Datasets:
vgainullin
/
xciting_data

Dataset card Data Studio Files
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INTRODUCTION
1
1
[ "b1", "b2", "b6", "b7", "b9" ]
17,142,221
pmid-12519985|pmid-16554755|pmid-12872131|pmid-12634792|pmid-12634793
These include a number of studies aimed at mapping the complete interactome by investigating the composition of protein complexes and specific protein–protein interactions, as well as other studies focused on proteome-wide post-translational modifications (2–6).
[ "1", "2", "6", "7", "9" ]
262
3,300
0
false
These include a number of studies aimed at mapping the complete interactome by investigating the composition of protein complexes and specific protein–protein interactions, as well as other studies focused on proteome-wide post-translational modifications.
[ "2–6" ]
These include a number of studies aimed at mapping the complete interactome by investigating the composition of protein complexes and specific protein–protein interactions, as well as other studies focused on proteome-wide post-translational modifications.
true
true
true
true
true
552
0
INTRODUCTION
1
1
[ "b1", "b2", "b6", "b7", "b9" ]
17,142,221
pmid-12519985|pmid-16554755|pmid-12872131|pmid-12634792|pmid-12634793
Much of this research has become possible due to the increased use of proteome chip technologies, such as protein microarrays, as well as technological advances in mass spectrometry-based proteomics that result in increased sensitivity and higher throughput (7–9).
[ "1", "2", "6", "7", "9" ]
264
3,301
0
false
Much of this research has become possible due to the increased use of proteome chip technologies, such as protein microarrays, as well as technological advances in mass spectrometry-based proteomics that result in increased sensitivity and higher throughput.
[ "7–9" ]
Much of this research has become possible due to the increased use of proteome chip technologies, such as protein microarrays, as well as technological advances in mass spectrometry-based proteomics that result in increased sensitivity and higher throughput.
true
true
true
true
true
552
1
INTRODUCTION
0
null
null
17,142,221
null
To meet the needs of both the traditional biochemist and the proteomics researcher, we have improved the integration and display of protein data at SGD by redesigning protein information pages, introducing a new sequence-based visualization tool and utilizing improved algorithms for the calculation of predictive inform...
null
363
3,302
0
false
null
null
To meet the needs of both the traditional biochemist and the proteomics researcher, we have improved the integration and display of protein data at SGD by redesigning protein information pages, introducing a new sequence-based visualization tool and utilizing improved algorithms for the calculation of predictive inform...
true
true
true
true
true
553
0
INTRODUCTION
1
1
[ "b1", "b2", "b3" ]
16,971,457
pmid-14686936|pmid-11303501|pmid-10704475
Host/virus interaction modes have provided windows to study microbial diversity (1) as well as genetic processes at the molecular level, in particular for prokaryotes, and hence have helped in clarifying the physiological mechanisms, the dependence on the specific biochemical environment and evolution of their host cel...
[ "1", "2", "3" ]
329
3,303
1
false
Host/virus interaction modes have provided windows to study microbial diversity as well as genetic processes at the molecular level, in particular for prokaryotes, and hence have helped in clarifying the physiological mechanisms, the dependence on the specific biochemical environment and evolution of their host cells.
[ "1", "2,3" ]
Host/virus interaction modes have provided windows to study microbial diversity as well as genetic processes at the molecular level, in particular for prokaryotes, and hence have helped in clarifying the physiological mechanisms, the dependence on the specific biochemical environment and evolution of their host cells.
true
true
true
true
true
554
1
INTRODUCTION
1
4
[ "b4", "b5", "b6", "b6", "b8", "b9", "b12" ]
16,971,457
pmid-8639330|pmid-12798234|pmid-14499933|pmid-14499933|pmid-9783157|pmid-10564466|pmid-14747560
Very few viruses have been identified from Archaea (4) as compared with Bacteria and Eukarya and detailed description has been reported for those from hyperthermophilic archaea (5,6) with representatives that replicate in the genus Sulfolobus being the majority within the kingdom Crenarchaeota (6–8).
[ "4", "5", "6", "6", "8", "9", "12" ]
301
3,304
1
false
Very few viruses have been identified from Archaea as compared with Bacteria and Eukarya and detailed description has been reported for those from hyperthermophilic archaea with representatives that replicate in the genus Sulfolobus being the majority within the kingdom Crenarchaeota.
[ "4", "5,6", "6–8" ]
Very few viruses have been identified from Archaea as compared with Bacteria and Eukarya and detailed description has been reported for those from hyperthermophilic archaea with representatives that replicate in the genus Sulfolobus being the majority within the kingdom Crenarchaeota.
true
true
true
true
true
555
1
INTRODUCTION
1
4
[ "b4", "b5", "b6", "b6", "b8", "b9", "b12" ]
16,971,457
pmid-8639330|pmid-12798234|pmid-14499933|pmid-14499933|pmid-9783157|pmid-10564466|pmid-14747560
To date, the Fuselloviridae are the most widespread on earth in the Sulfolobus genus with viruses sharing similar morphology as well as DNA genome size and organization (9–12).
[ "4", "5", "6", "6", "8", "9", "12" ]
176
3,305
0
false
To date, the Fuselloviridae are the most widespread on earth in the Sulfolobus genus with viruses sharing similar morphology as well as DNA genome size and organization.
[ "9–12" ]
To date, the Fuselloviridae are the most widespread on earth in the Sulfolobus genus with viruses sharing similar morphology as well as DNA genome size and organization.
true
true
true
true
true
555
2
INTRODUCTION
1
13
[ "b13", "b14", "b14", "b18" ]
16,971,457
pmid-16453555|pmid-1502176|pmid-1502176|pmid-12234006|pmid-8935654|pmid-9806856|pmid-11092863
Sulfolobus spindle-shaped virus 1 (SSV1) is the best studied member of this family and demonstrated to be temperate both in Sulfolobus shibatae and in non-natural but related Sulfolobus hosts, such as Sulfolobus solfataricus (13,14); infection, integration of DNA into the host chromosome and production of virions cause...
[ "13", "14", "14", "18" ]
521
3,306
0
false
Sulfolobus spindle-shaped virus 1 (SSV1) is the best studied member of this family and demonstrated to be temperate both in Sulfolobus shibatae and in non-natural but related Sulfolobus hosts, such as Sulfolobus solfataricus ; infection, integration of DNA into the host chromosome and production of virions cause appare...
[ "13,14", "14–18" ]
Sulfolobus spindle-shaped virus 1 is the best studied member of this family and demonstrated to be temperate both in Sulfolobus shibatae and in non-natural but related Sulfolobus hosts, such as Sulfolobus solfataricus ; infection, integration of DNA into the host chromosome and production of virions cause apparently no...
true
true
true
true
true
556
3
INTRODUCTION
1
19
[ "b19", "b12" ]
16,971,457
pmid-12798235|pmid-14747560|pmid-12787352|pmid-12787352
More recently, another fusellovirus, SSV2 from Sulfolobus islandicus strain 15/4 was isolated, characterized and its complete genomic sequence determined.
[ "19", "12" ]
154
3,307
0
false
More recently, another fusellovirus, SSV2 from Sulfolobus islandicus strain 15/4 was isolated, characterized and its complete genomic sequence determined.
[]
More recently, another fusellovirus, SSV2 from Sulfolobus islandicus strain 15/4 was isolated, characterized and its complete genomic sequence determined.
true
true
true
true
true
557
3
INTRODUCTION
1
19
[ "b19", "b12" ]
16,971,457
pmid-12798235|pmid-14747560|pmid-12787352|pmid-12787352
SSV2 shares with SSV1 similar morphology, replication and DNA size (19).
[ "19", "12" ]
72
3,308
1
false
SSV2 shares with SSV1 similar morphology, replication and DNA size.
[ "19" ]
SSV2 shares with SSV1 similar morphology, replication and DNA size.
true
true
true
true
true
557
3
INTRODUCTION
1
12
[ "b19", "b12" ]
16,971,457
pmid-12798235|pmid-14747560|pmid-12787352|pmid-12787352
The overall genome architecture is conserved but the low similarity in the sequences should be responsible for the higher copy number and the lack of a strong ultraviolet induction of episomal SSV2 DNA and particle production, as well as for the different integration of the SSV2 genome which occurs into the host chromo...
[ "19", "12" ]
383
3,309
1
false
The overall genome architecture is conserved but the low similarity in the sequences should be responsible for the higher copy number and the lack of a strong ultraviolet induction of episomal SSV2 DNA and particle production, as well as for the different integration of the SSV2 genome which occurs into the host chromo...
[ "12" ]
The overall genome architecture is conserved but the low similarity in the sequences should be responsible for the higher copy number and the lack of a strong ultraviolet induction of episomal SSV2 DNA and particle production, as well as for the different integration of the SSV2 genome which occurs into the host chromo...
true
true
true
true
true
557
4
INTRODUCTION
1
9
[ "b20", "b21", "b9", "b9", "b19" ]
16,971,457
pmid-10430561|pmid-11054282|pmid-10564466|pmid-10564466|pmid-12798235
S.islandicus REY15/4 harbors also a small plasmid, pSSVx, assigned to the pRN family (20,21) of Sulfolobales plasmids; pSSVx is also capable of spreading in the cell cultures of S.solfataricus but only in the presence of either SSV2 or SSV1, necessary as helpers (9).
[ "20", "21", "9", "9", "19" ]
267
3,310
1
false
S.islandicus REY15/4 harbors also a small plasmid, pSSVx, assigned to the pRN family of Sulfolobales plasmids; pSSVx is also capable of spreading in the cell cultures of S.solfataricus but only in the presence of either SSV2 or SSV1, necessary as helpers.
[ "20,21", "9" ]
S.islandicus REY15/4 harbors also a small plasmid, pSSVx, assigned to the pRN family of Sulfolobales plasmids; pSSVx is also capable of spreading in the cell cultures of S.solfataricus but only in the presence of either SSV2 or SSV1, necessary as helpers.
true
true
true
true
true
558
4
INTRODUCTION
1
20
[ "b20", "b21", "b9", "b9", "b19" ]
16,971,457
pmid-10430561|pmid-11054282|pmid-10564466|pmid-10564466|pmid-12798235
In fact, pSSVx contains two open reading frames showing high-sequence similarity to a tandem of ORFs in both SSV1 and SSV2 genomes; the proteins encoded by these ORFs are probably necessary for specific recognition of the pSSVx DNA but need viral helper components for capsid formation and packaging (9,19).
[ "20", "21", "9", "9", "19" ]
307
3,311
0
false
In fact, pSSVx contains two open reading frames showing high-sequence similarity to a tandem of ORFs in both SSV1 and SSV2 genomes; the proteins encoded by these ORFs are probably necessary for specific recognition of the pSSVx DNA but need viral helper components for capsid formation and packaging.
[ "9,19" ]
In fact, pSSVx contains two open reading frames showing high-sequence similarity to a tandem of ORFs in both SSV1 and SSV2 genomes; the proteins encoded by these ORFs are probably necessary for specific recognition of the pSSVx DNA but need viral helper components for capsid formation and packaging.
true
true
true
true
true
558
5
INTRODUCTION
1
22
[ "b22", "b23", "b24", "b25", "b26", "b27", "b28", "b29", "b32", "b33", "b34", "b35" ]
16,971,457
NA|pmid-11453458|pmid-12583906|pmid-11427726|pmid-8132506|pmid-16212434|pmid-16335965|pmid-8935654|pmid-12813089|NA|pmid-16391031|pmid-12787352
In general, the choice of S.solfataricus as a model for fundamental understanding of the genetics of extremely thermophilic archaea is due to growth conditions operatively non-prohibitive (22) and capability of maintaining and propagating either natural or genetically modified extrachromosomal DNAs (23,24) from other s...
[ "22", "23", "24", "25", "26", "27", "28", "29", "32", "33", "34", "35" ]
327
3,312
1
false
In general, the choice of S.solfataricus as a model for fundamental understanding of the genetics of extremely thermophilic archaea is due to growth conditions operatively non-prohibitive and capability of maintaining and propagating either natural or genetically modified extrachromosomal DNAs from other sources.
[ "22", "23,24" ]
In general, the choice of S.solfataricus as a model for fundamental understanding of the genetics of extremely thermophilic archaea is due to growth conditions operatively non-prohibitive and capability of maintaining and propagating either natural or genetically modified extrachromosomal DNAs from other sources.
true
true
true
true
true
559
5
INTRODUCTION
1
25
[ "b22", "b23", "b24", "b25", "b26", "b27", "b28", "b29", "b32", "b33", "b34", "b35" ]
16,971,457
NA|pmid-11453458|pmid-12583906|pmid-11427726|pmid-8132506|pmid-16212434|pmid-16335965|pmid-8935654|pmid-12813089|NA|pmid-16391031|pmid-12787352
The complete genome of S.solfataricus has also been determined (25), the biochemical characterization of many gene products obtained (26) and the development of post-genomics tools such as proteomics and metabolic pathway reconstruction recently attempted (27,28).
[ "22", "23", "24", "25", "26", "27", "28", "29", "32", "33", "34", "35" ]
264
3,313
1
false
The complete genome of S.solfataricus has also been determined, the biochemical characterization of many gene products obtained and the development of post-genomics tools such as proteomics and metabolic pathway reconstruction recently attempted.
[ "25", "26", "27,28" ]
The complete genome of S.solfataricus has also been determined, the biochemical characterization of many gene products obtained and the development of post-genomics tools such as proteomics and metabolic pathway reconstruction recently attempted.
true
true
true
true
true
559
5
INTRODUCTION
1
33
[ "b22", "b23", "b24", "b25", "b26", "b27", "b28", "b29", "b32", "b33", "b34", "b35" ]
16,971,457
NA|pmid-11453458|pmid-12583906|pmid-11427726|pmid-8132506|pmid-16212434|pmid-16335965|pmid-8935654|pmid-12813089|NA|pmid-16391031|pmid-12787352
Some progress has been made to develop stable transformation (29–32), specific gene disruption methods (33) as well as overexpression of foreign and homologous genes (34); nevertheless none of the systems described so far has been proven efficient for reproducibility and stability of gene cloning and protein expression...
[ "22", "23", "24", "25", "26", "27", "28", "29", "32", "33", "34", "35" ]
616
3,314
1
false
Some progress has been made to develop stable transformation, specific gene disruption methods as well as overexpression of foreign and homologous genes ; nevertheless none of the systems described so far has been proven efficient for reproducibility and stability of gene cloning and protein expression levels in Sulfol...
[ "29–32", "33", "34", "35" ]
Some progress has been made to develop stable transformation, specific gene disruption methods as well as overexpression of foreign and homologous genes ; nevertheless none of the systems described so far has been proven efficient for reproducibility and stability of gene cloning and protein expression levels in Sulfol...
true
true
true
true
true
559
6
INTRODUCTION
0
null
null
16,971,457
null
In this study, a genetic system for Sulfolobus was developed that is based on the satellite virus pSSVx from S. islandicus 15/4.
null
128
3,315
0
false
null
null
In this study, a genetic system for Sulfolobus was developed that is based on the satellite virus pSSVx from S. islandicus 15/4.
true
true
true
true
true
560
6
INTRODUCTION
0
null
null
16,971,457
null
The different recombinant Escherichia coli–Sulfolobus solfataricus shuttle vectors constructed retained the wild-type capability to replicate at high copy-number and to spread in cell cultures in the presence of its helper virus SSV2.
null
234
3,316
0
false
null
null
The different recombinant Escherichia coli–Sulfolobus solfataricus shuttle vectors constructed retained the wild-type capability to replicate at high copy-number and to spread in cell cultures in the presence of its helper virus SSV2.
true
true
true
true
true
560
6
INTRODUCTION
0
null
null
16,971,457
null
Sulfolobus transformants were demonstrated to be stable and propagate the pSSVx derived plasmids in a reproducible and constant fashion without any rearrangement, recombination or integration into the chromosome.
null
212
3,317
0
false
null
null
Sulfolobus transformants were demonstrated to be stable and propagate the pSSVx derived plasmids in a reproducible and constant fashion without any rearrangement, recombination or integration into the chromosome.
true
true
true
true
true
560
7
INTRODUCTION
1
32
[ "b32" ]
16,971,457
pmid-12813089
Moreover, stable complementation of a β-galactosidase mutant of S.solfataricus previously isolated and characterized in our laboratory (32) and reproducible gene expression levels were also obtained by introducing the β-galactosidase gene (lacS) as a reporter under the control of a strong and heat-inducible promoter in...
[ "32" ]
342
3,318
1
false
Moreover, stable complementation of a β-galactosidase mutant of S.solfataricus previously isolated and characterized in our laboratory and reproducible gene expression levels were also obtained by introducing the β-galactosidase gene (lacS) as a reporter under the control of a strong and heat-inducible promoter into th...
[ "32" ]
Moreover, stable complementation of a β-galactosidase mutant of S.solfataricus previously isolated and characterized in our laboratory and reproducible gene expression levels were also obtained by introducing the β-galactosidase gene (lacS) as a reporter under the control of a strong and heat-inducible promoter into th...
true
true
true
true
true
561
0
DISCUSSION
0
null
null
16,971,457
pmid-14686936|pmid-11303501|pmid-10704475
In this paper, we have developed a relatively small-sized and high copy number shuttle vector for S.solfataricus based on the satellite virus pSSVx from S.islandicus REY15/4.
null
174
3,319
0
false
null
null
In this paper, we have developed a relatively small-sized and high copy number shuttle vector for S.solfataricus based on the satellite virus pSSVx from S.islandicus REY15/4.
true
true
true
true
true
562
1
DISCUSSION
0
null
null
16,971,457
pmid-8639330|pmid-12798234|pmid-14499933|pmid-14499933|pmid-9783157|pmid-10564466|pmid-14747560
An extended intergenic region between the still uncharacterized ORFs c68 and 288 on the pSSVx genome sequence appeared potentially useful for inserting foreign DNA.
null
164
3,320
0
false
null
null
An extended intergenic region between the still uncharacterized ORFs c68 and 288 on the pSSVx genome sequence appeared potentially useful for inserting foreign DNA.
true
true
true
true
true
563
1
DISCUSSION
0
null
null
16,971,457
pmid-8639330|pmid-12798234|pmid-14499933|pmid-14499933|pmid-9783157|pmid-10564466|pmid-14747560
In fact, the vector pSSVrt clearly showed efficient replication and maintenance in SSV2 lysogens of the strains GθW and P2.
null
123
3,321
0
false
null
null
In fact, the vector pSSVrt clearly showed efficient replication and maintenance in SSV2 lysogens of the strains GθW and P2.
true
true
true
true
true
563
2
DISCUSSION
1
29
[ "b29", "b46", "b48" ]
16,971,457
pmid-16453555|pmid-1502176|pmid-1502176|pmid-12234006|pmid-8935654|pmid-9806856|pmid-11092863
The insertion of foreign sequences into the pSSVrt vector allowed also to determine the limiting upper size (∼11 kb) of the DNA to be accommodated in the virus particles.
[ "29", "46", "48" ]
170
3,322
0
false
The insertion of foreign sequences into the pSSVrt vector allowed also to determine the limiting upper size (∼11 kb) of the DNA to be accommodated in the virus particles.
[]
The insertion of foreign sequences into the pSSVrt vector allowed also to determine the limiting upper size (∼11 kb) of the DNA to be accommodated in the virus particles.
true
true
true
true
true
564
2
DISCUSSION
1
29
[ "b29", "b46", "b48" ]
16,971,457
pmid-16453555|pmid-1502176|pmid-1502176|pmid-12234006|pmid-8935654|pmid-9806856|pmid-11092863
The additional sequences severely affected packaging and spreading rather than the transfer and/or the replication/maintenance of the viral DNA.
[ "29", "46", "48" ]
144
3,323
0
false
The additional sequences severely affected packaging and spreading rather than the transfer and/or the replication/maintenance of the viral DNA.
[]
The additional sequences severely affected packaging and spreading rather than the transfer and/or the replication/maintenance of the viral DNA.
true
true
true
true
true
564
2
DISCUSSION
1
29
[ "b29", "b46", "b48" ]
16,971,457
pmid-16453555|pmid-1502176|pmid-1502176|pmid-12234006|pmid-8935654|pmid-9806856|pmid-11092863
These results also indicated that transport in viable virions and no other mechanism, such as conjugation (29,46–48), is responsible for cell-to-cell transfer of this genetic element.
[ "29", "46", "48" ]
183
3,324
0
false
These results also indicated that transport in viable virions and no other mechanism, such as conjugation, is responsible for cell-to-cell transfer of this genetic element.
[ "29,46–48" ]
These results also indicated that transport in viable virions and no other mechanism, such as conjugation, is responsible for cell-to-cell transfer of this genetic element.
true
true
true
true
true
564
3
DISCUSSION
1
35
[ "b35", "b35" ]
16,971,457
pmid-12798235|pmid-14747560|pmid-12787352|pmid-12787352
A ‘minimal’ vector pMSSV was devised to accommodate inserts of a wider size range at least up to the 2.0 kb of a smaller tf55α/lacS expression cassette (35).
[ "35", "35" ]
157
3,325
1
false
A ‘minimal’ vector pMSSV was devised to accommodate inserts of a wider size range at least up to the 2.0 kb of a smaller tf55α/lacS expression cassette.
[ "35" ]
A ‘minimal’ vector pMSSV was devised to accommodate inserts of a wider size range at least up to the 2.0 kb of a smaller tf55α/lacS expression cassette.
true
true
true
true
true
565
3
DISCUSSION
1
35
[ "b35", "b35" ]
16,971,457
pmid-12798235|pmid-14747560|pmid-12787352|pmid-12787352
In fact, the deletion of a region non-essential for replication and selection in E.coli and a shortened lacS 3′-UTR resulted in an efficient shuttle vector able to transform S.solfataricus and to spread in primary cultures.
[ "35", "35" ]
223
3,326
0
false
In fact, the deletion of a region non-essential for replication and selection in E.coli and a shortened lacS 3′-UTR resulted in an efficient shuttle vector able to transform S.solfataricus and to spread in primary cultures.
[]
In fact, the deletion of a region non-essential for replication and selection in E.coli and a shortened lacS 3′-UTR resulted in an efficient shuttle vector able to transform S.solfataricus and to spread in primary cultures.
true
true
true
true
true
565
3
DISCUSSION
1
35
[ "b35", "b35" ]
16,971,457
pmid-12798235|pmid-14747560|pmid-12787352|pmid-12787352
The vector did not suffer either integration into the host chromosome or rearrangements and resided with undetectable to 130 copies per chromosome, the number depending on the cell growth phase.
[ "35", "35" ]
194
3,327
0
false
The vector did not suffer either integration into the host chromosome or rearrangements and resided with undetectable to 130 copies per chromosome, the number depending on the cell growth phase.
[]
The vector did not suffer either integration into the host chromosome or rearrangements and resided with undetectable to 130 copies per chromosome, the number depending on the cell growth phase.
true
true
true
true
true
565
3
DISCUSSION
1
35
[ "b35", "b35" ]
16,971,457
pmid-12798235|pmid-14747560|pmid-12787352|pmid-12787352
Interestingly, β-galactosidase activity in complemented mutant cells followed an increasing trend which correlated to the plasmid accumulation up to stationary phase and was not dependent on the number of the generations.
[ "35", "35" ]
221
3,328
0
false
Interestingly, β-galactosidase activity in complemented mutant cells followed an increasing trend which correlated to the plasmid accumulation up to stationary phase and was not dependent on the number of the generations.
[]
Interestingly, β-galactosidase activity in complemented mutant cells followed an increasing trend which correlated to the plasmid accumulation up to stationary phase and was not dependent on the number of the generations.
true
true
true
true
true
565
3
DISCUSSION
1
35
[ "b35", "b35" ]
16,971,457
pmid-12798235|pmid-14747560|pmid-12787352|pmid-12787352
lacS gene expression was inducible by thermal stress, namely it was confirmed to be transcriptionally regulated by the chaperonin gene promoter.
[ "35", "35" ]
144
3,329
0
false
lacS gene expression was inducible by thermal stress, namely it was confirmed to be transcriptionally regulated by the chaperonin gene promoter.
[]
lacS gene expression was inducible by thermal stress, namely it was confirmed to be transcriptionally regulated by the chaperonin gene promoter.
false
true
true
true
false
565
3
DISCUSSION
1
35
[ "b35", "b35" ]
16,971,457
pmid-12798235|pmid-14747560|pmid-12787352|pmid-12787352
However, heat shock did not produce the same β-galactosidase activity increase (∼10-fold) described by Jonuscheit et al (35), although maximum gene expression resulted at comparable levels in the two host/vector systems (3 versus 5 U/mg).
[ "35", "35" ]
238
3,330
1
false
However, heat shock did not produce the same β-galactosidase activity increase (∼10-fold) described by Jonuscheit et al, although maximum gene expression resulted at comparable levels in the two host/vector systems (3 versus 5 U/mg).
[ "35" ]
However, heat shock did not produce the same β-galactosidase activity increase (∼10-fold) described by Jonuscheit et al, although maximum gene expression resulted at comparable levels in the two host/vector systems.
true
true
true
true
true
565
4
DISCUSSION
0
null
null
16,971,457
pmid-10430561|pmid-11054282|pmid-10564466|pmid-10564466|pmid-12798235
Maximum size for DNA insertion into pMSSVlacS was determined to be ∼1.3 kb (data not shown).
null
92
3,331
0
false
null
null
Maximum size for DNA insertion into pMSSVlacS was determined to be ∼1.3 kb (data not shown).
true
true
true
true
true
566
4
DISCUSSION
0
null
null
16,971,457
pmid-10430561|pmid-11054282|pmid-10564466|pmid-10564466|pmid-12798235
In principle longer inserts up to 3.1 kb can be accommodated after cloning in E.coli and excision of the bacterial sequences prior to the transfer into Sulfolobus.
null
163
3,332
0
false
null
null
In principle longer inserts up to 3.1 kb can be accommodated after cloning in E.coli and excision of the bacterial sequences prior to the transfer into Sulfolobus.
true
true
true
true
true
566
5
DISCUSSION
0
null
null
16,971,457
NA|pmid-11453458|pmid-12583906|pmid-11427726|pmid-8132506|pmid-16212434|pmid-16335965|pmid-8935654|pmid-12813089|NA|pmid-16391031|pmid-12787352
Maintenance of pMSSVlacS in early exponential grown and/or plated cells seemed to be the critical point for the efficacy of this system, because of both the low copy number (this work) and the reduced viral production in metabolically active cells (P. Contursi, unpublished data).
null
280
3,333
0
false
null
null
Maintenance of pMSSVlacS in early exponential grown and/or plated cells seemed to be the critical point for the efficacy of this system, because of both the low copy number (this work) and the reduced viral production in metabolically active cells (P. Contursi, unpublished data).
true
true
true
true
true
567
5
DISCUSSION
0
null
null
16,971,457
NA|pmid-11453458|pmid-12583906|pmid-11427726|pmid-8132506|pmid-16212434|pmid-16335965|pmid-8935654|pmid-12813089|NA|pmid-16391031|pmid-12787352
In fact, segregation of the plasmid in an actively dividing cell (in which SSV2 is also maintained at low copy number and hence hardly sustains active replication and/or particle proliferation of pSSVx and derivatives) can be very asymmetrical until it is lost.
null
261
3,334
0
false
null
null
In fact, segregation of the plasmid in an actively dividing cell (in which SSV2 is also maintained at low copy number and hence hardly sustains active replication and/or particle proliferation of pSSVx and derivatives) can be very asymmetrical until it is lost.
true
true
true
true
true
567
5
DISCUSSION
0
null
null
16,971,457
NA|pmid-11453458|pmid-12583906|pmid-11427726|pmid-8132506|pmid-16212434|pmid-16335965|pmid-8935654|pmid-12813089|NA|pmid-16391031|pmid-12787352
We were able to overcome this bottleneck; as expected, efficient selection and stabilization of single pMSSVlacS transformants was indeed obtained by plating cells grown up to stationary phase (maximum copy number and highest viral production), by avoiding critical dilutions in the resuspension of single colonies and/o...
null
388
3,335
0
false
null
null
We were able to overcome this bottleneck; as expected, efficient selection and stabilization of single pMSSVlacS transformants was indeed obtained by plating cells grown up to stationary phase (maximum copy number and highest viral production), by avoiding critical dilutions in the resuspension of single colonies and/o...
true
true
true
true
true
567
6
DISCUSSION
0
null
null
16,971,457
null
This system presents many advantages compared with others already mentioned: (i) after DNA transfer, the vector propagates efficiently throughout the culture as a virus, overcoming the usual low transformation efficiency of Sulfolobus cells; (ii) the vector is stably maintained at high-copy number with no integration i...
null
513
3,336
0
false
null
null
This system presents many advantages compared with others already mentioned: (i) after DNA transfer, the vector propagates efficiently throughout the culture as a virus, overcoming the usual low transformation efficiency of Sulfolobus cells; (ii) the vector is stably maintained at high-copy number with no integration i...
true
true
true
true
true
568
7
DISCUSSION
0
null
null
16,971,457
pmid-12813089
The availability of this new two-element transformation systems based on SSV2 and the engineered pSSVx will contribute to clarify the mechanisms responsible for the satellite/helper dependence as well as for replication, gene regulation and packaging of the episomal DNAs.
null
272
3,337
0
false
null
null
The availability of this new two-element transformation systems based on SSV2 and the engineered pSSVx will contribute to clarify the mechanisms responsible for the satellite/helper dependence as well as for replication, gene regulation and packaging of the episomal DNAs.
true
true
true
true
true
569
8
DISCUSSION
0
null
null
16,971,457
null
Further work will explore the use of this vector for the expression of both homologous and heterologous genes in S.solfataricus as well as for testing Sulfolobus regulatory sequences.
null
183
3,338
0
false
null
null
Further work will explore the use of this vector for the expression of both homologous and heterologous genes in S.solfataricus as well as for testing Sulfolobus regulatory sequences.
true
true
true
true
true
570
0
INTRODUCTION
1
1–7
[ "B1 B2 B3 B4 B5 B6 B7", "B8", "B9", "B10", "B11", "B12", "B10", "B13", "B14", "B15", "B16" ]
17,355,988
pmid-2850007|pmid-3052282|NA|pmid-16036556|pmid-15952889|pmid-16421093|pmid-16857582|pmid-7574479|pmid-368075|pmid-2997151|pmid-6393125|pmid-15090519|pmid-2997151|pmid-7005228|pmid-7478986|pmid-1349852|pmid-2040637|NA|NA|pmid-16505960
DNA polymerase III holoenzyme (Pol III HE), the enzyme responsible for Escherichia coli chromosomal DNA synthesis, is a complex of 10 different polypeptides (1–7).
[ "1–7", "8", "9", "10", "11", "12", "10", "13", "14", "15", "16" ]
163
3,339
1
false
DNA polymerase III holoenzyme (Pol III HE), the enzyme responsible for Escherichia coli chromosomal DNA synthesis, is a complex of 10 different polypeptides.
[ "1–7" ]
DNA polymerase III holoenzyme (Pol III HE), the enzyme responsible for Escherichia coli chromosomal DNA synthesis, is a complex of 10 different polypeptides.
true
true
true
true
true
571
0
INTRODUCTION
1
8
[ "B1 B2 B3 B4 B5 B6 B7", "B8", "B9", "B10", "B11", "B12", "B10", "B13", "B14", "B15", "B16" ]
17,355,988
pmid-2850007|pmid-3052282|NA|pmid-16036556|pmid-15952889|pmid-16421093|pmid-16857582|pmid-7574479|pmid-368075|pmid-2997151|pmid-6393125|pmid-15090519|pmid-2997151|pmid-7005228|pmid-7478986|pmid-1349852|pmid-2040637|NA|NA|pmid-16505960
It is comprised of three functionally distinct but interconnected subassemblies: the core polymerase, the sliding clamp and the clamp loader complex (8).
[ "1–7", "8", "9", "10", "11", "12", "10", "13", "14", "15", "16" ]
153
3,340
1
false
It is comprised of three functionally distinct but interconnected subassemblies: the core polymerase, the sliding clamp and the clamp loader complex.
[ "8" ]
It is comprised of three functionally distinct but interconnected subassemblies: the core polymerase, the sliding clamp and the clamp loader complex.
true
true
true
true
true
571
0
INTRODUCTION
1
9
[ "B1 B2 B3 B4 B5 B6 B7", "B8", "B9", "B10", "B11", "B12", "B10", "B13", "B14", "B15", "B16" ]
17,355,988
pmid-2850007|pmid-3052282|NA|pmid-16036556|pmid-15952889|pmid-16421093|pmid-16857582|pmid-7574479|pmid-368075|pmid-2997151|pmid-6393125|pmid-15090519|pmid-2997151|pmid-7005228|pmid-7478986|pmid-1349852|pmid-2040637|NA|NA|pmid-16505960
There are two core polymerases in the HE, each consisting of three different subunits (9): α, the DNA polymerase (10); ε, the proofreading exonuclease (11); and θ, which has a role in stabilizing ε (12).
[ "1–7", "8", "9", "10", "11", "12", "10", "13", "14", "15", "16" ]
203
3,341
1
false
There are two core polymerases in the HE, each consisting of three different subunits : α, the DNA polymerase ; ε, the proofreading exonuclease ; and θ, which has a role in stabilizing ε.
[ "9", "10", "11", "12" ]
There are two core polymerases in the HE, each consisting of three different subunits : α, the DNA polymerase ; ε, the proofreading exonuclease ; and θ, which has a role in stabilizing ε.
true
true
true
true
true
571
0
INTRODUCTION
1
10
[ "B1 B2 B3 B4 B5 B6 B7", "B8", "B9", "B10", "B11", "B12", "B10", "B13", "B14", "B15", "B16" ]
17,355,988
pmid-2850007|pmid-3052282|NA|pmid-16036556|pmid-15952889|pmid-16421093|pmid-16857582|pmid-7574479|pmid-368075|pmid-2997151|pmid-6393125|pmid-15090519|pmid-2997151|pmid-7005228|pmid-7478986|pmid-1349852|pmid-2040637|NA|NA|pmid-16505960
The core polymerase is neither highly processive nor rapid in DNA synthesis: it polymerizes nucleotides at a rate of ∼20/s (10) and dissociates from DNA after incorporating 10–20 nt (13).
[ "1–7", "8", "9", "10", "11", "12", "10", "13", "14", "15", "16" ]
187
3,342
1
false
The core polymerase is neither highly processive nor rapid in DNA synthesis: it polymerizes nucleotides at a rate of ∼20/s and dissociates from DNA after incorporating 10–20 nt.
[ "10", "13" ]
The core polymerase is neither highly processive nor rapid in DNA synthesis: it polymerizes nucleotides at a rate of ∼20/s and dissociates from DNA after incorporating 10–20 nt.
true
true
true
true
true
571
0
INTRODUCTION
1
14
[ "B1 B2 B3 B4 B5 B6 B7", "B8", "B9", "B10", "B11", "B12", "B10", "B13", "B14", "B15", "B16" ]
17,355,988
pmid-2850007|pmid-3052282|NA|pmid-16036556|pmid-15952889|pmid-16421093|pmid-16857582|pmid-7574479|pmid-368075|pmid-2997151|pmid-6393125|pmid-15090519|pmid-2997151|pmid-7005228|pmid-7478986|pmid-1349852|pmid-2040637|NA|NA|pmid-16505960
The β sliding clamp subunit, needed for rapid and highly processive DNA synthesis (14), is a ring-shaped head-to-tail dimer (15).
[ "1–7", "8", "9", "10", "11", "12", "10", "13", "14", "15", "16" ]
129
3,343
1
false
The β sliding clamp subunit, needed for rapid and highly processive DNA synthesis, is a ring-shaped head-to-tail dimer.
[ "14", "15" ]
The β sliding clamp subunit, needed for rapid and highly processive DNA synthesis, is a ring-shaped head-to-tail dimer.
true
true
true
true
true
571
0
INTRODUCTION
1
16
[ "B1 B2 B3 B4 B5 B6 B7", "B8", "B9", "B10", "B11", "B12", "B10", "B13", "B14", "B15", "B16" ]
17,355,988
pmid-2850007|pmid-3052282|NA|pmid-16036556|pmid-15952889|pmid-16421093|pmid-16857582|pmid-7574479|pmid-368075|pmid-2997151|pmid-6393125|pmid-15090519|pmid-2997151|pmid-7005228|pmid-7478986|pmid-1349852|pmid-2040637|NA|NA|pmid-16505960
Once it is assembled onto DNA by the clamp loader complex, interaction of β2 with the α subunit confers efficient synthesis on all core polymerase subassemblies (16).
[ "1–7", "8", "9", "10", "11", "12", "10", "13", "14", "15", "16" ]
166
3,344
1
false
Once it is assembled onto DNA by the clamp loader complex, interaction of β2 with the α subunit confers efficient synthesis on all core polymerase subassemblies.
[ "16" ]
Once it is assembled onto DNA by the clamp loader complex, interaction of β2 with the α subunit confers efficient synthesis on all core polymerase subassemblies.
true
true
true
true
true
571
1
INTRODUCTION
1
17
[ "B17", "B18 B19 B20 B21", "B22", "B23", "B24", "B25" ]
17,355,988
pmid-11101526|pmid-11719243|pmid-12519754|pmid-14610067|pmid-14610068|pmid-9722585|pmid-9989506|pmid-7768937|pmid-11525728|pmid-10550212|pmid-15943980
The single clamp loader within Pol III HE contains seven subunits, with composition τ2γδδ′χψ (17).
[ "17", "18–21", "22", "23", "24", "25" ]
98
3,345
1
false
The single clamp loader within Pol III HE contains seven subunits, with composition τ2γδδ′χψ.
[ "17" ]
The single clamp loader within Pol III HE contains seven subunits, with composition τ2γδδ′χψ.
true
true
true
true
true
572
1
INTRODUCTION
1
18–21
[ "B17", "B18 B19 B20 B21", "B22", "B23", "B24", "B25" ]
17,355,988
pmid-11101526|pmid-11719243|pmid-12519754|pmid-14610067|pmid-14610068|pmid-9722585|pmid-9989506|pmid-7768937|pmid-11525728|pmid-10550212|pmid-15943980
It hydrolyzes ATP in a DNA-dependent manner to load β2 clamps onto DNA for interaction with both core polymerases (18–21).
[ "17", "18–21", "22", "23", "24", "25" ]
122
3,346
1
false
It hydrolyzes ATP in a DNA-dependent manner to load β2 clamps onto DNA for interaction with both core polymerases.
[ "18–21" ]
It hydrolyzes ATP in a DNA-dependent manner to load β2 clamps onto DNA for interaction with both core polymerases.
true
true
true
true
true
572
1
INTRODUCTION
1
22
[ "B17", "B18 B19 B20 B21", "B22", "B23", "B24", "B25" ]
17,355,988
pmid-11101526|pmid-11719243|pmid-12519754|pmid-14610067|pmid-14610068|pmid-9722585|pmid-9989506|pmid-7768937|pmid-11525728|pmid-10550212|pmid-15943980
The χ and ψ subunits are involved in binding to ssDNA-binding protein (SSB) (22) and participate in the primase-to-polymerase switch on the lagging strand (23).
[ "17", "18–21", "22", "23", "24", "25" ]
160
3,347
1
false
The χ and ψ subunits are involved in binding to ssDNA-binding protein (SSB) and participate in the primase-to-polymerase switch on the lagging strand.
[ "22", "23" ]
The χ and ψ subunits are involved in binding to ssDNA-binding protein (SSB) and participate in the primase-to-polymerase switch on the lagging strand.
true
true
true
true
true
572
1
INTRODUCTION
1
24
[ "B17", "B18 B19 B20 B21", "B22", "B23", "B24", "B25" ]
17,355,988
pmid-11101526|pmid-11719243|pmid-12519754|pmid-14610067|pmid-14610068|pmid-9722585|pmid-9989506|pmid-7768937|pmid-11525728|pmid-10550212|pmid-15943980
In an interaction modulated by δ′, the δ subunit binds to β2 (24), inducing a conformational change in the clamp and subsequent opening of the β2 ring (25).
[ "17", "18–21", "22", "23", "24", "25" ]
156
3,348
1
false
In an interaction modulated by δ′, the δ subunit binds to β2, inducing a conformational change in the clamp and subsequent opening of the β2 ring.
[ "24", "25" ]
In an interaction modulated by δ′, the δ subunit binds to β2, inducing a conformational change in the clamp and subsequent opening of the β2 ring.
true
true
true
true
true
572
2
INTRODUCTION
1
26
[ "B26", "B27", "B28", "B29 B30 B31", "B32", "B33" ]
17,355,988
pmid-6316113|pmid-6358801|pmid-7037770|pmid-2181440|pmid-2187190|pmid-2186364|pmid-11525729|pmid-11078742|NA
The three ATP motor subunits of the clamp loader (γ and the two τ subunits) are encoded by the same gene, dnaX (26,27).
[ "26", "27", "28", "29–31", "32", "33" ]
119
3,349
0
false
The three ATP motor subunits of the clamp loader (γ and the two τ subunits) are encoded by the same gene, dnaX.
[ "26,27" ]
The three ATP motor subunits of the clamp loader (γ and the two τ subunits) are encoded by the same gene, dnaX.
true
true
true
true
true
573
2
INTRODUCTION
1
28
[ "B26", "B27", "B28", "B29 B30 B31", "B32", "B33" ]
17,355,988
pmid-6316113|pmid-6358801|pmid-7037770|pmid-2181440|pmid-2187190|pmid-2186364|pmid-11525729|pmid-11078742|NA
The 71-kDa τ subunit (28) is the full-length dnaX product whereas γ (47 kDa) is a truncated form produced as the result of a programmed translational frameshift (29–31).
[ "26", "27", "28", "29–31", "32", "33" ]
169
3,350
1
false
The 71-kDa τ subunit is the full-length dnaX product whereas γ (47 kDa) is a truncated form produced as the result of a programmed translational frameshift.
[ "28", "29–31" ]
The 71-kDa τ subunit is the full-length dnaX product whereas γ (47 kDa) is a truncated form produced as the result of a programmed translational frameshift.
true
true
true
true
true
573
2
INTRODUCTION
1
26
[ "B26", "B27", "B28", "B29 B30 B31", "B32", "B33" ]
17,355,988
pmid-6316113|pmid-6358801|pmid-7037770|pmid-2181440|pmid-2187190|pmid-2186364|pmid-11525729|pmid-11078742|NA
The γ subunit and the N-terminal portions of the two τ subunits bind δ and δ′, forming a circular pentamer that functions as the clamp loader (32,33).
[ "26", "27", "28", "29–31", "32", "33" ]
150
3,351
0
false
The γ subunit and the N-terminal portions of the two τ subunits bind δ and δ′, forming a circular pentamer that functions as the clamp loader.
[ "32,33" ]
The γ subunit and the N-terminal portions of the two τ subunits bind δ and δ′, forming a circular pentamer that functions as the clamp loader.
true
true
true
true
true
573
3
INTRODUCTION
1
34
[ "B34", "B35", "B34", "B36", "B37 B38 B39", "B39" ]
17,355,988
pmid-1918087|pmid-7768938|pmid-1918087|pmid-8702819|pmid-7768940|pmid-12620221|pmid-14630952|pmid-14630952|pmid-12620221|pmid-16959568|pmid-16959569
The holoenzyme contains two αεθ core polymerases to enable simultaneous replication of both the leading and the lagging strands (34).
[ "34", "35", "34", "36", "37–39", "39" ]
133
3,352
1
false
The holoenzyme contains two αεθ core polymerases to enable simultaneous replication of both the leading and the lagging strands.
[ "34" ]
The holoenzyme contains two αεθ core polymerases to enable simultaneous replication of both the leading and the lagging strands.
true
true
true
true
true
574
3
INTRODUCTION
1
34
[ "B34", "B35", "B34", "B36", "B37 B38 B39", "B39" ]
17,355,988
pmid-1918087|pmid-7768938|pmid-1918087|pmid-8702819|pmid-7768940|pmid-12620221|pmid-14630952|pmid-14630952|pmid-12620221|pmid-16959568|pmid-16959569
These and the clamp loader are held together by the two τ subunits (35) via the strong α –τ interaction (34).
[ "34", "35", "34", "36", "37–39", "39" ]
109
3,353
1
false
These and the clamp loader are held together by the two τ subunits via the strong α –τ interaction.
[ "35", "34" ]
These and the clamp loader are held together by the two τ subunits via the strong α –τ interaction.
true
true
true
true
true
574
3
INTRODUCTION
1
34
[ "B34", "B35", "B34", "B36", "B37 B38 B39", "B39" ]
17,355,988
pmid-1918087|pmid-7768938|pmid-1918087|pmid-8702819|pmid-7768940|pmid-12620221|pmid-14630952|pmid-14630952|pmid-12620221|pmid-16959568|pmid-16959569
Deletion of 48 residues from the C-terminus of α (residues 1113–1160) eliminates its binding to τ, while removal of 705 residues or more from the N-terminus also has a large effect on τ binding.
[ "34", "35", "34", "36", "37–39", "39" ]
194
3,354
0
false
Deletion of 48 residues from the C-terminus of α (residues 1113–1160) eliminates its binding to τ, while removal of 705 residues or more from the N-terminus also has a large effect on τ binding.
[]
Deletion of 48 residues from the C-terminus of α eliminates its binding to τ, while removal of 705 residues or more from the N-terminus also has a large effect on τ binding.
true
true
true
true
true
574
3
INTRODUCTION
1
34
[ "B34", "B35", "B34", "B36", "B37 B38 B39", "B39" ]
17,355,988
pmid-1918087|pmid-7768938|pmid-1918087|pmid-8702819|pmid-7768940|pmid-12620221|pmid-14630952|pmid-14630952|pmid-12620221|pmid-16959568|pmid-16959569
While this may indicate there are two regions of α that contact τ, the involvement of the N-terminal domains of α might be indirect through stabilization of the C-terminal region or through conformational changes that occur during function of the complex.
[ "34", "35", "34", "36", "37–39", "39" ]
255
3,355
0
false
While this may indicate there are two regions of α that contact τ, the involvement of the N-terminal domains of α might be indirect through stabilization of the C-terminal region or through conformational changes that occur during function of the complex.
[]
While this may indicate there are two regions of α that contact τ, the involvement of the N-terminal domains of α might be indirect through stabilization of the C-terminal region or through conformational changes that occur during function of the complex.
true
true
true
true
true
574
3
INTRODUCTION
1
37–39
[ "B34", "B35", "B34", "B36", "B37 B38 B39", "B39" ]
17,355,988
pmid-1918087|pmid-7768938|pmid-1918087|pmid-8702819|pmid-7768940|pmid-12620221|pmid-14630952|pmid-14630952|pmid-12620221|pmid-16959568|pmid-16959569
Indeed, there appear to be two different binding modes for the α–τ interaction (37–39) depending on whether or not the holoenzyme is bound to a primer-template DNA (39).
[ "34", "35", "34", "36", "37–39", "39" ]
169
3,356
1
false
Indeed, there appear to be two different binding modes for the α–τ interaction depending on whether or not the holoenzyme is bound to a primer-template DNA.
[ "37–39", "39" ]
Indeed, there appear to be two different binding modes for the α–τ interaction depending on whether or not the holoenzyme is bound to a primer-template DNA.
true
true
true
true
true
574
4
INTRODUCTION
1
40
[ "B40", "B38", "B41", "B38", "B39", "B42", "B40", "B43", "B43", "B44", "B43", "B64" ]
17,355,988
pmid-11078743|pmid-12620221|pmid-10748120|pmid-12620221|pmid-14630952|pmid-11078744|pmid-11078743|NA|NA|pmid-16505960|NA|pmid-8744573
As shown in Figure 1A, the τ subunit has a five-domain structure (40), the N-terminal Domains I–III being identical to γ.
[ "40", "38", "41", "38", "39", "42", "40", "43", "43", "44", "43", "64" ]
121
3,357
1
false
As shown in Figure 1A, the τ subunit has a five-domain structure, the N-terminal Domains I–III being identical to γ.
[ "40" ]
As shown in Figure 1A, the τ subunit has a five-domain structure, the N-terminal Domains I–III being identical to γ.
true
true
true
true
true
575
4
INTRODUCTION
1
38
[ "B40", "B38", "B41", "B38", "B39", "B42", "B40", "B43", "B43", "B44", "B43", "B64" ]
17,355,988
pmid-11078743|pmid-12620221|pmid-10748120|pmid-12620221|pmid-14630952|pmid-11078744|pmid-11078743|NA|NA|pmid-16505960|NA|pmid-8744573
The unique 24-kDa C-terminal fragment comprising most of Domain IV and all of Domain V (residues 430–643; referred to in this article as τC24) is connected to Domain III by a proline-rich tether that may be flexible (38).
[ "40", "38", "41", "38", "39", "42", "40", "43", "43", "44", "43", "64" ]
221
3,358
1
false
The unique 24-kDa C-terminal fragment comprising most of Domain IV and all of Domain V is connected to Domain III by a proline-rich tether that may be flexible.
[ "residues 430–643; referred to in this article as τC24", "38" ]
The unique 24-kDa C-terminal fragment comprising most of Domain IV and all of Domain V is connected to Domain III by a proline-rich tether that may be flexible.
true
true
true
true
true
575
4
INTRODUCTION
1
38
[ "B40", "B38", "B41", "B38", "B39", "B42", "B40", "B43", "B43", "B44", "B43", "B64" ]
17,355,988
pmid-11078743|pmid-12620221|pmid-10748120|pmid-12620221|pmid-14630952|pmid-11078744|pmid-11078743|NA|NA|pmid-16505960|NA|pmid-8744573
The τC24 protein can be isolated in monomeric form (41), and is reported to bind both to primed DNA (38) and to a 20-mer peptide from the C-terminus of α in an interaction modulated by DNA structure (39).
[ "40", "38", "41", "38", "39", "42", "40", "43", "43", "44", "43", "64" ]
204
3,359
1
false
The τC24 protein can be isolated in monomeric form, and is reported to bind both to primed DNA and to a 20-mer peptide from the C-terminus of α in an interaction modulated by DNA structure.
[ "41", "38", "39" ]
The τC24 protein can be isolated in monomeric form, and is reported to bind both to primed DNA and to a 20-mer peptide from the C-terminus of α in an interaction modulated by DNA structure.
true
true
true
true
true
575
4
INTRODUCTION
1
40
[ "B40", "B38", "B41", "B38", "B39", "B42", "B40", "B43", "B43", "B44", "B43", "B64" ]
17,355,988
pmid-11078743|pmid-12620221|pmid-10748120|pmid-12620221|pmid-14630952|pmid-11078744|pmid-11078743|NA|NA|pmid-16505960|NA|pmid-8744573
The 8-kDa N-terminal region of τC24 (termed Domain IVa, residues 430–498 of τ) is responsible for binding to DnaB helicase (42), and the 16-kDa C-terminal domain (Domain V; residues 499–643, here also referred to as τC16) binds to α (40).
[ "40", "38", "41", "38", "39", "42", "40", "43", "43", "44", "43", "64" ]
238
3,360
1
false
The 8-kDa N-terminal region of τC24 is responsible for binding to DnaB helicase, and the 16-kDa C-terminal domain binds to α.
[ "termed Domain IVa, residues 430–498 of τ", "42", "Domain V; residues 499–643, here also referred to as τC16", "40" ]
The 8-kDa N-terminal region of τC24 is responsible for binding to DnaB helicase, and the 16-kDa C-terminal domain binds to α.
true
true
true
true
true
575
4
INTRODUCTION
1
40
[ "B40", "B38", "B41", "B38", "B39", "B42", "B40", "B43", "B43", "B44", "B43", "B64" ]
17,355,988
pmid-11078743|pmid-12620221|pmid-10748120|pmid-12620221|pmid-14630952|pmid-11078744|pmid-11078743|NA|NA|pmid-16505960|NA|pmid-8744573
Figure 1.Domain structure of the τ subunit of E. coli DNA polymerase III holoenzyme.
[ "40", "38", "41", "38", "39", "42", "40", "43", "43", "44", "43", "64" ]
84
3,361
0
false
Figure 1.Domain structure of the τ subunit of E. coli DNA polymerase III holoenzyme.
[]
Figure 1.Domain structure of the τ subunit of E. coli DNA polymerase III holoenzyme.
true
true
true
true
true
575
4
INTRODUCTION
1
40
[ "B40", "B38", "B41", "B38", "B39", "B42", "B40", "B43", "B43", "B44", "B43", "B64" ]
17,355,988
pmid-11078743|pmid-12620221|pmid-10748120|pmid-12620221|pmid-14630952|pmid-11078744|pmid-11078743|NA|NA|pmid-16505960|NA|pmid-8744573
(A) τ is comprised of five domains; domain boundaries are indicated by residue numbers.
[ "40", "38", "41", "38", "39", "42", "40", "43", "43", "44", "43", "64" ]
87
3,362
0
false
(A) τ is comprised of five domains; domain boundaries are indicated by residue numbers.
[]
(A) τ is comprised of five domains; domain boundaries are indicated by residue numbers.
false
false
true
true
false
575
4
INTRODUCTION
1
40
[ "B40", "B38", "B41", "B38", "B39", "B42", "B40", "B43", "B43", "B44", "B43", "B64" ]
17,355,988
pmid-11078743|pmid-12620221|pmid-10748120|pmid-12620221|pmid-14630952|pmid-11078744|pmid-11078743|NA|NA|pmid-16505960|NA|pmid-8744573
Domains I–III are shared with the γ subunit, while most of the DnaB-binding Domain IV and all of the α-interacting Domain V (τC16) are unique to τ.
[ "40", "38", "41", "38", "39", "42", "40", "43", "43", "44", "43", "64" ]
147
3,363
0
false
Domains I–III are shared with the γ subunit, while most of the DnaB-binding Domain IV and all of the α-interacting Domain V (τC16) are unique to τ.
[]
Domains I–III are shared with the γ subunit, while most of the DnaB-binding Domain IV and all of the α-interacting Domain V (τC16) are unique to τ.
true
true
true
true
true
575
4
INTRODUCTION
1
40
[ "B40", "B38", "B41", "B38", "B39", "B42", "B40", "B43", "B43", "B44", "B43", "B64" ]
17,355,988
pmid-11078743|pmid-12620221|pmid-10748120|pmid-12620221|pmid-14630952|pmid-11078744|pmid-11078743|NA|NA|pmid-16505960|NA|pmid-8744573
Schematic representations of τC24 and τC16 derivatives used in this work are shown below; M+ indicates that τC24 and τC16 and derivatives constructed by deletion of the indicated numbers of residues from the unstructured C-terminus contain an N-terminal methionine introduced during cloning, followed by the indicated re...
[ "40", "38", "41", "38", "39", "42", "40", "43", "43", "44", "43", "64" ]
332
3,364
0
false
Schematic representations of τC24 and τC16 derivatives used in this work are shown below; M+ indicates that τC24 and τC16 and derivatives constructed by deletion of the indicated numbers of residues from the unstructured C-terminus contain an N-terminal methionine introduced during cloning, followed by the indicated re...
[]
Schematic representations of τC24 and τC16 derivatives used in this work are shown below; M+ indicates that τC24 and τC16 and derivatives constructed by deletion of the indicated numbers of residues from the unstructured C-terminus contain an N-terminal methionine introduced during cloning, followed by the indicated re...
true
true
true
true
true
575
4
INTRODUCTION
1
43
[ "B40", "B38", "B41", "B38", "B39", "B42", "B40", "B43", "B43", "B44", "B43", "B64" ]
17,355,988
pmid-11078743|pmid-12620221|pmid-10748120|pmid-12620221|pmid-14630952|pmid-11078744|pmid-11078743|NA|NA|pmid-16505960|NA|pmid-8744573
(B) Solution structure of the structured core of Domain V (residues Pro507–Ser617 of τ) determined by NMR (43).
[ "40", "38", "41", "38", "39", "42", "40", "43", "43", "44", "43", "64" ]
111
3,365
1
false
(B) Solution structure of the structured core of Domain V (residues Pro507–Ser617 of τ) determined by NMR.
[ "43" ]
(B) Solution structure of the structured core of Domain V (residues Pro507–Ser617 of τ) determined by NMR.
false
false
true
true
false
575
4
INTRODUCTION
1
43
[ "B40", "B38", "B41", "B38", "B39", "B42", "B40", "B43", "B43", "B44", "B43", "B64" ]
17,355,988
pmid-11078743|pmid-12620221|pmid-10748120|pmid-12620221|pmid-14630952|pmid-11078744|pmid-11078743|NA|NA|pmid-16505960|NA|pmid-8744573
The sequence of the unstructured region at the C-terminus (43,44) is given in single-letter code, with highly conserved residues (43) marked with larger font.
[ "40", "38", "41", "38", "39", "42", "40", "43", "43", "44", "43", "64" ]
158
3,366
1
false
The sequence of the unstructured region at the C-terminus is given in single-letter code, with highly conserved residues marked with larger font.
[ "43,44", "43" ]
The sequence of the unstructured region at the C-terminus is given in single-letter code, with highly conserved residues marked with larger font.
true
true
true
true
true
575
4
INTRODUCTION
1
40
[ "B40", "B38", "B41", "B38", "B39", "B42", "B40", "B43", "B43", "B44", "B43", "B64" ]
17,355,988
pmid-11078743|pmid-12620221|pmid-10748120|pmid-12620221|pmid-14630952|pmid-11078744|pmid-11078743|NA|NA|pmid-16505960|NA|pmid-8744573
Secondary structural elements that may be induced in this region on interaction with α are indicated below.
[ "40", "38", "41", "38", "39", "42", "40", "43", "43", "44", "43", "64" ]
107
3,367
0
false
Secondary structural elements that may be induced in this region on interaction with α are indicated below.
[]
Secondary structural elements that may be induced in this region on interaction with α are indicated below.
true
true
true
true
true
575
4
INTRODUCTION
1
64
[ "B40", "B38", "B41", "B38", "B39", "B42", "B40", "B43", "B43", "B44", "B43", "B64" ]
17,355,988
pmid-11078743|pmid-12620221|pmid-10748120|pmid-12620221|pmid-14630952|pmid-11078744|pmid-11078743|NA|NA|pmid-16505960|NA|pmid-8744573
Part of the figure was drawn using MOLMOL (64).
[ "40", "38", "41", "38", "39", "42", "40", "43", "43", "44", "43", "64" ]
47
3,368
1
false
Part of the figure was drawn using MOLMOL.
[ "64" ]
Part of the figure was drawn using MOLMOL.
true
true
true
true
true
575
5
INTRODUCTION
1
43
[ "B43", "B43", "B44", "B43", "B64" ]
17,355,988
NA|NA|pmid-16505960|NA|pmid-8744573|pmid-11078743|NA
Domain structure of the τ subunit of E. coli DNA polymerase III holoenzyme.
[ "43", "43", "44", "43", "64" ]
75
3,369
0
false
Domain structure of the τ subunit of E. coli DNA polymerase III holoenzyme.
[]
Domain structure of the τ subunit of E. coli DNA polymerase III holoenzyme.
true
true
true
true
true
576
5
INTRODUCTION
1
43
[ "B43", "B43", "B44", "B43", "B64" ]
17,355,988
NA|NA|pmid-16505960|NA|pmid-8744573|pmid-11078743|NA
(A) τ is comprised of five domains; domain boundaries are indicated by residue numbers.
[ "43", "43", "44", "43", "64" ]
87
3,370
0
false
(A) τ is comprised of five domains; domain boundaries are indicated by residue numbers.
[]
(A) τ is comprised of five domains; domain boundaries are indicated by residue numbers.
false
false
true
true
false
576
5
INTRODUCTION
1
43
[ "B43", "B43", "B44", "B43", "B64" ]
17,355,988
NA|NA|pmid-16505960|NA|pmid-8744573|pmid-11078743|NA
Domains I–III are shared with the γ subunit, while most of the DnaB-binding Domain IV and all of the α-interacting Domain V (τC16) are unique to τ.
[ "43", "43", "44", "43", "64" ]
147
3,371
0
false
Domains I–III are shared with the γ subunit, while most of the DnaB-binding Domain IV and all of the α-interacting Domain V (τC16) are unique to τ.
[]
Domains I–III are shared with the γ subunit, while most of the DnaB-binding Domain IV and all of the α-interacting Domain V (τC16) are unique to τ.
true
true
true
true
true
576
5
INTRODUCTION
1
43
[ "B43", "B43", "B44", "B43", "B64" ]
17,355,988
NA|NA|pmid-16505960|NA|pmid-8744573|pmid-11078743|NA
Schematic representations of τC24 and τC16 derivatives used in this work are shown below; M+ indicates that τC24 and τC16 and derivatives constructed by deletion of the indicated numbers of residues from the unstructured C-terminus contain an N-terminal methionine introduced during cloning, followed by the indicated re...
[ "43", "43", "44", "43", "64" ]
332
3,372
0
false
Schematic representations of τC24 and τC16 derivatives used in this work are shown below; M+ indicates that τC24 and τC16 and derivatives constructed by deletion of the indicated numbers of residues from the unstructured C-terminus contain an N-terminal methionine introduced during cloning, followed by the indicated re...
[]
Schematic representations of τC24 and τC16 derivatives used in this work are shown below; M+ indicates that τC24 and τC16 and derivatives constructed by deletion of the indicated numbers of residues from the unstructured C-terminus contain an N-terminal methionine introduced during cloning, followed by the indicated re...
true
true
true
true
true
576
5
INTRODUCTION
1
43
[ "B43", "B43", "B44", "B43", "B64" ]
17,355,988
NA|NA|pmid-16505960|NA|pmid-8744573|pmid-11078743|NA
(B) Solution structure of the structured core of Domain V (residues Pro507–Ser617 of τ) determined by NMR (43).
[ "43", "43", "44", "43", "64" ]
111
3,373
1
false
(B) Solution structure of the structured core of Domain V (residues Pro507–Ser617 of τ) determined by NMR.
[ "43" ]
(B) Solution structure of the structured core of Domain V (residues Pro507–Ser617 of τ) determined by NMR.
false
false
true
true
false
576
5
INTRODUCTION
1
43
[ "B43", "B43", "B44", "B43", "B64" ]
17,355,988
NA|NA|pmid-16505960|NA|pmid-8744573|pmid-11078743|NA
The sequence of the unstructured region at the C-terminus (43,44) is given in single-letter code, with highly conserved residues (43) marked with larger font.
[ "43", "43", "44", "43", "64" ]
158
3,374
1
false
The sequence of the unstructured region at the C-terminus is given in single-letter code, with highly conserved residues marked with larger font.
[ "43,44", "43" ]
The sequence of the unstructured region at the C-terminus is given in single-letter code, with highly conserved residues marked with larger font.
true
true
true
true
true
576
5
INTRODUCTION
1
43
[ "B43", "B43", "B44", "B43", "B64" ]
17,355,988
NA|NA|pmid-16505960|NA|pmid-8744573|pmid-11078743|NA
Secondary structural elements that may be induced in this region on interaction with α are indicated below.
[ "43", "43", "44", "43", "64" ]
107
3,375
0
false
Secondary structural elements that may be induced in this region on interaction with α are indicated below.
[]
Secondary structural elements that may be induced in this region on interaction with α are indicated below.
true
true
true
true
true
576
5
INTRODUCTION
1
64
[ "B43", "B43", "B44", "B43", "B64" ]
17,355,988
NA|NA|pmid-16505960|NA|pmid-8744573|pmid-11078743|NA
Part of the figure was drawn using MOLMOL (64).
[ "43", "43", "44", "43", "64" ]
47
3,376
1
false
Part of the figure was drawn using MOLMOL.
[ "64" ]
Part of the figure was drawn using MOLMOL.
true
true
true
true
true
576
6
INTRODUCTION
1
43
[ "B43", "B43", "B44" ]
17,355,988
NA|NA|pmid-16505960|pmid-16036556|pmid-15952889|pmid-16421093|pmid-16857582
The solution structure of the folded core of Domain V of E. coli τ, a 14.3-kDa protein (called τC14) derived from τC16 by deletion of 18 C-terminal residues, has been determined by NMR spectroscopy (Figure 1B), and is reported in the accompanying article (43).
[ "43", "43", "44" ]
260
3,377
1
false
The solution structure of the folded core of Domain V of E. coli τ, a 14.3-kDa protein (called τC14) derived from τC16 by deletion of 18 C-terminal residues, has been determined by NMR spectroscopy (Figure 1B), and is reported in the accompanying article.
[ "43" ]
The solution structure of the folded core of Domain V of E. coli τ, a 14.3-kDa protein derived from τC16 by deletion of 18 C-terminal residues, has been determined by NMR spectroscopy (Figure 1B), and is reported in the accompanying article.
true
true
true
true
true
577
6
INTRODUCTION
1
43
[ "B43", "B43", "B44" ]
17,355,988
NA|NA|pmid-16505960|pmid-16036556|pmid-15952889|pmid-16421093|pmid-16857582
Given that recent NMR studies (43,44) have also shown that all N- and/or C-terminal residues additional to the τC14 core in the longer protein constructs τC24, τC22 (τC24 lacking the C-terminal 18 residues), and τC16 (see Figure 1A) are intrinsically unstructured, we can now develop a near-complete picture of the struc...
[ "43", "43", "44" ]
638
3,378
0
false
Given that recent NMR studies have also shown that all N- and/or C-terminal residues additional to the τC14 core in the longer protein constructs τC24, τC22 (τC24 lacking the C-terminal 18 residues), and τC16 (see Figure 1A) are intrinsically unstructured, we can now develop a near-complete picture of the structure of ...
[ "43,44" ]
Given that recent NMR studies have also shown that all N- and/or C-terminal residues additional to the τC14 core in the longer protein constructs τC24, τC22, and τC16 (see Figure 1A) are intrinsically unstructured, we can now develop a near-complete picture of the structure of the τ subunit in which the structured part...
true
true
true
true
true
577
7
INTRODUCTION
1
44
[ "B44" ]
17,355,988
pmid-16505960|pmid-16421093|pmid-16857582|pmid-12620221|pmid-14630952|pmid-11078743|NA
In this article, we describe the genesis of the τC14 fragment and show that the additional residues in τC16 relative to τC14 are required for formation of an isolable complex with α.
[ "44" ]
182
3,379
0
false
In this article, we describe the genesis of the τC14 fragment and show that the additional residues in τC16 relative to τC14 are required for formation of an isolable complex with α.
[]
In this article, we describe the genesis of the τC14 fragment and show that the additional residues in τC16 relative to τC14 are required for formation of an isolable complex with α.
true
true
true
true
true
578
7
INTRODUCTION
1
44
[ "B44" ]
17,355,988
pmid-16505960|pmid-16421093|pmid-16857582|pmid-12620221|pmid-14630952|pmid-11078743|NA
Alignment and secondary structure prediction combined with point mutagenesis and deletion studies suggest the induction of α-helices within the otherwise flexible (44) C-terminal region of τC16 upon its interaction with α.
[ "44" ]
222
3,380
1
false
Alignment and secondary structure prediction combined with point mutagenesis and deletion studies suggest the induction of α-helices within the otherwise flexible C-terminal region of τC16 upon its interaction with α.
[ "44" ]
Alignment and secondary structure prediction combined with point mutagenesis and deletion studies suggest the induction of α-helices within the otherwise flexible C-terminal region of τC16 upon its interaction with α.
true
true
true
true
true
578
7
INTRODUCTION
1
44
[ "B44" ]
17,355,988
pmid-16505960|pmid-16421093|pmid-16857582|pmid-12620221|pmid-14630952|pmid-11078743|NA
We also show that although both τC22 and τC24 proteins bind weakly through predominantly electrostatic interactions to single-stranded (ss), double-stranded (ds) and primed DNA, τC16 does not.
[ "44" ]
192
3,381
0
false
We also show that although both τC22 and τC24 proteins bind weakly through predominantly electrostatic interactions to single-stranded (ss), double-stranded (ds) and primed DNA, τC16 does not.
[]
We also show that although both τC22 and τC24 proteins bind weakly through predominantly electrostatic interactions to single-stranded (ss), double-stranded (ds) and primed DNA, τC16 does not.
true
true
true
true
true
578
7
INTRODUCTION
1
44
[ "B44" ]
17,355,988
pmid-16505960|pmid-16421093|pmid-16857582|pmid-12620221|pmid-14630952|pmid-11078743|NA
This localizes the putative DNA-interaction site in τC24 to Domain IVa.
[ "44" ]
71
3,382
0
false
This localizes the putative DNA-interaction site in τC24 to Domain IVa.
[]
This localizes the putative DNA-interaction site in τC24 to Domain IVa.
true
true
true
true
true
578
7
INTRODUCTION
1
44
[ "B44" ]
17,355,988
pmid-16505960|pmid-16421093|pmid-16857582|pmid-12620221|pmid-14630952|pmid-11078743|NA
Implications for the role of this region of τ in switching processivity in Pol III HE are discussed.
[ "44" ]
100
3,383
0
false
Implications for the role of this region of τ in switching processivity in Pol III HE are discussed.
[]
Implications for the role of this region of τ in switching processivity in Pol III HE are discussed.
true
true
true
true
true
578
0
DISCUSSION
1
43
[ "B43", "B43", "B44" ]
17,355,988
pmid-2850007|pmid-3052282|NA|pmid-16036556|pmid-15952889|pmid-16421093|pmid-16857582|pmid-7574479|pmid-368075|pmid-2997151|pmid-6393125|pmid-15090519|pmid-2997151|pmid-7005228|pmid-7478986|pmid-1349852|pmid-2040637|NA|NA|pmid-16505960
This report shows the important role the extreme C-terminal region of the τ subunit of Pol III HE plays in its interaction with the α polymerase subunit.
[ "43", "43", "44" ]
153
3,384
0
false
This report shows the important role the extreme C-terminal region of the τ subunit of Pol III HE plays in its interaction with the α polymerase subunit.
[]
This report shows the important role the extreme C-terminal region of the τ subunit of Pol III HE plays in its interaction with the α polymerase subunit.
true
true
true
true
true
579
0
DISCUSSION
1
43
[ "B43", "B43", "B44" ]
17,355,988
pmid-2850007|pmid-3052282|NA|pmid-16036556|pmid-15952889|pmid-16421093|pmid-16857582|pmid-7574479|pmid-368075|pmid-2997151|pmid-6393125|pmid-15090519|pmid-2997151|pmid-7005228|pmid-7478986|pmid-1349852|pmid-2040637|NA|NA|pmid-16505960
In the accompanying article (43), we describe the solution structure of the folded core of the C-terminal Domain V of τ (i.e.
[ "43", "43", "44" ]
125
3,385
1
false
In the accompanying article, we describe the solution structure of the folded core of the C-terminal Domain V of τ (i.e.
[ "43" ]
In the accompanying article, we describe the solution structure of the folded core of the C-terminal Domain V of τ (i.e.
true
true
true
true
true
579
0
DISCUSSION
1
43
[ "B43", "B43", "B44" ]
17,355,988
pmid-2850007|pmid-3052282|NA|pmid-16036556|pmid-15952889|pmid-16421093|pmid-16857582|pmid-7574479|pmid-368075|pmid-2997151|pmid-6393125|pmid-15090519|pmid-2997151|pmid-7005228|pmid-7478986|pmid-1349852|pmid-2040637|NA|NA|pmid-16505960
τC14) determined by NMR spectroscopy.
[ "43", "43", "44" ]
37
3,386
0
false
τC14) determined by NMR spectroscopy.
[]
τC14) determined by NMR spectroscopy.
false
true
true
true
false
579
0
DISCUSSION
1
43
[ "B43", "B43", "B44" ]
17,355,988
pmid-2850007|pmid-3052282|NA|pmid-16036556|pmid-15952889|pmid-16421093|pmid-16857582|pmid-7574479|pmid-368075|pmid-2997151|pmid-6393125|pmid-15090519|pmid-2997151|pmid-7005228|pmid-7478986|pmid-1349852|pmid-2040637|NA|NA|pmid-16505960
The region between residues Pro507 and Ser617 of Domain V is structured; the last eight residues of τC14 were found to be mobile (43) and the following 18 residues present in τC16 beyond the end of τC14 (Figure 1A) are also unstructured and show no evidence of association with the folded core of Domain V (44).
[ "43", "43", "44" ]
311
3,387
1
false
The region between residues Pro507 and Ser617 of Domain V is structured; the last eight residues of τC14 were found to be mobile and the following 18 residues present in τC16 beyond the end of τC14 (Figure 1A) are also unstructured and show no evidence of association with the folded core of Domain V.
[ "43", "44" ]
The region between residues Pro507 and Ser617 of Domain V is structured; the last eight residues of τC14 were found to be mobile and the following 18 residues present in τC16 beyond the end of τC14 (Figure 1A) are also unstructured and show no evidence of association with the folded core of Domain V.
true
true
true
true
true
579
0
DISCUSSION
1
43
[ "B43", "B43", "B44" ]
17,355,988
pmid-2850007|pmid-3052282|NA|pmid-16036556|pmid-15952889|pmid-16421093|pmid-16857582|pmid-7574479|pmid-368075|pmid-2997151|pmid-6393125|pmid-15090519|pmid-2997151|pmid-7005228|pmid-7478986|pmid-1349852|pmid-2040637|NA|NA|pmid-16505960
Nevertheless, that a peptide comprising just the last 32 residues of τ (τCpep32) and including all of this unstructured region does not associate as strongly with α as τC16 (Table 1) suggests that some residues in the folded region of Domain V directly or indirectly contribute to the interaction with α.
[ "43", "43", "44" ]
304
3,388
0
false
Nevertheless, that a peptide comprising just the last 32 residues of τ (τCpep32) and including all of this unstructured region does not associate as strongly with α as τC16 (Table 1) suggests that some residues in the folded region of Domain V directly or indirectly contribute to the interaction with α.
[]
Nevertheless, that a peptide comprising just the last 32 residues of τ and including all of this unstructured region does not associate as strongly with α as τC16 (Table 1) suggests that some residues in the folded region of Domain V directly or indirectly contribute to the interaction with α.
true
true
true
true
true
579
1
DISCUSSION
1
59
[ "B59", "B60" ]
17,355,988
pmid-11101526|pmid-11719243|pmid-12519754|pmid-14610067|pmid-14610068|pmid-9722585|pmid-9989506|pmid-7768937|pmid-11525728|pmid-10550212|pmid-15943980
Sequence alignment reveals that certain residues in the C-terminal region of τC16 are highly conserved (Figure 1B, and ref.
[ "59", "60" ]
123
3,389
0
false
Sequence alignment reveals that certain residues in the C-terminal region of τC16 are highly conserved (Figure 1B, and ref.
[]
Sequence alignment reveals that certain residues in the C-terminal region of τC16 are highly conserved (Figure 1B, and ref.
true
true
true
true
true
580
1
DISCUSSION
1
59
[ "B59", "B60" ]
17,355,988
pmid-11101526|pmid-11719243|pmid-12519754|pmid-14610067|pmid-14610068|pmid-9722585|pmid-9989506|pmid-7768937|pmid-11525728|pmid-10550212|pmid-15943980
43), and our mutagenesis data suggest that these conserved residues are important for interaction with α.
[ "59", "60" ]
105
3,390
0
false
43), and our mutagenesis data suggest that these conserved residues are important for interaction with α.
[]
43), and our mutagenesis data suggest that these conserved residues are important for interaction with α.
false
false
true
true
false
580
1
DISCUSSION
1
59
[ "B59", "B60" ]
17,355,988
pmid-11101526|pmid-11719243|pmid-12519754|pmid-14610067|pmid-14610068|pmid-9722585|pmid-9989506|pmid-7768937|pmid-11525728|pmid-10550212|pmid-15943980
This interaction thus provides yet another example of how an intrinsically unstructured region of a protein can fold into a defined structure when it interacts with its binding partner (59,60).
[ "59", "60" ]
193
3,391
0
false
This interaction thus provides yet another example of how an intrinsically unstructured region of a protein can fold into a defined structure when it interacts with its binding partner.
[ "59,60" ]
This interaction thus provides yet another example of how an intrinsically unstructured region of a protein can fold into a defined structure when it interacts with its binding partner.
true
true
true
true
true
580
1
DISCUSSION
1
59
[ "B59", "B60" ]
17,355,988
pmid-11101526|pmid-11719243|pmid-12519754|pmid-14610067|pmid-14610068|pmid-9722585|pmid-9989506|pmid-7768937|pmid-11525728|pmid-10550212|pmid-15943980
Although this region contains many polar and charged amino acids, most of the conserved residues are non-polar and are spaced in such a way that suggests the folded structure of this part of τ in the α–τ complex comprises two amphipathic α-helices.
[ "59", "60" ]
248
3,392
0
false
Although this region contains many polar and charged amino acids, most of the conserved residues are non-polar and are spaced in such a way that suggests the folded structure of this part of τ in the α–τ complex comprises two amphipathic α-helices.
[]
Although this region contains many polar and charged amino acids, most of the conserved residues are non-polar and are spaced in such a way that suggests the folded structure of this part of τ in the α–τ complex comprises two amphipathic α-helices.
true
true
true
true
true
580
2
DISCUSSION
1
43
[ "B43" ]
17,355,988
pmid-6316113|pmid-6358801|pmid-7037770|pmid-2181440|pmid-2187190|pmid-2186364|pmid-11525729|pmid-11078742|NA
Secondary structure predictions suggest an extension of the C-terminal helix 6 of τC14 (43) which includes the conserved residues Ala614 and Ile618 (Figure 1B).
[ "43" ]
160
3,393
1
false
Secondary structure predictions suggest an extension of the C-terminal helix 6 of τC14 which includes the conserved residues Ala614 and Ile618 (Figure 1B).
[ "43" ]
Secondary structure predictions suggest an extension of the C-terminal helix 6 of τC14 which includes the conserved residues Ala614 and Ile618 (Figure 1B).
true
true
true
true
true
581
2
DISCUSSION
1
43
[ "B43" ]
17,355,988
pmid-6316113|pmid-6358801|pmid-7037770|pmid-2181440|pmid-2187190|pmid-2186364|pmid-11525729|pmid-11078742|NA
We studied two single point mutants from this region, S617P and I618T.
[ "43" ]
70
3,394
0
false
We studied two single point mutants from this region, S617P and I618T.
[]
We studied two single point mutants from this region, S617P and I618T.
true
true
true
true
true
581
2
DISCUSSION
1
43
[ "B43" ]
17,355,988
pmid-6316113|pmid-6358801|pmid-7037770|pmid-2181440|pmid-2187190|pmid-2186364|pmid-11525729|pmid-11078742|NA
While the I618T mutation had only a modest effect on α binding (ΔΔG° = 1.1 kcal/mol), the effect of the S617P mutation was larger (4.1 kcal/mol).
[ "43" ]
145
3,395
0
false
While the I618T mutation had only a modest effect on α binding (ΔΔG° = 1.1 kcal/mol), the effect of the S617P mutation was larger (4.1 kcal/mol).
[]
While the I618T mutation had only a modest effect on α binding (ΔΔG° = 1.1 kcal/mol), the effect of the S617P mutation was larger.
true
true
true
true
true
581
2
DISCUSSION
1
43
[ "B43" ]
17,355,988
pmid-6316113|pmid-6358801|pmid-7037770|pmid-2181440|pmid-2187190|pmid-2186364|pmid-11525729|pmid-11078742|NA
Since the proline substitution at Ser617 would be expected to disrupt an α-helix, this is consistent with the interactions with α occurring via an incipient helix.
[ "43" ]
163
3,396
0
false
Since the proline substitution at Ser617 would be expected to disrupt an α-helix, this is consistent with the interactions with α occurring via an incipient helix.
[]
Since the proline substitution at Ser617 would be expected to disrupt an α-helix, this is consistent with the interactions with α occurring via an incipient helix.
true
true
true
true
true
581
3
DISCUSSION
1
38
[ "B38", "B62", "B63" ]
17,355,988
pmid-1918087|pmid-7768938|pmid-1918087|pmid-8702819|pmid-7768940|pmid-12620221|pmid-14630952|pmid-14630952|pmid-12620221|pmid-16959568|pmid-16959569
Structure prediction further suggests a β-turn involving Asp621–Asn623 followed by a helix from Ile624 to Phe631 with high propensity, or to Leu635 with lower propensity.
[ "38", "62", "63" ]
170
3,397
0
false
Structure prediction further suggests a β-turn involving Asp621–Asn623 followed by a helix from Ile624 to Phe631 with high propensity, or to Leu635 with lower propensity.
[]
Structure prediction further suggests a β-turn involving Asp621–Asn623 followed by a helix from Ile624 to Phe631 with high propensity, or to Leu635 with lower propensity.
true
true
true
true
true
582
3
DISCUSSION
1
38
[ "B38", "B62", "B63" ]
17,355,988
pmid-1918087|pmid-7768938|pmid-1918087|pmid-8702819|pmid-7768940|pmid-12620221|pmid-14630952|pmid-14630952|pmid-12620221|pmid-16959568|pmid-16959569
This suggests that a second longer helix extending to Leu635 might be formed upon interaction with α.
[ "38", "62", "63" ]
101
3,398
0
false
This suggests that a second longer helix extending to Leu635 might be formed upon interaction with α.
[]
This suggests that a second longer helix extending to Leu635 might be formed upon interaction with α.
true
true
true
true
true
582
3
DISCUSSION
1
38
[ "B38", "B62", "B63" ]
17,355,988
pmid-1918087|pmid-7768938|pmid-1918087|pmid-8702819|pmid-7768940|pmid-12620221|pmid-14630952|pmid-14630952|pmid-12620221|pmid-16959568|pmid-16959569
Consistent with this is the fact that the conserved residue mutant L635P located at the end of this hypothetical helix (Figure 1B) still interacts relatively strongly with α (ΔΔG° = 1.7 kcal/mol) while the L627P mutation within it has the largest effect of those examined (5.4 kcal/mol).
[ "38", "62", "63" ]
287
3,399
0
false
Consistent with this is the fact that the conserved residue mutant L635P located at the end of this hypothetical helix (Figure 1B) still interacts relatively strongly with α (ΔΔG° = 1.7 kcal/mol) while the L627P mutation within it has the largest effect of those examined (5.4 kcal/mol).
[]
Consistent with this is the fact that the conserved residue mutant L635P located at the end of this hypothetical helix (Figure 1B) still interacts relatively strongly with α (ΔΔG° = 1.7 kcal/mol) while the L627P mutation within it has the largest effect of those examined (5.4 kcal/mol).
true
true
true
true
true
582