Datasets:
vgainullin
/
xciting_data

Dataset card Data Studio Files
xet
 Community
1
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int64
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2
INTRODUCTION
1
8
[ "b13", "b13", "b8", "b17" ]
17,130,153
pmid-11467933|pmid-11467933|pmid-11896624|pmid-16114885
Even some A/C mismatches are refractory to cleavage when located in a G/C rich sequence context, as exemplified in the G13D mutation in K-ras (8).
[ "13", "13", "8", "17" ]
146
5,800
1
false
Even some A/C mismatches are refractory to cleavage when located in a G/C rich sequence context, as exemplified in the G13D mutation in K-ras.
[ "8" ]
Even some A/C mismatches are refractory to cleavage when located in a G/C rich sequence context, as exemplified in the G13D mutation in K-ras.
true
true
true
true
true
965
2
INTRODUCTION
1
13
[ "b13", "b13", "b8", "b17" ]
17,130,153
pmid-11467933|pmid-11467933|pmid-11896624|pmid-16114885
Identification of endo V variants that can cleave C-containing mismatches will broaden the applicability of the endo V/ligase mutation scanning technique.
[ "13", "13", "8", "17" ]
154
5,801
0
false
Identification of endo V variants that can cleave C-containing mismatches will broaden the applicability of the endo V/ligase mutation scanning technique.
[]
Identification of endo V variants that can cleave C-containing mismatches will broaden the applicability of the endo V/ligase mutation scanning technique.
true
true
true
true
true
965
2
INTRODUCTION
1
17
[ "b13", "b13", "b8", "b17" ]
17,130,153
pmid-11467933|pmid-11467933|pmid-11896624|pmid-16114885
Although an endo V–DNA complex structure is not available, an extensive site-directed mutagenesis analysis has identified motifs and specific amino acid residues that influence base recognition and DNA–protein interactions (17).
[ "13", "13", "8", "17" ]
228
5,802
1
false
Although an endo V–DNA complex structure is not available, an extensive site-directed mutagenesis analysis has identified motifs and specific amino acid residues that influence base recognition and DNA–protein interactions.
[ "17" ]
Although an endo V–DNA complex structure is not available, an extensive site-directed mutagenesis analysis has identified motifs and specific amino acid residues that influence base recognition and DNA–protein interactions.
true
true
true
true
true
965
2
INTRODUCTION
1
13
[ "b13", "b13", "b8", "b17" ]
17,130,153
pmid-11467933|pmid-11467933|pmid-11896624|pmid-16114885
Taking advantage of a battery of over 60 endo V single-site mutants previously isolated, we screened for and identified endo V variants that possessed altered base preference in mismatch cleavage.
[ "13", "13", "8", "17" ]
196
5,803
0
false
Taking advantage of a battery of over 60 endo V single-site mutants previously isolated, we screened for and identified endo V variants that possessed altered base preference in mismatch cleavage.
[]
Taking advantage of a battery of over 60 endo V single-site mutants previously isolated, we screened for and identified endo V variants that possessed altered base preference in mismatch cleavage.
true
true
true
true
true
965
2
INTRODUCTION
1
13
[ "b13", "b13", "b8", "b17" ]
17,130,153
pmid-11467933|pmid-11467933|pmid-11896624|pmid-16114885
Y80A in motif III converted endo V to essentially a C-specific mismatch cleavage variant that was capable of nicking refractory A/C mismatches in the K-ras gene.
[ "13", "13", "8", "17" ]
161
5,804
0
false
Y80A in motif III converted endo V to essentially a C-specific mismatch cleavage variant that was capable of nicking refractory A/C mismatches in the K-ras gene.
[]
Y80A in motif III converted endo V to essentially a C-specific mismatch cleavage variant that was capable of nicking refractory A/C mismatches in the K-ras gene.
true
true
true
true
true
965
0
INTRODUCTION
1
1
[ "b1", "b3", "b2", "b4", "b5", "b6", "b2", "b4", "b5", "b7", "b8", "b14", "b15", "b16", "b17", "b18" ]
17,135,210
pmid-10916158|pmid-15168696|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11421359|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11967553|pmid-2137203|pmid-10485881|pmid-1331983|pmid-7988565|pmid-9858550|pmid-12114529|pmid-8769651|pmid-9660929|pmid-9660960
In higher eukaryotes, alternative pre-mRNA splicing is used as a common pathway to regulate the expression of genes (1–3).
[ "1", "3", "2", "4", "5", "6", "2", "4", "5", "7", "8", "14", "15", "16", "17", "18" ]
122
5,805
0
false
In higher eukaryotes, alternative pre-mRNA splicing is used as a common pathway to regulate the expression of genes.
[ "1–3" ]
In higher eukaryotes, alternative pre-mRNA splicing is used as a common pathway to regulate the expression of genes.
true
true
true
true
true
966
0
INTRODUCTION
1
1
[ "b1", "b3", "b2", "b4", "b5", "b6", "b2", "b4", "b5", "b7", "b8", "b14", "b15", "b16", "b17", "b18" ]
17,135,210
pmid-10916158|pmid-15168696|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11421359|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11967553|pmid-2137203|pmid-10485881|pmid-1331983|pmid-7988565|pmid-9858550|pmid-12114529|pmid-8769651|pmid-9660929|pmid-9660960
For classical cases of alternative splicing, it was shown that cis-acting RNA sequence elements increased exon inclusion by serving as binding sites for the assembly of multi-component splicing enhancer complexes.
[ "1", "3", "2", "4", "5", "6", "2", "4", "5", "7", "8", "14", "15", "16", "17", "18" ]
213
5,806
0
false
For classical cases of alternative splicing, it was shown that cis-acting RNA sequence elements increased exon inclusion by serving as binding sites for the assembly of multi-component splicing enhancer complexes.
[]
For classical cases of alternative splicing, it was shown that cis-acting RNA sequence elements increased exon inclusion by serving as binding sites for the assembly of multi-component splicing enhancer complexes.
true
true
true
true
true
966
0
INTRODUCTION
1
1
[ "b1", "b3", "b2", "b4", "b5", "b6", "b2", "b4", "b5", "b7", "b8", "b14", "b15", "b16", "b17", "b18" ]
17,135,210
pmid-10916158|pmid-15168696|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11421359|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11967553|pmid-2137203|pmid-10485881|pmid-1331983|pmid-7988565|pmid-9858550|pmid-12114529|pmid-8769651|pmid-9660929|pmid-9660960
Because these sequence elements were usually located within the regulated exon, they were defined as exonic splicing enhancers (ESEs) (2,4).
[ "1", "3", "2", "4", "5", "6", "2", "4", "5", "7", "8", "14", "15", "16", "17", "18" ]
140
5,807
0
false
Because these sequence elements were usually located within the regulated exon, they were defined as exonic splicing enhancers (ESEs).
[ "2,4" ]
Because these sequence elements were usually located within the regulated exon, they were defined as exonic splicing enhancers (ESEs).
true
true
true
true
true
966
0
INTRODUCTION
1
1
[ "b1", "b3", "b2", "b4", "b5", "b6", "b2", "b4", "b5", "b7", "b8", "b14", "b15", "b16", "b17", "b18" ]
17,135,210
pmid-10916158|pmid-15168696|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11421359|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11967553|pmid-2137203|pmid-10485881|pmid-1331983|pmid-7988565|pmid-9858550|pmid-12114529|pmid-8769651|pmid-9660929|pmid-9660960
It has been demonstrated that the recognition of weak splice-site signals can be augmented significantly by the presence of ESEs, and, in contrast, that ESEs have little or no detectable effect on the activation of strong splice sites that conform to the consensus sequence (5,6).
[ "1", "3", "2", "4", "5", "6", "2", "4", "5", "7", "8", "14", "15", "16", "17", "18" ]
280
5,808
0
false
It has been demonstrated that the recognition of weak splice-site signals can be augmented significantly by the presence of ESEs, and, in contrast, that ESEs have little or no detectable effect on the activation of strong splice sites that conform to the consensus sequence.
[ "5,6" ]
It has been demonstrated that the recognition of weak splice-site signals can be augmented significantly by the presence of ESEs, and, in contrast, that ESEs have little or no detectable effect on the activation of strong splice sites that conform to the consensus sequence.
true
true
true
true
true
966
0
INTRODUCTION
1
1
[ "b1", "b3", "b2", "b4", "b5", "b6", "b2", "b4", "b5", "b7", "b8", "b14", "b15", "b16", "b17", "b18" ]
17,135,210
pmid-10916158|pmid-15168696|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11421359|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11967553|pmid-2137203|pmid-10485881|pmid-1331983|pmid-7988565|pmid-9858550|pmid-12114529|pmid-8769651|pmid-9660929|pmid-9660960
ESEs are usually recognized by at least one member of the essential serine/arginine (SR)-rich protein family and recruit the splicing machinery to the adjacent intron (2,4,5,7).
[ "1", "3", "2", "4", "5", "6", "2", "4", "5", "7", "8", "14", "15", "16", "17", "18" ]
177
5,809
0
false
ESEs are usually recognized by at least one member of the essential serine/arginine (SR)-rich protein family and recruit the splicing machinery to the adjacent intron.
[ "2,4,5,7" ]
ESEs are usually recognized by at least one member of the essential serine/arginine (SR)-rich protein family and recruit the splicing machinery to the adjacent intron.
true
true
true
true
true
966
0
INTRODUCTION
1
1
[ "b1", "b3", "b2", "b4", "b5", "b6", "b2", "b4", "b5", "b7", "b8", "b14", "b15", "b16", "b17", "b18" ]
17,135,210
pmid-10916158|pmid-15168696|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11421359|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11967553|pmid-2137203|pmid-10485881|pmid-1331983|pmid-7988565|pmid-9858550|pmid-12114529|pmid-8769651|pmid-9660929|pmid-9660960
SR proteins act at several steps during the splicing reaction (8–14) and require phosphorylation and dephosphorylation for spliceosomal assembly (15,16).
[ "1", "3", "2", "4", "5", "6", "2", "4", "5", "7", "8", "14", "15", "16", "17", "18" ]
153
5,810
0
false
SR proteins act at several steps during the splicing reaction and require phosphorylation and dephosphorylation for spliceosomal assembly.
[ "8–14", "15,16" ]
SR proteins act at several steps during the splicing reaction and require phosphorylation and dephosphorylation for spliceosomal assembly.
true
true
true
true
true
966
0
INTRODUCTION
1
1
[ "b1", "b3", "b2", "b4", "b5", "b6", "b2", "b4", "b5", "b7", "b8", "b14", "b15", "b16", "b17", "b18" ]
17,135,210
pmid-10916158|pmid-15168696|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11421359|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11967553|pmid-2137203|pmid-10485881|pmid-1331983|pmid-7988565|pmid-9858550|pmid-12114529|pmid-8769651|pmid-9660929|pmid-9660960
Interestingly, SR protein-binding sites are present not only within alternatively spliced exons but also within the exons of constitutively spliced pre-mRNAs (17,18).
[ "1", "3", "2", "4", "5", "6", "2", "4", "5", "7", "8", "14", "15", "16", "17", "18" ]
166
5,811
0
false
Interestingly, SR protein-binding sites are present not only within alternatively spliced exons but also within the exons of constitutively spliced pre-mRNAs.
[ "17,18" ]
Interestingly, SR protein-binding sites are present not only within alternatively spliced exons but also within the exons of constitutively spliced pre-mRNAs.
true
true
true
true
true
966
0
INTRODUCTION
1
1
[ "b1", "b3", "b2", "b4", "b5", "b6", "b2", "b4", "b5", "b7", "b8", "b14", "b15", "b16", "b17", "b18" ]
17,135,210
pmid-10916158|pmid-15168696|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11421359|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11967553|pmid-2137203|pmid-10485881|pmid-1331983|pmid-7988565|pmid-9858550|pmid-12114529|pmid-8769651|pmid-9660929|pmid-9660960
It is therefore likely that SR proteins bind to sequences found in most, if not all, exons.
[ "1", "3", "2", "4", "5", "6", "2", "4", "5", "7", "8", "14", "15", "16", "17", "18" ]
91
5,812
0
false
It is therefore likely that SR proteins bind to sequences found in most, if not all, exons.
[]
It is therefore likely that SR proteins bind to sequences found in most, if not all, exons.
true
true
true
true
true
966
1
INTRODUCTION
1
5
[ "b5", "b19", "b20", "b2", "b21", "b22", "b23", "b24" ]
17,135,210
pmid-10999598|pmid-14967144|pmid-15525510|pmid-12626338|pmid-9159075|pmid-9889128|pmid-12403462|pmid-12646561|pmid-16407336
Although arginine-serine (RS) domains clearly function as activation domains, the mechanism by which they do so remains unclear.
[ "5", "19", "20", "2", "21", "22", "23", "24" ]
128
5,813
0
false
Although arginine-serine (RS) domains clearly function as activation domains, the mechanism by which they do so remains unclear.
[]
Although arginine-serine (RS) domains clearly function as activation domains, the mechanism by which they do so remains unclear.
true
true
true
true
true
967
1
INTRODUCTION
1
5
[ "b5", "b19", "b20", "b2", "b21", "b22", "b23", "b24" ]
17,135,210
pmid-10999598|pmid-14967144|pmid-15525510|pmid-12626338|pmid-9159075|pmid-9889128|pmid-12403462|pmid-12646561|pmid-16407336
One model for the mechanism of SR protein action proposes that the RS domain of an enhancer-bound SR protein interacts directly with other splicing factors containing an RS domain, thus facilitating the recruitment of the spliceosome (5).
[ "5", "19", "20", "2", "21", "22", "23", "24" ]
238
5,814
1
false
One model for the mechanism of SR protein action proposes that the RS domain of an enhancer-bound SR protein interacts directly with other splicing factors containing an RS domain, thus facilitating the recruitment of the spliceosome.
[ "5" ]
One model for the mechanism of SR protein action proposes that the RS domain of an enhancer-bound SR protein interacts directly with other splicing factors containing an RS domain, thus facilitating the recruitment of the spliceosome.
true
true
true
true
true
967
1
INTRODUCTION
1
5
[ "b5", "b19", "b20", "b2", "b21", "b22", "b23", "b24" ]
17,135,210
pmid-10999598|pmid-14967144|pmid-15525510|pmid-12626338|pmid-9159075|pmid-9889128|pmid-12403462|pmid-12646561|pmid-16407336
An alternative model was suggested by experiments demonstrating that RS domains of SR proteins within the functional spliceosome contact the pre-mRNA (19,20).
[ "5", "19", "20", "2", "21", "22", "23", "24" ]
158
5,815
0
false
An alternative model was suggested by experiments demonstrating that RS domains of SR proteins within the functional spliceosome contact the pre-mRNA.
[ "19,20" ]
An alternative model was suggested by experiments demonstrating that RS domains of SR proteins within the functional spliceosome contact the pre-mRNA.
true
true
true
true
true
967
1
INTRODUCTION
1
5
[ "b5", "b19", "b20", "b2", "b21", "b22", "b23", "b24" ]
17,135,210
pmid-10999598|pmid-14967144|pmid-15525510|pmid-12626338|pmid-9159075|pmid-9889128|pmid-12403462|pmid-12646561|pmid-16407336
The sequential character of these contacts suggested that RS domain interactions with RNA promote spliceosome assembly.
[ "5", "19", "20", "2", "21", "22", "23", "24" ]
119
5,816
0
false
The sequential character of these contacts suggested that RS domain interactions with RNA promote spliceosome assembly.
[]
The sequential character of these contacts suggested that RS domain interactions with RNA promote spliceosome assembly.
true
true
true
true
true
967
1
INTRODUCTION
1
5
[ "b5", "b19", "b20", "b2", "b21", "b22", "b23", "b24" ]
17,135,210
pmid-10999598|pmid-14967144|pmid-15525510|pmid-12626338|pmid-9159075|pmid-9889128|pmid-12403462|pmid-12646561|pmid-16407336
Irrespective of the mechanism of action, ESEs facilitate the recruitment of spliceosomal components to the regulated splice site (2,21,22).
[ "5", "19", "20", "2", "21", "22", "23", "24" ]
139
5,817
0
false
Irrespective of the mechanism of action, ESEs facilitate the recruitment of spliceosomal components to the regulated splice site.
[ "2,21,22" ]
Irrespective of the mechanism of action, ESEs facilitate the recruitment of spliceosomal components to the regulated splice site.
true
true
true
true
true
967
1
INTRODUCTION
1
5
[ "b5", "b19", "b20", "b2", "b21", "b22", "b23", "b24" ]
17,135,210
pmid-10999598|pmid-14967144|pmid-15525510|pmid-12626338|pmid-9159075|pmid-9889128|pmid-12403462|pmid-12646561|pmid-16407336
More recently, it was demonstrated that ESEs promote the recognition of both exon/intron junctions within the same step during exon definition.
[ "5", "19", "20", "2", "21", "22", "23", "24" ]
143
5,818
0
false
More recently, it was demonstrated that ESEs promote the recognition of both exon/intron junctions within the same step during exon definition.
[]
More recently, it was demonstrated that ESEs promote the recognition of both exon/intron junctions within the same step during exon definition.
true
true
true
true
true
967
1
INTRODUCTION
1
5
[ "b5", "b19", "b20", "b2", "b21", "b22", "b23", "b24" ]
17,135,210
pmid-10999598|pmid-14967144|pmid-15525510|pmid-12626338|pmid-9159075|pmid-9889128|pmid-12403462|pmid-12646561|pmid-16407336
These results suggested that ESEs recruit a multi-component complex that minimally contains components of the splicing machinery required for 5′ and 3′ splice-site selection (23,24).
[ "5", "19", "20", "2", "21", "22", "23", "24" ]
182
5,819
0
false
These results suggested that ESEs recruit a multi-component complex that minimally contains components of the splicing machinery required for 5′ and 3′ splice-site selection.
[ "23,24" ]
These results suggested that ESEs recruit a multi-component complex that minimally contains components of the splicing machinery required for 5′ and 3′ splice-site selection.
true
true
true
true
true
967
1
INTRODUCTION
1
5
[ "b5", "b19", "b20", "b2", "b21", "b22", "b23", "b24" ]
17,135,210
pmid-10999598|pmid-14967144|pmid-15525510|pmid-12626338|pmid-9159075|pmid-9889128|pmid-12403462|pmid-12646561|pmid-16407336
Thus, ESEs function as general activators of exon recognition.
[ "5", "19", "20", "2", "21", "22", "23", "24" ]
62
5,820
0
false
Thus, ESEs function as general activators of exon recognition.
[]
Thus, ESEs function as general activators of exon recognition.
true
true
true
true
true
967
2
INTRODUCTION
1
25
[ "b25", "b26" ]
17,135,210
pmid-9660960|pmid-9822617|pmid-11124808|pmid-11046128
The relative activities of SR proteins depend on their affinity for splicing enhancers and the strength of their activation domains.
[ "25", "26" ]
132
5,821
0
false
The relative activities of SR proteins depend on their affinity for splicing enhancers and the strength of their activation domains.
[]
The relative activities of SR proteins depend on their affinity for splicing enhancers and the strength of their activation domains.
true
true
true
true
true
968
2
INTRODUCTION
1
25
[ "b25", "b26" ]
17,135,210
pmid-9660960|pmid-9822617|pmid-11124808|pmid-11046128
Using an MS2 tethering approach it was possible to uncouple the spliceosomal recruitment and the RNA-binding activities of SR proteins (25).
[ "25", "26" ]
140
5,822
1
false
Using an MS2 tethering approach it was possible to uncouple the spliceosomal recruitment and the RNA-binding activities of SR proteins.
[ "25" ]
Using an MS2 tethering approach it was possible to uncouple the spliceosomal recruitment and the RNA-binding activities of SR proteins.
true
true
true
true
true
968
2
INTRODUCTION
1
26
[ "b25", "b26" ]
17,135,210
pmid-9660960|pmid-9822617|pmid-11124808|pmid-11046128
This system allowed a careful quantitative comparison of the activity of several RS domains (26) to demonstrate that the strength of ESEs is determined by the relative activities of the bound SR proteins, by the number of SR proteins assembled on ESEs, and by the distance between the enhancer and the intron.
[ "25", "26" ]
309
5,823
1
false
This system allowed a careful quantitative comparison of the activity of several RS domains to demonstrate that the strength of ESEs is determined by the relative activities of the bound SR proteins, by the number of SR proteins assembled on ESEs, and by the distance between the enhancer and the intron.
[ "26" ]
This system allowed a careful quantitative comparison of the activity of several RS domains to demonstrate that the strength of ESEs is determined by the relative activities of the bound SR proteins, by the number of SR proteins assembled on ESEs, and by the distance between the enhancer and the intron.
true
true
true
true
true
968
2
INTRODUCTION
1
25
[ "b25", "b26" ]
17,135,210
pmid-9660960|pmid-9822617|pmid-11124808|pmid-11046128
A mechanistically important observation was that the splicing activity of the bound SR proteins was proportional to the number of SR repeats contained within the RS domain of the proteins tested.
[ "25", "26" ]
195
5,824
0
false
A mechanistically important observation was that the splicing activity of the bound SR proteins was proportional to the number of SR repeats contained within the RS domain of the proteins tested.
[]
A mechanistically important observation was that the splicing activity of the bound SR proteins was proportional to the number of SR repeats contained within the RS domain of the proteins tested.
true
true
true
true
true
968
2
INTRODUCTION
1
25
[ "b25", "b26" ]
17,135,210
pmid-9660960|pmid-9822617|pmid-11124808|pmid-11046128
Thus, the quantity of SR repeats apparently dictates the activation potential of SR proteins.
[ "25", "26" ]
93
5,825
0
false
Thus, the quantity of SR repeats apparently dictates the activation potential of SR proteins.
[]
Thus, the quantity of SR repeats apparently dictates the activation potential of SR proteins.
true
true
true
true
true
968
3
INTRODUCTION
1
27
[ "b27", "b28", "b29", "b30", "b32", "b24", "b33", "b34", "b35" ]
17,135,210
pmid-2505080|pmid-1936994|pmid-8978612|pmid-2454747|pmid-2155161|pmid-12646561|pmid-9418892|pmid-8769651|pmid-9660929|pmid-8124712
Genes involved in Drosophila sex determination are prototypes for the study of positive and negative control of alternative splicing (27).
[ "27", "28", "29", "30", "32", "24", "33", "34", "35" ]
138
5,826
1
false
Genes involved in Drosophila sex determination are prototypes for the study of positive and negative control of alternative splicing.
[ "27" ]
Genes involved in Drosophila sex determination are prototypes for the study of positive and negative control of alternative splicing.
true
true
true
true
true
969
3
INTRODUCTION
1
27
[ "b27", "b28", "b29", "b30", "b32", "b24", "b33", "b34", "b35" ]
17,135,210
pmid-2505080|pmid-1936994|pmid-8978612|pmid-2454747|pmid-2155161|pmid-12646561|pmid-9418892|pmid-8769651|pmid-9660929|pmid-8124712
The best characterized are the doublesex (dsx) and fruitless (fru) genes, in which the use of two alternative 3′ (dsx) or 5′ (fru) splice sites leads to the expression of male- or female-specific gene products that initiate gender-specific sexual differentiation and orientation (28,29).
[ "27", "28", "29", "30", "32", "24", "33", "34", "35" ]
287
5,827
0
false
The best characterized are the doublesex (dsx) and fruitless (fru) genes, in which the use of two alternative 3′ (dsx) or 5′ (fru) splice sites leads to the expression of male- or female-specific gene products that initiate gender-specific sexual differentiation and orientation.
[ "28,29" ]
The best characterized are the doublesex (dsx) and fruitless (fru) genes, in which the use of two alternative 3′ (dsx) or 5′ (fru) splice sites leads to the expression of male- or female-specific gene products that initiate gender-specific sexual differentiation and orientation.
true
true
true
true
true
969
3
INTRODUCTION
1
27
[ "b27", "b28", "b29", "b30", "b32", "b24", "b33", "b34", "b35" ]
17,135,210
pmid-2505080|pmid-1936994|pmid-8978612|pmid-2454747|pmid-2155161|pmid-12646561|pmid-9418892|pmid-8769651|pmid-9660929|pmid-8124712
Female-specific splicing of dsx requires the production of two proteins, Transformer (Tra) and Transformer2 (Tra2), and an ESE (dsx ESE) consisting of six repeat elements (dsxRE) (30–32).
[ "27", "28", "29", "30", "32", "24", "33", "34", "35" ]
187
5,828
0
false
Female-specific splicing of dsx requires the production of two proteins, Transformer (Tra) and Transformer2 (Tra2), and an ESE (dsx ESE) consisting of six repeat elements (dsxRE).
[ "30–32" ]
Female-specific splicing of dsx requires the production of two proteins, Transformer (Tra) and Transformer2, and an ESE (dsx ESE) consisting of six repeat elements (dsxRE).
true
true
true
true
true
969
3
INTRODUCTION
1
27
[ "b27", "b28", "b29", "b30", "b32", "b24", "b33", "b34", "b35" ]
17,135,210
pmid-2505080|pmid-1936994|pmid-8978612|pmid-2454747|pmid-2155161|pmid-12646561|pmid-9418892|pmid-8769651|pmid-9660929|pmid-8124712
Similarly, female-specific splicing of fru depends on Tra, Tra2 and an ESE (fru ESE) consisting of three repeat elements identical to dsxREs (24,33).
[ "27", "28", "29", "30", "32", "24", "33", "34", "35" ]
149
5,829
0
false
Similarly, female-specific splicing of fru depends on Tra, Tra2 and an ESE (fru ESE) consisting of three repeat elements identical to dsxREs.
[ "24,33" ]
Similarly, female-specific splicing of fru depends on Tra, Tra2 and an ESE (fru ESE) consisting of three repeat elements identical to dsxREs.
true
true
true
true
true
969
3
INTRODUCTION
1
27
[ "b27", "b28", "b29", "b30", "b32", "b24", "b33", "b34", "b35" ]
17,135,210
pmid-2505080|pmid-1936994|pmid-8978612|pmid-2454747|pmid-2155161|pmid-12646561|pmid-9418892|pmid-8769651|pmid-9660929|pmid-8124712
Both Tra and Tra2 contain RS-rich domains.
[ "27", "28", "29", "30", "32", "24", "33", "34", "35" ]
42
5,830
0
false
Both Tra and Tra2 contain RS-rich domains.
[]
Both Tra and Tra2 contain RS-rich domains.
true
true
true
true
true
969
3
INTRODUCTION
1
27
[ "b27", "b28", "b29", "b30", "b32", "b24", "b33", "b34", "b35" ]
17,135,210
pmid-2505080|pmid-1936994|pmid-8978612|pmid-2454747|pmid-2155161|pmid-12646561|pmid-9418892|pmid-8769651|pmid-9660929|pmid-8124712
Previous in vitro studies in HeLa extracts demonstrated that Tra, Tra2 and the SR protein 9G8 (the human homologue of Drosophila RBP1) assemble cooperatively on each dsxRE (34,35).
[ "27", "28", "29", "30", "32", "24", "33", "34", "35" ]
180
5,831
0
false
Previous in vitro studies in HeLa extracts demonstrated that Tra, Tra2 and the SR protein 9G8 (the human homologue of Drosophila RBP1) assemble cooperatively on each dsxRE.
[ "34,35" ]
Previous in vitro studies in HeLa extracts demonstrated that Tra, Tra2 and the SR protein 9G8 (the human homologue of Drosophila RBP1) assemble cooperatively on each dsxRE.
true
true
true
true
true
969
3
INTRODUCTION
1
27
[ "b27", "b28", "b29", "b30", "b32", "b24", "b33", "b34", "b35" ]
17,135,210
pmid-2505080|pmid-1936994|pmid-8978612|pmid-2454747|pmid-2155161|pmid-12646561|pmid-9418892|pmid-8769651|pmid-9660929|pmid-8124712
While 9G8 and Tra2 bind to the 5′ and 3′ half, respectively, Tra appears to contact RNA only very weakly, if at all.
[ "27", "28", "29", "30", "32", "24", "33", "34", "35" ]
116
5,832
0
false
While 9G8 and Tra2 bind to the 5′ and 3′ half, respectively, Tra appears to contact RNA only very weakly, if at all.
[]
While 9G8 and Tra2 bind to the 5′ and 3′ half, respectively, Tra appears to contact RNA only very weakly, if at all.
true
true
true
true
true
969
3
INTRODUCTION
1
27
[ "b27", "b28", "b29", "b30", "b32", "b24", "b33", "b34", "b35" ]
17,135,210
pmid-2505080|pmid-1936994|pmid-8978612|pmid-2454747|pmid-2155161|pmid-12646561|pmid-9418892|pmid-8769651|pmid-9660929|pmid-8124712
Although the identity of the factors that make up the dsx enhancer complex has been revealed, it is currently unknown whether more than one molecule of each component is required for assembly.
[ "27", "28", "29", "30", "32", "24", "33", "34", "35" ]
192
5,833
0
false
Although the identity of the factors that make up the dsx enhancer complex has been revealed, it is currently unknown whether more than one molecule of each component is required for assembly.
[]
Although the identity of the factors that make up the dsx enhancer complex has been revealed, it is currently unknown whether more than one molecule of each component is required for assembly.
true
true
true
true
true
969
3
INTRODUCTION
1
27
[ "b27", "b28", "b29", "b30", "b32", "b24", "b33", "b34", "b35" ]
17,135,210
pmid-2505080|pmid-1936994|pmid-8978612|pmid-2454747|pmid-2155161|pmid-12646561|pmid-9418892|pmid-8769651|pmid-9660929|pmid-8124712
It is also unclear which one of the three proteins that make up a dsxRE complex is critical in communicating splice-site recognition to the splicing machinery.
[ "27", "28", "29", "30", "32", "24", "33", "34", "35" ]
159
5,834
0
false
It is also unclear which one of the three proteins that make up a dsxRE complex is critical in communicating splice-site recognition to the splicing machinery.
[]
It is also unclear which one of the three proteins that make up a dsxRE complex is critical in communicating splice-site recognition to the splicing machinery.
true
true
true
true
true
969
3
INTRODUCTION
1
27
[ "b27", "b28", "b29", "b30", "b32", "b24", "b33", "b34", "b35" ]
17,135,210
pmid-2505080|pmid-1936994|pmid-8978612|pmid-2454747|pmid-2155161|pmid-12646561|pmid-9418892|pmid-8769651|pmid-9660929|pmid-8124712
Each protein contains at least one SR domain that may be involved in crucial protein–protein interactions.
[ "27", "28", "29", "30", "32", "24", "33", "34", "35" ]
106
5,835
0
false
Each protein contains at least one SR domain that may be involved in crucial protein–protein interactions.
[]
Each protein contains at least one SR domain that may be involved in crucial protein–protein interactions.
true
true
true
true
true
969
3
INTRODUCTION
1
27
[ "b27", "b28", "b29", "b30", "b32", "b24", "b33", "b34", "b35" ]
17,135,210
pmid-2505080|pmid-1936994|pmid-8978612|pmid-2454747|pmid-2155161|pmid-12646561|pmid-9418892|pmid-8769651|pmid-9660929|pmid-8124712
Therefore, it is possible that the three proteins combined or one in particular function to recruit the splicing machinery.
[ "27", "28", "29", "30", "32", "24", "33", "34", "35" ]
123
5,836
0
false
Therefore, it is possible that the three proteins combined or one in particular function to recruit the splicing machinery.
[]
Therefore, it is possible that the three proteins combined or one in particular function to recruit the splicing machinery.
true
true
true
true
true
969
4
INTRODUCTION
0
null
null
17,135,210
null
Here we evaluated in detail the potency of the dsxRE.
null
53
5,837
0
false
null
null
Here we evaluated in detail the potency of the dsxRE.
true
true
true
true
true
970
4
INTRODUCTION
0
null
null
17,135,210
null
By taking advantage of the MS2-fusion approach, we were able to demonstrate that each of its components has an activation potential that is significantly higher than expected from SR dinucleotide content alone.
null
210
5,838
0
false
null
null
By taking advantage of the MS2-fusion approach, we were able to demonstrate that each of its components has an activation potential that is significantly higher than expected from SR dinucleotide content alone.
true
true
true
true
true
970
4
INTRODUCTION
0
null
null
17,135,210
null
Our quantitative analysis shows that the SR domains of each component are necessary but not sufficient for maximal activation.
null
126
5,839
0
false
null
null
Our quantitative analysis shows that the SR domains of each component are necessary but not sufficient for maximal activation.
true
true
true
true
true
970
4
INTRODUCTION
0
null
null
17,135,210
null
For 9G8, the RNA-binding domain contributes considerably to splice-site activation.
null
83
5,840
0
false
null
null
For 9G8, the RNA-binding domain contributes considerably to splice-site activation.
true
true
true
true
true
970
4
INTRODUCTION
0
null
null
17,135,210
null
Furthermore, each dsxRE enhancer complex is significantly more potent than canonical SR proteins.
null
97
5,841
0
false
null
null
Furthermore, each dsxRE enhancer complex is significantly more potent than canonical SR proteins.
true
true
true
true
true
970
4
INTRODUCTION
0
null
null
17,135,210
null
These experiments demonstrate that the splicing enhancer complex assembled on dsxREs has evolved to possess exceptional activation potency as is required to induce a complete switch in sex-specific alternative pre-mRNA splicing for the dsx and fru genes.
null
254
5,842
0
false
null
null
These experiments demonstrate that the splicing enhancer complex assembled on dsxREs has evolved to possess exceptional activation potency as is required to induce a complete switch in sex-specific alternative pre-mRNA splicing for the dsx and fru genes.
true
true
true
true
true
970
0
DISCUSSION
1
34
[ "b34", "b35", "b25" ]
17,135,210
pmid-10916158|pmid-15168696|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11421359|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11967553|pmid-2137203|pmid-10485881|pmid-1331983|pmid-7988565|pmid-9858550|pmid-12114529|pmid-8769651|pmid-9660929|pmid-9660960
The formation of splicing enhancer complexes is essential for the activation of most constitutive and differential splicing patterns.
[ "34", "35", "25" ]
133
5,843
0
false
The formation of splicing enhancer complexes is essential for the activation of most constitutive and differential splicing patterns.
[]
The formation of splicing enhancer complexes is essential for the activation of most constitutive and differential splicing patterns.
true
true
true
true
true
971
0
DISCUSSION
1
34
[ "b34", "b35", "b25" ]
17,135,210
pmid-10916158|pmid-15168696|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11421359|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11967553|pmid-2137203|pmid-10485881|pmid-1331983|pmid-7988565|pmid-9858550|pmid-12114529|pmid-8769651|pmid-9660929|pmid-9660960
To gain insights into the mechanisms of enhancer complex assembly and function, we investigated the role of Tra, Tra2 and 9G8 in the recruitment of the splicing machinery.
[ "34", "35", "25" ]
171
5,844
0
false
To gain insights into the mechanisms of enhancer complex assembly and function, we investigated the role of Tra, Tra2 and 9G8 in the recruitment of the splicing machinery.
[]
To gain insights into the mechanisms of enhancer complex assembly and function, we investigated the role of Tra, Tra2 and 9G8 in the recruitment of the splicing machinery.
true
true
true
true
true
971
0
DISCUSSION
1
34
[ "b34", "b35", "b25" ]
17,135,210
pmid-10916158|pmid-15168696|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11421359|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11967553|pmid-2137203|pmid-10485881|pmid-1331983|pmid-7988565|pmid-9858550|pmid-12114529|pmid-8769651|pmid-9660929|pmid-9660960
Each dsxRE serves as a binding platform for the cooperative assembly of multiple multi-component splicing enhancer complexes consisting of the SR proteins 9G8, Tra and Tra2 (34,35).
[ "34", "35", "25" ]
181
5,845
0
false
Each dsxRE serves as a binding platform for the cooperative assembly of multiple multi-component splicing enhancer complexes consisting of the SR proteins 9G8, Tra and Tra2.
[ "34,35" ]
Each dsxRE serves as a binding platform for the cooperative assembly of multiple multi-component splicing enhancer complexes consisting of the SR proteins 9G8, Tra and Tra2.
true
true
true
true
true
971
0
DISCUSSION
1
34
[ "b34", "b35", "b25" ]
17,135,210
pmid-10916158|pmid-15168696|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11421359|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11967553|pmid-2137203|pmid-10485881|pmid-1331983|pmid-7988565|pmid-9858550|pmid-12114529|pmid-8769651|pmid-9660929|pmid-9660960
To determine the activation potential of the SR proteins that comprise the dsxRE, we generated a series of fusion proteins between the MS2 coat protein and Tra, Tra2, 9G8 or other SR proteins.
[ "34", "35", "25" ]
192
5,846
0
false
To determine the activation potential of the SR proteins that comprise the dsxRE, we generated a series of fusion proteins between the MS2 coat protein and Tra, Tra2, 9G8 or other SR proteins.
[]
To determine the activation potential of the SR proteins that comprise the dsxRE, we generated a series of fusion proteins between the MS2 coat protein and Tra, Tra2, 9G8 or other SR proteins.
true
true
true
true
true
971
0
DISCUSSION
1
34
[ "b34", "b35", "b25" ]
17,135,210
pmid-10916158|pmid-15168696|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11421359|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11967553|pmid-2137203|pmid-10485881|pmid-1331983|pmid-7988565|pmid-9858550|pmid-12114529|pmid-8769651|pmid-9660929|pmid-9660960
Because MS2 interacts specifically with a hairpin loop, we were able to form stable interactions of individual components of the dsxRE complex in isolation.
[ "34", "35", "25" ]
156
5,847
0
false
Because MS2 interacts specifically with a hairpin loop, we were able to form stable interactions of individual components of the dsxRE complex in isolation.
[]
Because MS2 interacts specifically with a hairpin loop, we were able to form stable interactions of individual components of the dsxRE complex in isolation.
true
true
true
true
true
971
0
DISCUSSION
1
34
[ "b34", "b35", "b25" ]
17,135,210
pmid-10916158|pmid-15168696|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11421359|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11967553|pmid-2137203|pmid-10485881|pmid-1331983|pmid-7988565|pmid-9858550|pmid-12114529|pmid-8769651|pmid-9660929|pmid-9660960
Splice-site activation was tested in vitro with each of the fusion proteins present at concentrations that saturate binding to the MS2-hairpin but that did not support non-specific RNA binding.
[ "34", "35", "25" ]
193
5,848
0
false
Splice-site activation was tested in vitro with each of the fusion proteins present at concentrations that saturate binding to the MS2-hairpin but that did not support non-specific RNA binding.
[]
Splice-site activation was tested in vitro with each of the fusion proteins present at concentrations that saturate binding to the MS2-hairpin but that did not support non-specific RNA binding.
true
true
true
true
true
971
0
DISCUSSION
1
34
[ "b34", "b35", "b25" ]
17,135,210
pmid-10916158|pmid-15168696|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11421359|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11967553|pmid-2137203|pmid-10485881|pmid-1331983|pmid-7988565|pmid-9858550|pmid-12114529|pmid-8769651|pmid-9660929|pmid-9660960
Using this tethering approach, we demonstrated that each fusion protein in isolation was able to activate splicing.
[ "34", "35", "25" ]
115
5,849
0
false
Using this tethering approach, we demonstrated that each fusion protein in isolation was able to activate splicing.
[]
Using this tethering approach, we demonstrated that each fusion protein in isolation was able to activate splicing.
true
true
true
true
true
971
0
DISCUSSION
1
34
[ "b34", "b35", "b25" ]
17,135,210
pmid-10916158|pmid-15168696|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11421359|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11967553|pmid-2137203|pmid-10485881|pmid-1331983|pmid-7988565|pmid-9858550|pmid-12114529|pmid-8769651|pmid-9660929|pmid-9660960
However, they differed drastically in the extent of activation.
[ "34", "35", "25" ]
63
5,850
0
false
However, they differed drastically in the extent of activation.
[]
However, they differed drastically in the extent of activation.
true
true
true
true
true
971
0
DISCUSSION
1
25
[ "b34", "b35", "b25" ]
17,135,210
pmid-10916158|pmid-15168696|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11421359|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11967553|pmid-2137203|pmid-10485881|pmid-1331983|pmid-7988565|pmid-9858550|pmid-12114529|pmid-8769651|pmid-9660929|pmid-9660960
A previous work indicated that enhancer-dependent splice-site activation correlates with the number of RS dipeptide repeats present in each protein (25).
[ "34", "35", "25" ]
153
5,851
1
false
A previous work indicated that enhancer-dependent splice-site activation correlates with the number of RS dipeptide repeats present in each protein.
[ "25" ]
A previous work indicated that enhancer-dependent splice-site activation correlates with the number of RS dipeptide repeats present in each protein.
true
true
true
true
true
971
0
DISCUSSION
1
34
[ "b34", "b35", "b25" ]
17,135,210
pmid-10916158|pmid-15168696|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11421359|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11967553|pmid-2137203|pmid-10485881|pmid-1331983|pmid-7988565|pmid-9858550|pmid-12114529|pmid-8769651|pmid-9660929|pmid-9660960
Tra, Tra2 and 9G8 do not follow this trend, as they activate splicing much more efficiently than other SR proteins (Figure 3).
[ "34", "35", "25" ]
126
5,852
0
false
Tra, Tra2 and 9G8 do not follow this trend, as they activate splicing much more efficiently than other SR proteins (Figure 3).
[]
Tra, Tra2 and 9G8 do not follow this trend, as they activate splicing much more efficiently than other SR proteins.
true
true
true
true
true
971
0
DISCUSSION
1
34
[ "b34", "b35", "b25" ]
17,135,210
pmid-10916158|pmid-15168696|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11421359|pmid-12626338|pmid-10694877|pmid-10999598|pmid-11967553|pmid-2137203|pmid-10485881|pmid-1331983|pmid-7988565|pmid-9858550|pmid-12114529|pmid-8769651|pmid-9660929|pmid-9660960
Our analysis demonstrated that in the context of dsx, Tra, Tra2 and 9G8 are highly active splicing activators that may use mechanisms of activation distinct or in addition to those described for canonical SR proteins.
[ "34", "35", "25" ]
217
5,853
0
false
Our analysis demonstrated that in the context of dsx, Tra, Tra2 and 9G8 are highly active splicing activators that may use mechanisms of activation distinct or in addition to those described for canonical SR proteins.
[]
Our analysis demonstrated that in the context of dsx, Tra, Tra2 and 9G8 are highly active splicing activators that may use mechanisms of activation distinct or in addition to those described for canonical SR proteins.
true
true
true
true
true
971
1
DISCUSSION
1
38
[ "b38" ]
17,135,210
pmid-10999598|pmid-14967144|pmid-15525510|pmid-12626338|pmid-9159075|pmid-9889128|pmid-12403462|pmid-12646561|pmid-16407336
Tra, Tra2 and 9G8 mutants were generated to determine which domains are responsible for their high activation potential.
[ "38" ]
120
5,854
0
false
Tra, Tra2 and 9G8 mutants were generated to determine which domains are responsible for their high activation potential.
[]
Tra, Tra2 and 9G8 mutants were generated to determine which domains are responsible for their high activation potential.
true
true
true
true
true
972
1
DISCUSSION
1
38
[ "b38" ]
17,135,210
pmid-10999598|pmid-14967144|pmid-15525510|pmid-12626338|pmid-9159075|pmid-9889128|pmid-12403462|pmid-12646561|pmid-16407336
In all cases, the presence of their RS domains was required for maximal splice-site activation.
[ "38" ]
95
5,855
0
false
In all cases, the presence of their RS domains was required for maximal splice-site activation.
[]
In all cases, the presence of their RS domains was required for maximal splice-site activation.
true
true
true
true
true
972
1
DISCUSSION
1
38
[ "b38" ]
17,135,210
pmid-10999598|pmid-14967144|pmid-15525510|pmid-12626338|pmid-9159075|pmid-9889128|pmid-12403462|pmid-12646561|pmid-16407336
However, the overall contributions of the RS domains tested differed significantly.
[ "38" ]
83
5,856
0
false
However, the overall contributions of the RS domains tested differed significantly.
[]
However, the overall contributions of the RS domains tested differed significantly.
true
true
true
true
true
972
1
DISCUSSION
1
38
[ "b38" ]
17,135,210
pmid-10999598|pmid-14967144|pmid-15525510|pmid-12626338|pmid-9159075|pmid-9889128|pmid-12403462|pmid-12646561|pmid-16407336
In the case of the SR protein 9G8, the most significant drop in activity was observed when the Zn-knuckle was deleted from the fusion protein.
[ "38" ]
142
5,857
0
false
In the case of the SR protein 9G8, the most significant drop in activity was observed when the Zn-knuckle was deleted from the fusion protein.
[]
In the case of the SR protein 9G8, the most significant drop in activity was observed when the Zn-knuckle was deleted from the fusion protein.
true
true
true
true
true
972
1
DISCUSSION
1
38
[ "b38" ]
17,135,210
pmid-10999598|pmid-14967144|pmid-15525510|pmid-12626338|pmid-9159075|pmid-9889128|pmid-12403462|pmid-12646561|pmid-16407336
These observations suggest that the Zn-knuckle domain of 9G8 contains a stretch of amino acids that promotes splicing activity, however, it is unknown how the effect is mediated.
[ "38" ]
178
5,858
0
false
These observations suggest that the Zn-knuckle domain of 9G8 contains a stretch of amino acids that promotes splicing activity, however, it is unknown how the effect is mediated.
[]
These observations suggest that the Zn-knuckle domain of 9G8 contains a stretch of amino acids that promotes splicing activity, however, it is unknown how the effect is mediated.
true
true
true
true
true
972
1
DISCUSSION
1
38
[ "b38" ]
17,135,210
pmid-10999598|pmid-14967144|pmid-15525510|pmid-12626338|pmid-9159075|pmid-9889128|pmid-12403462|pmid-12646561|pmid-16407336
Perhaps, the Zn-knuckle domain could be involved in direct interactions with components of the splicing machinery.
[ "38" ]
114
5,859
0
false
Perhaps, the Zn-knuckle domain could be involved in direct interactions with components of the splicing machinery.
[]
Perhaps, the Zn-knuckle domain could be involved in direct interactions with components of the splicing machinery.
true
true
true
true
true
972
1
DISCUSSION
1
38
[ "b38" ]
17,135,210
pmid-10999598|pmid-14967144|pmid-15525510|pmid-12626338|pmid-9159075|pmid-9889128|pmid-12403462|pmid-12646561|pmid-16407336
Alternatively, the presence of the Zn-knuckle could induce a specific structural fold within the RS domain that renders it more potent or accessible for phosphorylation and dephosphorylation, thus overcoming the intrinsically disordered structure of RS domains (38).
[ "38" ]
266
5,860
1
false
Alternatively, the presence of the Zn-knuckle could induce a specific structural fold within the RS domain that renders it more potent or accessible for phosphorylation and dephosphorylation, thus overcoming the intrinsically disordered structure of RS domains.
[ "38" ]
Alternatively, the presence of the Zn-knuckle could induce a specific structural fold within the RS domain that renders it more potent or accessible for phosphorylation and dephosphorylation, thus overcoming the intrinsically disordered structure of RS domains.
true
true
true
true
true
972
2
DISCUSSION
1
39
[ "b39", "b40" ]
17,135,210
pmid-9660960|pmid-9822617|pmid-11124808|pmid-11046128
Previous studies suggested that the RNA-binding domain of the SR protein ASF/SF2 is directly involved in mediating spliceosomal assembly (39).
[ "39", "40" ]
142
5,861
1
false
Previous studies suggested that the RNA-binding domain of the SR protein ASF/SF2 is directly involved in mediating spliceosomal assembly.
[ "39" ]
Previous studies suggested that the RNA-binding domain of the SR protein ASF/SF2 is directly involved in mediating spliceosomal assembly.
true
true
true
true
true
973
2
DISCUSSION
1
39
[ "b39", "b40" ]
17,135,210
pmid-9660960|pmid-9822617|pmid-11124808|pmid-11046128
It is possible that the RRM of ASF/SF2 makes up a binding platform involved in specific protein–protein interactions.
[ "39", "40" ]
117
5,862
0
false
It is possible that the RRM of ASF/SF2 makes up a binding platform involved in specific protein–protein interactions.
[]
It is possible that the RRM of ASF/SF2 makes up a binding platform involved in specific protein–protein interactions.
true
true
true
true
true
973
2
DISCUSSION
1
40
[ "b39", "b40" ]
17,135,210
pmid-9660960|pmid-9822617|pmid-11124808|pmid-11046128
Alternatively, the RRM-mediated interaction of ASF/SF2 with the pre-mRNA may modulate splicing by competing with the binding of other regulatory factors, thus suggesting that antagonism between positive and negative splicing factors may be derived from competition for overlapping pre-mRNA binding sites (40).
[ "39", "40" ]
309
5,863
1
false
Alternatively, the RRM-mediated interaction of ASF/SF2 with the pre-mRNA may modulate splicing by competing with the binding of other regulatory factors, thus suggesting that antagonism between positive and negative splicing factors may be derived from competition for overlapping pre-mRNA binding sites.
[ "40" ]
Alternatively, the RRM-mediated interaction of ASF/SF2 with the pre-mRNA may modulate splicing by competing with the binding of other regulatory factors, thus suggesting that antagonism between positive and negative splicing factors may be derived from competition for overlapping pre-mRNA binding sites.
true
true
true
true
true
973
2
DISCUSSION
1
39
[ "b39", "b40" ]
17,135,210
pmid-9660960|pmid-9822617|pmid-11124808|pmid-11046128
Our observation that the Zn-knuckle of 9G8 drastically increases 9G8's activation potential is more consistent with the formation of a binding platform involved in specific protein–protein interactions.
[ "39", "40" ]
202
5,864
0
false
Our observation that the Zn-knuckle of 9G8 drastically increases 9G8's activation potential is more consistent with the formation of a binding platform involved in specific protein–protein interactions.
[]
Our observation that the Zn-knuckle of 9G8 drastically increases 9G8's activation potential is more consistent with the formation of a binding platform involved in specific protein–protein interactions.
true
true
true
true
true
973
2
DISCUSSION
1
39
[ "b39", "b40" ]
17,135,210
pmid-9660960|pmid-9822617|pmid-11124808|pmid-11046128
This is because all fusion proteins tested interacted with the same MS2-hairpin structure on the pre-mRNA.
[ "39", "40" ]
106
5,865
0
false
This is because all fusion proteins tested interacted with the same MS2-hairpin structure on the pre-mRNA.
[]
This is because all fusion proteins tested interacted with the same MS2-hairpin structure on the pre-mRNA.
true
true
true
true
true
973
2
DISCUSSION
1
39
[ "b39", "b40" ]
17,135,210
pmid-9660960|pmid-9822617|pmid-11124808|pmid-11046128
Thus, the potent splice-site activation of 9G8 is mediated not only by the RS domain but also by portions of its RRM.
[ "39", "40" ]
117
5,866
0
false
Thus, the potent splice-site activation of 9G8 is mediated not only by the RS domain but also by portions of its RRM.
[]
Thus, the potent splice-site activation of 9G8 is mediated not only by the RS domain but also by portions of its RRM.
true
true
true
true
true
973
3
DISCUSSION
1
41
[ "b41" ]
17,135,210
pmid-2505080|pmid-1936994|pmid-8978612|pmid-2454747|pmid-2155161|pmid-12646561|pmid-9418892|pmid-8769651|pmid-9660929|pmid-8124712
In the case of Tra2, both RS domains were shown to contribute to splicing activation, however, the N-terminal RS1 domain was at least 5-fold more potent than the C-terminal RS2 domain.
[ "41" ]
184
5,867
0
false
In the case of Tra2, both RS domains were shown to contribute to splicing activation, however, the N-terminal RS1 domain was at least 5-fold more potent than the C-terminal RS2 domain.
[]
In the case of Tra2, both RS domains were shown to contribute to splicing activation, however, the N-terminal RS1 domain was at least 5-fold more potent than the C-terminal RS2 domain.
true
true
true
true
true
974
3
DISCUSSION
1
41
[ "b41" ]
17,135,210
pmid-2505080|pmid-1936994|pmid-8978612|pmid-2454747|pmid-2155161|pmid-12646561|pmid-9418892|pmid-8769651|pmid-9660929|pmid-8124712
These observations appear to be in disagreement with results obtained from mutational analyses carried out in transgenic flies (41).
[ "41" ]
132
5,868
1
false
These observations appear to be in disagreement with results obtained from mutational analyses carried out in transgenic flies.
[ "41" ]
These observations appear to be in disagreement with results obtained from mutational analyses carried out in transgenic flies.
true
true
true
true
true
974
3
DISCUSSION
1
41
[ "b41" ]
17,135,210
pmid-2505080|pmid-1936994|pmid-8978612|pmid-2454747|pmid-2155161|pmid-12646561|pmid-9418892|pmid-8769651|pmid-9660929|pmid-8124712
It was demonstrated that the deletion of RS2 abolishes sex-specific dsx splicing in flies while the deletion of RS1 had only marginal effects.
[ "41" ]
142
5,869
0
false
It was demonstrated that the deletion of RS2 abolishes sex-specific dsx splicing in flies while the deletion of RS1 had only marginal effects.
[]
It was demonstrated that the deletion of RS2 abolishes sex-specific dsx splicing in flies while the deletion of RS1 had only marginal effects.
true
true
true
true
true
974
3
DISCUSSION
1
41
[ "b41" ]
17,135,210
pmid-2505080|pmid-1936994|pmid-8978612|pmid-2454747|pmid-2155161|pmid-12646561|pmid-9418892|pmid-8769651|pmid-9660929|pmid-8124712
Interestingly, the same study also showed that RS2 deletions of Tra2 significantly reduced protein interactions with other SR proteins.
[ "41" ]
135
5,870
0
false
Interestingly, the same study also showed that RS2 deletions of Tra2 significantly reduced protein interactions with other SR proteins.
[]
Interestingly, the same study also showed that RS2 deletions of Tra2 significantly reduced protein interactions with other SR proteins.
true
true
true
true
true
974
3
DISCUSSION
1
41
[ "b41" ]
17,135,210
pmid-2505080|pmid-1936994|pmid-8978612|pmid-2454747|pmid-2155161|pmid-12646561|pmid-9418892|pmid-8769651|pmid-9660929|pmid-8124712
However, the results from both studies can be reconciled by proposing that RS2 of Tra2 is essential for the formation of the heterotrimeric complex on each of the dsxREs.
[ "41" ]
170
5,871
0
false
However, the results from both studies can be reconciled by proposing that RS2 of Tra2 is essential for the formation of the heterotrimeric complex on each of the dsxREs.
[]
However, the results from both studies can be reconciled by proposing that RS2 of Tra2 is essential for the formation of the heterotrimeric complex on each of the dsxREs.
true
true
true
true
true
974
3
DISCUSSION
1
41
[ "b41" ]
17,135,210
pmid-2505080|pmid-1936994|pmid-8978612|pmid-2454747|pmid-2155161|pmid-12646561|pmid-9418892|pmid-8769651|pmid-9660929|pmid-8124712
This model suggests that in the absence of RS2 no stable heterotrimeric complex forms and female-specific splicing of dsx is severely compromised.
[ "41" ]
146
5,872
0
false
This model suggests that in the absence of RS2 no stable heterotrimeric complex forms and female-specific splicing of dsx is severely compromised.
[]
This model suggests that in the absence of RS2 no stable heterotrimeric complex forms and female-specific splicing of dsx is severely compromised.
true
true
true
true
true
974
3
DISCUSSION
1
41
[ "b41" ]
17,135,210
pmid-2505080|pmid-1936994|pmid-8978612|pmid-2454747|pmid-2155161|pmid-12646561|pmid-9418892|pmid-8769651|pmid-9660929|pmid-8124712
In the absence of RS1, heterotrimeric complex formation is still possible and the stable recruitment of 9G8 and Tra is sufficient to mediate female-specific splicing of dsx.
[ "41" ]
173
5,873
0
false
In the absence of RS1, heterotrimeric complex formation is still possible and the stable recruitment of 9G8 and Tra is sufficient to mediate female-specific splicing of dsx.
[]
In the absence of RS1, heterotrimeric complex formation is still possible and the stable recruitment of 9G8 and Tra is sufficient to mediate female-specific splicing of dsx.
true
true
true
true
true
974
3
DISCUSSION
1
41
[ "b41" ]
17,135,210
pmid-2505080|pmid-1936994|pmid-8978612|pmid-2454747|pmid-2155161|pmid-12646561|pmid-9418892|pmid-8769651|pmid-9660929|pmid-8124712
Thus, RS1 and RS2 of Tra2 may have distinct roles in activating female-specific splicing of dsx.
[ "41" ]
96
5,874
0
false
Thus, RS1 and RS2 of Tra2 may have distinct roles in activating female-specific splicing of dsx.
[]
Thus, RS1 and RS2 of Tra2 may have distinct roles in activating female-specific splicing of dsx.
true
true
true
true
true
974
3
DISCUSSION
1
41
[ "b41" ]
17,135,210
pmid-2505080|pmid-1936994|pmid-8978612|pmid-2454747|pmid-2155161|pmid-12646561|pmid-9418892|pmid-8769651|pmid-9660929|pmid-8124712
RS1 may be involved in recruiting spliceosomal components, whereas RS2 may be engaged in protein–protein interactions that ensure high stability of the heterotrimeric complex assembled on each dsxRE (Figure 7).
[ "41" ]
210
5,875
0
false
RS1 may be involved in recruiting spliceosomal components, whereas RS2 may be engaged in protein–protein interactions that ensure high stability of the heterotrimeric complex assembled on each dsxRE (Figure 7).
[]
RS1 may be involved in recruiting spliceosomal components, whereas RS2 may be engaged in protein–protein interactions that ensure high stability of the heterotrimeric complex assembled on each dsxRE (Figure 7).
true
true
true
true
true
974
4
DISCUSSION
0
null
null
17,135,210
null
In the case of Tra, the mutational analysis clearly indicates that the RS domain is sufficient to promote high levels of splice-site activation.
null
144
5,876
0
false
null
null
In the case of Tra, the mutational analysis clearly indicates that the RS domain is sufficient to promote high levels of splice-site activation.
true
true
true
true
true
975
4
DISCUSSION
0
null
null
17,135,210
null
No splicing activity was observed for the proline-rich domain of Tra, suggesting that this domain is not involved in direct interactions with the spliceosome.
null
158
5,877
0
false
null
null
No splicing activity was observed for the proline-rich domain of Tra, suggesting that this domain is not involved in direct interactions with the spliceosome.
true
true
true
true
true
975
5
DISCUSSION
1
34
[ "b34", "b35" ]
17,135,210
pmid-8769651|pmid-9660929
Because none of the fusion proteins alone, but the sum of all, can account for the activation potential of the fully assembled dsx enhancer complex (Figure 3), we propose that each component of the heterotrimeric enhancer complex participates in interactions with the spliceosome, generating an extended activation domai...
[ "34", "35" ]
433
5,878
0
false
Because none of the fusion proteins alone, but the sum of all, can account for the activation potential of the fully assembled dsx enhancer complex (Figure 3), we propose that each component of the heterotrimeric enhancer complex participates in interactions with the spliceosome, generating an extended activation domai...
[ "34,35" ]
Because none of the fusion proteins alone, but the sum of all, can account for the activation potential of the fully assembled dsx enhancer complex, we propose that each component of the heterotrimeric enhancer complex participates in interactions with the spliceosome, generating an extended activation domain that is s...
true
true
true
true
true
976
5
DISCUSSION
1
34
[ "b34", "b35" ]
17,135,210
pmid-8769651|pmid-9660929
Perhaps, this hypothesis could have been tested more directly by generating MS2-fusion proteins linking the SR domains of Tra, Tra2 and 9G8 or by creating a fusion between MS2 and all three full-length proteins.
[ "34", "35" ]
211
5,879
0
false
Perhaps, this hypothesis could have been tested more directly by generating MS2-fusion proteins linking the SR domains of Tra, Tra2 and 9G8 or by creating a fusion between MS2 and all three full-length proteins.
[]
Perhaps, this hypothesis could have been tested more directly by generating MS2-fusion proteins linking the SR domains of Tra, Tra2 and 9G8 or by creating a fusion between MS2 and all three full-length proteins.
true
true
true
true
true
976
5
DISCUSSION
1
34
[ "b34", "b35" ]
17,135,210
pmid-8769651|pmid-9660929
However, such fusion experiments did not guarantee to fully reproduce the cooperative interactions between RS1 and RS2 of Tra2 nor the contributions of the Zn-knuckle domain of 9G8.
[ "34", "35" ]
181
5,880
0
false
However, such fusion experiments did not guarantee to fully reproduce the cooperative interactions between RS1 and RS2 of Tra2 nor the contributions of the Zn-knuckle domain of 9G8.
[]
However, such fusion experiments did not guarantee to fully reproduce the cooperative interactions between RS1 and RS2 of Tra2 nor the contributions of the Zn-knuckle domain of 9G8.
true
true
true
true
true
976
6
DISCUSSION
1
42
[ "b42", "b43", "b44", "b35" ]
17,135,210
pmid-12494765|pmid-8849774|pmid-7958850|pmid-9660929
Tra and Tra2 regulate sexual differentiation and behavior of Drosophila through alternative splicing of the dsx and fru genes (42).
[ "42", "43", "44", "35" ]
131
5,881
1
false
Tra and Tra2 regulate sexual differentiation and behavior of Drosophila through alternative splicing of the dsx and fru genes.
[ "42" ]
Tra and Tra2 regulate sexual differentiation and behavior of Drosophila through alternative splicing of the dsx and fru genes.
true
true
true
true
true
977
6
DISCUSSION
1
42
[ "b42", "b43", "b44", "b35" ]
17,135,210
pmid-12494765|pmid-8849774|pmid-7958850|pmid-9660929
To avoid mixed expression of male- and female-specific transcription factors, the regulation of dsx and fru alternative splicing requires tight control and an efficient switch between male and female splicing.
[ "42", "43", "44", "35" ]
209
5,882
0
false
To avoid mixed expression of male- and female-specific transcription factors, the regulation of dsx and fru alternative splicing requires tight control and an efficient switch between male and female splicing.
[]
To avoid mixed expression of male- and female-specific transcription factors, the regulation of dsx and fru alternative splicing requires tight control and an efficient switch between male and female splicing.
true
true
true
true
true
977
6
DISCUSSION
1
43
[ "b42", "b43", "b44", "b35" ]
17,135,210
pmid-12494765|pmid-8849774|pmid-7958850|pmid-9660929
The composition and location of the dsx ESE 300 nt downstream of the regulated splice site is conserved among different Drosophila species, suggesting evolutionary influences in generating a unique exon architecture (43).
[ "42", "43", "44", "35" ]
221
5,883
1
false
The composition and location of the dsx ESE 300 nt downstream of the regulated splice site is conserved among different Drosophila species, suggesting evolutionary influences in generating a unique exon architecture.
[ "43" ]
The composition and location of the dsx ESE 300 nt downstream of the regulated splice site is conserved among different Drosophila species, suggesting evolutionary influences in generating a unique exon architecture.
true
true
true
true
true
977
6
DISCUSSION
1
42
[ "b42", "b43", "b44", "b35" ]
17,135,210
pmid-12494765|pmid-8849774|pmid-7958850|pmid-9660929
Indeed, it was shown that the regulation of dsx splicing could only be achieved if the dsx ESE is 300 nt downstream of the regulated splice site.
[ "42", "43", "44", "35" ]
145
5,884
0
false
Indeed, it was shown that the regulation of dsx splicing could only be achieved if the dsx ESE is 300 nt downstream of the regulated splice site.
[]
Indeed, it was shown that the regulation of dsx splicing could only be achieved if the dsx ESE is 300 nt downstream of the regulated splice site.
true
true
true
true
true
977
6
DISCUSSION
1
44
[ "b42", "b43", "b44", "b35" ]
17,135,210
pmid-12494765|pmid-8849774|pmid-7958850|pmid-9660929
Constitutive activation was observed when the dsx ESE was within 100 nt of the splice site (44).
[ "42", "43", "44", "35" ]
96
5,885
1
false
Constitutive activation was observed when the dsx ESE was within 100 nt of the splice site.
[ "44" ]
Constitutive activation was observed when the dsx ESE was within 100 nt of the splice site.
true
true
true
true
true
977
6
DISCUSSION
1
42
[ "b42", "b43", "b44", "b35" ]
17,135,210
pmid-12494765|pmid-8849774|pmid-7958850|pmid-9660929
Thus, the dsx ESE must have evolved to communicate female-specific splice-site recognition with high efficiency from a distance that usually does not support splicing regulation.
[ "42", "43", "44", "35" ]
178
5,886
0
false
Thus, the dsx ESE must have evolved to communicate female-specific splice-site recognition with high efficiency from a distance that usually does not support splicing regulation.
[]
Thus, the dsx ESE must have evolved to communicate female-specific splice-site recognition with high efficiency from a distance that usually does not support splicing regulation.
true
true
true
true
true
977
6
DISCUSSION
1
35
[ "b42", "b43", "b44", "b35" ]
17,135,210
pmid-12494765|pmid-8849774|pmid-7958850|pmid-9660929
We previously demonstrated that the cooperative assembly and the multiple presence of the dsxRE are contributing factors in achieving the elevated potency required for female-specific splicing (35).
[ "42", "43", "44", "35" ]
198
5,887
1
false
We previously demonstrated that the cooperative assembly and the multiple presence of the dsxRE are contributing factors in achieving the elevated potency required for female-specific splicing.
[ "35" ]
We previously demonstrated that the cooperative assembly and the multiple presence of the dsxRE are contributing factors in achieving the elevated potency required for female-specific splicing.
true
true
true
true
true
977
6
DISCUSSION
1
42
[ "b42", "b43", "b44", "b35" ]
17,135,210
pmid-12494765|pmid-8849774|pmid-7958850|pmid-9660929
The analysis presented here reveals an additional mechanism to ensure efficient splice-site selection.
[ "42", "43", "44", "35" ]
102
5,888
0
false
The analysis presented here reveals an additional mechanism to ensure efficient splice-site selection.
[]
The analysis presented here reveals an additional mechanism to ensure efficient splice-site selection.
true
true
true
true
true
977
6
DISCUSSION
1
42
[ "b42", "b43", "b44", "b35" ]
17,135,210
pmid-12494765|pmid-8849774|pmid-7958850|pmid-9660929
Each repeat element within the dsx ESE recruits the unusually effective splicing activators Tra, Tra2 and 9G8 to form a splicing enhancer complex of great potency.
[ "42", "43", "44", "35" ]
163
5,889
0
false
Each repeat element within the dsx ESE recruits the unusually effective splicing activators Tra, Tra2 and 9G8 to form a splicing enhancer complex of great potency.
[]
Each repeat element within the dsx ESE recruits the unusually effective splicing activators Tra, Tra2 and 9G8 to form a splicing enhancer complex of great potency.
true
true
true
true
true
977
6
DISCUSSION
1
42
[ "b42", "b43", "b44", "b35" ]
17,135,210
pmid-12494765|pmid-8849774|pmid-7958850|pmid-9660929
Thus, multiple enhancer complexes with high stability and elevated activity ensure practically exclusive alternative splicing of dsx and fru.
[ "42", "43", "44", "35" ]
141
5,890
0
false
Thus, multiple enhancer complexes with high stability and elevated activity ensure practically exclusive alternative splicing of dsx and fru.
[]
Thus, multiple enhancer complexes with high stability and elevated activity ensure practically exclusive alternative splicing of dsx and fru.
true
true
true
true
true
977
0
INTRODUCTION
1
1
[ "B1", "B2", "B3", "B4", "B5" ]
17,311,815
pmid-9872978|pmid-16255080|pmid-11726933|NA|pmid-15660941|pmid-15660941|NA
Single nucleotide polymorphisms (SNPs) represent the most widespread type of sequence variation in genomes (1) and provide the most commonly used genetic markers for the mapping of human disease genes (2) as well as experimentally induced mutations in model organisms (3).
[ "1", "2", "3", "4", "5" ]
272
5,891
1
false
Single nucleotide polymorphisms (SNPs) represent the most widespread type of sequence variation in genomes and provide the most commonly used genetic markers for the mapping of human disease genes as well as experimentally induced mutations in model organisms.
[ "1", "2", "3" ]
Single nucleotide polymorphisms (SNPs) represent the most widespread type of sequence variation in genomes and provide the most commonly used genetic markers for the mapping of human disease genes as well as experimentally induced mutations in model organisms.
true
true
true
true
true
978
0
INTRODUCTION
1
1
[ "B1", "B2", "B3", "B4", "B5" ]
17,311,815
pmid-9872978|pmid-16255080|pmid-11726933|NA|pmid-15660941|pmid-15660941|NA
Disciplines such as population ecology and conservation and evolutionary genetics would equally benefit from SNPs as genetic markers, but their use for such purposes has been limited due to the expenses and technical difficulties involved in the currently available SNP isolation strategies for non-model organisms.
[ "1", "2", "3", "4", "5" ]
315
5,892
0
false
Disciplines such as population ecology and conservation and evolutionary genetics would equally benefit from SNPs as genetic markers, but their use for such purposes has been limited due to the expenses and technical difficulties involved in the currently available SNP isolation strategies for non-model organisms.
[]
Disciplines such as population ecology and conservation and evolutionary genetics would equally benefit from SNPs as genetic markers, but their use for such purposes has been limited due to the expenses and technical difficulties involved in the currently available SNP isolation strategies for non-model organisms.
true
true
true
true
true
978
0
INTRODUCTION
1
1
[ "B1", "B2", "B3", "B4", "B5" ]
17,311,815
pmid-9872978|pmid-16255080|pmid-11726933|NA|pmid-15660941|pmid-15660941|NA
Any methodology that would streamline the SNP discovery process, particularly for non-model organisms, would be highly desirable (4,5).
[ "1", "2", "3", "4", "5" ]
135
5,893
0
false
Any methodology that would streamline the SNP discovery process, particularly for non-model organisms, would be highly desirable.
[ "4,5" ]
Any methodology that would streamline the SNP discovery process, particularly for non-model organisms, would be highly desirable.
true
true
true
true
true
978
1
INTRODUCTION
1
6
[ "B6", "B7", "B8" ]
17,311,815
pmid-15829236|pmid-15379655|pmid-15676075|pmid-8675443|NA
Typical direct SNP discovery strategies (6,7) involve sequencing of locus-specific amplification (LSA) products from multiple individuals or sequence determination of expressed sequence tags (EST-sequencing).
[ "6", "7", "8" ]
208
5,894
0
false
Typical direct SNP discovery strategies involve sequencing of locus-specific amplification (LSA) products from multiple individuals or sequence determination of expressed sequence tags (EST-sequencing).
[ "6,7" ]
Typical direct SNP discovery strategies involve sequencing of locus-specific amplification (LSA) products from multiple individuals or sequence determination of expressed sequence tags (EST-sequencing).
true
true
true
true
true
979
1
INTRODUCTION
1
6
[ "B6", "B7", "B8" ]
17,311,815
pmid-15829236|pmid-15379655|pmid-15676075|pmid-8675443|NA
Other direct strategies include whole genome (WGSS) and reduced representation (RRSS) shotgun sequencing approaches.
[ "6", "7", "8" ]
116
5,895
0
false
Other direct strategies include whole genome (WGSS) and reduced representation (RRSS) shotgun sequencing approaches.
[]
Other direct strategies include whole genome (WGSS) and reduced representation (RRSS) shotgun sequencing approaches.
true
true
true
true
true
979
1
INTRODUCTION
1
8
[ "B6", "B7", "B8" ]
17,311,815
pmid-15829236|pmid-15379655|pmid-15676075|pmid-8675443|NA
If comparative sequence data are available in public or other databases, various sequence comparison algorithms that identify nucleotide differences provide an alternative means to empirically discover SNPs (8).
[ "6", "7", "8" ]
211
5,896
1
false
If comparative sequence data are available in public or other databases, various sequence comparison algorithms that identify nucleotide differences provide an alternative means to empirically discover SNPs.
[ "8" ]
If comparative sequence data are available in public or other databases, various sequence comparison algorithms that identify nucleotide differences provide an alternative means to empirically discover SNPs.
true
true
true
true
true
979
2
INTRODUCTION
1
9
[ "B9", "B10 B11 B12", "B13", "B14", "B15", "B16", "B16" ]
17,311,815
pmid-2565038|pmid-369706|pmid-10380764|pmid-11385705|pmid-11524730|pmid-9600452|pmid-15141034|pmid-12177413|pmid-12177413
Indirect SNP discovery strategies include a prescreening phase prior to sequence determination, and these methodologies detect heteroduplexes on the basis of mismatch-induced altered DNA characteristics.
[ "9", "10–12", "13", "14", "15", "16", "16" ]
203
5,897
0
false
Indirect SNP discovery strategies include a prescreening phase prior to sequence determination, and these methodologies detect heteroduplexes on the basis of mismatch-induced altered DNA characteristics.
[]
Indirect SNP discovery strategies include a prescreening phase prior to sequence determination, and these methodologies detect heteroduplexes on the basis of mismatch-induced altered DNA characteristics.
true
true
true
true
true
980
2
INTRODUCTION
1
9
[ "B9", "B10 B11 B12", "B13", "B14", "B15", "B16", "B16" ]
17,311,815
pmid-2565038|pmid-369706|pmid-10380764|pmid-11385705|pmid-11524730|pmid-9600452|pmid-15141034|pmid-12177413|pmid-12177413
Physical differences are exploited in electrophoretic analyses such as single-strand conformational polymorphism (SSCP) that relies on conformation-dependent allele-specific migration differences of single strands (9).
[ "9", "10–12", "13", "14", "15", "16", "16" ]
218
5,898
1
false
Physical differences are exploited in electrophoretic analyses such as single-strand conformational polymorphism (SSCP) that relies on conformation-dependent allele-specific migration differences of single strands.
[ "9" ]
Physical differences are exploited in electrophoretic analyses such as single-strand conformational polymorphism (SSCP) that relies on conformation-dependent allele-specific migration differences of single strands.
true
true
true
true
true
980
2
INTRODUCTION
1
10–12
[ "B9", "B10 B11 B12", "B13", "B14", "B15", "B16", "B16" ]
17,311,815
pmid-2565038|pmid-369706|pmid-10380764|pmid-11385705|pmid-11524730|pmid-9600452|pmid-15141034|pmid-12177413|pmid-12177413
Similarly, altered melting behavior of mismatch-containing DNA fragment can be utilized to detect SNPs (10–12).
[ "9", "10–12", "13", "14", "15", "16", "16" ]
111
5,899
1
false
Similarly, altered melting behavior of mismatch-containing DNA fragment can be utilized to detect SNPs.
[ "10–12" ]
Similarly, altered melting behavior of mismatch-containing DNA fragment can be utilized to detect SNPs.
true
true
true
true
true
980