11884624|pmid-11884624|pmid-12226657|pmid-14643434|pmid-12724426
Moreover, we provide evidence suggesting that the RECQ5β protein is localized in the DNA replication factories in S phase nuclei and persists at the sites of stalled replication forks.
[ "33", "33", "34", "6", "35" ]
184
4,159
0
false
Moreover, we provide evidence suggesting that the RECQ5β protein is localized in the DNA replication factories in S phase nuclei and persists at the sites of stalled replication forks.
[]
Moreover, we provide evidence suggesting that the RECQ5β protein is localized in the DNA replication factories in S phase nuclei and persists at the sites of stalled replication forks.
true
true
true
true
true
708
0
DISCUSSION
1
33
[ "b33", "b33", "b34", "b6", "b35" ]
17,003,056
pmid-11700277|pmid-10373362|pmid-16387650|pmid-12612652|pmid-15935756|pmid-11700277|pmid-16387650|pmid-14643434|pmid-16452972|pmid-1255724|pmid-11700277|pmid-1255724|pmid-12142537|pmid-11884624|pmid-11884624|pmid-12226657|pmid-14643434|pmid-12724426
Based on these findings, we speculate that the RECQ5β helicase could mediate regression of stalled replication forks in vivo to facilitate DNA damage bypass by template-switching (Supplementary Figure S8).
[ "33", "33", "34", "6", "35" ]
205
4,160
0
false
Based on these findings, we speculate that the RECQ5β helicase could mediate regression of stalled replication forks in vivo to facilitate DNA damage bypass by template-switching (Supplementary Figure S8).
[]
Based on these findings, we speculate that the RECQ5β helicase could mediate regression of stalled replication forks in vivo to facilitate DNA damage bypass by template-switching (Supplementary Figure S8).
true
true
true
true
true
708
0
DISCUSSION
1
33
[ "b33", "b33", "b34", "b6", "b35" ]
17,003,056
pmid-11700277|pmid-10373362|pmid-16387650|pmid-12612652|pmid-15935756|pmid-11700277|pmid-16387650|pmid-14643434|pmid-16452972|pmid-1255724|pmid-11700277|pmid-1255724|pmid-12142537|pmid-11884624|pmid-11884624|pmid-12226657|pmid-14643434|pmid-12724426
As mentioned above, such a DNA damage tolerance mechanism has been postulated to exist in both prokaryotic and eukaryotic organisms, but remains to be substantiated experimentally.
[ "33", "33", "34", "6", "35" ]
180
4,161
0
false
As mentioned above, such a DNA damage tolerance mechanism has been postulated to exist in both prokaryotic and eukaryotic organisms, but remains to be substantiated experimentally.
[]
As mentioned above, such a DNA damage tolerance mechanism has been postulated to exist in both prokaryotic and eukaryotic organisms, but remains to be substantiated experimentally.
true
true
true
true
true
708
0
DISCUSSION
1
33
[ "b33", "b33", "b34", "b6", "b35" ]
17,003,056
pmid-11700277|pmid-10373362|pmid-16387650|pmid-12612652|pmid-15935756|pmid-11700277|pmid-16387650|pmid-14643434|pmid-16452972|pmid-1255724|pmid-11700277|pmid-1255724|pmid-12142537|pmid-11884624|pmid-11884624|pmid-12226657|pmid-14643434|pmid-12724426
In the budding yeast Saccharomyces cerevisiae, fork regression associated with template-switching is thought to be the underlying mechanism of the RAD5-subpathway of RAD6-dependent postreplicative repair, which is highly conserved from yeast to humans (33).
[ "33", "33", "34", "6", "35" ]
257
4,162
1
false
In the budding yeast Saccharomyces cerevisiae, fork regression associated with template-switching is thought to be the underlying mechanism of the RAD5-subpathway of RAD6-dependent postreplicative repair, which is highly conserved from yeast to humans.
[ "33" ]
In the budding yeast Saccharomyces cerevisiae, fork regression associated with template-switching is thought to be the underlying mechanism of the RAD5-subpathway of RAD6-dependent postreplicative repair, which is highly conserved from yeast to humans.
true
true
true
true
true
708
0
DISCUSSION
1
33
[ "b33", "b33", "b34", "b6", "b35" ]
17,003,056
pmid-11700277|pmid-10373362|pmid-16387650|pmid-12612652|pmid-15935756|pmid-11700277|pmid-16387650|pmid-14643434|pmid-16452972|pmid-1255724|pmid-11700277|pmid-1255724|pmid-12142537|pmid-11884624|pmid-11884624|pmid-12226657|pmid-14643434|pmid-12724426
As this DNA damage tolerance process, which involves non-destructive polyubiquitination of PCNA, is largely independent of the HR machinery, other means, such as helicase-promoted DNA unwinding, would be required to accomplish the strand-exchange events required for fork regression (33,34).
[ "33", "33", "34", "6", "35" ]
291
4,163
0
false
As this DNA damage tolerance process, which involves non-destructive polyubiquitination of PCNA, is largely independent of the HR machinery, other means, such as helicase-promoted DNA unwinding, would be required to accomplish the strand-exchange events required for fork regression.
[ "33,34" ]
As this DNA damage tolerance process, which involves non-destructive polyubiquitination of PCNA, is largely independent of the HR machinery, other means, such as helicase-promoted DNA unwinding, would be required to accomplish the strand-exchange events required for fork regression.
true
true
true
true
true
708
0
DISCUSSION
1
6
[ "b33", "b33", "b34", "b6", "b35" ]
17,003,056
pmid-11700277|pmid-10373362|pmid-16387650|pmid-12612652|pmid-15935756|pmid-11700277|pmid-16387650|pmid-14643434|pmid-16452972|pmid-1255724|pmid-11700277|pmid-1255724|pmid-12142537|pmid-11884624|pmid-11884624|pmid-12226657|pmid-14643434|pmid-12724426
At present, however, it is not clear whether Sgs1 helicase, the sole RecQ homologue in S.cerevisiae, is involved in the RAD6-dependent DNA damage tolerance, since the assessment of this possibility by epistatic analysis is complicated due to the involvement of Sgs1 in the HR pathway of postreplicative repair (6).
[ "33", "33", "34", "6", "35" ]
314
4,164
1
false
At present, however, it is not clear whether Sgs1 helicase, the sole RecQ homologue in S.cerevisiae, is involved in the RAD6-dependent DNA damage tolerance, since the assessment of this possibility by epistatic analysis is complicated due to the involvement of Sgs1 in the HR pathway of postreplicative repair.
[ "6" ]
At present, however, it is not clear whether Sgs1 helicase, the sole RecQ homologue in S.cerevisiae, is involved in the RAD6-dependent DNA damage tolerance, since the assessment of this possibility by epistatic analysis is complicated due to the involvement of Sgs1 in the HR pathway of postreplicative repair.
true
true
true
true
true
708
0
DISCUSSION
1
35
[ "b33", "b33", "b34", "b6", "b35" ]
17,003,056
pmid-11700277|pmid-10373362|pmid-16387650|pmid-12612652|pmid-15935756|pmid-11700277|pmid-16387650|pmid-14643434|pmid-16452972|pmid-1255724|pmid-11700277|pmid-1255724|pmid-12142537|pmid-11884624|pmid-11884624|pmid-12226657|pmid-14643434|pmid-12724426
Nevertheless, some evidence for such a function has been provided in the fission yeast Saccharomyces pombe by the observation that the formation of Rqh1 (Sgs1 homologue) foci upon UV irradiation is dependent on the presence of Rdh18/Rad18, a component of the Rad6 pathway (35).
[ "33", "33", "34", "6", "35" ]
277
4,165
1
false
Nevertheless, some evidence for such a function has been provided in the fission yeast Saccharomyces pombe by the observation that the formation of Rqh1 (Sgs1 homologue) foci upon UV irradiation is dependent on the presence of Rdh18/Rad18, a component of the Rad6 pathway.
[ "35" ]
Nevertheless, some evidence for such a function has been provided in the fission yeast Saccharomyces pombe by the observation that the formation of Rqh1 (Sgs1 homologue) foci upon UV irradiation is dependent on the presence of Rdh18/Rad18, a component of the Rad6 pathway.
true
true
true
true
true
708
1
DISCUSSION
1
17
[ "b17", "b36", "b37", "b38" ]
17,003,056
pmid-12803543|pmid-12803543|pmid-14685245|pmid-15591207|pmid-15200954|pmid-15960976|pmid-15831450|pmid-14745833|pmid-12748644|pmid-15565170
Our hypothesis that RECQ5β operates in the repair of damaged replication forks is consistent with the finding that inactivation of the mouse RECQ5β homologue is associated with a significant increase in the frequency of SCEs (17), as these may represent cross-over outcomes of the HR-mediated repair of broken replicatio...
[ "17", "36", "37", "38" ]
443
4,166
1
false
Our hypothesis that RECQ5β operates in the repair of damaged replication forks is consistent with the finding that inactivation of the mouse RECQ5β homologue is associated with a significant increase in the frequency of SCEs, as these may represent cross-over outcomes of the HR-mediated repair of broken replication for...
[ "17" ]
Our hypothesis that RECQ5β operates in the repair of damaged replication forks is consistent with the finding that inactivation of the mouse RECQ5β homologue is associated with a significant increase in the frequency of SCEs, as these may represent cross-over outcomes of the HR-mediated repair of broken replication for...
true
true
true
true
true
709
1
DISCUSSION
1
36
[ "b17", "b36", "b37", "b38" ]
17,003,056
pmid-12803543|pmid-12803543|pmid-14685245|pmid-15591207|pmid-15200954|pmid-15960976|pmid-15831450|pmid-14745833|pmid-12748644|pmid-15565170
Similarly, elevated SCE levels have been observed in DT40 chicken cells lacking the trans-lesion polymerases Polζ and Polκ, or the Rad18 ubiquitin ligase (36).
[ "17", "36", "37", "38" ]
159
4,167
1
false
Similarly, elevated SCE levels have been observed in DT40 chicken cells lacking the trans-lesion polymerases Polζ and Polκ, or the Rad18 ubiquitin ligase.
[ "36" ]
Similarly, elevated SCE levels have been observed in DT40 chicken cells lacking the trans-lesion polymerases Polζ and Polκ, or the Rad18 ubiquitin ligase.
true
true
true
true
true
709
1
DISCUSSION
1
17
[ "b17", "b36", "b37", "b38" ]
17,003,056
pmid-12803543|pmid-12803543|pmid-14685245|pmid-15591207|pmid-15200954|pmid-15960976|pmid-15831450|pmid-14745833|pmid-12748644|pmid-15565170
However, one cannot exclude the possibility that the increased level of mitotic recombination associated with RECQ5β deficiency results from a defect in another DNA repair mechanisms.
[ "17", "36", "37", "38" ]
183
4,168
0
false
However, one cannot exclude the possibility that the increased level of mitotic recombination associated with RECQ5β deficiency results from a defect in another DNA repair mechanisms.
[]
However, one cannot exclude the possibility that the increased level of mitotic recombination associated with RECQ5β deficiency results from a defect in another DNA repair mechanisms.
true
true
true
true
true
709
1
DISCUSSION
1
17
[ "b17", "b36", "b37", "b38" ]
17,003,056
pmid-12803543|pmid-12803543|pmid-14685245|pmid-15591207|pmid-15200954|pmid-15960976|pmid-15831450|pmid-14745833|pmid-12748644|pmid-15565170
For example, RECQ5β could operate in the synthesis-dependent strand-annealing pathway of DNA double-strand break repair by disrupting D-loops and promoting annealing of extended arms of the broken chromosome.
[ "17", "36", "37", "38" ]
208
4,169
0
false
For example, RECQ5β could operate in the synthesis-dependent strand-annealing pathway of DNA double-strand break repair by disrupting D-loops and promoting annealing of extended arms of the broken chromosome.
[]
For example, RECQ5β could operate in the synthesis-dependent strand-annealing pathway of DNA double-strand break repair by disrupting D-loops and promoting annealing of extended arms of the broken chromosome.
true
true
true
true
true
709
1
DISCUSSION
1
17
[ "b17", "b36", "b37", "b38" ]
17,003,056
pmid-12803543|pmid-12803543|pmid-14685245|pmid-15591207|pmid-15200954|pmid-15960976|pmid-15831450|pmid-14745833|pmid-12748644|pmid-15565170
Alternatively, RECQ5β could suppress unscheduled recombination during DNA replication by directly displacing inappropriately formed RAD51 filaments in the same manner as the Srs2 and UvrD helicases (37,38).
[ "17", "36", "37", "38" ]
206
4,170
0
false
Alternatively, RECQ5β could suppress unscheduled recombination during DNA replication by directly displacing inappropriately formed RAD51 filaments in the same manner as the Srs2 and UvrD helicases.
[ "37,38" ]
Alternatively, RECQ5β could suppress unscheduled recombination during DNA replication by directly displacing inappropriately formed RAD51 filaments in the same manner as the Srs2 and UvrD helicases.
true
true
true
true
true
709
2
DISCUSSION
1
39
[ "b39", "b40" ]
17,003,056
pmid-15831450|pmid-15831450|pmid-10710432|pmid-15241474|pmid-11459957|pmid-11595187
The biochemical and structural studies have revealed that the E.coli RecG helicase mediates fork regression by active unwinding of both the leading and lagging arms of the fork using a wedge domain that is simultaneously pushed into the lagging and the leading duplexes promoting strand displacement (39,40).
[ "39", "40" ]
308
4,171
0
false
The biochemical and structural studies have revealed that the E.coli RecG helicase mediates fork regression by active unwinding of both the leading and lagging arms of the fork using a wedge domain that is simultaneously pushed into the lagging and the leading duplexes promoting strand displacement.
[ "39,40" ]
The biochemical and structural studies have revealed that the E.coli RecG helicase mediates fork regression by active unwinding of both the leading and lagging arms of the fork using a wedge domain that is simultaneously pushed into the lagging and the leading duplexes promoting strand displacement.
true
true
true
true
true
710
2
DISCUSSION
1
39
[ "b39", "b40" ]
17,003,056
pmid-15831450|pmid-15831450|pmid-10710432|pmid-15241474|pmid-11459957|pmid-11595187
In contrast to RecG, the RECQ5β helicase was found to unwind only the lagging-strand duplex, which raises the question of how it can promote fork regression beyond the leading-strand gap.
[ "39", "40" ]
187
4,172
0
false
In contrast to RecG, the RECQ5β helicase was found to unwind only the lagging-strand duplex, which raises the question of how it can promote fork regression beyond the leading-strand gap.
[]
In contrast to RecG, the RECQ5β helicase was found to unwind only the lagging-strand duplex, which raises the question of how it can promote fork regression beyond the leading-strand gap.
true
true
true
true
true
710
2
DISCUSSION
1
39
[ "b39", "b40" ]
17,003,056
pmid-15831450|pmid-15831450|pmid-10710432|pmid-15241474|pmid-11459957|pmid-11595187
We propose a mechanism in which RECQ5β binds to the fork junction and subsequently translocates along the lagging-strand template in the 3′–5′ direction to unwind the lagging-strand duplex.
[ "39", "40" ]
189
4,173
0
false
We propose a mechanism in which RECQ5β binds to the fork junction and subsequently translocates along the lagging-strand template in the 3′–5′ direction to unwind the lagging-strand duplex.
[]
We propose a mechanism in which RECQ5β binds to the fork junction and subsequently translocates along the lagging-strand template in the 3′–5′ direction to unwind the lagging-strand duplex.
true
true
true
true
true
710
2
DISCUSSION
1
39
[ "b39", "b40" ]
17,003,056
pmid-15831450|pmid-15831450|pmid-10710432|pmid-15241474|pmid-11459957|pmid-11595187
As a result, the parental strands will be free to re-anneal.
[ "39", "40" ]
60
4,174
0
false
As a result, the parental strands will be free to re-anneal.
[]
As a result, the parental strands will be free to re-anneal.
true
true
true
true
true
710
2
DISCUSSION
1
39
[ "b39", "b40" ]
17,003,056
pmid-15831450|pmid-15831450|pmid-10710432|pmid-15241474|pmid-11459957|pmid-11595187
Interestingly, we identified a region of 90 amino acids, located within the non-conserved portion of RECQ5β, as being required for its ability to unwind the lagging arm of the fork, but not for RECQ5β-mediated unwinding of 3′-tailed DNA duplexes.
[ "39", "40" ]
246
4,175
0
false
Interestingly, we identified a region of 90 amino acids, located within the non-conserved portion of RECQ5β, as being required for its ability to unwind the lagging arm of the fork, but not for RECQ5β-mediated unwinding of 3′-tailed DNA duplexes.
[]
Interestingly, we identified a region of 90 amino acids, located within the non-conserved portion of RECQ5β, as being required for its ability to unwind the lagging arm of the fork, but not for RECQ5β-mediated unwinding of 3′-tailed DNA duplexes.
true
true
true
true
true
710
2
DISCUSSION
1
39
[ "b39", "b40" ]
17,003,056
pmid-15831450|pmid-15831450|pmid-10710432|pmid-15241474|pmid-11459957|pmid-11595187
It is therefore plausible to propose that this domain may govern the loading of the RECQ5β helicase on the fork junction, placing the helicase motor on the parental duplex in such an orientation as to allow translocation towards the lagging arm.
[ "39", "40" ]
245
4,176
0
false
It is therefore plausible to propose that this domain may govern the loading of the RECQ5β helicase on the fork junction, placing the helicase motor on the parental duplex in such an orientation as to allow translocation towards the lagging arm.
[]
It is therefore plausible to propose that this domain may govern the loading of the RECQ5β helicase on the fork junction, placing the helicase motor on the parental duplex in such an orientation as to allow translocation towards the lagging arm.
true
true
true
true
true
710
2
DISCUSSION
1
39
[ "b39", "b40" ]
17,003,056
pmid-15831450|pmid-15831450|pmid-10710432|pmid-15241474|pmid-11459957|pmid-11595187
Furthermore, we propose that when the moving junction encounters the leading strand, spontaneous strand exchange will take place, resulting in the displacement of the leading strand and its annealing to the displaced lagging strand to form a four-way junction.
[ "39", "40" ]
260
4,177
0
false
Furthermore, we propose that when the moving junction encounters the leading strand, spontaneous strand exchange will take place, resulting in the displacement of the leading strand and its annealing to the displaced lagging strand to form a four-way junction.
[]
Furthermore, we propose that when the moving junction encounters the leading strand, spontaneous strand exchange will take place, resulting in the displacement of the leading strand and its annealing to the displaced lagging strand to form a four-way junction.
true
true
true
true
true
710
2
DISCUSSION
1
39
[ "b39", "b40" ]
17,003,056
pmid-15831450|pmid-15831450|pmid-10710432|pmid-15241474|pmid-11459957|pmid-11595187
This reaction will be favoured due to the concomitant unwinding of the lagging arm by RECQ5β.
[ "39", "40" ]
93
4,178
0
false
This reaction will be favoured due to the concomitant unwinding of the lagging arm by RECQ5β.
[]
This reaction will be favoured due to the concomitant unwinding of the lagging arm by RECQ5β.
true
true
true
true
true
710
2
DISCUSSION
1
39
[ "b39", "b40" ]
17,003,056
pmid-15831450|pmid-15831450|pmid-10710432|pmid-15241474|pmid-11459957|pmid-11595187
It is also possible that the annealing events occurring during the fork regression process are promoted by the C-terminal strand-annealing domain of RECQ5β, since we found that the deletion variants RECQ51–725 and RECQ51–651 were dramatically compromised for the strand-annealing activity and showed reduced strand-excha...
[ "39", "40" ]
367
4,179
0
false
It is also possible that the annealing events occurring during the fork regression process are promoted by the C-terminal strand-annealing domain of RECQ5β, since we found that the deletion variants RECQ51–725 and RECQ51–651 were dramatically compromised for the strand-annealing activity and showed reduced strand-excha...
[]
It is also possible that the annealing events occurring during the fork regression process are promoted by the C-terminal strand-annealing domain of RECQ5β, since we found that the deletion variants RECQ51–725 and RECQ51–651 were dramatically compromised for the strand-annealing activity and showed reduced strand-excha...
true
true
true
true
true
710
3
DISCUSSION
1
41
[ "b41", "b42", "b27", "b43", "b44", "b45" ]
17,003,056
pmid-15845538|pmid-16766518|pmid-12791985|pmid-10825162|pmid-10373438|pmid-15289460
A previous study demonstrated that BLM and WRN have the capacity to promote strand exchange on oligonucleotide-based substrates through combining their strand-pairing and helicase activities (41).
[ "41", "42", "27", "43", "44", "45" ]
196
4,180
1
false
A previous study demonstrated that BLM and WRN have the capacity to promote strand exchange on oligonucleotide-based substrates through combining their strand-pairing and helicase activities.
[ "41" ]
A previous study demonstrated that BLM and WRN have the capacity to promote strand exchange on oligonucleotide-based substrates through combining their strand-pairing and helicase activities.
true
true
true
true
true
711
3
DISCUSSION
1
42
[ "b41", "b42", "b27", "b43", "b44", "b45" ]
17,003,056
pmid-15845538|pmid-16766518|pmid-12791985|pmid-10825162|pmid-10373438|pmid-15289460
More recently, the BLM helicase has been found to promote fork regression on plasmid-sized substrates, generating a four-way structure (42).
[ "41", "42", "27", "43", "44", "45" ]
140
4,181
1
false
More recently, the BLM helicase has been found to promote fork regression on plasmid-sized substrates, generating a four-way structure.
[ "42" ]
More recently, the BLM helicase has been found to promote fork regression on plasmid-sized substrates, generating a four-way structure.
true
true
true
true
true
711
3
DISCUSSION
1
27
[ "b41", "b42", "b27", "b43", "b44", "b45" ]
17,003,056
pmid-15845538|pmid-16766518|pmid-12791985|pmid-10825162|pmid-10373438|pmid-15289460
Interestingly, we found that hRPA, which covers single-stranded regions at stalled forks (27), strongly modulated the action of the BLM and WRN helicases at the fork to favour unwinding of the parental duplex, which is consistent with the previous reports demonstrating that hRPA increases the processivity of the BLM an...
[ "41", "42", "27", "43", "44", "45" ]
388
4,182
1
false
Interestingly, we found that hRPA, which covers single-stranded regions at stalled forks, strongly modulated the action of the BLM and WRN helicases at the fork to favour unwinding of the parental duplex, which is consistent with the previous reports demonstrating that hRPA increases the processivity of the BLM and WRN...
[ "27", "43,44" ]
Interestingly, we found that hRPA, which covers single-stranded regions at stalled forks, strongly modulated the action of the BLM and WRN helicases at the fork to favour unwinding of the parental duplex, which is consistent with the previous reports demonstrating that hRPA increases the processivity of the BLM and WRN...
true
true
true
true
true
711
3
DISCUSSION
1
45
[ "b41", "b42", "b27", "b43", "b44", "b45" ]
17,003,056
pmid-15845538|pmid-16766518|pmid-12791985|pmid-10825162|pmid-10373438|pmid-15289460
However, these experiments using short DNA substrates cannot account for the possibility that fork regression is mediated by another helicase molecule loaded on the liberated lagging-strand template, an model proposed for the E.coli RecQ helicase (45).
[ "41", "42", "27", "43", "44", "45" ]
252
4,183
1
false
However, these experiments using short DNA substrates cannot account for the possibility that fork regression is mediated by another helicase molecule loaded on the liberated lagging-strand template, an model proposed for the E.coli RecQ helicase.
[ "45" ]
However, these experiments using short DNA substrates cannot account for the possibility that fork regression is mediated by another helicase molecule loaded on the liberated lagging-strand template, an model proposed for the E.coli RecQ helicase.
true
true
true
true
true
711
3
DISCUSSION
1
41
[ "b41", "b42", "b27", "b43", "b44", "b45" ]
17,003,056
pmid-15845538|pmid-16766518|pmid-12791985|pmid-10825162|pmid-10373438|pmid-15289460
To assess which human RecQ helicase is more likely to promote fork regression in vivo, the effect of hRPA on fork regression by BLM, WRN and RECQ5β is currently being investigated using a plasmid-sized forked DNA structure containing an extensive leading-strand gap.
[ "41", "42", "27", "43", "44", "45" ]
266
4,184
0
false
To assess which human RecQ helicase is more likely to promote fork regression in vivo, the effect of hRPA on fork regression by BLM, WRN and RECQ5β is currently being investigated using a plasmid-sized forked DNA structure containing an extensive leading-strand gap.
[]
To assess which human RecQ helicase is more likely to promote fork regression in vivo, the effect of hRPA on fork regression by BLM, WRN and RECQ5β is currently being investigated using a plasmid-sized forked DNA structure containing an extensive leading-strand gap.
true
true
true
true
true
711
0
INTRODUCTION
1
1
[ "b1", "b2", "b3", "b4", "b5", "b10" ]
17,272,295
pmid-2666845|pmid-15489289|pmid-8203157|pmid-15226434|pmid-12110181|pmid-15022016|pmid-11864607|pmid-15100437
The majority of steps in ribosome synthesis take place within the nucleolus, a specialized subnuclear structure.
[ "1", "2", "3", "4", "5", "10" ]
112
4,185
0
false
The majority of steps in ribosome synthesis take place within the nucleolus, a specialized subnuclear structure.
[]
The majority of steps in ribosome synthesis take place within the nucleolus, a specialized subnuclear structure.
true
true
true
true
true
712
0
INTRODUCTION
1
1
[ "b1", "b2", "b3", "b4", "b5", "b10" ]
17,272,295
pmid-2666845|pmid-15489289|pmid-8203157|pmid-15226434|pmid-12110181|pmid-15022016|pmid-11864607|pmid-15100437
In the budding yeast Saccharomyces cerevisiae, the nucleolus is formed around the highly repetitive rDNA array on chromosome XII.
[ "1", "2", "3", "4", "5", "10" ]
129
4,186
0
false
In the budding yeast Saccharomyces cerevisiae, the nucleolus is formed around the highly repetitive rDNA array on chromosome XII.
[]
In the budding yeast Saccharomyces cerevisiae, the nucleolus is formed around the highly repetitive rDNA array on chromosome XII.
true
true
true
true
true
712
0
INTRODUCTION
1
1
[ "b1", "b2", "b3", "b4", "b5", "b10" ]
17,272,295
pmid-2666845|pmid-15489289|pmid-8203157|pmid-15226434|pmid-12110181|pmid-15022016|pmid-11864607|pmid-15100437
Here, the rDNA is transcribed into a large precursor RNA (pre-rRNA), which is subsequently modified and then matured by endonuclease and exonuclease processing to yield the mature 18S, 5.8S and 25S rRNAs (see Figure 1).
[ "1", "2", "3", "4", "5", "10" ]
219
4,187
0
false
Here, the rDNA is transcribed into a large precursor RNA (pre-rRNA), which is subsequently modified and then matured by endonuclease and exonuclease processing to yield the mature 18S, 5.8S and 25S rRNAs.
[ "see Figure 1" ]
Here, the rDNA is transcribed into a large precursor RNA (pre-rRNA), which is subsequently modified and then matured by endonuclease and exonuclease processing to yield the mature 18S, 5.8S and 25S rRNAs.
true
true
true
true
true
712
0
INTRODUCTION
1
1
[ "b1", "b2", "b3", "b4", "b5", "b10" ]
17,272,295
pmid-2666845|pmid-15489289|pmid-8203157|pmid-15226434|pmid-12110181|pmid-15022016|pmid-11864607|pmid-15100437
Ribosome synthesis is a major activity in the Eukaryotic cell and a rapidly growing yeast cell produces around 2000 ribosomes per minute.
[ "1", "2", "3", "4", "5", "10" ]
137
4,188
0
false
Ribosome synthesis is a major activity in the Eukaryotic cell and a rapidly growing yeast cell produces around 2000 ribosomes per minute.
[]
Ribosome synthesis is a major activity in the Eukaryotic cell and a rapidly growing yeast cell produces around 2000 ribosomes per minute.
true
true
true
true
true
712
0
INTRODUCTION
1
1
[ "b1", "b2", "b3", "b4", "b5", "b10" ]
17,272,295
pmid-2666845|pmid-15489289|pmid-8203157|pmid-15226434|pmid-12110181|pmid-15022016|pmid-11864607|pmid-15100437
Both the size of the cell at division and number of ribosomes per cell, are closely linked to growth rate [reviewed in (1,2)].
[ "1", "2", "3", "4", "5", "10" ]
126
4,189
0
false
Both the size of the cell at division and number of ribosomes per cell, are closely linked to growth rate.
[ "reviewed in (1,2)" ]
Both the size of the cell at division and number of ribosomes per cell, are closely linked to growth rate.
true
true
true
true
true
712
0
INTRODUCTION
1
3
[ "b1", "b2", "b3", "b4", "b5", "b10" ]
17,272,295
pmid-2666845|pmid-15489289|pmid-8203157|pmid-15226434|pmid-12110181|pmid-15022016|pmid-11864607|pmid-15100437
Moreover, both size at division and ribosome numbers anticipate the future growth rate suggesting a cross-talk mechanism between ribosome synthesis and mitotic cell division (3).
[ "1", "2", "3", "4", "5", "10" ]
178
4,190
1
false
Moreover, both size at division and ribosome numbers anticipate the future growth rate suggesting a cross-talk mechanism between ribosome synthesis and mitotic cell division.
[ "3" ]
Moreover, both size at division and ribosome numbers anticipate the future growth rate suggesting a cross-talk mechanism between ribosome synthesis and mitotic cell division.
true
true
true
true
true
712
0
INTRODUCTION
1
1
[ "b1", "b2", "b3", "b4", "b5", "b10" ]
17,272,295
pmid-2666845|pmid-15489289|pmid-8203157|pmid-15226434|pmid-12110181|pmid-15022016|pmid-11864607|pmid-15100437
Recent studies in yeast have identified several connections among the nucleolus, ribosome biogenesis and cell-cycle progression [reviewed in (4)].
[ "1", "2", "3", "4", "5", "10" ]
146
4,191
0
false
Recent studies in yeast have identified several connections among the nucleolus, ribosome biogenesis and cell-cycle progression.
[ "reviewed in (4)" ]
Recent studies in yeast have identified several connections among the nucleolus, ribosome biogenesis and cell-cycle progression.
true
true
true
true
true
712
0
INTRODUCTION
1
1
[ "b1", "b2", "b3", "b4", "b5", "b10" ]
17,272,295
pmid-2666845|pmid-15489289|pmid-8203157|pmid-15226434|pmid-12110181|pmid-15022016|pmid-11864607|pmid-15100437
A small number of ribosomal processing factors were found that appear to facilitate cross-talk between those processes, with mutations in these proteins affecting both ribosome synthesis and cell division (5–10).
[ "1", "2", "3", "4", "5", "10" ]
212
4,192
0
false
A small number of ribosomal processing factors were found that appear to facilitate cross-talk between those processes, with mutations in these proteins affecting both ribosome synthesis and cell division.
[ "5–10" ]
A small number of ribosomal processing factors were found that appear to facilitate cross-talk between those processes, with mutations in these proteins affecting both ribosome synthesis and cell division.
true
true
true
true
true
712
1
INTRODUCTION
0
null
null
17,272,295
pmid-15356263|pmid-12089449|NA|pmid-11489916
Yeast pre-rRNA and processing.
null
30
4,193
0
false
null
null
Yeast pre-rRNA and processing.
true
true
true
true
true
713
1
INTRODUCTION
0
null
null
17,272,295
pmid-15356263|pmid-12089449|NA|pmid-11489916
(A) Structure of the yeast pre-rRNA, with locations of oligonucleotides used as hybridization probes.
null
101
4,194
0
false
null
null
(A) Structure of the yeast pre-rRNA, with locations of oligonucleotides used as hybridization probes.
false
false
true
true
false
713
1
INTRODUCTION
0
null
null
17,272,295
pmid-15356263|pmid-12089449|NA|pmid-11489916
(B) Pre-rRNA processing pathway showing the intermediates detected by pulse-chase and northern analyses.
null
104
4,195
0
false
null
null
(B) Pre-rRNA processing pathway showing the intermediates detected by pulse-chase and northern analyses.
false
false
true
true
false
713
2
INTRODUCTION
1
11
[ "b11", "b12", "b13", "b14", "b16", "b11" ]
17,272,295
pmid-11489916|pmid-10662670|pmid-7748491|pmid-14734533|pmid-9367979|pmid-11489916|pmid-15684028
Ykl082c/Rrp14p is an essential protein that was initially characterized in two-hybrid analyses of a protein interaction network involved in the specification of cell polarity (11).
[ "11", "12", "13", "14", "16", "11" ]
180
4,196
1
false
Ykl082c/Rrp14p is an essential protein that was initially characterized in two-hybrid analyses of a protein interaction network involved in the specification of cell polarity.
[ "11" ]
Ykl082c/Rrp14p is an essential protein that was initially characterized in two-hybrid analyses of a protein interaction network involved in the specification of cell polarity.
true
true
true
true
true
714
2
INTRODUCTION
1
11
[ "b11", "b12", "b13", "b14", "b16", "b11" ]
17,272,295
pmid-11489916|pmid-10662670|pmid-7748491|pmid-14734533|pmid-9367979|pmid-11489916|pmid-15684028
Rrp14p interacted with Bud8p, a component of the distal bud site tag complex, Zds2p, a nucleolar protein with a role in cell polarity as well as gene silencing (12,13), and with Gic1p and Gic2p, which interact directly with the GTPase Cdc42, a key regulator of cell polarity (14–16).
[ "11", "12", "13", "14", "16", "11" ]
283
4,197
0
false
Rrp14p interacted with Bud8p, a component of the distal bud site tag complex, Zds2p, a nucleolar protein with a role in cell polarity as well as gene silencing, and with Gic1p and Gic2p, which interact directly with the GTPase Cdc42, a key regulator of cell polarity.
[ "12,13", "14–16" ]
Rrp14p interacted with Bud8p, a component of the distal bud site tag complex, Zds2p, a nucleolar protein with a role in cell polarity as well as gene silencing, and with Gic1p and Gic2p, which interact directly with the GTPase Cdc42, a key regulator of cell polarity.
true
true
true
true
true
714
2
INTRODUCTION
1
11
[ "b11", "b12", "b13", "b14", "b16", "b11" ]
17,272,295
pmid-11489916|pmid-10662670|pmid-7748491|pmid-14734533|pmid-9367979|pmid-11489916|pmid-15684028
Stains carrying gic1/2Δ have a depolarized actin and microtubule cytoskeleton, implicating these proteins in microtubule polarization and nuclear migration.
[ "11", "12", "13", "14", "16", "11" ]
156
4,198
0
false
Stains carrying gic1/2Δ have a depolarized actin and microtubule cytoskeleton, implicating these proteins in microtubule polarization and nuclear migration.
[]
Stains carrying gic1/2Δ have a depolarized actin and microtubule cytoskeleton, implicating these proteins in microtubule polarization and nuclear migration.
true
true
true
true
true
714
2
INTRODUCTION
1
11
[ "b11", "b12", "b13", "b14", "b16", "b11" ]
17,272,295
pmid-11489916|pmid-10662670|pmid-7748491|pmid-14734533|pmid-9367979|pmid-11489916|pmid-15684028
Rrp14p was therefore proposed to be involved in polarized growth and the establishment of bud sites, although direct physical interactions were not assessed (11).
[ "11", "12", "13", "14", "16", "11" ]
162
4,199
1
false
Rrp14p was therefore proposed to be involved in polarized growth and the establishment of bud sites, although direct physical interactions were not assessed.
[ "11" ]
Rrp14p was therefore proposed to be involved in polarized growth and the establishment of bud sites, although direct physical interactions were not assessed.
true
true
true
true
true
714