Datasets:
vgainullin
/
xciting_data

Dataset card Data Studio Files
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 Community
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6
DISCUSSION
0
null
null
17,355,990
null
This work represents a major step forward in identifying transcriptional regulatory networks in protozoan parasites and indicates that this statistical method can be broadly applied in other organisms.
null
201
10,900
0
false
null
null
This work represents a major step forward in identifying transcriptional regulatory networks in protozoan parasites and indicates that this statistical method can be broadly applied in other organisms.
true
true
true
true
true
1,735
0
INTRODUCTION
1
1–3
[ "B1 B2 B3", "B4 B5 B6" ]
17,308,347
pmid-16493006|pmid-16822457|pmid-11389461|pmid-16675878|pmid-16859679|pmid-15935541
A group of rare genetic conditions collectively defined as chromosome instability syndromes has received much attention in recent years, as their study continues to provide important insight into the molecular mechanisms responsible for the integrity of our genome.
[ "1–3", "4–6" ]
265
10,901
0
false
A group of rare genetic conditions collectively defined as chromosome instability syndromes has received much attention in recent years, as their study continues to provide important insight into the molecular mechanisms responsible for the integrity of our genome.
[]
A group of rare genetic conditions collectively defined as chromosome instability syndromes has received much attention in recent years, as their study continues to provide important insight into the molecular mechanisms responsible for the integrity of our genome.
true
true
true
true
true
1,736
0
INTRODUCTION
1
1–3
[ "B1 B2 B3", "B4 B5 B6" ]
17,308,347
pmid-16493006|pmid-16822457|pmid-11389461|pmid-16675878|pmid-16859679|pmid-15935541
One such condition is Fanconi Anaemia (FA), a genetically heterogeneous disorder characterized by congenital abnormalities, aplastic anaemia and predisposition to cancer, especially acute myeloid leukemia and squamous cell carcinomas (1–3).
[ "1–3", "4–6" ]
240
10,902
1
false
One such condition is Fanconi Anaemia (FA), a genetically heterogeneous disorder characterized by congenital abnormalities, aplastic anaemia and predisposition to cancer, especially acute myeloid leukemia and squamous cell carcinomas.
[ "1–3" ]
One such condition is Fanconi Anaemia (FA), a genetically heterogeneous disorder characterized by congenital abnormalities, aplastic anaemia and predisposition to cancer, especially acute myeloid leukemia and squamous cell carcinomas.
true
true
true
true
true
1,736
0
INTRODUCTION
1
1–3
[ "B1 B2 B3", "B4 B5 B6" ]
17,308,347
pmid-16493006|pmid-16822457|pmid-11389461|pmid-16675878|pmid-16859679|pmid-15935541
A conspicuous cellular feature of FA is chromosomal fragility and hypersensitivity to DNA cross-linking agents such as mitomycin C, diepoxybutane and cisplatin.
[ "1–3", "4–6" ]
160
10,903
0
false
A conspicuous cellular feature of FA is chromosomal fragility and hypersensitivity to DNA cross-linking agents such as mitomycin C, diepoxybutane and cisplatin.
[]
A conspicuous cellular feature of FA is chromosomal fragility and hypersensitivity to DNA cross-linking agents such as mitomycin C, diepoxybutane and cisplatin.
true
true
true
true
true
1,736
0
INTRODUCTION
1
4–6
[ "B1 B2 B3", "B4 B5 B6" ]
17,308,347
pmid-16493006|pmid-16822457|pmid-11389461|pmid-16675878|pmid-16859679|pmid-15935541
Sensitivity to genotoxic agents suggests that the pathogenic effects of FA are due to defects in the molecular mechanisms of DNA damage signalling and repair (4–6).
[ "1–3", "4–6" ]
164
10,904
1
false
Sensitivity to genotoxic agents suggests that the pathogenic effects of FA are due to defects in the molecular mechanisms of DNA damage signalling and repair.
[ "4–6" ]
Sensitivity to genotoxic agents suggests that the pathogenic effects of FA are due to defects in the molecular mechanisms of DNA damage signalling and repair.
true
true
true
true
true
1,736
1
INTRODUCTION
1
7
[ "B7", "B8", "B9", "B10", "B11", "B12", "B13", "B14", "B15", "B15 B16 B17", "B18", "B19", "B20" ]
17,308,347
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Twelve different FA subtypes (A, B, C, D1, D2, E, F, G, I, J, L, M) have been isolated, and the genes for all but type I have been cloned (7).
[ "7", "8", "9", "10", "11", "12", "13", "14", "15", "15–17", "18", "19", "20" ]
142
10,905
1
false
Twelve different FA subtypes (A, B, C, D1, D2, E, F, G, I, J, L, M) have been isolated, and the genes for all but type I have been cloned.
[ "7" ]
Twelve different FA subtypes (A, B, C, D1, D2, E, F, G, I, J, L, M) have been isolated, and the genes for all but type I have been cloned.
true
true
true
true
true
1,737
1
INTRODUCTION
1
7
[ "B7", "B8", "B9", "B10", "B11", "B12", "B13", "B14", "B15", "B15 B16 B17", "B18", "B19", "B20" ]
17,308,347
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The majority of FA proteins do not possess clear functional motifs, and only a subset of them have been associated with an enzymatic activity, including a E3 ubiquitin ligase, FANCL (8,9), and two helicases, FANCJ (10,11) and FANCM (12,13).
[ "7", "8", "9", "10", "11", "12", "13", "14", "15", "15–17", "18", "19", "20" ]
240
10,906
0
false
The majority of FA proteins do not possess clear functional motifs, and only a subset of them have been associated with an enzymatic activity, including a E3 ubiquitin ligase, FANCL, and two helicases, FANCJ and FANCM.
[ "8,9", "10,11", "12,13" ]
The majority of FA proteins do not possess clear functional motifs, and only a subset of them have been associated with an enzymatic activity, including a E3 ubiquitin ligase, FANCL, and two helicases, FANCJ and FANCM.
true
true
true
true
true
1,737
1
INTRODUCTION
1
14
[ "B7", "B8", "B9", "B10", "B11", "B12", "B13", "B14", "B15", "B15 B16 B17", "B18", "B19", "B20" ]
17,308,347
pmid-16377561|pmid-12973351|pmid-14712086|NA|pmid-16153896|pmid-16116422|pmid-16116434|pmid-11157805|pmid-11239454|pmid-11239454|pmid-12239151|pmid-15115758|pmid-16720839|pmid-16127171|pmid-16168378|pmid-15537541
A nuclear multi-subunit complex of at least eight FA proteins (FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL and FANCM), the FA core complex (14), adds a single ubiquitin chain to FANCD2 following DNA damage or replicative stress (15) (Figure 1A).
[ "7", "8", "9", "10", "11", "12", "13", "14", "15", "15–17", "18", "19", "20" ]
249
10,907
1
false
A nuclear multi-subunit complex of at least eight FA proteins (FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL and FANCM), the FA core complex, adds a single ubiquitin chain to FANCD2 following DNA damage or replicative stress (Figure 1A).
[ "14", "15" ]
A nuclear multi-subunit complex of at least eight FA proteins (FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL and FANCM), the FA core complex, adds a single ubiquitin chain to FANCD2 following DNA damage or replicative stress.
true
true
true
true
true
1,737
1
INTRODUCTION
1
15–17
[ "B7", "B8", "B9", "B10", "B11", "B12", "B13", "B14", "B15", "B15 B16 B17", "B18", "B19", "B20" ]
17,308,347
pmid-16377561|pmid-12973351|pmid-14712086|NA|pmid-16153896|pmid-16116422|pmid-16116434|pmid-11157805|pmid-11239454|pmid-11239454|pmid-12239151|pmid-15115758|pmid-16720839|pmid-16127171|pmid-16168378|pmid-15537541
Monoubiquitination acts as a signal for FANCD2 recruitment to nuclear foci where it colocalizes with cell-cycle checkpoint regulation and DNA repair proteins such as BRCA1, BRCA2 and RAD51 (15–17).
[ "7", "8", "9", "10", "11", "12", "13", "14", "15", "15–17", "18", "19", "20" ]
197
10,908
1
false
Monoubiquitination acts as a signal for FANCD2 recruitment to nuclear foci where it colocalizes with cell-cycle checkpoint regulation and DNA repair proteins such as BRCA1, BRCA2 and RAD51.
[ "15–17" ]
Monoubiquitination acts as a signal for FANCD2 recruitment to nuclear foci where it colocalizes with cell-cycle checkpoint regulation and DNA repair proteins such as BRCA1, BRCA2 and RAD51.
true
true
true
true
true
1,737
1
INTRODUCTION
1
7
[ "B7", "B8", "B9", "B10", "B11", "B12", "B13", "B14", "B15", "B15 B16 B17", "B18", "B19", "B20" ]
17,308,347
pmid-16377561|pmid-12973351|pmid-14712086|NA|pmid-16153896|pmid-16116422|pmid-16116434|pmid-11157805|pmid-11239454|pmid-11239454|pmid-12239151|pmid-15115758|pmid-16720839|pmid-16127171|pmid-16168378|pmid-15537541
Within the FA core complex, individual constituents engage in multiple interactions with each other, giving rise to functional subcomplexes (18,19).
[ "7", "8", "9", "10", "11", "12", "13", "14", "15", "15–17", "18", "19", "20" ]
148
10,909
0
false
Within the FA core complex, individual constituents engage in multiple interactions with each other, giving rise to functional subcomplexes.
[ "18,19" ]
Within the FA core complex, individual constituents engage in multiple interactions with each other, giving rise to functional subcomplexes.
true
true
true
true
true
1,737
1
INTRODUCTION
1
20
[ "B7", "B8", "B9", "B10", "B11", "B12", "B13", "B14", "B15", "B15 B16 B17", "B18", "B19", "B20" ]
17,308,347
pmid-16377561|pmid-12973351|pmid-14712086|NA|pmid-16153896|pmid-16116422|pmid-16116434|pmid-11157805|pmid-11239454|pmid-11239454|pmid-12239151|pmid-15115758|pmid-16720839|pmid-16127171|pmid-16168378|pmid-15537541
Recent evidence also points to additional roles of the FA core complex besides FANCD2 ubiquitination (20).
[ "7", "8", "9", "10", "11", "12", "13", "14", "15", "15–17", "18", "19", "20" ]
106
10,910
1
false
Recent evidence also points to additional roles of the FA core complex besides FANCD2 ubiquitination.
[ "20" ]
Recent evidence also points to additional roles of the FA core complex besides FANCD2 ubiquitination.
true
true
true
true
true
1,737
1
INTRODUCTION
1
7
[ "B7", "B8", "B9", "B10", "B11", "B12", "B13", "B14", "B15", "B15 B16 B17", "B18", "B19", "B20" ]
17,308,347
pmid-16377561|pmid-12973351|pmid-14712086|NA|pmid-16153896|pmid-16116422|pmid-16116434|pmid-11157805|pmid-11239454|pmid-11239454|pmid-12239151|pmid-15115758|pmid-16720839|pmid-16127171|pmid-16168378|pmid-15537541
Although much has been learned about the role of the FA proteins in maintenance of genome stability, our understanding of the molecular mechanisms underlying their function remains largely incomplete.
[ "7", "8", "9", "10", "11", "12", "13", "14", "15", "15–17", "18", "19", "20" ]
200
10,911
0
false
Although much has been learned about the role of the FA proteins in maintenance of genome stability, our understanding of the molecular mechanisms underlying their function remains largely incomplete.
[]
Although much has been learned about the role of the FA proteins in maintenance of genome stability, our understanding of the molecular mechanisms underlying their function remains largely incomplete.
true
true
true
true
true
1,737
1
INTRODUCTION
1
7
[ "B7", "B8", "B9", "B10", "B11", "B12", "B13", "B14", "B15", "B15 B16 B17", "B18", "B19", "B20" ]
17,308,347
pmid-16377561|pmid-12973351|pmid-14712086|NA|pmid-16153896|pmid-16116422|pmid-16116434|pmid-11157805|pmid-11239454|pmid-11239454|pmid-12239151|pmid-15115758|pmid-16720839|pmid-16127171|pmid-16168378|pmid-15537541
Figure 1.Structure of human FANCE.
[ "7", "8", "9", "10", "11", "12", "13", "14", "15", "15–17", "18", "19", "20" ]
34
10,912
0
false
Figure 1.Structure of human FANCE.
[]
Figure 1.Structure of human FANCE.
true
true
true
true
true
1,737
1
INTRODUCTION
1
7
[ "B7", "B8", "B9", "B10", "B11", "B12", "B13", "B14", "B15", "B15 B16 B17", "B18", "B19", "B20" ]
17,308,347
pmid-16377561|pmid-12973351|pmid-14712086|NA|pmid-16153896|pmid-16116422|pmid-16116434|pmid-11157805|pmid-11239454|pmid-11239454|pmid-12239151|pmid-15115758|pmid-16720839|pmid-16127171|pmid-16168378|pmid-15537541
In response to DNA damage or replicative stress, the FA core complex monoubiquitinates FANCD2.
[ "7", "8", "9", "10", "11", "12", "13", "14", "15", "15–17", "18", "19", "20" ]
94
10,913
0
false
In response to DNA damage or replicative stress, the FA core complex monoubiquitinates FANCD2.
[]
In response to DNA damage or replicative stress, the FA core complex monoubiquitinates FANCD2.
true
true
true
true
true
1,737
1
INTRODUCTION
1
7
[ "B7", "B8", "B9", "B10", "B11", "B12", "B13", "B14", "B15", "B15 B16 B17", "B18", "B19", "B20" ]
17,308,347
pmid-16377561|pmid-12973351|pmid-14712086|NA|pmid-16153896|pmid-16116422|pmid-16116434|pmid-11157805|pmid-11239454|pmid-11239454|pmid-12239151|pmid-15115758|pmid-16720839|pmid-16127171|pmid-16168378|pmid-15537541
The eight identified subunits of the FA complex are shown.
[ "7", "8", "9", "10", "11", "12", "13", "14", "15", "15–17", "18", "19", "20" ]
58
10,914
0
false
The eight identified subunits of the FA complex are shown.
[]
The eight identified subunits of the FA complex are shown.
true
true
true
true
true
1,737
1
INTRODUCTION
1
7
[ "B7", "B8", "B9", "B10", "B11", "B12", "B13", "B14", "B15", "B15 B16 B17", "B18", "B19", "B20" ]
17,308,347
pmid-16377561|pmid-12973351|pmid-14712086|NA|pmid-16153896|pmid-16116422|pmid-16116434|pmid-11157805|pmid-11239454|pmid-11239454|pmid-12239151|pmid-15115758|pmid-16720839|pmid-16127171|pmid-16168378|pmid-15537541
(B) Schematic representation of the domain structure of the FANCE protein.
[ "7", "8", "9", "10", "11", "12", "13", "14", "15", "15–17", "18", "19", "20" ]
74
10,915
0
false
(B) Schematic representation of the domain structure of the FANCE protein.
[]
(B) Schematic representation of the domain structure of the FANCE protein.
false
false
true
true
false
1,737
1
INTRODUCTION
1
7
[ "B7", "B8", "B9", "B10", "B11", "B12", "B13", "B14", "B15", "B15 B16 B17", "B18", "B19", "B20" ]
17,308,347
pmid-16377561|pmid-12973351|pmid-14712086|NA|pmid-16153896|pmid-16116422|pmid-16116434|pmid-11157805|pmid-11239454|pmid-11239454|pmid-12239151|pmid-15115758|pmid-16720839|pmid-16127171|pmid-16168378|pmid-15537541
Orange boxes represent regions of the protein that are predicted to constitute independently folded domains.
[ "7", "8", "9", "10", "11", "12", "13", "14", "15", "15–17", "18", "19", "20" ]
108
10,916
0
false
Orange boxes represent regions of the protein that are predicted to constitute independently folded domains.
[]
Orange boxes represent regions of the protein that are predicted to constitute independently folded domains.
true
true
true
true
true
1,737
1
INTRODUCTION
1
7
[ "B7", "B8", "B9", "B10", "B11", "B12", "B13", "B14", "B15", "B15 B16 B17", "B18", "B19", "B20" ]
17,308,347
pmid-16377561|pmid-12973351|pmid-14712086|NA|pmid-16153896|pmid-16116422|pmid-16116434|pmid-11157805|pmid-11239454|pmid-11239454|pmid-12239151|pmid-15115758|pmid-16720839|pmid-16127171|pmid-16168378|pmid-15537541
The two nuclear localization sequences in the middle section of the protein are drawn in black.
[ "7", "8", "9", "10", "11", "12", "13", "14", "15", "15–17", "18", "19", "20" ]
95
10,917
0
false
The two nuclear localization sequences in the middle section of the protein are drawn in black.
[]
The two nuclear localization sequences in the middle section of the protein are drawn in black.
true
true
true
true
true
1,737
1
INTRODUCTION
1
7
[ "B7", "B8", "B9", "B10", "B11", "B12", "B13", "B14", "B15", "B15 B16 B17", "B18", "B19", "B20" ]
17,308,347
pmid-16377561|pmid-12973351|pmid-14712086|NA|pmid-16153896|pmid-16116422|pmid-16116434|pmid-11157805|pmid-11239454|pmid-11239454|pmid-12239151|pmid-15115758|pmid-16720839|pmid-16127171|pmid-16168378|pmid-15537541
(C) Cartoon representation of the crystal structure of amino acids 273 to 536 of human FANCE.
[ "7", "8", "9", "10", "11", "12", "13", "14", "15", "15–17", "18", "19", "20" ]
93
10,918
0
false
(C) Cartoon representation of the crystal structure of amino acids 273 to 536 of human FANCE.
[]
(C) Cartoon representation of the crystal structure of amino acids 273 to 536 of human FANCE.
false
false
true
true
false
1,737
1
INTRODUCTION
1
7
[ "B7", "B8", "B9", "B10", "B11", "B12", "B13", "B14", "B15", "B15 B16 B17", "B18", "B19", "B20" ]
17,308,347
pmid-16377561|pmid-12973351|pmid-14712086|NA|pmid-16153896|pmid-16116422|pmid-16116434|pmid-11157805|pmid-11239454|pmid-11239454|pmid-12239151|pmid-15115758|pmid-16720839|pmid-16127171|pmid-16168378|pmid-15537541
The protein chain is shown as a ribbon, rainbow-coloured from blue at the N-terminal end to red at the C-terminal end.
[ "7", "8", "9", "10", "11", "12", "13", "14", "15", "15–17", "18", "19", "20" ]
118
10,919
0
false
The protein chain is shown as a ribbon, rainbow-coloured from blue at the N-terminal end to red at the C-terminal end.
[]
The protein chain is shown as a ribbon, rainbow-coloured from blue at the N-terminal end to red at the C-terminal end.
true
true
true
true
true
1,737
1
INTRODUCTION
1
7
[ "B7", "B8", "B9", "B10", "B11", "B12", "B13", "B14", "B15", "B15 B16 B17", "B18", "B19", "B20" ]
17,308,347
pmid-16377561|pmid-12973351|pmid-14712086|NA|pmid-16153896|pmid-16116422|pmid-16116434|pmid-11157805|pmid-11239454|pmid-11239454|pmid-12239151|pmid-15115758|pmid-16720839|pmid-16127171|pmid-16168378|pmid-15537541
Two views are shown, differing by a 90Β° rotation around an axis aligned to the long dimension of the molecule.
[ "7", "8", "9", "10", "11", "12", "13", "14", "15", "15–17", "18", "19", "20" ]
110
10,920
0
false
Two views are shown, differing by a 90Β° rotation around an axis aligned to the long dimension of the molecule.
[]
Two views are shown, differing by a 90Β° rotation around an axis aligned to the long dimension of the molecule.
true
true
true
true
true
1,737
1
INTRODUCTION
1
7
[ "B7", "B8", "B9", "B10", "B11", "B12", "B13", "B14", "B15", "B15 B16 B17", "B18", "B19", "B20" ]
17,308,347
pmid-16377561|pmid-12973351|pmid-14712086|NA|pmid-16153896|pmid-16116422|pmid-16116434|pmid-11157805|pmid-11239454|pmid-11239454|pmid-12239151|pmid-15115758|pmid-16720839|pmid-16127171|pmid-16168378|pmid-15537541
The alpha-helical segments in the structure are labelled, Ξ±1 to Ξ±14.
[ "7", "8", "9", "10", "11", "12", "13", "14", "15", "15–17", "18", "19", "20" ]
68
10,921
0
false
The alpha-helical segments in the structure are labelled, Ξ±1 to Ξ±14.
[]
The alpha-helical segments in the structure are labelled, Ξ±1 to Ξ±14.
true
true
true
true
true
1,737
1
INTRODUCTION
1
7
[ "B7", "B8", "B9", "B10", "B11", "B12", "B13", "B14", "B15", "B15 B16 B17", "B18", "B19", "B20" ]
17,308,347
pmid-16377561|pmid-12973351|pmid-14712086|NA|pmid-16153896|pmid-16116422|pmid-16116434|pmid-11157805|pmid-11239454|pmid-11239454|pmid-12239151|pmid-15115758|pmid-16720839|pmid-16127171|pmid-16168378|pmid-15537541
The positions of the five helical repeats identified in FANCE are indicated next to the structure.
[ "7", "8", "9", "10", "11", "12", "13", "14", "15", "15–17", "18", "19", "20" ]
98
10,922
0
false
The positions of the five helical repeats identified in FANCE are indicated next to the structure.
[]
The positions of the five helical repeats identified in FANCE are indicated next to the structure.
true
true
true
true
true
1,737
2
INTRODUCTION
0
null
null
17,308,347
null
Structure of human FANCE.
null
25
10,923
0
false
null
null
Structure of human FANCE.
true
true
true
true
true
1,738
2
INTRODUCTION
0
null
null
17,308,347
null
In response to DNA damage or replicative stress, the FA core complex monoubiquitinates FANCD2.
null
94
10,924
0
false
null
null
In response to DNA damage or replicative stress, the FA core complex monoubiquitinates FANCD2.
true
true
true
true
true
1,738
2
INTRODUCTION
0
null
null
17,308,347
null
The eight identified subunits of the FA complex are shown.
null
58
10,925
0
false
null
null
The eight identified subunits of the FA complex are shown.
true
true
true
true
true
1,738
2
INTRODUCTION
0
null
null
17,308,347
null
(B) Schematic representation of the domain structure of the FANCE protein.
null
74
10,926
0
false
null
null
(B) Schematic representation of the domain structure of the FANCE protein.
false
false
true
true
false
1,738
2
INTRODUCTION
0
null
null
17,308,347
null
Orange boxes represent regions of the protein that are predicted to constitute independently folded domains.
null
108
10,927
0
false
null
null
Orange boxes represent regions of the protein that are predicted to constitute independently folded domains.
true
true
true
true
true
1,738
2
INTRODUCTION
0
null
null
17,308,347
null
The two nuclear localization sequences in the middle section of the protein are drawn in black.
null
95
10,928
0
false
null
null
The two nuclear localization sequences in the middle section of the protein are drawn in black.
true
true
true
true
true
1,738
2
INTRODUCTION
0
null
null
17,308,347
null
(C) Cartoon representation of the crystal structure of amino acids 273 to 536 of human FANCE.
null
93
10,929
0
false
null
null
(C) Cartoon representation of the crystal structure of amino acids 273 to 536 of human FANCE.
false
false
true
true
false
1,738
2
INTRODUCTION
0
null
null
17,308,347
null
The protein chain is shown as a ribbon, rainbow-coloured from blue at the N-terminal end to red at the C-terminal end.
null
118
10,930
0
false
null
null
The protein chain is shown as a ribbon, rainbow-coloured from blue at the N-terminal end to red at the C-terminal end.
true
true
true
true
true
1,738
2
INTRODUCTION
0
null
null
17,308,347
null
Two views are shown, differing by a 90Β° rotation around an axis aligned to the long dimension of the molecule.
null
110
10,931
0
false
null
null
Two views are shown, differing by a 90Β° rotation around an axis aligned to the long dimension of the molecule.
true
true
true
true
true
1,738
2
INTRODUCTION
0
null
null
17,308,347
null
The alpha-helical segments in the structure are labelled, Ξ±1 to Ξ±14.
null
68
10,932
0
false
null
null
The alpha-helical segments in the structure are labelled, Ξ±1 to Ξ±14.
true
true
true
true
true
1,738
2
INTRODUCTION
0
null
null
17,308,347
null
The positions of the five helical repeats identified in FANCE are indicated next to the structure.
null
98
10,933
0
false
null
null
The positions of the five helical repeats identified in FANCE are indicated next to the structure.
true
true
true
true
true
1,738
3
INTRODUCTION
1
21
[ "B21", "B22", "B21", "B23", "B21", "B19", "B21", "B22" ]
17,308,347
pmid-12093742|pmid-16513431|pmid-12093742|pmid-15199141|pmid-12093742|pmid-16127171|pmid-12093742|pmid-16513431
FANCE is essential for FANCC accumulation in the nucleus and assembly of the FA core complex (21,22).
[ "21", "22", "21", "23", "21", "19", "21", "22" ]
101
10,934
0
false
FANCE is essential for FANCC accumulation in the nucleus and assembly of the FA core complex.
[ "21,22" ]
FANCE is essential for FANCC accumulation in the nucleus and assembly of the FA core complex.
true
true
true
true
true
1,739
3
INTRODUCTION
1
21
[ "B21", "B22", "B21", "B23", "B21", "B19", "B21", "B22" ]
17,308,347
pmid-12093742|pmid-16513431|pmid-12093742|pmid-15199141|pmid-12093742|pmid-16127171|pmid-12093742|pmid-16513431
Moreover, FANCE localizes to constitutive nuclear foci (21) and becomes associated with ubiquitinated FANCD2 and BRCA2 in a chromatin complex (23).
[ "21", "22", "21", "23", "21", "19", "21", "22" ]
147
10,935
1
false
Moreover, FANCE localizes to constitutive nuclear foci and becomes associated with ubiquitinated FANCD2 and BRCA2 in a chromatin complex.
[ "21", "23" ]
Moreover, FANCE localizes to constitutive nuclear foci and becomes associated with ubiquitinated FANCD2 and BRCA2 in a chromatin complex.
true
true
true
true
true
1,739
3
INTRODUCTION
1
21
[ "B21", "B22", "B21", "B23", "B21", "B19", "B21", "B22" ]
17,308,347
pmid-12093742|pmid-16513431|pmid-12093742|pmid-15199141|pmid-12093742|pmid-16127171|pmid-12093742|pmid-16513431
FANCE is the only member of the FA core complex for which a direct association with FANCD2 has been demonstrated (21).
[ "21", "22", "21", "23", "21", "19", "21", "22" ]
118
10,936
1
false
FANCE is the only member of the FA core complex for which a direct association with FANCD2 has been demonstrated.
[ "21" ]
FANCE is the only member of the FA core complex for which a direct association with FANCD2 has been demonstrated.
true
true
true
true
true
1,739
3
INTRODUCTION
1
21
[ "B21", "B22", "B21", "B23", "B21", "B19", "B21", "B22" ]
17,308,347
pmid-12093742|pmid-16513431|pmid-12093742|pmid-15199141|pmid-12093742|pmid-16127171|pmid-12093742|pmid-16513431
Indeed, it has been proposed that FANCE represents the essential link between the FA core complex and FANCD2 (19,21,22).
[ "21", "22", "21", "23", "21", "19", "21", "22" ]
120
10,937
0
false
Indeed, it has been proposed that FANCE represents the essential link between the FA core complex and FANCD2.
[ "19,21,22" ]
Indeed, it has been proposed that FANCE represents the essential link between the FA core complex and FANCD2.
true
true
true
true
true
1,739
4
INTRODUCTION
0
null
null
17,308,347
null
Here we describe the identification and crystallographic analysis of a large, evolutionarily conserved region of human FANCE.
null
125
10,938
0
false
null
null
Here we describe the identification and crystallographic analysis of a large, evolutionarily conserved region of human FANCE.
true
true
true
true
true
1,740
4
INTRODUCTION
0
null
null
17,308,347
null
The first structure of a FA protein reveals the presence of a repeated helical motif, which was not apparent from the analysis of its amino acid sequence and represents a structural template for other proteins defective in Fanconi Anaemia.
null
239
10,939
0
false
null
null
The first structure of a FA protein reveals the presence of a repeated helical motif, which was not apparent from the analysis of its amino acid sequence and represents a structural template for other proteins defective in Fanconi Anaemia.
true
true
true
true
true
1,740
4
INTRODUCTION
0
null
null
17,308,347
null
We demonstrate that the FANCE region defined by the structure is sufficient for interaction with FANCD2 and identify an epitope on the FANCE surface that is critical for FANCD2 binding.
null
185
10,940
0
false
null
null
We demonstrate that the FANCE region defined by the structure is sufficient for interaction with FANCD2 and identify an epitope on the FANCE surface that is critical for FANCD2 binding.
true
true
true
true
true
1,740
4
INTRODUCTION
0
null
null
17,308,347
null
Disease-associated mutations in FANCE and FANCD2 disrupt the FANCE–FANCD2 interaction, providing a structural rationale for their pathological effect in FA patients.
null
165
10,941
0
false
null
null
Disease-associated mutations in FANCE and FANCD2 disrupt the FANCE–FANCD2 interaction, providing a structural rationale for their pathological effect in FA patients.
true
true
true
true
true
1,740
0
DISCUSSION
0
null
null
17,308,347
pmid-16493006|pmid-16822457|pmid-11389461|pmid-16675878|pmid-16859679|pmid-15935541
Here we have described the crystal structure of a large, evolutionarily conserved region of FANCE, an essential component of the FA pathway of DNA repair.
null
154
10,942
0
false
null
null
Here we have described the crystal structure of a large, evolutionarily conserved region of FANCE, an essential component of the FA pathway of DNA repair.
true
true
true
true
true
1,741
0
DISCUSSION
0
null
null
17,308,347
pmid-16493006|pmid-16822457|pmid-11389461|pmid-16675878|pmid-16859679|pmid-15935541
The structure reveals a non-globular, solenoidal conformation assembled by tandem repeats of a short helical motif.
null
115
10,943
0
false
null
null
The structure reveals a non-globular, solenoidal conformation assembled by tandem repeats of a short helical motif.
true
true
true
true
true
1,741
0
DISCUSSION
0
null
null
17,308,347
pmid-16493006|pmid-16822457|pmid-11389461|pmid-16675878|pmid-16859679|pmid-15935541
Remarkably, FANCE folding requires only general conservation of amino acid type at a small set of repeat positions, which makes detection of such a motif difficult and explains why its presence had not been noted before.
null
220
10,944
0
false
null
null
Remarkably, FANCE folding requires only general conservation of amino acid type at a small set of repeat positions, which makes detection of such a motif difficult and explains why its presence had not been noted before.
true
true
true
true
true
1,741
0
DISCUSSION
0
null
null
17,308,347
pmid-16493006|pmid-16822457|pmid-11389461|pmid-16675878|pmid-16859679|pmid-15935541
Packing in the hydrophobic core of helical repeat proteins relies on aliphatic side chains of hydrophobic residues, such as leucine.
null
132
10,945
0
false
null
null
Packing in the hydrophobic core of helical repeat proteins relies on aliphatic side chains of hydrophobic residues, such as leucine.
true
true
true
true
true
1,741
0
DISCUSSION
0
null
null
17,308,347
pmid-16493006|pmid-16822457|pmid-11389461|pmid-16675878|pmid-16859679|pmid-15935541
The structure of the FANCE protein therefore provides a rationale for the high leucine content of its sequence and suggests that other FA proteins rich in leucines will adopt a comparable fold.
null
193
10,946
0
false
null
null
The structure of the FANCE protein therefore provides a rationale for the high leucine content of its sequence and suggests that other FA proteins rich in leucines will adopt a comparable fold.
true
true
true
true
true
1,741
1
DISCUSSION
1
37
[ "B37" ]
17,308,347
pmid-16377561|pmid-12973351|pmid-14712086|NA|pmid-16153896|pmid-16116422|pmid-16116434|pmid-11157805|pmid-11239454|pmid-11239454|pmid-12239151|pmid-15115758|pmid-16720839|pmid-16127171|pmid-16168378|pmid-15537541
Multiple arrays of short helical motifs have evolved as a convenient protein architecture in order to mediate protein–protein association.
[ "37" ]
138
10,947
0
false
Multiple arrays of short helical motifs have evolved as a convenient protein architecture in order to mediate protein–protein association.
[]
Multiple arrays of short helical motifs have evolved as a convenient protein architecture in order to mediate protein–protein association.
true
true
true
true
true
1,742
1
DISCUSSION
1
37
[ "B37" ]
17,308,347
pmid-16377561|pmid-12973351|pmid-14712086|NA|pmid-16153896|pmid-16116422|pmid-16116434|pmid-11157805|pmid-11239454|pmid-11239454|pmid-12239151|pmid-15115758|pmid-16720839|pmid-16127171|pmid-16168378|pmid-15537541
Indeed, helical repeat proteins are usually involved in constitutive or regulated interactions as part of binary or multi-subunit complexes; a cogent example is the regulation of the SCF multi-subunit ubiquitin ligase complex by the HEAT-repeat protein Cand1 (37).
[ "37" ]
264
10,948
1
false
Indeed, helical repeat proteins are usually involved in constitutive or regulated interactions as part of binary or multi-subunit complexes; a cogent example is the regulation of the SCF multi-subunit ubiquitin ligase complex by the HEAT-repeat protein Cand1.
[ "37" ]
Indeed, helical repeat proteins are usually involved in constitutive or regulated interactions as part of binary or multi-subunit complexes; a cogent example is the regulation of the SCF multi-subunit ubiquitin ligase complex by the HEAT-repeat protein Cand1.
true
true
true
true
true
1,742
1
DISCUSSION
1
37
[ "B37" ]
17,308,347
pmid-16377561|pmid-12973351|pmid-14712086|NA|pmid-16153896|pmid-16116422|pmid-16116434|pmid-11157805|pmid-11239454|pmid-11239454|pmid-12239151|pmid-15115758|pmid-16720839|pmid-16127171|pmid-16168378|pmid-15537541
A tertiary structure based on arrays of helical repeats, such as that observed in FANCE, would therefore be well suited to the function of the FA proteins, which take part in a complex web of constitutive and regulatory interactions within and outside the FA core complex.
[ "37" ]
272
10,949
0
false
A tertiary structure based on arrays of helical repeats, such as that observed in FANCE, would therefore be well suited to the function of the FA proteins, which take part in a complex web of constitutive and regulatory interactions within and outside the FA core complex.
[]
A tertiary structure based on arrays of helical repeats, such as that observed in FANCE, would therefore be well suited to the function of the FA proteins, which take part in a complex web of constitutive and regulatory interactions within and outside the FA core complex.
true
true
true
true
true
1,742
2
DISCUSSION
0
null
null
17,308,347
null
Our data indicate that the region of FANCE defined by the crystallographic analysis is sufficient for interaction with FANCD2.
null
126
10,950
0
false
null
null
Our data indicate that the region of FANCE defined by the crystallographic analysis is sufficient for interaction with FANCD2.
true
true
true
true
true
1,743
2
DISCUSSION
0
null
null
17,308,347
null
Our results therefore provide insight into the process of FANCD2 association with the FA core complex, a necessary step in the activation of the FA pathway of DNA repair.
null
170
10,951
0
false
null
null
Our results therefore provide insight into the process of FANCD2 association with the FA core complex, a necessary step in the activation of the FA pathway of DNA repair.
true
true
true
true
true
1,743
2
DISCUSSION
0
null
null
17,308,347
null
Taken together with the existing evidence concerning the interaction of FANCE with FANCC and FANCD2, our finding of a large soluble segment of FANCE able of independent binding to FANCD2, but not to FANCC, suggests a model of FANCE function.
null
241
10,952
0
false
null
null
Taken together with the existing evidence concerning the interaction of FANCE with FANCC and FANCD2, our finding of a large soluble segment of FANCE able of independent binding to FANCD2, but not to FANCC, suggests a model of FANCE function.
true
true
true
true
true
1,743
2
DISCUSSION
0
null
null
17,308,347
null
In the model, FANCE would be anchored to the FA core complex through a constitutive interaction with FANCC, whereas the C-terminal region of FANCE identified here would be free of contacts with the rest of the core complex and poised to interact with FANCD2 in a regulated way.
null
277
10,953
0
false
null
null
In the model, FANCE would be anchored to the FA core complex through a constitutive interaction with FANCC, whereas the C-terminal region of FANCE identified here would be free of contacts with the rest of the core complex and poised to interact with FANCD2 in a regulated way.
true
true
true
true
true
1,743
2
DISCUSSION
0
null
null
17,308,347
null
Furthermore, our bioinformatic and experimental analysis defines an epitope on the FANCE surface that is critical for FANCD2 binding.
null
133
10,954
0
false
null
null
Furthermore, our bioinformatic and experimental analysis defines an epitope on the FANCE surface that is critical for FANCD2 binding.
true
true
true
true
true
1,743
2
DISCUSSION
0
null
null
17,308,347
null
In principle, the development of small molecules designed to disrupt the FANCE–FANCD2 interface could be useful in tumour therapy based on DNA cross-linking agents.
null
164
10,955
0
false
null
null
In principle, the development of small molecules designed to disrupt the FANCE–FANCD2 interface could be useful in tumour therapy based on DNA cross-linking agents.
true
true
true
true
true
1,743
3
DISCUSSION
0
null
null
17,308,347
pmid-12093742|pmid-16513431|pmid-12093742|pmid-15199141|pmid-12093742|pmid-16127171|pmid-12093742|pmid-16513431
In summary, the work described here represents an important first step in the structural rationalization of the molecular processes involved in FA.
null
147
10,956
0
false
null
null
In summary, the work described here represents an important first step in the structural rationalization of the molecular processes involved in FA.
true
true
true
true
true
1,744
3
DISCUSSION
0
null
null
17,308,347
pmid-12093742|pmid-16513431|pmid-12093742|pmid-15199141|pmid-12093742|pmid-16127171|pmid-12093742|pmid-16513431
Although the FANCE–FANCD2 interaction is clearly essential, it is one example of a set of concomitant binary interactions that result in FANCD2 monoubiquitination.
null
163
10,957
0
false
null
null
Although the FANCE–FANCD2 interaction is clearly essential, it is one example of a set of concomitant binary interactions that result in FANCD2 monoubiquitination.
true
true
true
true
true
1,744
3
DISCUSSION
0
null
null
17,308,347
pmid-12093742|pmid-16513431|pmid-12093742|pmid-15199141|pmid-12093742|pmid-16127171|pmid-12093742|pmid-16513431
Future research will investigate the structural basis for the interactions between FANCE, FANCD2 and the other components of the FA core complex that are necessary in order to activate the FA pathway of DNA repair.
null
214
10,958
0
false
null
null
Future research will investigate the structural basis for the interactions between FANCE, FANCD2 and the other components of the FA core complex that are necessary in order to activate the FA pathway of DNA repair.
true
true
true
true
true
1,744
4
DISCUSSION
0
null
null
17,308,347
null
NOTE ADDED IN PROOF
null
19
10,959
0
false
null
null
NOTE ADDED IN PROOF
true
true
false
true
false
1,745
4
DISCUSSION
0
null
null
17,308,347
null
Whilst our manuscript was in production, a structural analysis of the human FANCF protein appeared in print (Kowal, P., Gurtan, A.M., Stuckert, P., D'Andrea, A.D., and Ellenberger, T. (2007) Structural determinants of human FANCF protein that function in the assembly of a DNA damage signalling complex J. Biol.
null
311
10,960
0
false
null
null
Whilst our manuscript was in production, a structural analysis of the human FANCF protein appeared in print (Kowal, P., Gurtan, A.M., Stuckert, P., D'Andrea, A.D., and Ellenberger, T. (2007) Structural determinants of human FANCF protein that function in the assembly of a DNA damage signalling complex J. Biol.
true
true
true
true
true
1,745
4
DISCUSSION
0
null
null
17,308,347
null
Chem., 282, 2047-2055).
null
23
10,961
0
false
null
null
Chem., 282, 2047-2055).
true
true
true
true
true
1,745
4
DISCUSSION
0
null
null
17,308,347
null
The study shows that the C-terminal domain of FANCF folds into a solenoid comprised of repeated helical hairpins, in agreement with our prediction about the widespread adoption of this structural motif among Fanconi Anaemia proteins.
null
233
10,962
0
false
null
null
The study shows that the C-terminal domain of FANCF folds into a solenoid comprised of repeated helical hairpins, in agreement with our prediction about the widespread adoption of this structural motif among Fanconi Anaemia proteins.
true
true
true
true
true
1,745
0
INTRODUCTION
1
1
[ "b1", "b2", "b3" ]
17,145,717
NA|pmid-13619786|pmid-16118666
The standard sequence-to-structure-to-function paradigm for proteins assumes that each protein first folds into a three-dimensional (3D) structure and that the resulting structure enables function via the lock and key (1) or the induced fit (2) models.
[ "1", "2", "3" ]
252
10,963
1
false
The standard sequence-to-structure-to-function paradigm for proteins assumes that each protein first folds into a three-dimensional structure and that the resulting structure enables function via the lock and key or the induced fit models.
[ "3D", "1", "2" ]
The standard sequence-to-structure-to-function paradigm for proteins assumes that each protein first folds into a three-dimensional structure and that the resulting structure enables function via the lock and key or the induced fit models.
true
true
true
true
true
1,746
0
INTRODUCTION
1
1
[ "b1", "b2", "b3" ]
17,145,717
NA|pmid-13619786|pmid-16118666
Enzymes and their functions, which were traditionally the focus of studies in biochemistry, provided the basis for the lock and key and induced fit models; hence, as expected these models generally and perhaps universally explain enzymatic function.
[ "1", "2", "3" ]
249
10,964
0
false
Enzymes and their functions, which were traditionally the focus of studies in biochemistry, provided the basis for the lock and key and induced fit models; hence, as expected these models generally and perhaps universally explain enzymatic function.
[]
Enzymes and their functions, which were traditionally the focus of studies in biochemistry, provided the basis for the lock and key and induced fit models; hence, as expected these models generally and perhaps universally explain enzymatic function.
true
true
true
true
true
1,746
0
INTRODUCTION
1
3
[ "b1", "b2", "b3" ]
17,145,717
NA|pmid-13619786|pmid-16118666
One reflection of the intimate relationship between protein structure and catalytic function is the relatively higher coverage of enzymes in the Protein Data Bank (PDB) as compared with other protein types (3).
[ "1", "2", "3" ]
210
10,965
1
false
One reflection of the intimate relationship between protein structure and catalytic function is the relatively higher coverage of enzymes in the Protein Data Bank (PDB) as compared with other protein types.
[ "3" ]
One reflection of the intimate relationship between protein structure and catalytic function is the relatively higher coverage of enzymes in the Protein Data Bank (PDB) as compared with other protein types.
true
true
true
true
true
1,746
1
INTRODUCTION
1
4
[ "b4", "b8" ]
17,145,717
NA|NA
Non-catalytic protein functions relating to signaling, regulation and control, such as protein–protein interactions, protein–DNA interactions, protein–RNA interactions, post-translational modifications and linker activities to name a few, are increasingly being studied.
[ "4", "8" ]
270
10,966
0
false
Non-catalytic protein functions relating to signaling, regulation and control, such as protein–protein interactions, protein–DNA interactions, protein–RNA interactions, post-translational modifications and linker activities to name a few, are increasingly being studied.
[]
Non-catalytic protein functions relating to signaling, regulation and control, such as protein–protein interactions, protein–DNA interactions, protein–RNA interactions, post-translational modifications and linker activities to name a few, are increasingly being studied.
true
true
true
true
true
1,747
1
INTRODUCTION
1
4
[ "b4", "b8" ]
17,145,717
NA|NA
Many of these non-catalytic functions have been suggested to depend on, or have been experimentally demonstrated to depend on, proteins that lack fixed 3D structure, with interesting publications on this topic dating up to 70 years ago (4–8).
[ "4", "8" ]
242
10,967
0
false
Many of these non-catalytic functions have been suggested to depend on, or have been experimentally demonstrated to depend on, proteins that lack fixed 3D structure, with interesting publications on this topic dating up to 70 years ago.
[ "4–8" ]
Many of these non-catalytic functions have been suggested to depend on, or have been experimentally demonstrated to depend on, proteins that lack fixed 3D structure, with interesting publications on this topic dating up to 70 years ago.
true
true
true
true
true
1,747
2
INTRODUCTION
1
9
[ "b9", "b10", "b11", "b12" ]
17,145,717
NA|pmid-8901511|pmid-10550212|pmid-12022860|pmid-12022860|pmid-12368089
Functional proteins that lack the relatively fixed structure of enzymes and other globular proteins have been called β€˜rheomormorphic’ (9), β€˜natively unfolded’ (10), β€˜intrinsically unstructured’ (11) and β€˜natively or intrinsically disordered’ (12), among other terms.
[ "9", "10", "11", "12" ]
266
10,968
1
false
Functional proteins that lack the relatively fixed structure of enzymes and other globular proteins have been called β€˜rheomormorphic’, β€˜natively unfolded’, β€˜intrinsically unstructured’ and β€˜natively or intrinsically disordered’, among other terms.
[ "9", "10", "11", "12" ]
Functional proteins that lack the relatively fixed structure of enzymes and other globular proteins have been called β€˜rheomormorphic’, β€˜natively unfolded’, β€˜intrinsically unstructured’ and β€˜natively or intrinsically disordered’, among other terms.
true
true
true
true
true
1,748
2
INTRODUCTION
1
9
[ "b9", "b10", "b11", "b12" ]
17,145,717
NA|pmid-8901511|pmid-10550212|pmid-12022860|pmid-12022860|pmid-12368089
These proteins or protein regions exist as interconverting, dynamic ensembles of structures instead of folding into a single structure and many of their signaling or regulatory functions depend on their highly flexible nature.
[ "9", "10", "11", "12" ]
226
10,969
0
false
These proteins or protein regions exist as interconverting, dynamic ensembles of structures instead of folding into a single structure and many of their signaling or regulatory functions depend on their highly flexible nature.
[]
These proteins or protein regions exist as interconverting, dynamic ensembles of structures instead of folding into a single structure and many of their signaling or regulatory functions depend on their highly flexible nature.
true
true
true
true
true
1,748
3
INTRODUCTION
1
13
[ "b13", "b14", "b16" ]
17,145,717
pmid-9230460|pmid-2550456|pmid-15723043|pmid-16935303|pmid-15321724|pmid-16935303|pmid-16131486|pmid-16110343|pmid-16444738|pmid-15111064
Conformational flexibility facilitates a number of post-translational modifications, such as phosphorylation (13) and ubiquitination (14–16) for example, possibly because similar sequence segments in different proteins can use this flexibility to conform to the active sites of the modifying enzymes.
[ "13", "14", "16" ]
300
10,970
1
false
Conformational flexibility facilitates a number of post-translational modifications, such as phosphorylation and ubiquitination for example, possibly because similar sequence segments in different proteins can use this flexibility to conform to the active sites of the modifying enzymes.
[ "13", "14–16" ]
Conformational flexibility facilitates a number of post-translational modifications, such as phosphorylation and ubiquitination for example, possibly because similar sequence segments in different proteins can use this flexibility to conform to the active sites of the modifying enzymes.
true
true
true
true
true
1,749
4
INTRODUCTION
1
17
[ "b17", "b21", "b22", "b8" ]
17,145,717
pmid-9405336|pmid-15943979|pmid-8303294|NA|pmid-12824381|pmid-15943979|pmid-12824383|pmid-12824381
Many protein-binding interactions important for signaling and regulation involve modular binding domains that often associate with rather short linear motifs (17–21).
[ "17", "21", "22", "8" ]
166
10,971
0
false
Many protein-binding interactions important for signaling and regulation involve modular binding domains that often associate with rather short linear motifs.
[ "17–21" ]
Many protein-binding interactions important for signaling and regulation involve modular binding domains that often associate with rather short linear motifs.
true
true
true
true
true
1,750
4
INTRODUCTION
1
17
[ "b17", "b21", "b22", "b8" ]
17,145,717
pmid-9405336|pmid-15943979|pmid-8303294|NA|pmid-12824381|pmid-15943979|pmid-12824383|pmid-12824381
In many cases, these interactions involve disorder-to-order transitions for at least one of the partners.
[ "17", "21", "22", "8" ]
105
10,972
0
false
In many cases, these interactions involve disorder-to-order transitions for at least one of the partners.
[]
In many cases, these interactions involve disorder-to-order transitions for at least one of the partners.
true
true
true
true
true
1,750
4
INTRODUCTION
1
22
[ "b17", "b21", "b22", "b8" ]
17,145,717
pmid-9405336|pmid-15943979|pmid-8303294|NA|pmid-12824381|pmid-15943979|pmid-12824383|pmid-12824381
Such complex formation by coupled folding and binding (22) provides an important mechanism for achieving both high specificity and low affinity (8), which is an ideal combination for signaling and regulation.
[ "17", "21", "22", "8" ]
208
10,973
1
false
Such complex formation by coupled folding and binding provides an important mechanism for achieving both high specificity and low affinity, which is an ideal combination for signaling and regulation.
[ "22", "8" ]
Such complex formation by coupled folding and binding provides an important mechanism for achieving both high specificity and low affinity, which is an ideal combination for signaling and regulation.
true
true
true
true
true
1,750
5
INTRODUCTION
1
24
[ "b4", "b6", "b23", "b24" ]
17,145,717
NA|NA|pmid-8876165|pmid-16444738
Not only can individual disordered proteins and regions bind to multiple partners (4–6,23), but also multiple disordered sequences can each adapt to fit one partner (24).
[ "4", "6", "23", "24" ]
170
10,974
1
false
Not only can individual disordered proteins and regions bind to multiple partners, but also multiple disordered sequences can each adapt to fit one partner.
[ "4–6,23", "24" ]
Not only can individual disordered proteins and regions bind to multiple partners, but also multiple disordered sequences can each adapt to fit one partner.
true
true
true
true
true
1,751
5
INTRODUCTION
1
4
[ "b4", "b6", "b23", "b24" ]
17,145,717
NA|NA|pmid-8876165|pmid-16444738
These partnering abilities of disordered proteins suggest their importance and common usage in protein interaction and signaling networks.
[ "4", "6", "23", "24" ]
138
10,975
0
false
These partnering abilities of disordered proteins suggest their importance and common usage in protein interaction and signaling networks.
[]
These partnering abilities of disordered proteins suggest their importance and common usage in protein interaction and signaling networks.
true
true
true
true
true
1,751
6
INTRODUCTION
1
7
[ "b7" ]
17,145,717
pmid-591912
Some biological functions involve the flexibility itself, one important example being the ball and chain model for inactivation of voltage-gated ion channels (7).
[ "7" ]
162
10,976
1
false
Some biological functions involve the flexibility itself, one important example being the ball and chain model for inactivation of voltage-gated ion channels.
[ "7" ]
Some biological functions involve the flexibility itself, one important example being the ball and chain model for inactivation of voltage-gated ion channels.
true
true
true
true
true
1,752
6
INTRODUCTION
1
7
[ "b7" ]
17,145,717
pmid-591912
Often the flexibility of disordered regions provides a linker function to enable structured (or unstructured) functional domains to move relative to each other, which can lead to enhanced affinity.
[ "7" ]
197
10,977
0
false
Often the flexibility of disordered regions provides a linker function to enable structured (or unstructured) functional domains to move relative to each other, which can lead to enhanced affinity.
[]
Often the flexibility of disordered regions provides a linker function to enable structured (or unstructured) functional domains to move relative to each other, which can lead to enhanced affinity.
true
true
true
true
true
1,752
7
INTRODUCTION
0
null
null
17,145,717
null
The experimental data describing intrinsically disordered proteins (IDPs) are growing rapidly due in part to the increasing interest in signaling, regulation and control.
null
170
10,978
0
false
null
null
The experimental data describing intrinsically disordered proteins (IDPs) are growing rapidly due in part to the increasing interest in signaling, regulation and control.
true
true
true
true
true
1,753
7
INTRODUCTION
0
null
null
17,145,717
null
The rapidly increasing number of IDP examples has generated the need for a publicly accessible repository.
null
106
10,979
0
false
null
null
The rapidly increasing number of IDP examples has generated the need for a publicly accessible repository.
true
true
true
true
true
1,753
7
INTRODUCTION
0
null
null
17,145,717
null
To facilitate efficient management and annotation of IDP information, the Database of Disordered Proteins (DisProt) was created.
null
128
10,980
0
false
null
null
To facilitate efficient management and annotation of IDP information, the Database of Disordered Proteins (DisProt) was created.
true
true
true
true
true
1,753
7
INTRODUCTION
0
null
null
17,145,717
null
As of Release 3.4 (August 15, 2006), DisProt contained 460 IDPs and 1103 disordered regions, encompassing 35 functional categoriesβ€”all based on published experimental data.
null
172
10,981
0
false
null
null
As of Release 3.4 (August 15, 2006), DisProt contained 460 IDPs and 1103 disordered regions, encompassing 35 functional categoriesβ€”all based on published experimental data.
true
true
true
true
true
1,753
0
DISCUSSION
0
null
null
17,145,717
NA|pmid-13619786|pmid-16118666
DisProt is the central repository for structure–function annotations associated with protein intrinsic disorder.
null
112
10,982
0
false
null
null
DisProt is the central repository for structure–function annotations associated with protein intrinsic disorder.
true
true
true
true
true
1,754
0
DISCUSSION
0
null
null
17,145,717
NA|pmid-13619786|pmid-16118666
The database has been used by researchers from over 35 countries worldwide.
null
75
10,983
0
false
null
null
The database has been used by researchers from over 35 countries worldwide.
true
true
true
true
true
1,754
0
DISCUSSION
0
null
null
17,145,717
NA|pmid-13619786|pmid-16118666
These users are involved in many branches of protein science and are from a variety of different organization types, including academic, industry and government.
null
161
10,984
0
false
null
null
These users are involved in many branches of protein science and are from a variety of different organization types, including academic, industry and government.
true
true
true
true
true
1,754
1
DISCUSSION
0
null
null
17,145,717
NA|NA
Interest in IDPs is growing rapidly.
null
36
10,985
0
false
null
null
Interest in IDPs is growing rapidly.
true
true
true
true
true
1,755
1
DISCUSSION
0
null
null
17,145,717
NA|NA
The nearly 450 papers published in 2005 is about twice the number published in 2004, and the number of papers in 2006, although the year is not complete as of this writing, shows clear evidence of a continued rapid rise (Figure 2).
null
231
10,986
0
false
null
null
The nearly 450 papers published in 2005 is about twice the number published in 2004, and the number of papers in 2006, although the year is not complete as of this writing, shows clear evidence of a continued rapid rise (Figure 2).
true
true
true
true
true
1,755
1
DISCUSSION
0
null
null
17,145,717
NA|NA
Because inconsistent nomenclature is used to describe these proteins, the bibliography in DisProt is very useful to researchers in this rapidly growing field.
null
158
10,987
0
false
null
null
Because inconsistent nomenclature is used to describe these proteins, the bibliography in DisProt is very useful to researchers in this rapidly growing field.
true
true
true
true
true
1,755
1
DISCUSSION
0
null
null
17,145,717
NA|NA
The rapid growth of disorder-related publications argues for the importance of having an organized database such as DisProt.
null
124
10,988
0
false
null
null
The rapid growth of disorder-related publications argues for the importance of having an organized database such as DisProt.
true
true
true
true
true
1,755
1
DISCUSSION
0
null
null
17,145,717
NA|NA
Researchers who study IDPs are encouraged to look over this bibliography and to send us the citations of papers that we have missed.
null
132
10,989
0
false
null
null
Researchers who study IDPs are encouraged to look over this bibliography and to send us the citations of papers that we have missed.
true
true
true
true
true
1,755
2
DISCUSSION
1
12
[ "b12", "b30" ]
17,145,717
NA|pmid-8901511|pmid-10550212|pmid-12022860|pmid-12022860|pmid-12368089
Our initial attempt to identify disorder-function relationships led to 28 specific functions that we grouped into four classes (12).
[ "12", "30" ]
132
10,990
1
false
Our initial attempt to identify disorder-function relationships led to 28 specific functions that we grouped into four classes.
[ "12" ]
Our initial attempt to identify disorder-function relationships led to 28 specific functions that we grouped into four classes.
true
true
true
true
true
1,756
2
DISCUSSION
1
30
[ "b12", "b30" ]
17,145,717
NA|pmid-8901511|pmid-10550212|pmid-12022860|pmid-12022860|pmid-12368089
A different schema was proposed at about the same time that led to additional functions being added (30).
[ "12", "30" ]
105
10,991
1
false
A different schema was proposed at about the same time that led to additional functions being added.
[ "30" ]
A different schema was proposed at about the same time that led to additional functions being added.
true
true
true
true
true
1,756
2
DISCUSSION
1
12
[ "b12", "b30" ]
17,145,717
NA|pmid-8901511|pmid-10550212|pmid-12022860|pmid-12022860|pmid-12368089
The 7 and 35 functional classes and subclasses, respectfully, in the current DisProt came mostly from these prior publications, but with a number of additions that were discovered during the process of annotating proteins.
[ "12", "30" ]
222
10,992
0
false
The 7 and 35 functional classes and subclasses, respectfully, in the current DisProt came mostly from these prior publications, but with a number of additions that were discovered during the process of annotating proteins.
[]
The 7 and 35 functional classes and subclasses, respectfully, in the current DisProt came mostly from these prior publications, but with a number of additions that were discovered during the process of annotating proteins.
true
true
true
true
true
1,756
3
DISCUSSION
1
31
[ "b31", "b32", "b31", "b33", "b34", "b24", "b35" ]
17,145,717
pmid-9230460|pmid-2550456|pmid-15723043|pmid-16935303|pmid-15321724|pmid-16935303|pmid-16131486|pmid-16110343|pmid-16444738|pmid-15111064
A major usage of intrinsic disorder is for molecular recognition and binding.
[ "31", "32", "31", "33", "34", "24", "35" ]
77
10,993
0
false
A major usage of intrinsic disorder is for molecular recognition and binding.
[]
A major usage of intrinsic disorder is for molecular recognition and binding.
true
true
true
true
true
1,757
3
DISCUSSION
1
31
[ "b31", "b32", "b31", "b33", "b34", "b24", "b35" ]
17,145,717
pmid-9230460|pmid-2550456|pmid-15723043|pmid-16935303|pmid-15321724|pmid-16935303|pmid-16131486|pmid-16110343|pmid-16444738|pmid-15111064
A search of the PDB for short segments called molecular recognition features, MoRFs, was carried out.
[ "31", "32", "31", "33", "34", "24", "35" ]
101
10,994
0
false
A search of the PDB for short segments called molecular recognition features, MoRFs, was carried out.
[]
A search of the PDB for short segments called molecular recognition features, MoRFs, was carried out.
true
true
true
true
true
1,757
3
DISCUSSION
1
31
[ "b31", "b32", "b31", "b33", "b34", "b24", "b35" ]
17,145,717
pmid-9230460|pmid-2550456|pmid-15723043|pmid-16935303|pmid-15321724|pmid-16935303|pmid-16131486|pmid-16110343|pmid-16444738|pmid-15111064
MoRFs undergo disorder-to-order transitions upon binding to their partners, which typically have globular structure.
[ "31", "32", "31", "33", "34", "24", "35" ]
116
10,995
0
false
MoRFs undergo disorder-to-order transitions upon binding to their partners, which typically have globular structure.
[]
MoRFs undergo disorder-to-order transitions upon binding to their partners, which typically have globular structure.
true
true
true
true
true
1,757
3
DISCUSSION
1
31
[ "b31", "b32", "b31", "b33", "b34", "b24", "b35" ]
17,145,717
pmid-9230460|pmid-2550456|pmid-15723043|pmid-16935303|pmid-15321724|pmid-16935303|pmid-16131486|pmid-16110343|pmid-16444738|pmid-15111064
This search yielded 1261 MoRFs that were clustered into 372 sets on the basis of high-sequence identity among members of a given set (31).
[ "31", "32", "31", "33", "34", "24", "35" ]
138
10,996
1
false
This search yielded 1261 MoRFs that were clustered into 372 sets on the basis of high-sequence identity among members of a given set.
[ "31" ]
This search yielded 1261 MoRFs that were clustered into 372 sets on the basis of high-sequence identity among members of a given set.
true
true
true
true
true
1,757
3
DISCUSSION
1
31
[ "b31", "b32", "b31", "b33", "b34", "b24", "b35" ]
17,145,717
pmid-9230460|pmid-2550456|pmid-15723043|pmid-16935303|pmid-15321724|pmid-16935303|pmid-16131486|pmid-16110343|pmid-16444738|pmid-15111064
Many of these MoRFs have experimental data supporting disorder-to-order transitions upon binding.
[ "31", "32", "31", "33", "34", "24", "35" ]
97
10,997
0
false
Many of these MoRFs have experimental data supporting disorder-to-order transitions upon binding.
[]
Many of these MoRFs have experimental data supporting disorder-to-order transitions upon binding.
true
true
true
true
true
1,757
3
DISCUSSION
1
31
[ "b31", "b32", "b31", "b33", "b34", "b24", "b35" ]
17,145,717
pmid-9230460|pmid-2550456|pmid-15723043|pmid-16935303|pmid-15321724|pmid-16935303|pmid-16131486|pmid-16110343|pmid-16444738|pmid-15111064
In addition, proteins that undergo disorder-to-order transitions upon complex formation are distinguishable from globular proteins that associate with one another.
[ "31", "32", "31", "33", "34", "24", "35" ]
163
10,998
0
false
In addition, proteins that undergo disorder-to-order transitions upon complex formation are distinguishable from globular proteins that associate with one another.
[]
In addition, proteins that undergo disorder-to-order transitions upon complex formation are distinguishable from globular proteins that associate with one another.
true
true
true
true
true
1,757
3
DISCUSSION
1
32
[ "b31", "b32", "b31", "b33", "b34", "b24", "b35" ]
17,145,717
pmid-9230460|pmid-2550456|pmid-15723043|pmid-16935303|pmid-15321724|pmid-16935303|pmid-16131486|pmid-16110343|pmid-16444738|pmid-15111064
The disorder-based complexes have larger monomer surface areas and larger interaction surface areas as compared to interacting globular proteins (32).
[ "31", "32", "31", "33", "34", "24", "35" ]
150
10,999
1
false
The disorder-based complexes have larger monomer surface areas and larger interaction surface areas as compared to interacting globular proteins.
[ "32" ]
The disorder-based complexes have larger monomer surface areas and larger interaction surface areas as compared to interacting globular proteins.
true
true
true
true
true
1,757