paragraph_index int64 | sec string | p_has_citation int64 | cites string | citeids list | pmid int64 | cited_id string | sentences string | all_sent_cites list | sent_len int64 | sentence_batch_index int64 | sent_has_citation float64 | qc_fail bool | cited_sentence string | cites_in_sentence list | cln_sentence string | is_cap bool | is_alpha bool | ends_wp bool | cit_qc bool | lgtm bool | __index_level_0__ int64 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
0 | DISCUSSION | 1 | 12 | [
"B12"
] | 17,329,375 | NA|pmid-11839499|pmid-16469698 | In wild-type Mfd, the translocation activity is repressed by the action of D7 (red). | [
"12"
] | 84 | 8,700 | 0 | false | In wild-type Mfd, the translocation activity is repressed by the action of D7 (red). | [] | In wild-type Mfd, the translocation activity is repressed by the action of D7 (red). | true | true | true | true | true | 1,395 |
0 | DISCUSSION | 1 | 12 | [
"B12"
] | 17,329,375 | NA|pmid-11839499|pmid-16469698 | The autoinhibitory effect can be relieved by deletion of D7, and the truncated protein can displace a TFO in the absence of other factors. | [
"12"
] | 138 | 8,701 | 0 | false | The autoinhibitory effect can be relieved by deletion of D7, and the truncated protein can displace a TFO in the absence of other factors. | [] | The autoinhibitory effect can be relieved by deletion of D7, and the truncated protein can displace a TFO in the absence of other factors. | true | true | true | true | true | 1,395 |
0 | DISCUSSION | 1 | 12 | [
"B12"
] | 17,329,375 | NA|pmid-11839499|pmid-16469698 | The autoinhibitory effect is also relieved by the interaction of wild-type Mfd with RNAP. | [
"12"
] | 89 | 8,702 | 0 | false | The autoinhibitory effect is also relieved by the interaction of wild-type Mfd with RNAP. | [] | The autoinhibitory effect is also relieved by the interaction of wild-type Mfd with RNAP. | true | true | true | true | true | 1,395 |
0 | DISCUSSION | 1 | 12 | [
"B12"
] | 17,329,375 | NA|pmid-11839499|pmid-16469698 | Mfd binds to RNAP via the RID (magenta), and D7 is repositioned. | [
"12"
] | 64 | 8,703 | 0 | false | Mfd binds to RNAP via the RID (magenta), and D7 is repositioned. | [] | Mfd binds to RNAP via the RID (magenta), and D7 is repositioned. | true | true | true | true | true | 1,395 |
0 | DISCUSSION | 1 | 12 | [
"B12"
] | 17,329,375 | NA|pmid-11839499|pmid-16469698 | The repositioning of D7 activates the DNA translocation activity of Mfd, and may also reveal a binding site for UvrA (white ellipse: (12)). | [
"12"
] | 139 | 8,704 | 0 | false | The repositioning of D7 activates the DNA translocation activity of Mfd, and may also reveal a binding site for UvrA ). | [
"white ellipse: (12"
] | The repositioning of D7 activates the DNA translocation activity of Mfd, and may also reveal a binding site for UvrA ). | true | true | true | true | true | 1,395 |
0 | DISCUSSION | 1 | 12 | [
"B12"
] | 17,329,375 | NA|pmid-11839499|pmid-16469698 | TFO displacement may result either from RNAP being pushed through the TFO-binding site (as shown), or by Mfd continuing to translocate DNA after displacing RNAP. | [
"12"
] | 161 | 8,705 | 0 | false | TFO displacement may result either from RNAP being pushed through the TFO-binding site (as shown), or by Mfd continuing to translocate DNA after displacing RNAP. | [] | TFO displacement may result either from RNAP being pushed through the TFO-binding site (as shown), or by Mfd continuing to translocate DNA after displacing RNAP. | true | true | true | true | true | 1,395 |
1 | DISCUSSION | 1 | 12 | [
"B12"
] | 17,329,375 | pmid-8465200|pmid-10214918|pmid-15474416|pmid-16464015|pmid-8465200|pmid-2250027|pmid-2554145|pmid-3664636|pmid-9535092|pmid-12787667|pmid-16469698 | Model for the control of Mfd activity by autoinhibitory domain D7. | [
"12"
] | 66 | 8,706 | 0 | false | Model for the control of Mfd activity by autoinhibitory domain D7. | [] | Model for the control of Mfd activity by autoinhibitory domain D7. | true | true | true | true | true | 1,396 |
1 | DISCUSSION | 1 | 12 | [
"B12"
] | 17,329,375 | pmid-8465200|pmid-10214918|pmid-15474416|pmid-16464015|pmid-8465200|pmid-2250027|pmid-2554145|pmid-3664636|pmid-9535092|pmid-12787667|pmid-16469698 | In wild-type Mfd, the translocation activity is repressed by the action of D7 (red). | [
"12"
] | 84 | 8,707 | 0 | false | In wild-type Mfd, the translocation activity is repressed by the action of D7 (red). | [] | In wild-type Mfd, the translocation activity is repressed by the action of D7 (red). | true | true | true | true | true | 1,396 |
1 | DISCUSSION | 1 | 12 | [
"B12"
] | 17,329,375 | pmid-8465200|pmid-10214918|pmid-15474416|pmid-16464015|pmid-8465200|pmid-2250027|pmid-2554145|pmid-3664636|pmid-9535092|pmid-12787667|pmid-16469698 | The autoinhibitory effect can be relieved by deletion of D7, and the truncated protein can displace a TFO in the absence of other factors. | [
"12"
] | 138 | 8,708 | 0 | false | The autoinhibitory effect can be relieved by deletion of D7, and the truncated protein can displace a TFO in the absence of other factors. | [] | The autoinhibitory effect can be relieved by deletion of D7, and the truncated protein can displace a TFO in the absence of other factors. | true | true | true | true | true | 1,396 |
1 | DISCUSSION | 1 | 12 | [
"B12"
] | 17,329,375 | pmid-8465200|pmid-10214918|pmid-15474416|pmid-16464015|pmid-8465200|pmid-2250027|pmid-2554145|pmid-3664636|pmid-9535092|pmid-12787667|pmid-16469698 | The autoinhibitory effect is also relieved by the interaction of wild-type Mfd with RNAP. | [
"12"
] | 89 | 8,709 | 0 | false | The autoinhibitory effect is also relieved by the interaction of wild-type Mfd with RNAP. | [] | The autoinhibitory effect is also relieved by the interaction of wild-type Mfd with RNAP. | true | true | true | true | true | 1,396 |
1 | DISCUSSION | 1 | 12 | [
"B12"
] | 17,329,375 | pmid-8465200|pmid-10214918|pmid-15474416|pmid-16464015|pmid-8465200|pmid-2250027|pmid-2554145|pmid-3664636|pmid-9535092|pmid-12787667|pmid-16469698 | Mfd binds to RNAP via the RID (magenta), and D7 is repositioned. | [
"12"
] | 64 | 8,710 | 0 | false | Mfd binds to RNAP via the RID (magenta), and D7 is repositioned. | [] | Mfd binds to RNAP via the RID (magenta), and D7 is repositioned. | true | true | true | true | true | 1,396 |
1 | DISCUSSION | 1 | 12 | [
"B12"
] | 17,329,375 | pmid-8465200|pmid-10214918|pmid-15474416|pmid-16464015|pmid-8465200|pmid-2250027|pmid-2554145|pmid-3664636|pmid-9535092|pmid-12787667|pmid-16469698 | The repositioning of D7 activates the DNA translocation activity of Mfd, and may also reveal a binding site for UvrA (white ellipse: (12)). | [
"12"
] | 139 | 8,711 | 0 | false | The repositioning of D7 activates the DNA translocation activity of Mfd, and may also reveal a binding site for UvrA ). | [
"white ellipse: (12"
] | The repositioning of D7 activates the DNA translocation activity of Mfd, and may also reveal a binding site for UvrA ). | true | true | true | true | true | 1,396 |
1 | DISCUSSION | 1 | 12 | [
"B12"
] | 17,329,375 | pmid-8465200|pmid-10214918|pmid-15474416|pmid-16464015|pmid-8465200|pmid-2250027|pmid-2554145|pmid-3664636|pmid-9535092|pmid-12787667|pmid-16469698 | TFO displacement may result either from RNAP being pushed through the TFO-binding site (as shown), or by Mfd continuing to translocate DNA after displacing RNAP. | [
"12"
] | 161 | 8,712 | 0 | false | TFO displacement may result either from RNAP being pushed through the TFO-binding site (as shown), or by Mfd continuing to translocate DNA after displacing RNAP. | [] | TFO displacement may result either from RNAP being pushed through the TFO-binding site (as shown), or by Mfd continuing to translocate DNA after displacing RNAP. | true | true | true | true | true | 1,396 |
2 | DISCUSSION | 0 | null | null | 17,329,375 | pmid-8465200|pmid-16469698|pmid-16469698|pmid-16309703|pmid-7876261|pmid-16469698|pmid-12086674|pmid-12554672|pmid-14602898|pmid-16469698|pmid-16469698 | How might D7 inhibit DNA translocation activity? | null | 48 | 8,713 | 0 | false | null | null | How might D7 inhibit DNA translocation activity? | true | true | true | true | true | 1,397 |
2 | DISCUSSION | 0 | null | null | 17,329,375 | pmid-8465200|pmid-16469698|pmid-16469698|pmid-16309703|pmid-7876261|pmid-16469698|pmid-12086674|pmid-12554672|pmid-14602898|pmid-16469698|pmid-16469698 | Deletion of D7 increased the ATPase activity of the protein even in the absence of DNA. | null | 87 | 8,714 | 0 | false | null | null | Deletion of D7 increased the ATPase activity of the protein even in the absence of DNA. | true | true | true | true | true | 1,397 |
2 | DISCUSSION | 0 | null | null | 17,329,375 | pmid-8465200|pmid-16469698|pmid-16469698|pmid-16309703|pmid-7876261|pmid-16469698|pmid-12086674|pmid-12554672|pmid-14602898|pmid-16469698|pmid-16469698 | This indicates that the inhibitory effect of the domain occurs at least in part by preventing nucleotide binding, hydrolysis and/or release in a manner that is independent of the interaction of Mfd with its DNA substrate. | null | 221 | 8,715 | 0 | false | null | null | This indicates that the inhibitory effect of the domain occurs at least in part by preventing nucleotide binding, hydrolysis and/or release in a manner that is independent of the interaction of Mfd with its DNA substrate. | true | true | true | true | true | 1,397 |
2 | DISCUSSION | 0 | null | null | 17,329,375 | pmid-8465200|pmid-16469698|pmid-16469698|pmid-16309703|pmid-7876261|pmid-16469698|pmid-12086674|pmid-12554672|pmid-14602898|pmid-16469698|pmid-16469698 | In the crystal structure of Mfd, D7 is not close to the predicted path of DNA across the protein and does not interact directly with domains D5 and D6, which contain the motifs important for ATP hydrolysis and DNA translocation (although it is important to note that the crystal structure was obtained in the absence of ... | null | 414 | 8,716 | 0 | false | null | null | In the crystal structure of Mfd, D7 is not close to the predicted path of DNA across the protein and does not interact directly with domains D5 and D6, which contain the motifs important for ATP hydrolysis and DNA translocation (although it is important to note that the crystal structure was obtained in the absence of ... | true | true | true | true | true | 1,397 |
2 | DISCUSSION | 0 | null | null | 17,329,375 | pmid-8465200|pmid-16469698|pmid-16469698|pmid-16309703|pmid-7876261|pmid-16469698|pmid-12086674|pmid-12554672|pmid-14602898|pmid-16469698|pmid-16469698 | However, D7 is structurally linked to the translocase domains via the hook helices, which lead on from the TRG motif and interact with the relay helix linking the translocase domains to the RID (Figure 1). | null | 205 | 8,717 | 0 | false | null | null | However, D7 is structurally linked to the translocase domains via the hook helices, which lead on from the TRG motif and interact with the relay helix linking the translocase domains to the RID (Figure 1). | true | true | true | true | true | 1,397 |
2 | DISCUSSION | 0 | null | null | 17,329,375 | pmid-8465200|pmid-16469698|pmid-16469698|pmid-16309703|pmid-7876261|pmid-16469698|pmid-12086674|pmid-12554672|pmid-14602898|pmid-16469698|pmid-16469698 | It is therefore feasible that deletion or movement of D7 could affect ATPase and translocation activity via transmission of conformational changes through the structure. | null | 169 | 8,718 | 0 | false | null | null | It is therefore feasible that deletion or movement of D7 could affect ATPase and translocation activity via transmission of conformational changes through the structure. | true | true | true | true | true | 1,397 |
2 | DISCUSSION | 0 | null | null | 17,329,375 | pmid-8465200|pmid-16469698|pmid-16469698|pmid-16309703|pmid-7876261|pmid-16469698|pmid-12086674|pmid-12554672|pmid-14602898|pmid-16469698|pmid-16469698 | In any such allosteric effects of D7 the TRG motif is likely to play an important role. | null | 87 | 8,719 | 0 | false | null | null | In any such allosteric effects of D7 the TRG motif is likely to play an important role. | true | true | true | true | true | 1,397 |
3 | DISCUSSION | 1 | 12 | [
"B12",
"B16",
"B12",
"B16",
"B12"
] | 17,329,375 | pmid-16469698|pmid-16469698|pmid-12554672|pmid-16469698|pmid-12554672|pmid-16469698 | The TRG motif contains a pair of helices that interact with helicase motif VI, providing a link to the ATPase catalytic site (12,16). | [
"12",
"16",
"12",
"16",
"12"
] | 133 | 8,720 | 0 | false | The TRG motif contains a pair of helices that interact with helicase motif VI, providing a link to the ATPase catalytic site. | [
"12,16"
] | The TRG motif contains a pair of helices that interact with helicase motif VI, providing a link to the ATPase catalytic site. | true | true | true | true | true | 1,398 |
3 | DISCUSSION | 1 | 12 | [
"B12",
"B16",
"B12",
"B16",
"B12"
] | 17,329,375 | pmid-16469698|pmid-16469698|pmid-12554672|pmid-16469698|pmid-12554672|pmid-16469698 | In the RecG–ADP–DNA structure, these helices form a hairpin with two closely juxtaposed arginine residues at the base, whereas in the Mfd structure, which contains no nucleotide, these helices have moved apart (12,16). | [
"12",
"16",
"12",
"16",
"12"
] | 218 | 8,721 | 0 | false | In the RecG–ADP–DNA structure, these helices form a hairpin with two closely juxtaposed arginine residues at the base, whereas in the Mfd structure, which contains no nucleotide, these helices have moved apart. | [
"12,16"
] | In the RecG–ADP–DNA structure, these helices form a hairpin with two closely juxtaposed arginine residues at the base, whereas in the Mfd structure, which contains no nucleotide, these helices have moved apart. | true | true | true | true | true | 1,398 |
3 | DISCUSSION | 1 | 12 | [
"B12",
"B16",
"B12",
"B16",
"B12"
] | 17,329,375 | pmid-16469698|pmid-16469698|pmid-12554672|pmid-16469698|pmid-12554672|pmid-16469698 | It seems that this structure forms a ‘spring-loaded’ switch that changes conformation during the nucleotide hydrolysis cycle: nucleotide binding stabilizes the closed conformation, and charge repulsion between the two arginines favours the open conformation. | [
"12",
"16",
"12",
"16",
"12"
] | 258 | 8,722 | 0 | false | It seems that this structure forms a ‘spring-loaded’ switch that changes conformation during the nucleotide hydrolysis cycle: nucleotide binding stabilizes the closed conformation, and charge repulsion between the two arginines favours the open conformation. | [] | It seems that this structure forms a ‘spring-loaded’ switch that changes conformation during the nucleotide hydrolysis cycle: nucleotide binding stabilizes the closed conformation, and charge repulsion between the two arginines favours the open conformation. | true | true | true | true | true | 1,398 |
3 | DISCUSSION | 1 | 12 | [
"B12",
"B16",
"B12",
"B16",
"B12"
] | 17,329,375 | pmid-16469698|pmid-16469698|pmid-12554672|pmid-16469698|pmid-12554672|pmid-16469698 | It has previously been proposed that opening and closing of the TRG helical hairpin may be transmitted to the RID and D7 via the hook helices, and so the state of the TRG motif could control the position of these domains (12). | [
"12",
"16",
"12",
"16",
"12"
] | 226 | 8,723 | 1 | false | It has previously been proposed that opening and closing of the TRG helical hairpin may be transmitted to the RID and D7 via the hook helices, and so the state of the TRG motif could control the position of these domains. | [
"12"
] | It has previously been proposed that opening and closing of the TRG helical hairpin may be transmitted to the RID and D7 via the hook helices, and so the state of the TRG motif could control the position of these domains. | true | true | true | true | true | 1,398 |
3 | DISCUSSION | 1 | 12 | [
"B12",
"B16",
"B12",
"B16",
"B12"
] | 17,329,375 | pmid-16469698|pmid-16469698|pmid-12554672|pmid-16469698|pmid-12554672|pmid-16469698 | Our findings suggest the relationship may be reciprocal, and D7 may regulate ATPase and DNA translocation activities by controlling the position of the hook helices and TRG motif. | [
"12",
"16",
"12",
"16",
"12"
] | 179 | 8,724 | 0 | false | Our findings suggest the relationship may be reciprocal, and D7 may regulate ATPase and DNA translocation activities by controlling the position of the hook helices and TRG motif. | [] | Our findings suggest the relationship may be reciprocal, and D7 may regulate ATPase and DNA translocation activities by controlling the position of the hook helices and TRG motif. | true | true | true | true | true | 1,398 |
3 | DISCUSSION | 1 | 12 | [
"B12",
"B16",
"B12",
"B16",
"B12"
] | 17,329,375 | pmid-16469698|pmid-16469698|pmid-12554672|pmid-16469698|pmid-12554672|pmid-16469698 | In the isolated full-length protein, D7 may occupy a conformation that constrains the opening and closing of the TRG motif and hence inhibits ATPase activity and DNA translocation; if D7 is deleted this constraint is removed. | [
"12",
"16",
"12",
"16",
"12"
] | 225 | 8,725 | 0 | false | In the isolated full-length protein, D7 may occupy a conformation that constrains the opening and closing of the TRG motif and hence inhibits ATPase activity and DNA translocation; if D7 is deleted this constraint is removed. | [] | In the isolated full-length protein, D7 may occupy a conformation that constrains the opening and closing of the TRG motif and hence inhibits ATPase activity and DNA translocation; if D7 is deleted this constraint is removed. | true | true | true | true | true | 1,398 |
3 | DISCUSSION | 1 | 12 | [
"B12",
"B16",
"B12",
"B16",
"B12"
] | 17,329,375 | pmid-16469698|pmid-16469698|pmid-12554672|pmid-16469698|pmid-12554672|pmid-16469698 | However, the TRG motif does not function solely as a relay in the autoinhibitory mechanism as it is clear that the TRG motif is essential for Mfd function even in the absence of D7. | [
"12",
"16",
"12",
"16",
"12"
] | 181 | 8,726 | 0 | false | However, the TRG motif does not function solely as a relay in the autoinhibitory mechanism as it is clear that the TRG motif is essential for Mfd function even in the absence of D7. | [] | However, the TRG motif does not function solely as a relay in the autoinhibitory mechanism as it is clear that the TRG motif is essential for Mfd function even in the absence of D7. | true | true | true | true | true | 1,398 |
3 | DISCUSSION | 1 | 12 | [
"B12",
"B16",
"B12",
"B16",
"B12"
] | 17,329,375 | pmid-16469698|pmid-16469698|pmid-12554672|pmid-16469698|pmid-12554672|pmid-16469698 | The RA953 substitution, which removes one of the two key arginines within the TRG motif, abolishes the DNA translocation activity of MfdΔD7. | [
"12",
"16",
"12",
"16",
"12"
] | 140 | 8,727 | 0 | false | The RA953 substitution, which removes one of the two key arginines within the TRG motif, abolishes the DNA translocation activity of MfdΔD7. | [] | The RA953 substitution, which removes one of the two key arginines within the TRG motif, abolishes the DNA translocation activity of MfdΔD7. | true | true | true | true | true | 1,398 |
3 | DISCUSSION | 1 | 12 | [
"B12",
"B16",
"B12",
"B16",
"B12"
] | 17,329,375 | pmid-16469698|pmid-16469698|pmid-12554672|pmid-16469698|pmid-12554672|pmid-16469698 | Furthermore, although disruption of the TRG motif has no effect on the ATPase activity of MfdΔD7 in the absence of DNA it reduces the ability of DNA to stimulate the ATPase activity. | [
"12",
"16",
"12",
"16",
"12"
] | 182 | 8,728 | 0 | false | Furthermore, although disruption of the TRG motif has no effect on the ATPase activity of MfdΔD7 in the absence of DNA it reduces the ability of DNA to stimulate the ATPase activity. | [] | Furthermore, although disruption of the TRG motif has no effect on the ATPase activity of MfdΔD7 in the absence of DNA it reduces the ability of DNA to stimulate the ATPase activity. | true | true | true | true | true | 1,398 |
4 | DISCUSSION | 1 | 14 | [
"B14"
] | 17,329,375 | pmid-12086674|pmid-16551743|pmid-16551743|pmid-12086674|pmid-15695524|pmid-11595187|pmid-11595187|pmid-12086674|pmid-15687384|pmid-7876261 | How might interaction with RNAP relieve the inhibitory effect of D7? | [
"14"
] | 68 | 8,729 | 0 | false | How might interaction with RNAP relieve the inhibitory effect of D7? | [] | How might interaction with RNAP relieve the inhibitory effect of D7? | true | true | true | true | true | 1,399 |
4 | DISCUSSION | 1 | 14 | [
"B14"
] | 17,329,375 | pmid-12086674|pmid-16551743|pmid-16551743|pmid-12086674|pmid-15695524|pmid-11595187|pmid-11595187|pmid-12086674|pmid-15687384|pmid-7876261 | The simplest explanation is that interaction between Mfd and RNAP causes D7 to be repositioned. | [
"14"
] | 95 | 8,730 | 0 | false | The simplest explanation is that interaction between Mfd and RNAP causes D7 to be repositioned. | [] | The simplest explanation is that interaction between Mfd and RNAP causes D7 to be repositioned. | true | true | true | true | true | 1,399 |
4 | DISCUSSION | 1 | 14 | [
"B14"
] | 17,329,375 | pmid-12086674|pmid-16551743|pmid-16551743|pmid-12086674|pmid-15695524|pmid-11595187|pmid-11595187|pmid-12086674|pmid-15687384|pmid-7876261 | In the Mfd crystal structure, D7 packs between D2 and D4 (the RID). | [
"14"
] | 67 | 8,731 | 0 | false | In the Mfd crystal structure, D7 packs between D2 and D4 (the RID). | [] | In the Mfd crystal structure, D7 packs between D2 and D4 (the RID). | true | true | true | true | true | 1,399 |
4 | DISCUSSION | 1 | 14 | [
"B14"
] | 17,329,375 | pmid-12086674|pmid-16551743|pmid-16551743|pmid-12086674|pmid-15695524|pmid-11595187|pmid-11595187|pmid-12086674|pmid-15687384|pmid-7876261 | As discussed above the juxtaposition of D4, D7 and the TRG motif is also potentially linked by changes in the interaction between the hook and relay helices. | [
"14"
] | 157 | 8,732 | 0 | false | As discussed above the juxtaposition of D4, D7 and the TRG motif is also potentially linked by changes in the interaction between the hook and relay helices. | [] | As discussed above the juxtaposition of D4, D7 and the TRG motif is also potentially linked by changes in the interaction between the hook and relay helices. | true | true | true | true | true | 1,399 |
4 | DISCUSSION | 1 | 14 | [
"B14"
] | 17,329,375 | pmid-12086674|pmid-16551743|pmid-16551743|pmid-12086674|pmid-15695524|pmid-11595187|pmid-11595187|pmid-12086674|pmid-15687384|pmid-7876261 | Interaction of RNAP with the RID may therefore directly affect the position of D7. | [
"14"
] | 82 | 8,733 | 0 | false | Interaction of RNAP with the RID may therefore directly affect the position of D7. | [] | Interaction of RNAP with the RID may therefore directly affect the position of D7. | true | true | true | true | true | 1,399 |
4 | DISCUSSION | 1 | 14 | [
"B14"
] | 17,329,375 | pmid-12086674|pmid-16551743|pmid-16551743|pmid-12086674|pmid-15695524|pmid-11595187|pmid-11595187|pmid-12086674|pmid-15687384|pmid-7876261 | Alternatively, D7 may make a separate interaction with RNAP that results in its repositioning. | [
"14"
] | 94 | 8,734 | 0 | false | Alternatively, D7 may make a separate interaction with RNAP that results in its repositioning. | [] | Alternatively, D7 may make a separate interaction with RNAP that results in its repositioning. | true | true | true | true | true | 1,399 |
4 | DISCUSSION | 1 | 14 | [
"B14"
] | 17,329,375 | pmid-12086674|pmid-16551743|pmid-16551743|pmid-12086674|pmid-15695524|pmid-11595187|pmid-11595187|pmid-12086674|pmid-15687384|pmid-7876261 | If this is the case this secondary interaction is presumably weaker than the characterized RID–β subunit interaction, as a C-terminal fragment of Mfd containing D7 did not bind to RNAP in pull-down assays that detected the interaction made by fragments that included the RID (14). | [
"14"
] | 280 | 8,735 | 1 | false | If this is the case this secondary interaction is presumably weaker than the characterized RID–β subunit interaction, as a C-terminal fragment of Mfd containing D7 did not bind to RNAP in pull-down assays that detected the interaction made by fragments that included the RID. | [
"14"
] | If this is the case this secondary interaction is presumably weaker than the characterized RID–β subunit interaction, as a C-terminal fragment of Mfd containing D7 did not bind to RNAP in pull-down assays that detected the interaction made by fragments that included the RID. | true | true | true | true | true | 1,399 |
5 | DISCUSSION | 1 | 29 | [
"B29",
"B21",
"B18",
"B30",
"B31",
"B19"
] | 17,329,375 | pmid-8465200|pmid-12581657|pmid-15687384|pmid-16551743|pmid-9182561|pmid-9094712|pmid-15695524 | The RID contact site lies within the mobile β1 domain of the RNAP β subunit, movement of which is one of the conformational changes associated with the opening and closing of the main channel of RNAP (29). | [
"29",
"21",
"18",
"30",
"31",
"19"
] | 205 | 8,736 | 1 | false | The RID contact site lies within the mobile β1 domain of the RNAP β subunit, movement of which is one of the conformational changes associated with the opening and closing of the main channel of RNAP. | [
"29"
] | The RID contact site lies within the mobile β1 domain of the RNAP β subunit, movement of which is one of the conformational changes associated with the opening and closing of the main channel of RNAP. | true | true | true | true | true | 1,400 |
5 | DISCUSSION | 1 | 29 | [
"B29",
"B21",
"B18",
"B30",
"B31",
"B19"
] | 17,329,375 | pmid-8465200|pmid-12581657|pmid-15687384|pmid-16551743|pmid-9182561|pmid-9094712|pmid-15695524 | In this work, we found that the interaction between Mfd and the β subunit of RNAP was essential for RNAP displacement by MfdΔD7, despite the fact that the truncated protein was able to rapidly displace a TFO from DNA. | [
"29",
"21",
"18",
"30",
"31",
"19"
] | 217 | 8,737 | 0 | false | In this work, we found that the interaction between Mfd and the β subunit of RNAP was essential for RNAP displacement by MfdΔD7, despite the fact that the truncated protein was able to rapidly displace a TFO from DNA. | [] | In this work, we found that the interaction between Mfd and the β subunit of RNAP was essential for RNAP displacement by MfdΔD7, despite the fact that the truncated protein was able to rapidly displace a TFO from DNA. | true | true | true | true | true | 1,400 |
5 | DISCUSSION | 1 | 29 | [
"B29",
"B21",
"B18",
"B30",
"B31",
"B19"
] | 17,329,375 | pmid-8465200|pmid-12581657|pmid-15687384|pmid-16551743|pmid-9182561|pmid-9094712|pmid-15695524 | This result shows that DNA translocation activity alone is not sufficient to enable MfdΔD7 to displace a stalled transcription complex from DNA: it must also bind to RNAP. | [
"29",
"21",
"18",
"30",
"31",
"19"
] | 171 | 8,738 | 0 | false | This result shows that DNA translocation activity alone is not sufficient to enable MfdΔD7 to displace a stalled transcription complex from DNA: it must also bind to RNAP. | [] | This result shows that DNA translocation activity alone is not sufficient to enable MfdΔD7 to displace a stalled transcription complex from DNA: it must also bind to RNAP. | true | true | true | true | true | 1,400 |
5 | DISCUSSION | 1 | 29 | [
"B29",
"B21",
"B18",
"B30",
"B31",
"B19"
] | 17,329,375 | pmid-8465200|pmid-12581657|pmid-15687384|pmid-16551743|pmid-9182561|pmid-9094712|pmid-15695524 | Why must the MfdΔD7 motor be tethered to RNAP in order to displace it? | [
"29",
"21",
"18",
"30",
"31",
"19"
] | 70 | 8,739 | 0 | false | Why must the MfdΔD7 motor be tethered to RNAP in order to displace it? | [] | Why must the MfdΔD7 motor be tethered to RNAP in order to displace it? | true | true | true | true | true | 1,400 |
5 | DISCUSSION | 1 | 21 | [
"B29",
"B21",
"B18",
"B30",
"B31",
"B19"
] | 17,329,375 | pmid-8465200|pmid-12581657|pmid-15687384|pmid-16551743|pmid-9182561|pmid-9094712|pmid-15695524 | We have suggested previously that translocation by Mfd tethered to β1 might drive a remodelling process that opens the RNAP main channel (21), in addition to rewinding the transcription bubble (18), and this would be consistent with the findings reported here. | [
"29",
"21",
"18",
"30",
"31",
"19"
] | 260 | 8,740 | 1 | false | We have suggested previously that translocation by Mfd tethered to β1 might drive a remodelling process that opens the RNAP main channel, in addition to rewinding the transcription bubble, and this would be consistent with the findings reported here. | [
"21",
"18"
] | We have suggested previously that translocation by Mfd tethered to β1 might drive a remodelling process that opens the RNAP main channel, in addition to rewinding the transcription bubble, and this would be consistent with the findings reported here. | true | true | true | true | true | 1,400 |
5 | DISCUSSION | 1 | 29 | [
"B29",
"B21",
"B18",
"B30",
"B31",
"B19"
] | 17,329,375 | pmid-8465200|pmid-12581657|pmid-15687384|pmid-16551743|pmid-9182561|pmid-9094712|pmid-15695524 | An alternative possibility is that the Mfd–RNAP interaction may allow RNAP to act as a ‘processivity factor’ for Mfd, ensuring that Mfd continues to push against the transcription complex until it is displaced. | [
"29",
"21",
"18",
"30",
"31",
"19"
] | 210 | 8,741 | 0 | false | An alternative possibility is that the Mfd–RNAP interaction may allow RNAP to act as a ‘processivity factor’ for Mfd, ensuring that Mfd continues to push against the transcription complex until it is displaced. | [] | An alternative possibility is that the Mfd–RNAP interaction may allow RNAP to act as a ‘processivity factor’ for Mfd, ensuring that Mfd continues to push against the transcription complex until it is displaced. | true | true | true | true | true | 1,400 |
5 | DISCUSSION | 1 | 29 | [
"B29",
"B21",
"B18",
"B30",
"B31",
"B19"
] | 17,329,375 | pmid-8465200|pmid-12581657|pmid-15687384|pmid-16551743|pmid-9182561|pmid-9094712|pmid-15695524 | Stalled transcription complexes are stabilized by multiple interactions between proteins, RNA and DNA, and are likely to present more of an obstacle to a translocating motor protein than a triplex does. | [
"29",
"21",
"18",
"30",
"31",
"19"
] | 202 | 8,742 | 0 | false | Stalled transcription complexes are stabilized by multiple interactions between proteins, RNA and DNA, and are likely to present more of an obstacle to a translocating motor protein than a triplex does. | [] | Stalled transcription complexes are stabilized by multiple interactions between proteins, RNA and DNA, and are likely to present more of an obstacle to a translocating motor protein than a triplex does. | true | true | true | true | true | 1,400 |
5 | DISCUSSION | 1 | 29 | [
"B29",
"B21",
"B18",
"B30",
"B31",
"B19"
] | 17,329,375 | pmid-8465200|pmid-12581657|pmid-15687384|pmid-16551743|pmid-9182561|pmid-9094712|pmid-15695524 | We do not know how many ATPase cycles are required for Mfd to displace a transcription complex, and unlike a TFO the transcription complex is dynamic and may slide backwards to its starting position if Mfd dissociates before displacement is complete (30,31). | [
"29",
"21",
"18",
"30",
"31",
"19"
] | 258 | 8,743 | 0 | false | We do not know how many ATPase cycles are required for Mfd to displace a transcription complex, and unlike a TFO the transcription complex is dynamic and may slide backwards to its starting position if Mfd dissociates before displacement is complete. | [
"30,31"
] | We do not know how many ATPase cycles are required for Mfd to displace a transcription complex, and unlike a TFO the transcription complex is dynamic and may slide backwards to its starting position if Mfd dissociates before displacement is complete. | true | true | true | true | true | 1,400 |
5 | DISCUSSION | 1 | 29 | [
"B29",
"B21",
"B18",
"B30",
"B31",
"B19"
] | 17,329,375 | pmid-8465200|pmid-12581657|pmid-15687384|pmid-16551743|pmid-9182561|pmid-9094712|pmid-15695524 | When associated with a transcription complex Mfd is tethered to the DNA both directly, via its translocase domains, and indirectly, via the contact of the RID with the transcription complex. | [
"29",
"21",
"18",
"30",
"31",
"19"
] | 190 | 8,744 | 0 | false | When associated with a transcription complex Mfd is tethered to the DNA both directly, via its translocase domains, and indirectly, via the contact of the RID with the transcription complex. | [] | When associated with a transcription complex Mfd is tethered to the DNA both directly, via its translocase domains, and indirectly, via the contact of the RID with the transcription complex. | true | true | true | true | true | 1,400 |
5 | DISCUSSION | 1 | 29 | [
"B29",
"B21",
"B18",
"B30",
"B31",
"B19"
] | 17,329,375 | pmid-8465200|pmid-12581657|pmid-15687384|pmid-16551743|pmid-9182561|pmid-9094712|pmid-15695524 | This means that translocation will not necessarily terminate if the translocase domains transiently dissociate from the DNA (in contrast to the situation that would arise with free MfdΔD7). | [
"29",
"21",
"18",
"30",
"31",
"19"
] | 189 | 8,745 | 0 | false | This means that translocation will not necessarily terminate if the translocase domains transiently dissociate from the DNA (in contrast to the situation that would arise with free MfdΔD7). | [] | This means that translocation will not necessarily terminate if the translocase domains transiently dissociate from the DNA (in contrast to the situation that would arise with free MfdΔD7). | true | true | true | true | true | 1,400 |
5 | DISCUSSION | 1 | 19 | [
"B29",
"B21",
"B18",
"B30",
"B31",
"B19"
] | 17,329,375 | pmid-8465200|pmid-12581657|pmid-15687384|pmid-16551743|pmid-9182561|pmid-9094712|pmid-15695524 | In this context, the transcription complex may therefore play a similar role to the wedge domain of RecG, which increases the processivity of that motor by acting as a sliding clamp on the DNA (19). | [
"29",
"21",
"18",
"30",
"31",
"19"
] | 198 | 8,746 | 1 | false | In this context, the transcription complex may therefore play a similar role to the wedge domain of RecG, which increases the processivity of that motor by acting as a sliding clamp on the DNA. | [
"19"
] | In this context, the transcription complex may therefore play a similar role to the wedge domain of RecG, which increases the processivity of that motor by acting as a sliding clamp on the DNA. | true | true | true | true | true | 1,400 |
6 | DISCUSSION | 1 | 32 | [
"B32",
"B33"
] | 17,329,375 | pmid-16009938|pmid-16595666 | Autoinhibition and context-specific activation may prove to be a widespread strategy for the control of helicase proteins that function within macromolecular assemblies. | [
"32",
"33"
] | 169 | 8,747 | 0 | false | Autoinhibition and context-specific activation may prove to be a widespread strategy for the control of helicase proteins that function within macromolecular assemblies. | [] | Autoinhibition and context-specific activation may prove to be a widespread strategy for the control of helicase proteins that function within macromolecular assemblies. | true | true | true | true | true | 1,401 |
6 | DISCUSSION | 1 | 32 | [
"B32",
"B33"
] | 17,329,375 | pmid-16009938|pmid-16595666 | It is important that the activity of such enzymes is strictly regulated, as their activities are costly to the cell in terms of ATP hydrolysis and likely to be deleterious if performed inappropriately. | [
"32",
"33"
] | 201 | 8,748 | 0 | false | It is important that the activity of such enzymes is strictly regulated, as their activities are costly to the cell in terms of ATP hydrolysis and likely to be deleterious if performed inappropriately. | [] | It is important that the activity of such enzymes is strictly regulated, as their activities are costly to the cell in terms of ATP hydrolysis and likely to be deleterious if performed inappropriately. | true | true | true | true | true | 1,401 |
6 | DISCUSSION | 1 | 32 | [
"B32",
"B33"
] | 17,329,375 | pmid-16009938|pmid-16595666 | The helicase activity of the E. coli Rep protein (a superfamily 1 helicase that functions in DNA replication), and the ATPase and DNA-binding activities of UvrB (a superfamily 2 helicase that detects DNA damage in complex with UvrA) have both been shown recently to be regulated by autoinhibitory domains (32,33). | [
"32",
"33"
] | 313 | 8,749 | 0 | false | The helicase activity of the E. coli Rep protein (a superfamily 1 helicase that functions in DNA replication), and the ATPase and DNA-binding activities of UvrB (a superfamily 2 helicase that detects DNA damage in complex with UvrA) have both been shown recently to be regulated by autoinhibitory domains. | [
"32,33"
] | The helicase activity of the E. coli Rep protein (a superfamily 1 helicase that functions in DNA replication), and the ATPase and DNA-binding activities of UvrB have both been shown recently to be regulated by autoinhibitory domains. | true | true | true | true | true | 1,401 |
6 | DISCUSSION | 1 | 32 | [
"B32",
"B33"
] | 17,329,375 | pmid-16009938|pmid-16595666 | Rep autoinhibition is thought to be relieved by dimerization, and it has been suggested that autoinhibition of UvrB may be relieved by interaction with UvrA. | [
"32",
"33"
] | 157 | 8,750 | 0 | false | Rep autoinhibition is thought to be relieved by dimerization, and it has been suggested that autoinhibition of UvrB may be relieved by interaction with UvrA. | [] | Rep autoinhibition is thought to be relieved by dimerization, and it has been suggested that autoinhibition of UvrB may be relieved by interaction with UvrA. | true | true | true | true | true | 1,401 |
6 | DISCUSSION | 1 | 32 | [
"B32",
"B33"
] | 17,329,375 | pmid-16009938|pmid-16595666 | The regulatory mechanism uncovered in our work ensures that DNA translocation by Mfd occurs only in the correct context of an Mfd–RNAP complex. | [
"32",
"33"
] | 143 | 8,751 | 0 | false | The regulatory mechanism uncovered in our work ensures that DNA translocation by Mfd occurs only in the correct context of an Mfd–RNAP complex. | [] | The regulatory mechanism uncovered in our work ensures that DNA translocation by Mfd occurs only in the correct context of an Mfd–RNAP complex. | true | true | true | true | true | 1,401 |
6 | DISCUSSION | 1 | 32 | [
"B32",
"B33"
] | 17,329,375 | pmid-16009938|pmid-16595666 | The fact that the control process involves domain D7, which is also implicated in regulating the interaction of Mfd with the repair protein UvrA, suggests that the transcription-coupled repair process as a whole is highly coordinated. | [
"32",
"33"
] | 234 | 8,752 | 0 | false | The fact that the control process involves domain D7, which is also implicated in regulating the interaction of Mfd with the repair protein UvrA, suggests that the transcription-coupled repair process as a whole is highly coordinated. | [] | The fact that the control process involves domain D7, which is also implicated in regulating the interaction of Mfd with the repair protein UvrA, suggests that the transcription-coupled repair process as a whole is highly coordinated. | true | true | true | true | true | 1,401 |
0 | INTRODUCTION | 1 | 1 | [
"b1",
"b2"
] | 16,935,872 | pmid-10357855|pmid-15328417 | Homologous recombination (HR) is a high fidelity and template-dependent DNA repair pathway found in all organisms studied. | [
"1",
"2"
] | 122 | 8,753 | 0 | false | Homologous recombination (HR) is a high fidelity and template-dependent DNA repair pathway found in all organisms studied. | [] | Homologous recombination (HR) is a high fidelity and template-dependent DNA repair pathway found in all organisms studied. | true | true | true | true | true | 1,402 |
0 | INTRODUCTION | 1 | 1 | [
"b1",
"b2"
] | 16,935,872 | pmid-10357855|pmid-15328417 | HR serves in the non-mutagenic tolerance of DNA damage, in the repair of complex DNA damage, such as single-stranded DNA (ssDNA) gaps, double-stranded DNA breaks (DSBs) and interstrand crosslinks, as well as in the recovery of stalled and collapsed replication forks (1,2). | [
"1",
"2"
] | 273 | 8,754 | 0 | false | HR serves in the non-mutagenic tolerance of DNA damage, in the repair of complex DNA damage, such as single-stranded DNA (ssDNA) gaps, double-stranded DNA breaks (DSBs) and interstrand crosslinks, as well as in the recovery of stalled and collapsed replication forks. | [
"1,2"
] | HR serves in the non-mutagenic tolerance of DNA damage, in the repair of complex DNA damage, such as single-stranded DNA (ssDNA) gaps, double-stranded DNA breaks (DSBs) and interstrand crosslinks, as well as in the recovery of stalled and collapsed replication forks. | true | true | true | true | true | 1,402 |
0 | INTRODUCTION | 1 | 1 | [
"b1",
"b2"
] | 16,935,872 | pmid-10357855|pmid-15328417 | Historically prominent is the role of HR during prophase of the first meiotic division, where it contributes to high fidelity segregation of the homologs and to the generation of genetic diversity among the meiotic products. | [
"1",
"2"
] | 224 | 8,755 | 0 | false | Historically prominent is the role of HR during prophase of the first meiotic division, where it contributes to high fidelity segregation of the homologs and to the generation of genetic diversity among the meiotic products. | [] | Historically prominent is the role of HR during prophase of the first meiotic division, where it contributes to high fidelity segregation of the homologs and to the generation of genetic diversity among the meiotic products. | true | true | true | true | true | 1,402 |
1 | INTRODUCTION | 1 | 3 | [
"b3",
"b4"
] | 16,935,872 | NA|pmid-9118215 | RAD54 is a core constituent of the RAD52 epistasis group that encodes the proteins that are essential for HR in eukaryotes. | [
"3",
"4"
] | 123 | 8,756 | 0 | false | RAD54 is a core constituent of the RAD52 epistasis group that encodes the proteins that are essential for HR in eukaryotes. | [] | RAD54 is a core constituent of the RAD52 epistasis group that encodes the proteins that are essential for HR in eukaryotes. | true | true | true | true | true | 1,403 |
1 | INTRODUCTION | 1 | 3 | [
"b3",
"b4"
] | 16,935,872 | NA|pmid-9118215 | Rad54 protein is a member of the Snf2-family of SF2 helicases that contains many prominent chromatin-remodeling proteins including Snf2, ISWI and others. | [
"3",
"4"
] | 153 | 8,757 | 0 | false | Rad54 protein is a member of the Snf2-family of SF2 helicases that contains many prominent chromatin-remodeling proteins including Snf2, ISWI and others. | [] | Rad54 protein is a member of the Snf2-family of SF2 helicases that contains many prominent chromatin-remodeling proteins including Snf2, ISWI and others. | true | true | true | true | true | 1,403 |
1 | INTRODUCTION | 1 | 3 | [
"b3",
"b4"
] | 16,935,872 | NA|pmid-9118215 | This group of proteins shares a common core that includes seven motifs proposed to identify helicases (3). | [
"3",
"4"
] | 106 | 8,758 | 1 | false | This group of proteins shares a common core that includes seven motifs proposed to identify helicases. | [
"3"
] | This group of proteins shares a common core that includes seven motifs proposed to identify helicases. | true | true | true | true | true | 1,403 |
1 | INTRODUCTION | 1 | 4 | [
"b3",
"b4"
] | 16,935,872 | NA|pmid-9118215 | However, rather than operating like DNA helicases, which are capable of separating the strands of duplex DNA, the Snf2-related proteins are viewed as motor proteins that translocate on duplex DNA and remodel specific protein–duplex DNA complexes (4). | [
"3",
"4"
] | 250 | 8,759 | 1 | false | However, rather than operating like DNA helicases, which are capable of separating the strands of duplex DNA, the Snf2-related proteins are viewed as motor proteins that translocate on duplex DNA and remodel specific protein–duplex DNA complexes. | [
"4"
] | However, rather than operating like DNA helicases, which are capable of separating the strands of duplex DNA, the Snf2-related proteins are viewed as motor proteins that translocate on duplex DNA and remodel specific protein–duplex DNA complexes. | true | true | true | true | true | 1,403 |
1 | INTRODUCTION | 1 | 3 | [
"b3",
"b4"
] | 16,935,872 | NA|pmid-9118215 | The particular functions of these proteins appear to involve specific protein interactions mediated by domains outside the core motor domain. | [
"3",
"4"
] | 141 | 8,760 | 0 | false | The particular functions of these proteins appear to involve specific protein interactions mediated by domains outside the core motor domain. | [] | The particular functions of these proteins appear to involve specific protein interactions mediated by domains outside the core motor domain. | true | true | true | true | true | 1,403 |
1 | INTRODUCTION | 1 | 3 | [
"b3",
"b4"
] | 16,935,872 | NA|pmid-9118215 | The budding yeast Saccharomyces cerevisiae genome encodes 17 Snf2-related proteins (Table 1). | [
"3",
"4"
] | 93 | 8,761 | 0 | false | The budding yeast Saccharomyces cerevisiae genome encodes 17 Snf2-related proteins (Table 1). | [] | The budding yeast Saccharomyces cerevisiae genome encodes 17 Snf2-related proteins (Table 1). | true | true | true | true | true | 1,403 |
1 | INTRODUCTION | 1 | 3 | [
"b3",
"b4"
] | 16,935,872 | NA|pmid-9118215 | Interestingly, at least seven of them, Rad54, Rdh54/Tid1, Rad5, Rad16, Rad26/CS-B, as well as the Ino80 and Swr1 complex, have specific functions during DNA repair. | [
"3",
"4"
] | 164 | 8,762 | 0 | false | Interestingly, at least seven of them, Rad54, Rdh54/Tid1, Rad5, Rad16, Rad26/CS-B, as well as the Ino80 and Swr1 complex, have specific functions during DNA repair. | [] | Interestingly, at least seven of them, Rad54, Rdh54/Tid1, Rad5, Rad16, Rad26/CS-B, as well as the Ino80 and Swr1 complex, have specific functions during DNA repair. | true | true | true | true | true | 1,403 |
2 | INTRODUCTION | 1 | 1 | [
"b1",
"b5",
"b8",
"b9",
"b11",
"b12"
] | 16,935,872 | pmid-10357855|pmid-10915877|pmid-12778123|pmid-10688638|pmid-12672490|pmid-12826279 | Previous reviews provide excellent overall outlines of HR and the RAD52 group proteins (1,5–8), as well as detailed discussions of the Snf2-related chromatin remodeling factors (9–11). | [
"1",
"5",
"8",
"9",
"11",
"12"
] | 184 | 8,763 | 0 | false | Previous reviews provide excellent overall outlines of HR and the RAD52 group proteins, as well as detailed discussions of the Snf2-related chromatin remodeling factors. | [
"1,5–8",
"9–11"
] | Previous reviews provide excellent overall outlines of HR and the RAD52 group proteins, as well as detailed discussions of the Snf2-related chromatin remodeling factors. | true | true | true | true | true | 1,404 |
2 | INTRODUCTION | 1 | 1 | [
"b1",
"b5",
"b8",
"b9",
"b11",
"b12"
] | 16,935,872 | pmid-10357855|pmid-10915877|pmid-12778123|pmid-10688638|pmid-12672490|pmid-12826279 | In this review, we focus on the Rad54 protein. | [
"1",
"5",
"8",
"9",
"11",
"12"
] | 46 | 8,764 | 0 | false | In this review, we focus on the Rad54 protein. | [] | In this review, we focus on the Rad54 protein. | true | true | true | true | true | 1,404 |
2 | INTRODUCTION | 1 | 1 | [
"b1",
"b5",
"b8",
"b9",
"b11",
"b12"
] | 16,935,872 | pmid-10357855|pmid-10915877|pmid-12778123|pmid-10688638|pmid-12672490|pmid-12826279 | Versatile like the proverbial Swiss Army knife, Rad54 has been postulated to function at multiple stages during HR. | [
"1",
"5",
"8",
"9",
"11",
"12"
] | 115 | 8,765 | 0 | false | Versatile like the proverbial Swiss Army knife, Rad54 has been postulated to function at multiple stages during HR. | [] | Versatile like the proverbial Swiss Army knife, Rad54 has been postulated to function at multiple stages during HR. | true | true | true | true | true | 1,404 |
2 | INTRODUCTION | 1 | 12 | [
"b1",
"b5",
"b8",
"b9",
"b11",
"b12"
] | 16,935,872 | pmid-10357855|pmid-10915877|pmid-12778123|pmid-10688638|pmid-12672490|pmid-12826279 | Biochemical analyses of complex in vitro recombination assays led to a number of mutually non-exclusive models, as reviewed previously (12). | [
"1",
"5",
"8",
"9",
"11",
"12"
] | 140 | 8,766 | 1 | false | Biochemical analyses of complex in vitro recombination assays led to a number of mutually non-exclusive models, as reviewed previously. | [
"12"
] | Biochemical analyses of complex in vitro recombination assays led to a number of mutually non-exclusive models, as reviewed previously. | true | true | true | true | true | 1,404 |
2 | INTRODUCTION | 1 | 1 | [
"b1",
"b5",
"b8",
"b9",
"b11",
"b12"
] | 16,935,872 | pmid-10357855|pmid-10915877|pmid-12778123|pmid-10688638|pmid-12672490|pmid-12826279 | We will discuss results from genetic, biochemical and cytological experiments, as well as insights from the recently accomplished determinations of the Rad54 protein structure to highlight the mechanistic models for the function of Rad54 during HR. | [
"1",
"5",
"8",
"9",
"11",
"12"
] | 248 | 8,767 | 0 | false | We will discuss results from genetic, biochemical and cytological experiments, as well as insights from the recently accomplished determinations of the Rad54 protein structure to highlight the mechanistic models for the function of Rad54 during HR. | [] | We will discuss results from genetic, biochemical and cytological experiments, as well as insights from the recently accomplished determinations of the Rad54 protein structure to highlight the mechanistic models for the function of Rad54 during HR. | true | true | true | true | true | 1,404 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2 B3 B4",
"B5"
] | 17,537,820 | pmid-12517228|pmid-2021692|pmid-11875246|pmid-85614|NA | Infections with influenza A viruses continue to be a public health problem, causing seasonal epidemics and sporadic but devastating pandemics. | [
"1",
"2–4",
"5"
] | 142 | 8,768 | 0 | false | Infections with influenza A viruses continue to be a public health problem, causing seasonal epidemics and sporadic but devastating pandemics. | [] | Infections with influenza A viruses continue to be a public health problem, causing seasonal epidemics and sporadic but devastating pandemics. | true | true | true | true | true | 1,405 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2 B3 B4",
"B5"
] | 17,537,820 | pmid-12517228|pmid-2021692|pmid-11875246|pmid-85614|NA | Each year in the US, influenza epidemics cause more than 200 000 hospitalizations and result in over 30 000 influenza-related deaths (1). | [
"1",
"2–4",
"5"
] | 137 | 8,769 | 1 | false | Each year in the US, influenza epidemics cause more than 200 000 hospitalizations and result in over 30 000 influenza-related deaths. | [
"1"
] | Each year in the US, influenza epidemics cause more than 200 000 hospitalizations and result in over 30 000 influenza-related deaths. | true | true | true | true | true | 1,405 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2 B3 B4",
"B5"
] | 17,537,820 | pmid-12517228|pmid-2021692|pmid-11875246|pmid-85614|NA | Influenza pandemics are infrequent but they can result in high mortality. | [
"1",
"2–4",
"5"
] | 73 | 8,770 | 0 | false | Influenza pandemics are infrequent but they can result in high mortality. | [] | Influenza pandemics are infrequent but they can result in high mortality. | true | true | true | true | true | 1,405 |
0 | INTRODUCTION | 1 | 2–4 | [
"B1",
"B2 B3 B4",
"B5"
] | 17,537,820 | pmid-12517228|pmid-2021692|pmid-11875246|pmid-85614|NA | It is estimated that ∼20–100 million people were killed worldwide by the 1918–1919 influenza pandemic (2–4). | [
"1",
"2–4",
"5"
] | 108 | 8,771 | 1 | false | It is estimated that ∼20–100 million people were killed worldwide by the 1918–1919 influenza pandemic. | [
"2–4"
] | It is estimated that ∼20–100 million people were killed worldwide by the 1918–1919 influenza pandemic. | true | true | true | true | true | 1,405 |
0 | INTRODUCTION | 1 | 5 | [
"B1",
"B2 B3 B4",
"B5"
] | 17,537,820 | pmid-12517228|pmid-2021692|pmid-11875246|pmid-85614|NA | The current level of pandemic alert is at the highest level, phase 3, since the most recent pandemic of 1968 (5). | [
"1",
"2–4",
"5"
] | 113 | 8,772 | 1 | false | The current level of pandemic alert is at the highest level, phase 3, since the most recent pandemic of 1968. | [
"5"
] | The current level of pandemic alert is at the highest level, phase 3, since the most recent pandemic of 1968. | true | true | true | true | true | 1,405 |
1 | INTRODUCTION | 1 | 6 | [
"B6",
"B7",
"B6",
"B8",
"B6",
"B9"
] | 17,537,820 | pmid-1579108|pmid-11779385|pmid-1579108|pmid-15280485|pmid-1579108|pmid-16627734 | Influenza viruses belong to the family Orthomyxoviridae and are classified into three types, A, B and C based on the identity of major internal protein antigens (6). | [
"6",
"7",
"6",
"8",
"6",
"9"
] | 165 | 8,773 | 1 | false | Influenza viruses belong to the family Orthomyxoviridae and are classified into three types, A, B and C based on the identity of major internal protein antigens. | [
"6"
] | Influenza viruses belong to the family Orthomyxoviridae and are classified into three types, A, B and C based on the identity of major internal protein antigens. | true | true | true | true | true | 1,406 |
1 | INTRODUCTION | 1 | 7 | [
"B6",
"B7",
"B6",
"B8",
"B6",
"B9"
] | 17,537,820 | pmid-1579108|pmid-11779385|pmid-1579108|pmid-15280485|pmid-1579108|pmid-16627734 | Influenza A and C viruses can infect multiple mammalian species, while influenza B virus is almost exclusively a human pathogen (7). | [
"6",
"7",
"6",
"8",
"6",
"9"
] | 132 | 8,774 | 1 | false | Influenza A and C viruses can infect multiple mammalian species, while influenza B virus is almost exclusively a human pathogen. | [
"7"
] | Influenza A and C viruses can infect multiple mammalian species, while influenza B virus is almost exclusively a human pathogen. | true | true | true | true | true | 1,406 |
1 | INTRODUCTION | 1 | 6 | [
"B6",
"B7",
"B6",
"B8",
"B6",
"B9"
] | 17,537,820 | pmid-1579108|pmid-11779385|pmid-1579108|pmid-15280485|pmid-1579108|pmid-16627734 | Influenza A viruses cause the greatest morbidity and mortality in humans. | [
"6",
"7",
"6",
"8",
"6",
"9"
] | 73 | 8,775 | 0 | false | Influenza A viruses cause the greatest morbidity and mortality in humans. | [] | Influenza A viruses cause the greatest morbidity and mortality in humans. | true | true | true | true | true | 1,406 |
1 | INTRODUCTION | 1 | 6 | [
"B6",
"B7",
"B6",
"B8",
"B6",
"B9"
] | 17,537,820 | pmid-1579108|pmid-11779385|pmid-1579108|pmid-15280485|pmid-1579108|pmid-16627734 | Interestingly, the largest pool of influenza A viruses is maintained by horizontal spread in wild aquatic birds, in which the virus does not normally cause any disease (6,8). | [
"6",
"7",
"6",
"8",
"6",
"9"
] | 174 | 8,776 | 0 | false | Interestingly, the largest pool of influenza A viruses is maintained by horizontal spread in wild aquatic birds, in which the virus does not normally cause any disease. | [
"6,8"
] | Interestingly, the largest pool of influenza A viruses is maintained by horizontal spread in wild aquatic birds, in which the virus does not normally cause any disease. | true | true | true | true | true | 1,406 |
1 | INTRODUCTION | 1 | 6 | [
"B6",
"B7",
"B6",
"B8",
"B6",
"B9"
] | 17,537,820 | pmid-1579108|pmid-11779385|pmid-1579108|pmid-15280485|pmid-1579108|pmid-16627734 | Food and companion animal populations such as poultry, swine, horses and dogs support sustained replication of certain lineages of influenza A, with minimal to lethal disease depending on the virulence of the strain (6). | [
"6",
"7",
"6",
"8",
"6",
"9"
] | 220 | 8,777 | 1 | false | Food and companion animal populations such as poultry, swine, horses and dogs support sustained replication of certain lineages of influenza A, with minimal to lethal disease depending on the virulence of the strain. | [
"6"
] | Food and companion animal populations such as poultry, swine, horses and dogs support sustained replication of certain lineages of influenza A, with minimal to lethal disease depending on the virulence of the strain. | true | true | true | true | true | 1,406 |
1 | INTRODUCTION | 1 | 9 | [
"B6",
"B7",
"B6",
"B8",
"B6",
"B9"
] | 17,537,820 | pmid-1579108|pmid-11779385|pmid-1579108|pmid-15280485|pmid-1579108|pmid-16627734 | Influenza viruses have evolved in association with their various hosts in different continents for extended periods of time (9). | [
"6",
"7",
"6",
"8",
"6",
"9"
] | 128 | 8,778 | 1 | false | Influenza viruses have evolved in association with their various hosts in different continents for extended periods of time. | [
"9"
] | Influenza viruses have evolved in association with their various hosts in different continents for extended periods of time. | true | true | true | true | true | 1,406 |
1 | INTRODUCTION | 1 | 6 | [
"B6",
"B7",
"B6",
"B8",
"B6",
"B9"
] | 17,537,820 | pmid-1579108|pmid-11779385|pmid-1579108|pmid-15280485|pmid-1579108|pmid-16627734 | This co-evolution has resulted in extensive genetic divergence among the extant viruses currently available for analysis. | [
"6",
"7",
"6",
"8",
"6",
"9"
] | 121 | 8,779 | 0 | false | This co-evolution has resulted in extensive genetic divergence among the extant viruses currently available for analysis. | [] | This co-evolution has resulted in extensive genetic divergence among the extant viruses currently available for analysis. | true | true | true | true | true | 1,406 |
2 | INTRODUCTION | 1 | 10 | [
"B10",
"B11"
] | 17,537,820 | pmid-15735418|pmid-16690910 | Influenza A viruses are classified into subtypes on the basis of antigenic analysis of hemagglutinin (HA) and neuraminidase (NA) glycoproteins. | [
"10",
"11"
] | 143 | 8,780 | 0 | false | Influenza A viruses are classified into subtypes on the basis of antigenic analysis of hemagglutinin (HA) and neuraminidase (NA) glycoproteins. | [] | Influenza A viruses are classified into subtypes on the basis of antigenic analysis of hemagglutinin (HA) and neuraminidase (NA) glycoproteins. | true | true | true | true | true | 1,407 |
2 | INTRODUCTION | 1 | 10 | [
"B10",
"B11"
] | 17,537,820 | pmid-15735418|pmid-16690910 | So far, 16 HA subtypes and 9 NA subtypes have been found (10). | [
"10",
"11"
] | 62 | 8,781 | 1 | false | So far, 16 HA subtypes and 9 NA subtypes have been found. | [
"10"
] | So far, 16 HA subtypes and 9 NA subtypes have been found. | true | true | true | true | true | 1,407 |
2 | INTRODUCTION | 1 | 10 | [
"B10",
"B11"
] | 17,537,820 | pmid-15735418|pmid-16690910 | In recent years, gene sequences have become available for a large number of viral strains creating a diverse pool of influenza A viruses from historical and current isolates collected in multiple geographic regions. | [
"10",
"11"
] | 215 | 8,782 | 0 | false | In recent years, gene sequences have become available for a large number of viral strains creating a diverse pool of influenza A viruses from historical and current isolates collected in multiple geographic regions. | [] | In recent years, gene sequences have become available for a large number of viral strains creating a diverse pool of influenza A viruses from historical and current isolates collected in multiple geographic regions. | true | true | true | true | true | 1,407 |
2 | INTRODUCTION | 1 | 10 | [
"B10",
"B11"
] | 17,537,820 | pmid-15735418|pmid-16690910 | Comparison of the deduced amino acid sequences of the HA and NA revealed an excellent agreement between the results of clustering viruses by the antigenic reactivity and sequence similarity. | [
"10",
"11"
] | 190 | 8,783 | 0 | false | Comparison of the deduced amino acid sequences of the HA and NA revealed an excellent agreement between the results of clustering viruses by the antigenic reactivity and sequence similarity. | [] | Comparison of the deduced amino acid sequences of the HA and NA revealed an excellent agreement between the results of clustering viruses by the antigenic reactivity and sequence similarity. | true | true | true | true | true | 1,407 |
2 | INTRODUCTION | 1 | 11 | [
"B10",
"B11"
] | 17,537,820 | pmid-15735418|pmid-16690910 | However, molecular genetic analysis allows a comprehensive analysis of the entire viral genome and is gaining popularity because it is more practical for most laboratories as a method for classification (11). | [
"10",
"11"
] | 208 | 8,784 | 1 | false | However, molecular genetic analysis allows a comprehensive analysis of the entire viral genome and is gaining popularity because it is more practical for most laboratories as a method for classification. | [
"11"
] | However, molecular genetic analysis allows a comprehensive analysis of the entire viral genome and is gaining popularity because it is more practical for most laboratories as a method for classification. | true | true | true | true | true | 1,407 |
2 | INTRODUCTION | 1 | 10 | [
"B10",
"B11"
] | 17,537,820 | pmid-15735418|pmid-16690910 | Most importantly, study of the influenza genomic structure, namely genotyping, could reveal mechanisms of virus evolution, spread and disease pathogenesis. | [
"10",
"11"
] | 155 | 8,785 | 0 | false | Most importantly, study of the influenza genomic structure, namely genotyping, could reveal mechanisms of virus evolution, spread and disease pathogenesis. | [] | Most importantly, study of the influenza genomic structure, namely genotyping, could reveal mechanisms of virus evolution, spread and disease pathogenesis. | true | true | true | true | true | 1,407 |
3 | INTRODUCTION | 1 | 12 | [
"B12",
"B13",
"B14",
"B15 B16 B17 B18 B19",
"B20",
"B21"
] | 17,537,820 | pmid-6351727|pmid-8387212|pmid-9882316|pmid-2769232|pmid-2939560|pmid-1895397|pmid-2398532|pmid-2800339|pmid-4549487|pmid-277933 | The influenza A genome consists of eight negative-stranded RNA segments that encode at least 10 viral proteins (12). | [
"12",
"13",
"14",
"15–19",
"20",
"21"
] | 116 | 8,786 | 1 | false | The influenza A genome consists of eight negative-stranded RNA segments that encode at least 10 viral proteins. | [
"12"
] | The influenza A genome consists of eight negative-stranded RNA segments that encode at least 10 viral proteins. | true | true | true | true | true | 1,408 |
3 | INTRODUCTION | 1 | 13 | [
"B12",
"B13",
"B14",
"B15 B16 B17 B18 B19",
"B20",
"B21"
] | 17,537,820 | pmid-6351727|pmid-8387212|pmid-9882316|pmid-2769232|pmid-2939560|pmid-1895397|pmid-2398532|pmid-2800339|pmid-4549487|pmid-277933 | The viral genome evolves through accumulation of mutation by the viral RNA-dependent RNA polymerase which lacks proofreading ability and through reassortment of entire gene segments(13). | [
"12",
"13",
"14",
"15–19",
"20",
"21"
] | 186 | 8,787 | 1 | false | The viral genome evolves through accumulation of mutation by the viral RNA-dependent RNA polymerase which lacks proofreading ability and through reassortment of entire gene segments. | [
"13"
] | The viral genome evolves through accumulation of mutation by the viral RNA-dependent RNA polymerase which lacks proofreading ability and through reassortment of entire gene segments. | true | true | true | true | true | 1,408 |
3 | INTRODUCTION | 1 | 14 | [
"B12",
"B13",
"B14",
"B15 B16 B17 B18 B19",
"B20",
"B21"
] | 17,537,820 | pmid-6351727|pmid-8387212|pmid-9882316|pmid-2769232|pmid-2939560|pmid-1895397|pmid-2398532|pmid-2800339|pmid-4549487|pmid-277933 | Forces selecting viral variants such as the neutralizing antibody response of vertebrate hosts as well as species-related structural variation can also promote rapid evolution (14). | [
"12",
"13",
"14",
"15–19",
"20",
"21"
] | 181 | 8,788 | 1 | false | Forces selecting viral variants such as the neutralizing antibody response of vertebrate hosts as well as species-related structural variation can also promote rapid evolution. | [
"14"
] | Forces selecting viral variants such as the neutralizing antibody response of vertebrate hosts as well as species-related structural variation can also promote rapid evolution. | true | true | true | true | true | 1,408 |
3 | INTRODUCTION | 1 | 15–19 | [
"B12",
"B13",
"B14",
"B15 B16 B17 B18 B19",
"B20",
"B21"
] | 17,537,820 | pmid-6351727|pmid-8387212|pmid-9882316|pmid-2769232|pmid-2939560|pmid-1895397|pmid-2398532|pmid-2800339|pmid-4549487|pmid-277933 | Each of the segments can evolve at a different rate if they are subject to differential selective pressures and functional constraints (15–19). | [
"12",
"13",
"14",
"15–19",
"20",
"21"
] | 143 | 8,789 | 1 | false | Each of the segments can evolve at a different rate if they are subject to differential selective pressures and functional constraints. | [
"15–19"
] | Each of the segments can evolve at a different rate if they are subject to differential selective pressures and functional constraints. | true | true | true | true | true | 1,408 |
3 | INTRODUCTION | 1 | 12 | [
"B12",
"B13",
"B14",
"B15 B16 B17 B18 B19",
"B20",
"B21"
] | 17,537,820 | pmid-6351727|pmid-8387212|pmid-9882316|pmid-2769232|pmid-2939560|pmid-1895397|pmid-2398532|pmid-2800339|pmid-4549487|pmid-277933 | The segmented nature of the viral genome allows for segment exchange (termed reassortment) when two distinct viruses co-infect a cell and generate progeny with a mixed genome (20,21). | [
"12",
"13",
"14",
"15–19",
"20",
"21"
] | 183 | 8,790 | 0 | false | The segmented nature of the viral genome allows for segment exchange (termed reassortment) when two distinct viruses co-infect a cell and generate progeny with a mixed genome. | [
"20,21"
] | The segmented nature of the viral genome allows for segment exchange (termed reassortment) when two distinct viruses co-infect a cell and generate progeny with a mixed genome. | true | true | true | true | true | 1,408 |
3 | INTRODUCTION | 1 | 12 | [
"B12",
"B13",
"B14",
"B15 B16 B17 B18 B19",
"B20",
"B21"
] | 17,537,820 | pmid-6351727|pmid-8387212|pmid-9882316|pmid-2769232|pmid-2939560|pmid-1895397|pmid-2398532|pmid-2800339|pmid-4549487|pmid-277933 | Reassortment may theoretically yield 254 (28 – 2) different combinations of gene segments from two parent viruses. | [
"12",
"13",
"14",
"15–19",
"20",
"21"
] | 114 | 8,791 | 0 | false | Reassortment may theoretically yield 254 (28 – 2) different combinations of gene segments from two parent viruses. | [] | Reassortment may theoretically yield 254 different combinations of gene segments from two parent viruses. | true | true | true | true | true | 1,408 |
4 | INTRODUCTION | 0 | null | null | 17,537,820 | null | A comprehensive influenza genotype database that can be searched using a web tool for the genotyping viruses is not available. | null | 126 | 8,792 | 0 | false | null | null | A comprehensive influenza genotype database that can be searched using a web tool for the genotyping viruses is not available. | true | true | true | true | true | 1,409 |
4 | INTRODUCTION | 0 | null | null | 17,537,820 | null | Unlike HIV and HCV, the influenza A virus has a segmented genome, so eight separate phylogenies must be analyzed to establish a genotype. | null | 137 | 8,793 | 0 | false | null | null | Unlike HIV and HCV, the influenza A virus has a segmented genome, so eight separate phylogenies must be analyzed to establish a genotype. | true | true | true | true | true | 1,409 |
5 | INTRODUCTION | 0 | null | null | 17,537,820 | null | We approached the problem of genotyping influenza A viruses by analyzing each gene segment independently, segregating gene segments into subtypes and subsequently into lineages. | null | 177 | 8,794 | 0 | false | null | null | We approached the problem of genotyping influenza A viruses by analyzing each gene segment independently, segregating gene segments into subtypes and subsequently into lineages. | true | true | true | true | true | 1,410 |
5 | INTRODUCTION | 0 | null | null | 17,537,820 | null | The genotype of an influenza A viral strain is the sequential aggregate of the eight assigned gene segment lineages. | null | 116 | 8,795 | 0 | false | null | null | The genotype of an influenza A viral strain is the sequential aggregate of the eight assigned gene segment lineages. | true | true | true | true | true | 1,410 |
5 | INTRODUCTION | 0 | null | null | 17,537,820 | null | A nomenclature for influenza A viral genotypes will allow researchers to unequivocally describe influenza A viral genotypes to analyze, compare and communicate the molecular epidemiology of the virus. | null | 200 | 8,796 | 0 | false | null | null | A nomenclature for influenza A viral genotypes will allow researchers to unequivocally describe influenza A viral genotypes to analyze, compare and communicate the molecular epidemiology of the virus. | true | true | true | true | true | 1,410 |
5 | INTRODUCTION | 0 | null | null | 17,537,820 | null | In this report, we define a nomenclature for influenza A viral genotypes and describe a web tool developed for genotyping influenza A viruses from genome sequences. | null | 164 | 8,797 | 0 | false | null | null | In this report, we define a nomenclature for influenza A viral genotypes and describe a web tool developed for genotyping influenza A viruses from genome sequences. | true | true | true | true | true | 1,410 |
5 | INTRODUCTION | 0 | null | null | 17,537,820 | null | Our tool facilitates identification of reassortment events between divergent lineages. | null | 86 | 8,798 | 0 | false | null | null | Our tool facilitates identification of reassortment events between divergent lineages. | true | true | true | true | true | 1,410 |
0 | INTRODUCTION | 1 | 1 | [
"b1",
"b12",
"b8",
"b13",
"b14",
"b12",
"b14",
"b1",
"b12",
"b15",
"b1",
"b9",
"b12",
"b15",
"b20",
"b1",
"b9",
"b21"
] | 16,757,578 | pmid-15952899|pmid-15063845|pmid-15948945|pmid-3047111|pmid-15305055|pmid-15063845|pmid-15305055|pmid-15952899|pmid-15063845|pmid-12540921|pmid-15952899|pmid-15519691|pmid-15063845|pmid-12540921|pmid-6397469|pmid-15952899|pmid-15519691|pmid-15659173|pmid-10651244|pmid-8855390|pmid-10385624|pmid-15087487|pmid-8636997|pm... | Two levels of DNA organization in bacterial nucleoid and eukaryotic chromatin have been suggested by earlier physical and chemical studies, these being the supramolecular looped organization and short-range structure (1–12). | [
"1",
"12",
"8",
"13",
"14",
"12",
"14",
"1",
"12",
"15",
"1",
"9",
"12",
"15",
"20",
"1",
"9",
"21"
] | 224 | 8,799 | 0 | false | Two levels of DNA organization in bacterial nucleoid and eukaryotic chromatin have been suggested by earlier physical and chemical studies, these being the supramolecular looped organization and short-range structure. | [
"1–12"
] | Two levels of DNA organization in bacterial nucleoid and eukaryotic chromatin have been suggested by earlier physical and chemical studies, these being the supramolecular looped organization and short-range structure. | true | true | true | true | true | 1,411 |
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