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 | 7 | [
"b7",
"b21",
"b7",
"b14",
"b35",
"b36",
"b7",
"b32"
] | 17,164,285 | NA|pmid-11250910|pmid-2477553|pmid-12692229|pmid-9649446|pmid-11044073|pmid-15890925|pmid-9649446|pmid-15183342|pmid-9649446|pmid-11044073|pmid-10775614|pmid-9882295|pmid-9649446|pmid-8764039 | For example, in one remarkable instance in SIV, poly(A) insertion resulted in a 36 nt PPT (7). | [
"7",
"21",
"7",
"14",
"35",
"36",
"7",
"32"
] | 94 | 2,200 | 1 | false | For example, in one remarkable instance in SIV, poly(A) insertion resulted in a 36 nt PPT. | [
"7"
] | For example, in one remarkable instance in SIV, poly(A) insertion resulted in a 36 nt PPT. | true | true | true | true | true | 382 |
0 | DISCUSSION | 1 | 7 | [
"b7",
"b21",
"b7",
"b14",
"b35",
"b36",
"b7",
"b32"
] | 17,164,285 | NA|pmid-11250910|pmid-2477553|pmid-12692229|pmid-9649446|pmid-11044073|pmid-15890925|pmid-9649446|pmid-15183342|pmid-9649446|pmid-11044073|pmid-10775614|pmid-9882295|pmid-9649446|pmid-8764039 | These findings support conclusions derived from the current work, namely, (i) that rU:dA and rA:dT tracts adjacent to and within the PPT, respectively, are to some extent functionally interchangeable (Figure 2a and b, lanes 3) and (ii) that a minimum (+)-strand primer length of 15–17 nt is required for optimal PPT func... | [
"7",
"21",
"7",
"14",
"35",
"36",
"7",
"32"
] | 325 | 2,201 | 0 | false | These findings support conclusions derived from the current work, namely, (i) that rU:dA and rA:dT tracts adjacent to and within the PPT, respectively, are to some extent functionally interchangeable (Figure 2a and b, lanes 3) and (ii) that a minimum (+)-strand primer length of 15–17 nt is required for optimal PPT func... | [] | These findings support conclusions derived from the current work, namely, (i) that rU:dA and rA:dT tracts adjacent to and within the PPT, respectively, are to some extent functionally interchangeable (Figure 2a and b, lanes 3) and (ii) that a minimum (+)-strand primer length of 15–17 nt is required for optimal PPT func... | true | true | true | true | true | 382 |
0 | DISCUSSION | 1 | 32 | [
"b7",
"b21",
"b7",
"b14",
"b35",
"b36",
"b7",
"b32"
] | 17,164,285 | NA|pmid-11250910|pmid-2477553|pmid-12692229|pmid-9649446|pmid-11044073|pmid-15890925|pmid-9649446|pmid-15183342|pmid-9649446|pmid-11044073|pmid-10775614|pmid-9882295|pmid-9649446|pmid-8764039 | Finally, it must be noted that our results contrast with a previous biochemical analysis indicating that the rU:dA tract does not play a role in PPT primer selection or initiation of (+) strand DNA synthesis (32). | [
"7",
"21",
"7",
"14",
"35",
"36",
"7",
"32"
] | 213 | 2,202 | 1 | false | Finally, it must be noted that our results contrast with a previous biochemical analysis indicating that the rU:dA tract does not play a role in PPT primer selection or initiation of (+) strand DNA synthesis. | [
"32"
] | Finally, it must be noted that our results contrast with a previous biochemical analysis indicating that the rU:dA tract does not play a role in PPT primer selection or initiation of (+) strand DNA synthesis. | true | true | true | true | true | 382 |
0 | DISCUSSION | 1 | 7 | [
"b7",
"b21",
"b7",
"b14",
"b35",
"b36",
"b7",
"b32"
] | 17,164,285 | NA|pmid-11250910|pmid-2477553|pmid-12692229|pmid-9649446|pmid-11044073|pmid-15890925|pmid-9649446|pmid-15183342|pmid-9649446|pmid-11044073|pmid-10775614|pmid-9882295|pmid-9649446|pmid-8764039 | This apparent discrepancy may be due to differences in experimental procedure, most notably, the higher stringency of our assay with respect to enzyme and salt concentration. | [
"7",
"21",
"7",
"14",
"35",
"36",
"7",
"32"
] | 174 | 2,203 | 0 | false | This apparent discrepancy may be due to differences in experimental procedure, most notably, the higher stringency of our assay with respect to enzyme and salt concentration. | [] | This apparent discrepancy may be due to differences in experimental procedure, most notably, the higher stringency of our assay with respect to enzyme and salt concentration. | true | true | true | true | true | 382 |
1 | DISCUSSION | 1 | 7 | [
"b7",
"b2",
"b37",
"b38",
"b29",
"b32",
"b39"
] | 17,164,285 | pmid-11250910|pmid-12730227|pmid-12972638|pmid-15778225|pmid-16306041|pmid-15004241|pmid-12972638|pmid-15004241|pmid-15778225|pmid-9649446|pmid-11250910|pmid-11875059|pmid-14512562|pmid-7681062|pmid-8764039|pmid-3040055 | The interrupted rA:dT tract constituting the upstream portion of the HIV-1 PPT does not appear to contain determinants for cleavage at the 5′ or 3′ terminus of the (+)-strand primer (Figure 1b and c, lane 6; Figure 2). | [
"7",
"2",
"37",
"38",
"29",
"32",
"39"
] | 218 | 2,204 | 0 | false | The interrupted rA:dT tract constituting the upstream portion of the HIV-1 PPT does not appear to contain determinants for cleavage at the 5′ or 3′ terminus of the (+)-strand primer. | [
"Figure 1b and c, lane 6; Figure 2"
] | The interrupted rA:dT tract constituting the upstream portion of the HIV-1 PPT does not appear to contain determinants for cleavage at the 5′ or 3′ terminus of the (+)-strand primer. | true | true | true | true | true | 383 |
1 | DISCUSSION | 1 | 7 | [
"b7",
"b2",
"b37",
"b38",
"b29",
"b32",
"b39"
] | 17,164,285 | pmid-11250910|pmid-12730227|pmid-12972638|pmid-15778225|pmid-16306041|pmid-15004241|pmid-12972638|pmid-15004241|pmid-15778225|pmid-9649446|pmid-11250910|pmid-11875059|pmid-14512562|pmid-7681062|pmid-8764039|pmid-3040055 | Instead, the role of this element is to add length to the primer while minimizing internal cleavage (Figure 2). | [
"7",
"2",
"37",
"38",
"29",
"32",
"39"
] | 111 | 2,205 | 0 | false | Instead, the role of this element is to add length to the primer while minimizing internal cleavage. | [
"Figure 2"
] | Instead, the role of this element is to add length to the primer while minimizing internal cleavage. | true | true | true | true | true | 383 |
1 | DISCUSSION | 1 | 7 | [
"b7",
"b2",
"b37",
"b38",
"b29",
"b32",
"b39"
] | 17,164,285 | pmid-11250910|pmid-12730227|pmid-12972638|pmid-15778225|pmid-16306041|pmid-15004241|pmid-12972638|pmid-15004241|pmid-15778225|pmid-9649446|pmid-11250910|pmid-11875059|pmid-14512562|pmid-7681062|pmid-8764039|pmid-3040055 | Of the three sub-motifs, the rA:dT tract sequence is least conserved among retroviruses, and is essentially absent in bovine leukemia virus and avian myeloblastoma virus (7). | [
"7",
"2",
"37",
"38",
"29",
"32",
"39"
] | 174 | 2,206 | 1 | false | Of the three sub-motifs, the rA:dT tract sequence is least conserved among retroviruses, and is essentially absent in bovine leukemia virus and avian myeloblastoma virus. | [
"7"
] | Of the three sub-motifs, the rA:dT tract sequence is least conserved among retroviruses, and is essentially absent in bovine leukemia virus and avian myeloblastoma virus. | true | true | true | true | true | 383 |
1 | DISCUSSION | 1 | 7 | [
"b7",
"b2",
"b37",
"b38",
"b29",
"b32",
"b39"
] | 17,164,285 | pmid-11250910|pmid-12730227|pmid-12972638|pmid-15778225|pmid-16306041|pmid-15004241|pmid-12972638|pmid-15004241|pmid-15778225|pmid-9649446|pmid-11250910|pmid-11875059|pmid-14512562|pmid-7681062|pmid-8764039|pmid-3040055 | Furthermore, the length of this element is highly variable, ranging from as few as 4 to as many as 17 nt, and it is usually discontinuous, being interrupted once or twice by one or more Gs or Cs. | [
"7",
"2",
"37",
"38",
"29",
"32",
"39"
] | 195 | 2,207 | 0 | false | Furthermore, the length of this element is highly variable, ranging from as few as 4 to as many as 17 nt, and it is usually discontinuous, being interrupted once or twice by one or more Gs or Cs. | [] | Furthermore, the length of this element is highly variable, ranging from as few as 4 to as many as 17 nt, and it is usually discontinuous, being interrupted once or twice by one or more Gs or Cs. | true | true | true | true | true | 383 |
1 | DISCUSSION | 1 | 7 | [
"b7",
"b2",
"b37",
"b38",
"b29",
"b32",
"b39"
] | 17,164,285 | pmid-11250910|pmid-12730227|pmid-12972638|pmid-15778225|pmid-16306041|pmid-15004241|pmid-12972638|pmid-15004241|pmid-15778225|pmid-9649446|pmid-11250910|pmid-11875059|pmid-14512562|pmid-7681062|pmid-8764039|pmid-3040055 | Despite this, interrupted rA:dT tracts usually contain a stretch of at least four consecutive rA:dTs, suggesting minor groove narrowing, helical rigidity and other structural features associated with homopolymeric A/T tracts may render the PPT resistant to RNase H. Altered inter-strand base pairing, noted to occur near... | [
"7",
"2",
"37",
"38",
"29",
"32",
"39"
] | 433 | 2,208 | 0 | false | Despite this, interrupted rA:dT tracts usually contain a stretch of at least four consecutive rA:dTs, suggesting minor groove narrowing, helical rigidity and other structural features associated with homopolymeric A/T tracts may render the PPT resistant to RNase H. Altered inter-strand base pairing, noted to occur near... | [
"2,37"
] | Despite this, interrupted rA:dT tracts usually contain a stretch of at least four consecutive rA:dTs, suggesting minor groove narrowing, helical rigidity and other structural features associated with homopolymeric A/T tracts may render the PPT resistant to RNase H. Altered inter-strand base pairing, noted to occur near... | true | true | true | true | true | 383 |
1 | DISCUSSION | 1 | 38 | [
"b7",
"b2",
"b37",
"b38",
"b29",
"b32",
"b39"
] | 17,164,285 | pmid-11250910|pmid-12730227|pmid-12972638|pmid-15778225|pmid-16306041|pmid-15004241|pmid-12972638|pmid-15004241|pmid-15778225|pmid-9649446|pmid-11250910|pmid-11875059|pmid-14512562|pmid-7681062|pmid-8764039|pmid-3040055 | However, this sub-motif has proven relatively insensitive to mutation in vivo (38) as well as in vitro (29,32), and in the current study, complete disruption of the rA:dT tract via multiple A→G mutations had little effect on (+)-strand initiation (Figure 1b and c, lane 4). | [
"7",
"2",
"37",
"38",
"29",
"32",
"39"
] | 273 | 2,209 | 1 | false | However, this sub-motif has proven relatively insensitive to mutation in vivo as well as in vitro, and in the current study, complete disruption of the rA:dT tract via multiple A→G mutations had little effect on (+)-strand initiation (Figure 1b and c, lane 4). | [
"38",
"29,32"
] | However, this sub-motif has proven relatively insensitive to mutation in vivo as well as in vitro, and in the current study, complete disruption of the rA:dT tract via multiple A→G mutations had little effect on (+)-strand initiation (Figure 1b and c, lane 4). | true | true | true | true | true | 383 |
1 | DISCUSSION | 1 | 7 | [
"b7",
"b2",
"b37",
"b38",
"b29",
"b32",
"b39"
] | 17,164,285 | pmid-11250910|pmid-12730227|pmid-12972638|pmid-15778225|pmid-16306041|pmid-15004241|pmid-12972638|pmid-15004241|pmid-15778225|pmid-9649446|pmid-11250910|pmid-11875059|pmid-14512562|pmid-7681062|pmid-8764039|pmid-3040055 | Amino acid coding requirements may also play a role in determining rA:dT tract composition. | [
"7",
"2",
"37",
"38",
"29",
"32",
"39"
] | 91 | 2,210 | 0 | false | Amino acid coding requirements may also play a role in determining rA:dT tract composition. | [] | Amino acid coding requirements may also play a role in determining rA:dT tract composition. | true | true | true | true | true | 383 |
1 | DISCUSSION | 1 | 39 | [
"b7",
"b2",
"b37",
"b38",
"b29",
"b32",
"b39"
] | 17,164,285 | pmid-11250910|pmid-12730227|pmid-12972638|pmid-15778225|pmid-16306041|pmid-15004241|pmid-12972638|pmid-15004241|pmid-15778225|pmid-9649446|pmid-11250910|pmid-11875059|pmid-14512562|pmid-7681062|pmid-8764039|pmid-3040055 | The HIV-1 3′ PPT, for example, is embedded within the nef open reading frame, while the central PPT lies within the coding sequence for integrase (39). | [
"7",
"2",
"37",
"38",
"29",
"32",
"39"
] | 151 | 2,211 | 1 | false | The HIV-1 3′ PPT, for example, is embedded within the nef open reading frame, while the central PPT lies within the coding sequence for integrase. | [
"39"
] | The HIV-1 3′ PPT, for example, is embedded within the nef open reading frame, while the central PPT lies within the coding sequence for integrase. | true | true | true | true | true | 383 |
1 | DISCUSSION | 1 | 7 | [
"b7",
"b2",
"b37",
"b38",
"b29",
"b32",
"b39"
] | 17,164,285 | pmid-11250910|pmid-12730227|pmid-12972638|pmid-15778225|pmid-16306041|pmid-15004241|pmid-12972638|pmid-15004241|pmid-15778225|pmid-9649446|pmid-11250910|pmid-11875059|pmid-14512562|pmid-7681062|pmid-8764039|pmid-3040055 | Finally, accessory proteins, such as NC may alter the sequence requirements of PPT selection/utilization in vivo in a manner not predicted by our simple assays. | [
"7",
"2",
"37",
"38",
"29",
"32",
"39"
] | 160 | 2,212 | 0 | false | Finally, accessory proteins, such as NC may alter the sequence requirements of PPT selection/utilization in vivo in a manner not predicted by our simple assays. | [] | Finally, accessory proteins, such as NC may alter the sequence requirements of PPT selection/utilization in vivo in a manner not predicted by our simple assays. | true | true | true | true | true | 383 |
2 | DISCUSSION | 1 | 40 | [
"b40",
"b41",
"b42",
"b43",
"b44",
"b45"
] | 17,164,285 | pmid-9649446|pmid-15183342|pmid-15183342|pmid-15909999|pmid-1913209|pmid-11250910|pmid-1720554|pmid-1374166|pmid-8567660|pmid-11035788|pmid-10956669|pmid-7545436 | The results of Figure 2 suggest that the optimum length of the plus-strand primer is ∼17 nt, the length of which is roughly equivalent to the distance between the DNA polymerase and RNase H active sites of HIV-1 RT (40,41). | [
"40",
"41",
"42",
"43",
"44",
"45"
] | 223 | 2,213 | 0 | false | The results of Figure 2 suggest that the optimum length of the plus-strand primer is ∼17 nt, the length of which is roughly equivalent to the distance between the DNA polymerase and RNase H active sites of HIV-1 RT. | [
"40,41"
] | The results of Figure 2 suggest that the optimum length of the plus-strand primer is ∼17 nt, the length of which is roughly equivalent to the distance between the DNA polymerase and RNase H active sites of HIV-1 RT. | true | true | true | true | true | 384 |
2 | DISCUSSION | 1 | 40 | [
"b40",
"b41",
"b42",
"b43",
"b44",
"b45"
] | 17,164,285 | pmid-9649446|pmid-15183342|pmid-15183342|pmid-15909999|pmid-1913209|pmid-11250910|pmid-1720554|pmid-1374166|pmid-8567660|pmid-11035788|pmid-10956669|pmid-7545436 | This suggests that positioning of RT over the hybrid duplex may play an important role in hydrolysis at the PPT-U3 junction. | [
"40",
"41",
"42",
"43",
"44",
"45"
] | 124 | 2,214 | 0 | false | This suggests that positioning of RT over the hybrid duplex may play an important role in hydrolysis at the PPT-U3 junction. | [] | This suggests that positioning of RT over the hybrid duplex may play an important role in hydrolysis at the PPT-U3 junction. | true | true | true | true | true | 384 |
2 | DISCUSSION | 1 | 42 | [
"b40",
"b41",
"b42",
"b43",
"b44",
"b45"
] | 17,164,285 | pmid-9649446|pmid-15183342|pmid-15183342|pmid-15909999|pmid-1913209|pmid-11250910|pmid-1720554|pmid-1374166|pmid-8567660|pmid-11035788|pmid-10956669|pmid-7545436 | Normally, HIV-1 RT binds a hybrid duplex containing two recessed RNA termini such that the polymerase active site is located over the DNA strand opposite the RNA 5′ terminus (42). | [
"40",
"41",
"42",
"43",
"44",
"45"
] | 179 | 2,215 | 1 | false | Normally, HIV-1 RT binds a hybrid duplex containing two recessed RNA termini such that the polymerase active site is located over the DNA strand opposite the RNA 5′ terminus. | [
"42"
] | Normally, HIV-1 RT binds a hybrid duplex containing two recessed RNA termini such that the polymerase active site is located over the DNA strand opposite the RNA 5′ terminus. | true | true | true | true | true | 384 |
2 | DISCUSSION | 1 | 40 | [
"b40",
"b41",
"b42",
"b43",
"b44",
"b45"
] | 17,164,285 | pmid-9649446|pmid-15183342|pmid-15183342|pmid-15909999|pmid-1913209|pmid-11250910|pmid-1720554|pmid-1374166|pmid-8567660|pmid-11035788|pmid-10956669|pmid-7545436 | In the case of the (+)-strand primer/DNA hybrid, this would place the RNase H domain over the RNA strand near the PPT-U3 junction. | [
"40",
"41",
"42",
"43",
"44",
"45"
] | 130 | 2,216 | 0 | false | In the case of the (+)-strand primer/DNA hybrid, this would place the RNase H domain over the RNA strand near the PPT-U3 junction. | [] | In the case of the (+)-strand primer/DNA hybrid, this would place the RNase H domain over the RNA strand near the PPT-U3 junction. | true | true | true | true | true | 384 |
2 | DISCUSSION | 1 | 40 | [
"b40",
"b41",
"b42",
"b43",
"b44",
"b45"
] | 17,164,285 | pmid-9649446|pmid-15183342|pmid-15183342|pmid-15909999|pmid-1913209|pmid-11250910|pmid-1720554|pmid-1374166|pmid-8567660|pmid-11035788|pmid-10956669|pmid-7545436 | This preferred mode of binding may explain why G-tract mutations (i.e. | [
"40",
"41",
"42",
"43",
"44",
"45"
] | 70 | 2,217 | 0 | false | This preferred mode of binding may explain why G-tract mutations (i.e. | [] | This preferred mode of binding may explain why G-tract mutations (i.e. | true | true | true | true | true | 384 |
2 | DISCUSSION | 1 | 40 | [
"b40",
"b41",
"b42",
"b43",
"b44",
"b45"
] | 17,164,285 | pmid-9649446|pmid-15183342|pmid-15183342|pmid-15909999|pmid-1913209|pmid-11250910|pmid-1720554|pmid-1374166|pmid-8567660|pmid-11035788|pmid-10956669|pmid-7545436 | rG→rA) are more likely to result in internal PPT cleavage than the inverse substitutions (rA→rG) within the rA:dT tract, since the RNase H domain of HIV-1 RT (located at or near PPT position −1) would be expected to be in much closer proximity to the former sub-motif. | [
"40",
"41",
"42",
"43",
"44",
"45"
] | 268 | 2,218 | 0 | false | rG→rA) are more likely to result in internal PPT cleavage than the inverse substitutions (rA→rG) within the rA:dT tract, since the RNase H domain of HIV-1 RT (located at or near PPT position −1) would be expected to be in much closer proximity to the former sub-motif. | [] | rG→rA) are more likely to result in internal PPT cleavage than the inverse substitutions (rA→rG) within the rA:dT tract, since the RNase H domain of HIV-1 RT (located at or near PPT position −1) would be expected to be in much closer proximity to the former sub-motif. | false | true | true | true | false | 384 |
2 | DISCUSSION | 1 | 40 | [
"b40",
"b41",
"b42",
"b43",
"b44",
"b45"
] | 17,164,285 | pmid-9649446|pmid-15183342|pmid-15183342|pmid-15909999|pmid-1913209|pmid-11250910|pmid-1720554|pmid-1374166|pmid-8567660|pmid-11035788|pmid-10956669|pmid-7545436 | It also appears, however, that in contrast to an RNA/DNA hybrid of random sequence, positioning of RT on a PPT/DNA hybrid is largely independent of the location of the primer 5′ terminus, since (+)-strand initiation is unaffected by the 5′-AAAAG-3′ insertion in substrate PS-9 (Figure 2a and b, lanes W and 2). | [
"40",
"41",
"42",
"43",
"44",
"45"
] | 310 | 2,219 | 0 | false | It also appears, however, that in contrast to an RNA/DNA hybrid of random sequence, positioning of RT on a PPT/DNA hybrid is largely independent of the location of the primer 5′ terminus, since (+)-strand initiation is unaffected by the 5′-AAAAG-3′ insertion in substrate PS-9 (Figure 2a and b, lanes W and 2). | [] | It also appears, however, that in contrast to an RNA/DNA hybrid of random sequence, positioning of RT on a PPT/DNA hybrid is largely independent of the location of the primer 5′ terminus, since (+)-strand initiation is unaffected by the 5′-AAAAG-3′ insertion in substrate PS-9 (Figure 2a and b, lanes W and 2). | true | true | true | true | true | 384 |
2 | DISCUSSION | 1 | 40 | [
"b40",
"b41",
"b42",
"b43",
"b44",
"b45"
] | 17,164,285 | pmid-9649446|pmid-15183342|pmid-15183342|pmid-15909999|pmid-1913209|pmid-11250910|pmid-1720554|pmid-1374166|pmid-8567660|pmid-11035788|pmid-10956669|pmid-7545436 | This also argues that stepwise digestion of the substrate from the RNA 5′ terminus (43,44) may not be essential for PPT selection. | [
"40",
"41",
"42",
"43",
"44",
"45"
] | 130 | 2,220 | 0 | false | This also argues that stepwise digestion of the substrate from the RNA 5′ terminus may not be essential for PPT selection. | [
"43,44"
] | This also argues that stepwise digestion of the substrate from the RNA 5′ terminus may not be essential for PPT selection. | true | true | true | true | true | 384 |
2 | DISCUSSION | 1 | 40 | [
"b40",
"b41",
"b42",
"b43",
"b44",
"b45"
] | 17,164,285 | pmid-9649446|pmid-15183342|pmid-15183342|pmid-15909999|pmid-1913209|pmid-11250910|pmid-1720554|pmid-1374166|pmid-8567660|pmid-11035788|pmid-10956669|pmid-7545436 | However, it is clear that shortening the primer adversely affects both (+)-strand initiation and primer removal (Figure 2), most likely due to reduced affinity of RT for the smaller hybrid. | [
"40",
"41",
"42",
"43",
"44",
"45"
] | 189 | 2,221 | 0 | false | However, it is clear that shortening the primer adversely affects both (+)-strand initiation and primer removal (Figure 2), most likely due to reduced affinity of RT for the smaller hybrid. | [] | However, it is clear that shortening the primer adversely affects both (+)-strand initiation and primer removal (Figure 2), most likely due to reduced affinity of RT for the smaller hybrid. | true | true | true | true | true | 384 |
2 | DISCUSSION | 1 | 45 | [
"b40",
"b41",
"b42",
"b43",
"b44",
"b45"
] | 17,164,285 | pmid-9649446|pmid-15183342|pmid-15183342|pmid-15909999|pmid-1913209|pmid-11250910|pmid-1720554|pmid-1374166|pmid-8567660|pmid-11035788|pmid-10956669|pmid-7545436 | Dissociation of the hybrid is probably not an important factor, since the Tm of even the shortest primer evaluated (substrate PS-13; Figure 2a and b, lane 6) would be expected to exceed 42°C (45). | [
"40",
"41",
"42",
"43",
"44",
"45"
] | 196 | 2,222 | 1 | false | Dissociation of the hybrid is probably not an important factor, since the Tm of even the shortest primer evaluated (substrate PS-13; Figure 2a and b, lane 6) would be expected to exceed 42°C. | [
"45"
] | Dissociation of the hybrid is probably not an important factor, since the Tm of even the shortest primer evaluated (substrate PS-13; Figure 2a and b, lane 6) would be expected to exceed 42°C. | true | true | true | true | true | 384 |
3 | DISCUSSION | 1 | 34 | [
"b34",
"b2",
"b20",
"b37",
"b31"
] | 17,164,285 | pmid-7681062|pmid-11250910|pmid-11939780|pmid-16306040|pmid-11250910|pmid-15004241|pmid-11875059|pmid-14636594 | Finally, our results indicate that in HIV-1, determinants for cleavage at, and initiation from the PPT-U3 junction reside within and immediately adjacent to the rG:dC tract, even when this is displaced to other locations within the PPT (Figure 1b, lanes 1 and 2). | [
"34",
"2",
"20",
"37",
"31"
] | 263 | 2,223 | 0 | false | Finally, our results indicate that in HIV-1, determinants for cleavage at, and initiation from the PPT-U3 junction reside within and immediately adjacent to the rG:dC tract, even when this is displaced to other locations within the PPT. | [
"Figure 1b, lanes 1 and 2"
] | Finally, our results indicate that in HIV-1, determinants for cleavage at, and initiation from the PPT-U3 junction reside within and immediately adjacent to the rG:dC tract, even when this is displaced to other locations within the PPT. | true | true | true | true | true | 385 |
3 | DISCUSSION | 1 | 34 | [
"b34",
"b2",
"b20",
"b37",
"b31"
] | 17,164,285 | pmid-7681062|pmid-11250910|pmid-11939780|pmid-16306040|pmid-11250910|pmid-15004241|pmid-11875059|pmid-14636594 | Furthermore, in agreement with the recent findings of Schultz et al. | [
"34",
"2",
"20",
"37",
"31"
] | 68 | 2,224 | 0 | false | Furthermore, in agreement with the recent findings of Schultz et al. | [] | Furthermore, in agreement with the recent findings of Schultz et al. | true | true | true | true | true | 385 |
3 | DISCUSSION | 1 | 34 | [
"b34",
"b2",
"b20",
"b37",
"b31"
] | 17,164,285 | pmid-7681062|pmid-11250910|pmid-11939780|pmid-16306040|pmid-11250910|pmid-15004241|pmid-11875059|pmid-14636594 | (34), −4rG, −2rG and +1rA were found to be of particular significance in defining cleavage specificity. | [
"34",
"2",
"20",
"37",
"31"
] | 103 | 2,225 | 1 | false | , −4rG, −2rG and +1rA were found to be of particular significance in defining cleavage specificity. | [
"34"
] | , −4rG, −2rG and +1rA were found to be of particular significance in defining cleavage specificity. | false | false | true | true | false | 385 |
3 | DISCUSSION | 1 | 34 | [
"b34",
"b2",
"b20",
"b37",
"b31"
] | 17,164,285 | pmid-7681062|pmid-11250910|pmid-11939780|pmid-16306040|pmid-11250910|pmid-15004241|pmid-11875059|pmid-14636594 | Using nucleoside analogs, we were able to modulate the chemical composition of purines at these positions to determine which exocyclic moieties were critical in this regard. | [
"34",
"2",
"20",
"37",
"31"
] | 173 | 2,226 | 0 | false | Using nucleoside analogs, we were able to modulate the chemical composition of purines at these positions to determine which exocyclic moieties were critical in this regard. | [] | Using nucleoside analogs, we were able to modulate the chemical composition of purines at these positions to determine which exocyclic moieties were critical in this regard. | true | true | true | true | true | 385 |
3 | DISCUSSION | 1 | 34 | [
"b34",
"b2",
"b20",
"b37",
"b31"
] | 17,164,285 | pmid-7681062|pmid-11250910|pmid-11939780|pmid-16306040|pmid-11250910|pmid-15004241|pmid-11875059|pmid-14636594 | The presence of a 2-NH2 group at position −2 and the absence of this group at position +1, proved essential for directing cleavage at the PPT-U3 junction. | [
"34",
"2",
"20",
"37",
"31"
] | 154 | 2,227 | 0 | false | The presence of a 2-NH2 group at position −2 and the absence of this group at position +1, proved essential for directing cleavage at the PPT-U3 junction. | [] | The presence of a 2-NH2 group at position −2 and the absence of this group at position +1, proved essential for directing cleavage at the PPT-U3 junction. | true | true | true | true | true | 385 |
3 | DISCUSSION | 1 | 34 | [
"b34",
"b2",
"b20",
"b37",
"b31"
] | 17,164,285 | pmid-7681062|pmid-11250910|pmid-11939780|pmid-16306040|pmid-11250910|pmid-15004241|pmid-11875059|pmid-14636594 | In the former case, the 2-NH2 group also plays a role in preventing internal cleavage of the PPT at or near position −2. | [
"34",
"2",
"20",
"37",
"31"
] | 120 | 2,228 | 0 | false | In the former case, the 2-NH2 group also plays a role in preventing internal cleavage of the PPT at or near position −2. | [] | In the former case, the 2-NH2 group also plays a role in preventing internal cleavage of the PPT at or near position −2. | true | true | true | true | true | 385 |
3 | DISCUSSION | 1 | 2 | [
"b34",
"b2",
"b20",
"b37",
"b31"
] | 17,164,285 | pmid-7681062|pmid-11250910|pmid-11939780|pmid-16306040|pmid-11250910|pmid-15004241|pmid-11875059|pmid-14636594 | Intriguingly, only two residues directly contact RNA bases in the vicinity of the RNase H domain in the HIV-1 RT-PPT/DNA co-crystal structure, namely Q475 and R448 of the RNase H primer grip at positions −2 and +1, respectively, relative to the scissile phosphate identified in that structure (2). | [
"34",
"2",
"20",
"37",
"31"
] | 297 | 2,229 | 1 | false | Intriguingly, only two residues directly contact RNA bases in the vicinity of the RNase H domain in the HIV-1 RT-PPT/DNA co-crystal structure, namely Q475 and R448 of the RNase H primer grip at positions −2 and +1, respectively, relative to the scissile phosphate identified in that structure. | [
"2"
] | Intriguingly, only two residues directly contact RNA bases in the vicinity of the RNase H domain in the HIV-1 RT-PPT/DNA co-crystal structure, namely Q475 and R448 of the RNase H primer grip at positions −2 and +1, respectively, relative to the scissile phosphate identified in that structure. | true | true | true | true | true | 385 |
3 | DISCUSSION | 1 | 34 | [
"b34",
"b2",
"b20",
"b37",
"b31"
] | 17,164,285 | pmid-7681062|pmid-11250910|pmid-11939780|pmid-16306040|pmid-11250910|pmid-15004241|pmid-11875059|pmid-14636594 | Furthermore, contacts occur at or near position 2 of the purines in these locations. | [
"34",
"2",
"20",
"37",
"31"
] | 84 | 2,230 | 0 | false | Furthermore, contacts occur at or near position 2 of the purines in these locations. | [] | Furthermore, contacts occur at or near position 2 of the purines in these locations. | true | true | true | true | true | 385 |
3 | DISCUSSION | 1 | 34 | [
"b34",
"b2",
"b20",
"b37",
"b31"
] | 17,164,285 | pmid-7681062|pmid-11250910|pmid-11939780|pmid-16306040|pmid-11250910|pmid-15004241|pmid-11875059|pmid-14636594 | This raises the possibility that steric interference and/or disruption of specific hydrogen bonds at positions −2 and +1 may directly influence whether or not cleavage occurs at the PPT-U3 junction. | [
"34",
"2",
"20",
"37",
"31"
] | 198 | 2,231 | 0 | false | This raises the possibility that steric interference and/or disruption of specific hydrogen bonds at positions −2 and +1 may directly influence whether or not cleavage occurs at the PPT-U3 junction. | [] | This raises the possibility that steric interference and/or disruption of specific hydrogen bonds at positions −2 and +1 may directly influence whether or not cleavage occurs at the PPT-U3 junction. | true | true | true | true | true | 385 |
3 | DISCUSSION | 1 | 34 | [
"b34",
"b2",
"b20",
"b37",
"b31"
] | 17,164,285 | pmid-7681062|pmid-11250910|pmid-11939780|pmid-16306040|pmid-11250910|pmid-15004241|pmid-11875059|pmid-14636594 | For example, a +1rA→rG substitution would be expected to create a steric clash with residue R448 of HIV-1 RT by introducing a relatively bulky amino group at position 2 of the the purine. | [
"34",
"2",
"20",
"37",
"31"
] | 187 | 2,232 | 0 | false | For example, a +1rA→rG substitution would be expected to create a steric clash with residue R448 of HIV-1 RT by introducing a relatively bulky amino group at position 2 of the the purine. | [] | For example, a +1rA→rG substitution would be expected to create a steric clash with residue R448 of HIV-1 RT by introducing a relatively bulky amino group at position 2 of the the purine. | true | true | true | true | true | 385 |
3 | DISCUSSION | 1 | 34 | [
"b34",
"b2",
"b20",
"b37",
"b31"
] | 17,164,285 | pmid-7681062|pmid-11250910|pmid-11939780|pmid-16306040|pmid-11250910|pmid-15004241|pmid-11875059|pmid-14636594 | In contrast, a −2rA→rI substitution, which would not change the constituent at the purine 2-position, would have no apparent effect. | [
"34",
"2",
"20",
"37",
"31"
] | 132 | 2,233 | 0 | false | In contrast, a −2rA→rI substitution, which would not change the constituent at the purine 2-position, would have no apparent effect. | [] | In contrast, a −2rA→rI substitution, which would not change the constituent at the purine 2-position, would have no apparent effect. | true | true | true | true | true | 385 |
3 | DISCUSSION | 1 | 34 | [
"b34",
"b2",
"b20",
"b37",
"b31"
] | 17,164,285 | pmid-7681062|pmid-11250910|pmid-11939780|pmid-16306040|pmid-11250910|pmid-15004241|pmid-11875059|pmid-14636594 | A model depicting such a scenario is shown in Figure 7. | [
"34",
"2",
"20",
"37",
"31"
] | 55 | 2,234 | 0 | false | A model depicting such a scenario is shown in Figure 7. | [] | A model depicting such a scenario is shown in Figure 7. | true | true | true | true | true | 385 |
3 | DISCUSSION | 1 | 31 | [
"b34",
"b2",
"b20",
"b37",
"b31"
] | 17,164,285 | pmid-7681062|pmid-11250910|pmid-11939780|pmid-16306040|pmid-11250910|pmid-15004241|pmid-11875059|pmid-14636594 | Alternatively, the importance of −2rG and +1rA may stem from unusual base pairing at these positions (20,37), wherein the 2-NH2-substituted purine may disrupt important cis-acting signals directing RT-binding and cleavage, and/or enhanced helical flexibility noted to occur within 5′-rArGrA-3′ steps (31). | [
"34",
"2",
"20",
"37",
"31"
] | 305 | 2,235 | 1 | false | Alternatively, the importance of −2rG and +1rA may stem from unusual base pairing at these positions, wherein the 2-NH2-substituted purine may disrupt important cis-acting signals directing RT-binding and cleavage, and/or enhanced helical flexibility noted to occur within 5′-rArGrA-3′ steps. | [
"20,37",
"31"
] | Alternatively, the importance of −2rG and +1rA may stem from unusual base pairing at these positions, wherein the 2-NH2-substituted purine may disrupt important cis-acting signals directing RT-binding and cleavage, and/or enhanced helical flexibility noted to occur within 5′-rArGrA-3′ steps. | true | true | true | true | true | 385 |
4 | DISCUSSION | 1 | 2 | [
"b2"
] | 17,164,285 | pmid-11250910 | Steric interference upon rA→rG substitution at position +1. | [
"2"
] | 59 | 2,236 | 0 | false | Steric interference upon rA→rG substitution at position +1. | [] | Steric interference upon rA→rG substitution at position +1. | true | true | true | true | true | 386 |
4 | DISCUSSION | 1 | 2 | [
"b2"
] | 17,164,285 | pmid-11250910 | Panels reflect changes to the RT–nucleic acid interface when A, G or I is present 1 nt 3′ of the scissile phosphate. | [
"2"
] | 116 | 2,237 | 0 | false | Panels reflect changes to the RT–nucleic acid interface when A, G or I is present 1 nt 3′ of the scissile phosphate. | [] | Panels reflect changes to the RT–nucleic acid interface when A, G or I is present 1 nt 3′ of the scissile phosphate. | true | true | true | true | true | 386 |
4 | DISCUSSION | 1 | 2 | [
"b2"
] | 17,164,285 | pmid-11250910 | R448 of the RNase H primer grip and the base at position +1 are shown in yellow. | [
"2"
] | 80 | 2,238 | 0 | false | R448 of the RNase H primer grip and the base at position +1 are shown in yellow. | [] | R448 of the RNase H primer grip and the base at position +1 are shown in yellow. | true | true | true | true | true | 386 |
4 | DISCUSSION | 1 | 2 | [
"b2"
] | 17,164,285 | pmid-11250910 | Space-filled atoms include the 2-H and 2-NH2 groups of A/I and G, respectively, as well as side-chain amine hydrogen of R448. | [
"2"
] | 125 | 2,239 | 0 | false | Space-filled atoms include the 2-H and 2-NH2 groups of A/I and G, respectively, as well as side-chain amine hydrogen of R448. | [] | Space-filled atoms include the 2-H and 2-NH2 groups of A/I and G, respectively, as well as side-chain amine hydrogen of R448. | true | true | true | true | true | 386 |
4 | DISCUSSION | 1 | 2 | [
"b2"
] | 17,164,285 | pmid-11250910 | Models are derived from the HIV-1 RT-PPT/DNA crystal structure (2), and nucleoside variants constructed using DS Viewer (Accelyrs, San Diego, CA). | [
"2"
] | 146 | 2,240 | 1 | false | Models are derived from the HIV-1 RT-PPT/DNA crystal structure, and nucleoside variants constructed using DS Viewer (Accelyrs, San Diego, CA). | [
"2"
] | Models are derived from the HIV-1 RT-PPT/DNA crystal structure, and nucleoside variants constructed using DS Viewer (Accelyrs, San Diego, CA). | true | true | true | true | true | 386 |
5 | DISCUSSION | 1 | 46 | [
"b46",
"b47",
"b48",
"b49",
"b48"
] | 17,164,285 | pmid-8554595|pmid-15788750|pmid-12717729|pmid-521211|pmid-12717729 | Although there appears to be no single structural feature to explain the effects of each analog substitution at position −4rG (Figure 6), it is clear that a 6-NH2-substituted purine is poorly tolerated at that position, as is the reversal in exocyclic group orientation resulting from rG→riG substitution. | [
"46",
"47",
"48",
"49",
"48"
] | 305 | 2,241 | 0 | false | Although there appears to be no single structural feature to explain the effects of each analog substitution at position −4rG (Figure 6), it is clear that a 6-NH2-substituted purine is poorly tolerated at that position, as is the reversal in exocyclic group orientation resulting from rG→riG substitution. | [] | Although there appears to be no single structural feature to explain the effects of each analog substitution at position −4rG, it is clear that a 6-NH2-substituted purine is poorly tolerated at that position, as is the reversal in exocyclic group orientation resulting from rG→riG substitution. | true | true | true | true | true | 387 |
5 | DISCUSSION | 1 | 46 | [
"b46",
"b47",
"b48",
"b49",
"b48"
] | 17,164,285 | pmid-8554595|pmid-15788750|pmid-12717729|pmid-521211|pmid-12717729 | Since no direct contact between HIV-1 RT and the RNA strand of an RNA–DNA hybrid is predicted to occur at PPT position −4 (relative to the scissile phosphate), local steric interference with RT-binding is an unlikely explanation for our observations. | [
"46",
"47",
"48",
"49",
"48"
] | 250 | 2,242 | 0 | false | Since no direct contact between HIV-1 RT and the RNA strand of an RNA–DNA hybrid is predicted to occur at PPT position −4 (relative to the scissile phosphate), local steric interference with RT-binding is an unlikely explanation for our observations. | [] | Since no direct contact between HIV-1 RT and the RNA strand of an RNA–DNA hybrid is predicted to occur at PPT position −4 (relative to the scissile phosphate), local steric interference with RT-binding is an unlikely explanation for our observations. | true | true | true | true | true | 387 |
5 | DISCUSSION | 1 | 46 | [
"b46",
"b47",
"b48",
"b49",
"b48"
] | 17,164,285 | pmid-8554595|pmid-15788750|pmid-12717729|pmid-521211|pmid-12717729 | However, it is possible that curvature of the helix is affected by substitution of an amino group for the 6-oxygen moiety of −4rG, which could indirectly affect the manner in which the duplex is contacted by HIV-1 RT. | [
"46",
"47",
"48",
"49",
"48"
] | 217 | 2,243 | 0 | false | However, it is possible that curvature of the helix is affected by substitution of an amino group for the 6-oxygen moiety of −4rG, which could indirectly affect the manner in which the duplex is contacted by HIV-1 RT. | [] | However, it is possible that curvature of the helix is affected by substitution of an amino group for the 6-oxygen moiety of −4rG, which could indirectly affect the manner in which the duplex is contacted by HIV-1 RT. | true | true | true | true | true | 387 |
5 | DISCUSSION | 1 | 48 | [
"b46",
"b47",
"b48",
"b49",
"b48"
] | 17,164,285 | pmid-8554595|pmid-15788750|pmid-12717729|pmid-521211|pmid-12717729 | This might manifest itself via electronic effects on base stacking (46,47), altered coordination of solvent cations (48), or perhaps most intriguingly, by direct electronic (or steric) interaction between/among exocyclic groups on adjacent purines. | [
"46",
"47",
"48",
"49",
"48"
] | 248 | 2,244 | 1 | false | This might manifest itself via electronic effects on base stacking, altered coordination of solvent cations, or perhaps most intriguingly, by direct electronic (or steric) interaction between/among exocyclic groups on adjacent purines. | [
"46,47",
"48"
] | This might manifest itself via electronic effects on base stacking, altered coordination of solvent cations, or perhaps most intriguingly, by direct electronic (or steric) interaction between/among exocyclic groups on adjacent purines. | true | true | true | true | true | 387 |
5 | DISCUSSION | 1 | 49 | [
"b46",
"b47",
"b48",
"b49",
"b48"
] | 17,164,285 | pmid-8554595|pmid-15788750|pmid-12717729|pmid-521211|pmid-12717729 | For example, within the interrupted A-tract of the HIV-1 PPT the interatomic distances between 6-NH2 nitrogens of adjacent purines are as little as 2.9 Å, suggesting the possibility of direct electronic interaction between bases (49). | [
"46",
"47",
"48",
"49",
"48"
] | 234 | 2,245 | 1 | false | For example, within the interrupted A-tract of the HIV-1 PPT the interatomic distances between 6-NH2 nitrogens of adjacent purines are as little as 2.9 Å, suggesting the possibility of direct electronic interaction between bases. | [
"49"
] | For example, within the interrupted A-tract of the HIV-1 PPT the interatomic distances between 6-NH2 nitrogens of adjacent purines are as little as 2.9 Å, suggesting the possibility of direct electronic interaction between bases. | true | true | true | true | true | 387 |
5 | DISCUSSION | 1 | 46 | [
"b46",
"b47",
"b48",
"b49",
"b48"
] | 17,164,285 | pmid-8554595|pmid-15788750|pmid-12717729|pmid-521211|pmid-12717729 | One could envision, therefore, that inserting an amino group into a string of adjacent 6-oxygen moieties within a G-tract could alter the trajectory of the helix. | [
"46",
"47",
"48",
"49",
"48"
] | 162 | 2,246 | 0 | false | One could envision, therefore, that inserting an amino group into a string of adjacent 6-oxygen moieties within a G-tract could alter the trajectory of the helix. | [] | One could envision, therefore, that inserting an amino group into a string of adjacent 6-oxygen moieties within a G-tract could alter the trajectory of the helix. | true | true | true | true | true | 387 |
5 | DISCUSSION | 1 | 48 | [
"b46",
"b47",
"b48",
"b49",
"b48"
] | 17,164,285 | pmid-8554595|pmid-15788750|pmid-12717729|pmid-521211|pmid-12717729 | This is particularly plausible since elements bonded at the purine 6-position comprise one wall of the helical major groove, which like the minor groove in dA:dT and rA:dT tracts, is compressed in homopolymeric dG:dC stretches (48). | [
"46",
"47",
"48",
"49",
"48"
] | 232 | 2,247 | 1 | false | This is particularly plausible since elements bonded at the purine 6-position comprise one wall of the helical major groove, which like the minor groove in dA:dT and rA:dT tracts, is compressed in homopolymeric dG:dC stretches. | [
"48"
] | This is particularly plausible since elements bonded at the purine 6-position comprise one wall of the helical major groove, which like the minor groove in dA:dT and rA:dT tracts, is compressed in homopolymeric dG:dC stretches. | true | true | true | true | true | 387 |
5 | DISCUSSION | 1 | 46 | [
"b46",
"b47",
"b48",
"b49",
"b48"
] | 17,164,285 | pmid-8554595|pmid-15788750|pmid-12717729|pmid-521211|pmid-12717729 | However, since a homopolymeric rG:dC tract has never been resolved by X-ray crystallography or NMR, the spatial relationship between 6-oxygen groups on adjacent purines in this context remains speculative. | [
"46",
"47",
"48",
"49",
"48"
] | 205 | 2,248 | 0 | false | However, since a homopolymeric rG:dC tract has never been resolved by X-ray crystallography or NMR, the spatial relationship between 6-oxygen groups on adjacent purines in this context remains speculative. | [] | However, since a homopolymeric rG:dC tract has never been resolved by X-ray crystallography or NMR, the spatial relationship between 6-oxygen groups on adjacent purines in this context remains speculative. | true | true | true | true | true | 387 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5",
"B6",
"B7"
] | 17,426,122 | pmid-12637589|pmid-8845856|pmid-4330040|pmid-15934135|NA|pmid-16081283|NA|pmid-15934135 | The biologically active form of vitamin D, 1α, 25-dihydroxyvitamin D3 (1α,25(OH)2D3)), is required for mineral homeostasis and skeletal integrity, as well as controlling cell growth and differentiation in several tissues (1). | [
"1",
"2",
"3",
"4",
"5",
"6",
"7"
] | 225 | 2,249 | 1 | false | The biologically active form of vitamin D, 1α, 25-dihydroxyvitamin D3 2D3)), is required for mineral homeostasis and skeletal integrity, as well as controlling cell growth and differentiation in several tissues. | [
"1α,25(OH",
"1"
] | The biologically active form of vitamin D, 1α, 25-dihydroxyvitamin D3 2D3)), is required for mineral homeostasis and skeletal integrity, as well as controlling cell growth and differentiation in several tissues. | true | true | true | true | true | 388 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5",
"B6",
"B7"
] | 17,426,122 | pmid-12637589|pmid-8845856|pmid-4330040|pmid-15934135|NA|pmid-16081283|NA|pmid-15934135 | In the body, the amount of 1α,25(OH)2D3 is tightly controlled by several enzymes that are transcribed from genes belonging to the cytochrome P450 (CYP) family. | [
"1",
"2",
"3",
"4",
"5",
"6",
"7"
] | 159 | 2,250 | 0 | false | In the body, the amount of 1α,25(OH)2D3 is tightly controlled by several enzymes that are transcribed from genes belonging to the cytochrome P450 (CYP) family. | [] | In the body, the amount of 1α,25(OH)2D3 is tightly controlled by several enzymes that are transcribed from genes belonging to the cytochrome P450 (CYP) family. | true | true | true | true | true | 388 |
0 | INTRODUCTION | 1 | 2 | [
"B1",
"B2",
"B3",
"B4",
"B5",
"B6",
"B7"
] | 17,426,122 | pmid-12637589|pmid-8845856|pmid-4330040|pmid-15934135|NA|pmid-16081283|NA|pmid-15934135 | This gene family encodes a wide variety of enzymes that are needed in the oxidative metabolism of a number of endogenous and exogenous compounds (2). | [
"1",
"2",
"3",
"4",
"5",
"6",
"7"
] | 149 | 2,251 | 1 | false | This gene family encodes a wide variety of enzymes that are needed in the oxidative metabolism of a number of endogenous and exogenous compounds. | [
"2"
] | This gene family encodes a wide variety of enzymes that are needed in the oxidative metabolism of a number of endogenous and exogenous compounds. | true | true | true | true | true | 388 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5",
"B6",
"B7"
] | 17,426,122 | pmid-12637589|pmid-8845856|pmid-4330040|pmid-15934135|NA|pmid-16081283|NA|pmid-15934135 | One of the enzymes needed in the metabolism of 1α,25(OH)2D3 is the protein product of the CYP27B1 gene, 25-hydroxyvitamin D3 (25(OH)D3) | [
"1",
"2",
"3",
"4",
"5",
"6",
"7"
] | 135 | 2,252 | 0 | false | One of the enzymes needed in the metabolism of 1α,25(OH)2D3 is the protein product of the CYP27B1 gene, 25-hydroxyvitamin D3 D3) | [
"25(OH"
] | One of the enzymes needed in the metabolism of 1α,25(OH)2D3 is the protein product of the CYP27B1 gene, 25-hydroxyvitamin D3 D3) | true | true | false | true | false | 388 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5",
"B6",
"B7"
] | 17,426,122 | pmid-12637589|pmid-8845856|pmid-4330040|pmid-15934135|NA|pmid-16081283|NA|pmid-15934135 | 1α -hydroxylase. | [
"1",
"2",
"3",
"4",
"5",
"6",
"7"
] | 16 | 2,253 | 0 | false | 1α -hydroxylase. | [] | 1α -hydroxylase. | false | false | true | true | false | 388 |
0 | INTRODUCTION | 1 | 3 | [
"B1",
"B2",
"B3",
"B4",
"B5",
"B6",
"B7"
] | 17,426,122 | pmid-12637589|pmid-8845856|pmid-4330040|pmid-15934135|NA|pmid-16081283|NA|pmid-15934135 | It has an important role in the synthesis of 1α,25(OH)2D3 because it catalyzes the metabolic activation of the main circulating form of vitamin D, 25(OH)D3, into 1α,25(OH)2D3 (3). | [
"1",
"2",
"3",
"4",
"5",
"6",
"7"
] | 179 | 2,254 | 1 | false | It has an important role in the synthesis of 1α,25(OH)2D3 because it catalyzes the metabolic activation of the main circulating form of vitamin D, 25(OH)D3, into 1α,25(OH)2D3. | [
"3"
] | It has an important role in the synthesis of 1α,25(OH)2D3 because it catalyzes the metabolic activation of the main circulating form of vitamin D, 25(OH)D3, into 1α,25(OH)2D3. | true | true | true | true | true | 388 |
0 | INTRODUCTION | 1 | 4 | [
"B1",
"B2",
"B3",
"B4",
"B5",
"B6",
"B7"
] | 17,426,122 | pmid-12637589|pmid-8845856|pmid-4330040|pmid-15934135|NA|pmid-16081283|NA|pmid-15934135 | CYP27B1 gene expression is negatively regulated by 1α,25(OH)2D3, and this has been proposed to occur via a negative vitamin D response element (nVDRE), located ∼500 bp upstream from transcription start site (TSS) (4). | [
"1",
"2",
"3",
"4",
"5",
"6",
"7"
] | 217 | 2,255 | 1 | false | CYP27B1 gene expression is negatively regulated by 1α,25(OH)2D3, and this has been proposed to occur via a negative vitamin D response element (nVDRE), located ∼500 bp upstream from transcription start site (TSS). | [
"4"
] | CYP27B1 gene expression is negatively regulated by 1α,25(OH)2D3, and this has been proposed to occur via a negative vitamin D response element (nVDRE), located ∼500 bp upstream from transcription start site (TSS). | true | true | true | true | true | 388 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5",
"B6",
"B7"
] | 17,426,122 | pmid-12637589|pmid-8845856|pmid-4330040|pmid-15934135|NA|pmid-16081283|NA|pmid-15934135 | The down-regulation of this gene by 1α,25(OH)2D3 is a cell-type and tissue-restricted phenomenon. | [
"1",
"2",
"3",
"4",
"5",
"6",
"7"
] | 97 | 2,256 | 0 | false | The down-regulation of this gene by 1α,25(OH)2D3 is a cell-type and tissue-restricted phenomenon. | [] | The down-regulation of this gene by 1α,25(OH)2D3 is a cell-type and tissue-restricted phenomenon. | true | true | true | true | true | 388 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5",
"B6",
"B7"
] | 17,426,122 | pmid-12637589|pmid-8845856|pmid-4330040|pmid-15934135|NA|pmid-16081283|NA|pmid-15934135 | In the body, the major expression site of the CYP27B1 gene and its protein product, 25(OH)D3 1α-hydroxylase (CYP27B1), is the kidney. | [
"1",
"2",
"3",
"4",
"5",
"6",
"7"
] | 133 | 2,257 | 0 | false | In the body, the major expression site of the CYP27B1 gene and its protein product, 25(OH)D3 1α-hydroxylase, is the kidney. | [
"CYP27B1"
] | In the body, the major expression site of the CYP27B1 gene and its protein product, 25(OH)D3 1α-hydroxylase, is the kidney. | true | true | true | true | true | 388 |
0 | INTRODUCTION | 1 | 5 | [
"B1",
"B2",
"B3",
"B4",
"B5",
"B6",
"B7"
] | 17,426,122 | pmid-12637589|pmid-8845856|pmid-4330040|pmid-15934135|NA|pmid-16081283|NA|pmid-15934135 | Within this organ, both the mRNA and the protein product have been observed to be repressed in the presence of 1α,25(OH)2D3 in the proximal tubules only (5). | [
"1",
"2",
"3",
"4",
"5",
"6",
"7"
] | 157 | 2,258 | 1 | false | Within this organ, both the mRNA and the protein product have been observed to be repressed in the presence of 1α,25(OH)2D3 in the proximal tubules only. | [
"5"
] | Within this organ, both the mRNA and the protein product have been observed to be repressed in the presence of 1α,25(OH)2D3 in the proximal tubules only. | true | true | true | true | true | 388 |
0 | INTRODUCTION | 1 | 6 | [
"B1",
"B2",
"B3",
"B4",
"B5",
"B6",
"B7"
] | 17,426,122 | pmid-12637589|pmid-8845856|pmid-4330040|pmid-15934135|NA|pmid-16081283|NA|pmid-15934135 | The CYP27B1 gene is also expressed in extra renal sites (6), however the suppression of the gene by 1α,25(OH)2D3 has been described only in a few other cell lines derived from other tissues, such as colon-derived cells (7). | [
"1",
"2",
"3",
"4",
"5",
"6",
"7"
] | 223 | 2,259 | 1 | false | The CYP27B1 gene is also expressed in extra renal sites, however the suppression of the gene by 1α,25(OH)2D3 has been described only in a few other cell lines derived from other tissues, such as colon-derived cells. | [
"6",
"7"
] | The CYP27B1 gene is also expressed in extra renal sites, however the suppression of the gene by 1α,25(OH)2D3 has been described only in a few other cell lines derived from other tissues, such as colon-derived cells. | true | true | true | true | true | 388 |
1 | INTRODUCTION | 1 | 8 | [
"B8",
"B9",
"B10 B11 B12",
"B4"
] | 17,426,122 | pmid-9673449|pmid-10677278|pmid-1325645|pmid-8776727|pmid-8663213|pmid-15934135|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | The effects of 1α,25(OH)2D3 are mediated via the vitamin D receptor (VDR), a member of the nuclear receptor superfamily, to which 1α,25(OH)2D3 binds with high affinity. | [
"8",
"9",
"10–12",
"4"
] | 168 | 2,260 | 0 | false | The effects of 1α,25(OH)2D3 are mediated via the vitamin D receptor (VDR), a member of the nuclear receptor superfamily, to which 1α,25(OH)2D3 binds with high affinity. | [] | The effects of 1α,25(OH)2D3 are mediated via the vitamin D receptor (VDR), a member of the nuclear receptor superfamily, to which 1α,25(OH)2D3 binds with high affinity. | true | true | true | true | true | 389 |
1 | INTRODUCTION | 1 | 8 | [
"B8",
"B9",
"B10 B11 B12",
"B4"
] | 17,426,122 | pmid-9673449|pmid-10677278|pmid-1325645|pmid-8776727|pmid-8663213|pmid-15934135|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | Responsiveness of a given gene to 1α,25(OH)2D3 requires that its regulatory regions contain a VDRE. | [
"8",
"9",
"10–12",
"4"
] | 99 | 2,261 | 0 | false | Responsiveness of a given gene to 1α,25(OH)2D3 requires that its regulatory regions contain a VDRE. | [] | Responsiveness of a given gene to 1α,25(OH)2D3 requires that its regulatory regions contain a VDRE. | true | true | true | true | true | 389 |
1 | INTRODUCTION | 1 | 8 | [
"B8",
"B9",
"B10 B11 B12",
"B4"
] | 17,426,122 | pmid-9673449|pmid-10677278|pmid-1325645|pmid-8776727|pmid-8663213|pmid-15934135|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | The VDREs of positively regulated genes are direct repeats of two hexameric-core-binding motifs spaced by 3 or 4 nt (DR3 or DR4, respectively) or everted repeats spaced by 6–9 nt (ER6 and ER9, respectively) (8,9). | [
"8",
"9",
"10–12",
"4"
] | 213 | 2,262 | 0 | false | The VDREs of positively regulated genes are direct repeats of two hexameric-core-binding motifs spaced by 3 or 4 nt or everted repeats spaced by 6–9 nt. | [
"DR3 or DR4, respectively",
"ER6 and ER9, respectively",
"8,9"
] | The VDREs of positively regulated genes are direct repeats of two hexameric-core-binding motifs spaced by 3 or 4 nt or everted repeats spaced by 6–9 nt. | true | true | true | true | true | 389 |
1 | INTRODUCTION | 1 | 8 | [
"B8",
"B9",
"B10 B11 B12",
"B4"
] | 17,426,122 | pmid-9673449|pmid-10677278|pmid-1325645|pmid-8776727|pmid-8663213|pmid-15934135|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | The hexameric sequences of the response elements of the primary 1α,25(OH)2D3 target genes usually have the consensus sequence RGKTSA (R = A or G, K = G or T, S = C or G). | [
"8",
"9",
"10–12",
"4"
] | 170 | 2,263 | 0 | false | The hexameric sequences of the response elements of the primary 1α,25(OH)2D3 target genes usually have the consensus sequence RGKTSA (R = A or G, K = G or T, S = C or G). | [] | The hexameric sequences of the response elements of the primary 1α,25(OH)2D3 target genes usually have the consensus sequence RGKTSA (R = A or G, K = G or T, S = C or G). | true | true | true | true | true | 389 |
1 | INTRODUCTION | 1 | 10–12 | [
"B8",
"B9",
"B10 B11 B12",
"B4"
] | 17,426,122 | pmid-9673449|pmid-10677278|pmid-1325645|pmid-8776727|pmid-8663213|pmid-15934135|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | The VDREs of most previously studied negatively regulated genes resemble those of positively regulated genes, although negative regulation may not necessarily require both VDRE half sites (10–12). | [
"8",
"9",
"10–12",
"4"
] | 196 | 2,264 | 1 | false | The VDREs of most previously studied negatively regulated genes resemble those of positively regulated genes, although negative regulation may not necessarily require both VDRE half sites. | [
"10–12"
] | The VDREs of most previously studied negatively regulated genes resemble those of positively regulated genes, although negative regulation may not necessarily require both VDRE half sites. | true | true | true | true | true | 389 |
1 | INTRODUCTION | 1 | 4 | [
"B8",
"B9",
"B10 B11 B12",
"B4"
] | 17,426,122 | pmid-9673449|pmid-10677278|pmid-1325645|pmid-8776727|pmid-8663213|pmid-15934135|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | The reported negative VDRE of the CYP27B1 is an exception, because it does not contain a consensus sequence (4). | [
"8",
"9",
"10–12",
"4"
] | 112 | 2,265 | 1 | false | The reported negative VDRE of the CYP27B1 is an exception, because it does not contain a consensus sequence. | [
"4"
] | The reported negative VDRE of the CYP27B1 is an exception, because it does not contain a consensus sequence. | true | true | true | true | true | 389 |
1 | INTRODUCTION | 1 | 8 | [
"B8",
"B9",
"B10 B11 B12",
"B4"
] | 17,426,122 | pmid-9673449|pmid-10677278|pmid-1325645|pmid-8776727|pmid-8663213|pmid-15934135|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | In addition, the authors proposed that the regulation of the CYP27B1 gene involves an indirect binding of VDR to DNA, where VDR associates with the nVDRE ligand-dependently via another transcription factor, the VDR interacting repressor (VDIR). | [
"8",
"9",
"10–12",
"4"
] | 244 | 2,266 | 0 | false | In addition, the authors proposed that the regulation of the CYP27B1 gene involves an indirect binding of VDR to DNA, where VDR associates with the nVDRE ligand-dependently via another transcription factor, the VDR interacting repressor (VDIR). | [] | In addition, the authors proposed that the regulation of the CYP27B1 gene involves an indirect binding of VDR to DNA, where VDR associates with the nVDRE ligand-dependently via another transcription factor, the VDR interacting repressor (VDIR). | true | true | true | true | true | 389 |
2 | INTRODUCTION | 1 | 13 | [
"B13",
"B14",
"B15",
"B16",
"B17",
"B18"
] | 17,426,122 | pmid-10322133|pmid-7566127|pmid-7566114|pmid-10877839|pmid-16094445|pmid-11559745|pmid-15934135|pmid-1325645|pmid-8776727|pmid-8663213 | Binding of 1α,25(OH)2D3 causes a conformational change within the ligand-binding domain of the VDR, which modulates its interactions with nuclear proteins, such as coactivator (CoA) and corepressor (CoR) proteins (13). | [
"13",
"14",
"15",
"16",
"17",
"18"
] | 218 | 2,267 | 1 | false | Binding of 1α,25(OH)2D3 causes a conformational change within the ligand-binding domain of the VDR, which modulates its interactions with nuclear proteins, such as coactivator (CoA) and corepressor (CoR) proteins. | [
"13"
] | Binding of 1α,25(OH)2D3 causes a conformational change within the ligand-binding domain of the VDR, which modulates its interactions with nuclear proteins, such as coactivator (CoA) and corepressor (CoR) proteins. | true | true | true | true | true | 390 |
2 | INTRODUCTION | 1 | 14 | [
"B13",
"B14",
"B15",
"B16",
"B17",
"B18"
] | 17,426,122 | pmid-10322133|pmid-7566127|pmid-7566114|pmid-10877839|pmid-16094445|pmid-11559745|pmid-15934135|pmid-1325645|pmid-8776727|pmid-8663213 | CoR proteins, such as NCoR1 (14) and SMRT/NCoR2 (15), link non-liganded, DNA-bound VDR to enzymes with histone deacetylase activity that cause chromatin condensation (16). | [
"13",
"14",
"15",
"16",
"17",
"18"
] | 171 | 2,268 | 1 | false | CoR proteins, such as NCoR1 and SMRT/NCoR2, link non-liganded, DNA-bound VDR to enzymes with histone deacetylase activity that cause chromatin condensation. | [
"14",
"15",
"16"
] | CoR proteins, such as NCoR1 and SMRT/NCoR2, link non-liganded, DNA-bound VDR to enzymes with histone deacetylase activity that cause chromatin condensation. | true | true | true | true | true | 390 |
2 | INTRODUCTION | 1 | 17 | [
"B13",
"B14",
"B15",
"B16",
"B17",
"B18"
] | 17,426,122 | pmid-10322133|pmid-7566127|pmid-7566114|pmid-10877839|pmid-16094445|pmid-11559745|pmid-15934135|pmid-1325645|pmid-8776727|pmid-8663213 | The conformational change within VDR’s ligand-binding domain results in the replacement of a CoR by a CoA protein of the p160 family, such as SRC-1, SRC-2 or SRC-3 (17). | [
"13",
"14",
"15",
"16",
"17",
"18"
] | 169 | 2,269 | 1 | false | The conformational change within VDR’s ligand-binding domain results in the replacement of a CoR by a CoA protein of the p160 family, such as SRC-1, SRC-2 or SRC-3. | [
"17"
] | The conformational change within VDR’s ligand-binding domain results in the replacement of a CoR by a CoA protein of the p160 family, such as SRC-1, SRC-2 or SRC-3. | true | true | true | true | true | 390 |
2 | INTRODUCTION | 1 | 18 | [
"B13",
"B14",
"B15",
"B16",
"B17",
"B18"
] | 17,426,122 | pmid-10322133|pmid-7566127|pmid-7566114|pmid-10877839|pmid-16094445|pmid-11559745|pmid-15934135|pmid-1325645|pmid-8776727|pmid-8663213 | These CoAs link the ligand-activated VDR to enzymes displaying histone acetyltransferase (HAT) activity, such as CBP, that cause chromatin relaxation by their action on histone tails and thereby reversing the action of unliganded VDR (18). | [
"13",
"14",
"15",
"16",
"17",
"18"
] | 239 | 2,270 | 1 | false | These CoAs link the ligand-activated VDR to enzymes displaying histone acetyltransferase (HAT) activity, such as CBP, that cause chromatin relaxation by their action on histone tails and thereby reversing the action of unliganded VDR. | [
"18"
] | These CoAs link the ligand-activated VDR to enzymes displaying histone acetyltransferase (HAT) activity, such as CBP, that cause chromatin relaxation by their action on histone tails and thereby reversing the action of unliganded VDR. | true | true | true | true | true | 390 |
3 | INTRODUCTION | 1 | 19–22 | [
"B19 B20 B21 B22",
"B23",
"B24",
"B25",
"B26",
"B4",
"B27 B28 B29"
] | 17,426,122 | pmid-7632726|pmid-8036172|pmid-8060315|pmid-7829502|pmid-15863722|pmid-15919092|pmid-16186133|pmid-16497728|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | Traditionally, VDREs are thought to locate relatively close to the TSS of 1α,25(OH)2D3 target genes. | [
"19–22",
"23",
"24",
"25",
"26",
"4",
"27–29"
] | 100 | 2,271 | 0 | false | Traditionally, VDREs are thought to locate relatively close to the TSS of 1α,25(OH)2D3 target genes. | [] | Traditionally, VDREs are thought to locate relatively close to the TSS of 1α,25(OH)2D3 target genes. | true | true | true | true | true | 391 |
3 | INTRODUCTION | 1 | 19–22 | [
"B19 B20 B21 B22",
"B23",
"B24",
"B25",
"B26",
"B4",
"B27 B28 B29"
] | 17,426,122 | pmid-7632726|pmid-8036172|pmid-8060315|pmid-7829502|pmid-15863722|pmid-15919092|pmid-16186133|pmid-16497728|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | For example, both human and rat vitamin D 24-hydroxylase (CYP24) genes have a cluster of VDREs in their proximal promoters (approximate position −140 to −300) (19–22). | [
"19–22",
"23",
"24",
"25",
"26",
"4",
"27–29"
] | 167 | 2,272 | 1 | false | For example, both human and rat vitamin D 24-hydroxylase genes have a cluster of VDREs in their proximal promoters. | [
"CYP24",
"approximate position −140 to −300",
"19–22"
] | For example, both human and rat vitamin D 24-hydroxylase genes have a cluster of VDREs in their proximal promoters. | true | true | true | true | true | 391 |
3 | INTRODUCTION | 1 | 19–22 | [
"B19 B20 B21 B22",
"B23",
"B24",
"B25",
"B26",
"B4",
"B27 B28 B29"
] | 17,426,122 | pmid-7632726|pmid-8036172|pmid-8060315|pmid-7829502|pmid-15863722|pmid-15919092|pmid-16186133|pmid-16497728|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | However, recently several promoter studies have revealed that the gene promoters may contain multiple response elements that locate not only within proximal promoters but also in more distal regions (23,24) and even within coding regions (25,26). | [
"19–22",
"23",
"24",
"25",
"26",
"4",
"27–29"
] | 246 | 2,273 | 0 | false | However, recently several promoter studies have revealed that the gene promoters may contain multiple response elements that locate not only within proximal promoters but also in more distal regions and even within coding regions. | [
"23,24",
"25,26"
] | However, recently several promoter studies have revealed that the gene promoters may contain multiple response elements that locate not only within proximal promoters but also in more distal regions and even within coding regions. | true | true | true | true | true | 391 |
3 | INTRODUCTION | 1 | 19–22 | [
"B19 B20 B21 B22",
"B23",
"B24",
"B25",
"B26",
"B4",
"B27 B28 B29"
] | 17,426,122 | pmid-7632726|pmid-8036172|pmid-8060315|pmid-7829502|pmid-15863722|pmid-15919092|pmid-16186133|pmid-16497728|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | These studies have so far concerned with only positively regulated genes. | [
"19–22",
"23",
"24",
"25",
"26",
"4",
"27–29"
] | 73 | 2,274 | 0 | false | These studies have so far concerned with only positively regulated genes. | [] | These studies have so far concerned with only positively regulated genes. | true | true | true | true | true | 391 |
3 | INTRODUCTION | 1 | 19–22 | [
"B19 B20 B21 B22",
"B23",
"B24",
"B25",
"B26",
"B4",
"B27 B28 B29"
] | 17,426,122 | pmid-7632726|pmid-8036172|pmid-8060315|pmid-7829502|pmid-15863722|pmid-15919092|pmid-16186133|pmid-16497728|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | This raises a question, whether negatively regulated genes also have multiple response elements. | [
"19–22",
"23",
"24",
"25",
"26",
"4",
"27–29"
] | 96 | 2,275 | 0 | false | This raises a question, whether negatively regulated genes also have multiple response elements. | [] | This raises a question, whether negatively regulated genes also have multiple response elements. | true | true | true | true | true | 391 |
3 | INTRODUCTION | 1 | 19–22 | [
"B19 B20 B21 B22",
"B23",
"B24",
"B25",
"B26",
"B4",
"B27 B28 B29"
] | 17,426,122 | pmid-7632726|pmid-8036172|pmid-8060315|pmid-7829502|pmid-15863722|pmid-15919092|pmid-16186133|pmid-16497728|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | Since the promoter studies of the human CYP27B1 gene have so far been limited to the first 1.7 kb upstream of the TSS (4,27–29), in this study, we have extended the promoter analysis further upstream and examined the role of distal promoter regions to the regulation of the human CYP27B1 gene by 1α,25(OH)2D3. | [
"19–22",
"23",
"24",
"25",
"26",
"4",
"27–29"
] | 309 | 2,276 | 0 | false | Since the promoter studies of the human CYP27B1 gene have so far been limited to the first 1.7 kb upstream of the TSS, in this study, we have extended the promoter analysis further upstream and examined the role of distal promoter regions to the regulation of the human CYP27B1 gene by 1α,25(OH)2D3. | [
"4,27–29"
] | Since the promoter studies of the human CYP27B1 gene have so far been limited to the first 1.7 kb upstream of the TSS, in this study, we have extended the promoter analysis further upstream and examined the role of distal promoter regions to the regulation of the human CYP27B1 gene by 1α,25(OH)2D3. | true | true | true | true | true | 391 |
3 | INTRODUCTION | 1 | 19–22 | [
"B19 B20 B21 B22",
"B23",
"B24",
"B25",
"B26",
"B4",
"B27 B28 B29"
] | 17,426,122 | pmid-7632726|pmid-8036172|pmid-8060315|pmid-7829502|pmid-15863722|pmid-15919092|pmid-16186133|pmid-16497728|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | We analyzed 13 contiguous genomic regions spanning 5.4 kb of the CYP27B1 promoter by chromatin immunoprecipitation (ChIP) scanning. | [
"19–22",
"23",
"24",
"25",
"26",
"4",
"27–29"
] | 131 | 2,277 | 0 | false | We analyzed 13 contiguous genomic regions spanning 5.4 kb of the CYP27B1 promoter by chromatin immunoprecipitation (ChIP) scanning. | [] | We analyzed 13 contiguous genomic regions spanning 5.4 kb of the CYP27B1 promoter by chromatin immunoprecipitation (ChIP) scanning. | true | true | true | true | true | 391 |
3 | INTRODUCTION | 1 | 19–22 | [
"B19 B20 B21 B22",
"B23",
"B24",
"B25",
"B26",
"B4",
"B27 B28 B29"
] | 17,426,122 | pmid-7632726|pmid-8036172|pmid-8060315|pmid-7829502|pmid-15863722|pmid-15919092|pmid-16186133|pmid-16497728|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | Our studies revealed two new 1α,25(OH)2D3-responsive regions in the distal promoter 2.6 and 3.2 kb upstream from the TSS. | [
"19–22",
"23",
"24",
"25",
"26",
"4",
"27–29"
] | 121 | 2,278 | 0 | false | Our studies revealed two new 1α,25(OH)2D3-responsive regions in the distal promoter 2.6 and 3.2 kb upstream from the TSS. | [] | Our studies revealed two new 1α,25(OH)2D3-responsive regions in the distal promoter 2.6 and 3.2 kb upstream from the TSS. | true | true | true | true | true | 391 |
3 | INTRODUCTION | 1 | 19–22 | [
"B19 B20 B21 B22",
"B23",
"B24",
"B25",
"B26",
"B4",
"B27 B28 B29"
] | 17,426,122 | pmid-7632726|pmid-8036172|pmid-8060315|pmid-7829502|pmid-15863722|pmid-15919092|pmid-16186133|pmid-16497728|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | Interestingly, in contrast to the nVDRE-containing region, in silico screening revealed that both of the new 1α,25(OH)2D3-responsive regions contained classical VDRE sequences that were shown to directly bind VDR–retinoid X receptor (RXR) heterodimers in a ligand-dependent manner, when studied by gel shift assays. | [
"19–22",
"23",
"24",
"25",
"26",
"4",
"27–29"
] | 315 | 2,279 | 0 | false | Interestingly, in contrast to the nVDRE-containing region, in silico screening revealed that both of the new 1α,25(OH)2D3-responsive regions contained classical VDRE sequences that were shown to directly bind VDR–retinoid X receptor (RXR) heterodimers in a ligand-dependent manner, when studied by gel shift assays. | [] | Interestingly, in contrast to the nVDRE-containing region, in silico screening revealed that both of the new 1α,25(OH)2D3-responsive regions contained classical VDRE sequences that were shown to directly bind VDR–retinoid X receptor (RXR) heterodimers in a ligand-dependent manner, when studied by gel shift assays. | true | true | true | true | true | 391 |
3 | INTRODUCTION | 1 | 19–22 | [
"B19 B20 B21 B22",
"B23",
"B24",
"B25",
"B26",
"B4",
"B27 B28 B29"
] | 17,426,122 | pmid-7632726|pmid-8036172|pmid-8060315|pmid-7829502|pmid-15863722|pmid-15919092|pmid-16186133|pmid-16497728|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | Extensive ChIP analysis suggested that the new regions have a number of similarities with the established nVDRE in the recruitment of different cofactors, as well as recruiting both VDR and RXR, supporting the idea that the putative VDREs are functional. | [
"19–22",
"23",
"24",
"25",
"26",
"4",
"27–29"
] | 254 | 2,280 | 0 | false | Extensive ChIP analysis suggested that the new regions have a number of similarities with the established nVDRE in the recruitment of different cofactors, as well as recruiting both VDR and RXR, supporting the idea that the putative VDREs are functional. | [] | Extensive ChIP analysis suggested that the new regions have a number of similarities with the established nVDRE in the recruitment of different cofactors, as well as recruiting both VDR and RXR, supporting the idea that the putative VDREs are functional. | true | true | true | true | true | 391 |
3 | INTRODUCTION | 1 | 19–22 | [
"B19 B20 B21 B22",
"B23",
"B24",
"B25",
"B26",
"B4",
"B27 B28 B29"
] | 17,426,122 | pmid-7632726|pmid-8036172|pmid-8060315|pmid-7829502|pmid-15863722|pmid-15919092|pmid-16186133|pmid-16497728|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | In addition, chromatin conformation capture (3C) analysis suggested that the new regions are directly connected with the TSS via chromatin looping in a ligand-dependent and cell-specific manner. | [
"19–22",
"23",
"24",
"25",
"26",
"4",
"27–29"
] | 194 | 2,281 | 0 | false | In addition, chromatin conformation capture (3C) analysis suggested that the new regions are directly connected with the TSS via chromatin looping in a ligand-dependent and cell-specific manner. | [] | In addition, chromatin conformation capture (3C) analysis suggested that the new regions are directly connected with the TSS via chromatin looping in a ligand-dependent and cell-specific manner. | true | true | true | true | true | 391 |
0 | DISCUSSION | 1 | 4 | [
"B4"
] | 17,426,122 | pmid-12637589|pmid-8845856|pmid-4330040|pmid-15934135|NA|pmid-16081283|NA|pmid-15934135 | The mechanism of negative gene regulation by nuclear receptors is still poorly understood, but the human CYP27B1 gene and its down-regulation in the presence of 1α,25(OH)2D3 may be so far the most detailed model (4). | [
"4"
] | 216 | 2,282 | 1 | false | The mechanism of negative gene regulation by nuclear receptors is still poorly understood, but the human CYP27B1 gene and its down-regulation in the presence of 1α,25(OH)2D3 may be so far the most detailed model. | [
"4"
] | The mechanism of negative gene regulation by nuclear receptors is still poorly understood, but the human CYP27B1 gene and its down-regulation in the presence of 1α,25(OH)2D3 may be so far the most detailed model. | true | true | true | true | true | 392 |
0 | DISCUSSION | 1 | 4 | [
"B4"
] | 17,426,122 | pmid-12637589|pmid-8845856|pmid-4330040|pmid-15934135|NA|pmid-16081283|NA|pmid-15934135 | Since the model takes account only the proximal promoter of the CYP27B1 gene, we aimed in this study to test the hypothesis that also in the case of gene repression multiple response elements located in more distal regions may be involved in the regulation. | [
"4"
] | 257 | 2,283 | 0 | false | Since the model takes account only the proximal promoter of the CYP27B1 gene, we aimed in this study to test the hypothesis that also in the case of gene repression multiple response elements located in more distal regions may be involved in the regulation. | [] | Since the model takes account only the proximal promoter of the CYP27B1 gene, we aimed in this study to test the hypothesis that also in the case of gene repression multiple response elements located in more distal regions may be involved in the regulation. | true | true | true | true | true | 392 |
1 | DISCUSSION | 1 | 4 | [
"B4",
"B27 B28 B29"
] | 17,426,122 | pmid-9673449|pmid-10677278|pmid-1325645|pmid-8776727|pmid-8663213|pmid-15934135|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | The distance between the TSSs of the neighboring genes CYP27B1 and METTL1 is only 5.4 kb (Figure 2A), with the METTL1 gene being read in the same direction as CYP27B1 (its last exon ends only 1.2 kb upstream of the TSS of the CYP27B1gene). | [
"4",
"27–29"
] | 239 | 2,284 | 0 | false | The distance between the TSSs of the neighboring genes CYP27B1 and METTL1 is only 5.4 kb (Figure 2A), with the METTL1 gene being read in the same direction as CYP27B1 (its last exon ends only 1.2 kb upstream of the TSS of the CYP27B1gene). | [] | The distance between the TSSs of the neighboring genes CYP27B1 and METTL1 is only 5.4 kb (Figure 2A), with the METTL1 gene being read in the same direction as CYP27B1 (its last exon ends only 1.2 kb upstream of the TSS of the CYP27B1gene). | true | true | true | true | true | 393 |
1 | DISCUSSION | 1 | 4 | [
"B4",
"B27 B28 B29"
] | 17,426,122 | pmid-9673449|pmid-10677278|pmid-1325645|pmid-8776727|pmid-8663213|pmid-15934135|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | Thus, the promoter of CYP27B1 seems to be only 1.2 kb in size. | [
"4",
"27–29"
] | 62 | 2,285 | 0 | false | Thus, the promoter of CYP27B1 seems to be only 1.2 kb in size. | [] | Thus, the promoter of CYP27B1 seems to be only 1.2 kb in size. | true | true | true | true | true | 393 |
1 | DISCUSSION | 1 | 4 | [
"B4",
"B27 B28 B29"
] | 17,426,122 | pmid-9673449|pmid-10677278|pmid-1325645|pmid-8776727|pmid-8663213|pmid-15934135|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | Indeed, the studies of human and mouse CYP27B1 promoters have so far considered only the first 1.7 kb upstream from the TSS of CYP27B1 (4,27–29). | [
"4",
"27–29"
] | 145 | 2,286 | 0 | false | Indeed, the studies of human and mouse CYP27B1 promoters have so far considered only the first 1.7 kb upstream from the TSS of CYP27B1. | [
"4,27–29"
] | Indeed, the studies of human and mouse CYP27B1 promoters have so far considered only the first 1.7 kb upstream from the TSS of CYP27B1. | true | true | true | true | true | 393 |
1 | DISCUSSION | 1 | 4 | [
"B4",
"B27 B28 B29"
] | 17,426,122 | pmid-9673449|pmid-10677278|pmid-1325645|pmid-8776727|pmid-8663213|pmid-15934135|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | Therefore, it is interesting that the combined results of our in silico screening and promoter ChIP scanning suggested that within the studied CYP27B1 promoter region, two additional VDREs, located in regions 7 and 9 (being within introns of the METTL1 gene) upstream from region 2 carrying the nVDRE. | [
"4",
"27–29"
] | 301 | 2,287 | 0 | false | Therefore, it is interesting that the combined results of our in silico screening and promoter ChIP scanning suggested that within the studied CYP27B1 promoter region, two additional VDREs, located in regions 7 and 9 (being within introns of the METTL1 gene) upstream from region 2 carrying the nVDRE. | [] | Therefore, it is interesting that the combined results of our in silico screening and promoter ChIP scanning suggested that within the studied CYP27B1 promoter region, two additional VDREs, located in regions 7 and 9 (being within introns of the METTL1 gene) upstream from region 2 carrying the nVDRE. | true | true | true | true | true | 393 |
1 | DISCUSSION | 1 | 4 | [
"B4",
"B27 B28 B29"
] | 17,426,122 | pmid-9673449|pmid-10677278|pmid-1325645|pmid-8776727|pmid-8663213|pmid-15934135|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | According to our ChIP scanning of the CYP27B1 promoter, the time-dependent binding profile of VDR was similar both in MCF-7 cells and HEK-293 cells with one exception. | [
"4",
"27–29"
] | 167 | 2,288 | 0 | false | According to our ChIP scanning of the CYP27B1 promoter, the time-dependent binding profile of VDR was similar both in MCF-7 cells and HEK-293 cells with one exception. | [] | According to our ChIP scanning of the CYP27B1 promoter, the time-dependent binding profile of VDR was similar both in MCF-7 cells and HEK-293 cells with one exception. | true | true | true | true | true | 393 |
1 | DISCUSSION | 1 | 4 | [
"B4",
"B27 B28 B29"
] | 17,426,122 | pmid-9673449|pmid-10677278|pmid-1325645|pmid-8776727|pmid-8663213|pmid-15934135|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | In HEK-293 cells, the VDR seemed to associate with the described CYP27B1 gene TSS stronger than in MCF-7 cells (Figure 2). | [
"4",
"27–29"
] | 122 | 2,289 | 0 | false | In HEK-293 cells, the VDR seemed to associate with the described CYP27B1 gene TSS stronger than in MCF-7 cells (Figure 2). | [] | In HEK-293 cells, the VDR seemed to associate with the described CYP27B1 gene TSS stronger than in MCF-7 cells (Figure 2). | true | true | true | true | true | 393 |
1 | DISCUSSION | 1 | 4 | [
"B4",
"B27 B28 B29"
] | 17,426,122 | pmid-9673449|pmid-10677278|pmid-1325645|pmid-8776727|pmid-8663213|pmid-15934135|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | Since region 1 possesses neither an nVDRE nor a regular VDRE, this may suggest that the protein bridge exists between the VDR-binding regions and the TSS in HEK-293, but not in MCF-7 cells. | [
"4",
"27–29"
] | 189 | 2,290 | 0 | false | Since region 1 possesses neither an nVDRE nor a regular VDRE, this may suggest that the protein bridge exists between the VDR-binding regions and the TSS in HEK-293, but not in MCF-7 cells. | [] | Since region 1 possesses neither an nVDRE nor a regular VDRE, this may suggest that the protein bridge exists between the VDR-binding regions and the TSS in HEK-293, but not in MCF-7 cells. | true | true | true | true | true | 393 |
2 | DISCUSSION | 1 | 4 | [
"B4",
"B10 B11 B12"
] | 17,426,122 | pmid-10322133|pmid-7566127|pmid-7566114|pmid-10877839|pmid-16094445|pmid-11559745|pmid-15934135|pmid-1325645|pmid-8776727|pmid-8663213 | According to Murayama and colleagues (4), the association of the VDR–RXR heterodimer to the nVDRE is not a direct binding to DNA, but occurs via the transcription factor VDIR. | [
"4",
"10–12"
] | 175 | 2,291 | 1 | false | According to Murayama and colleagues, the association of the VDR–RXR heterodimer to the nVDRE is not a direct binding to DNA, but occurs via the transcription factor VDIR. | [
"4"
] | According to Murayama and colleagues, the association of the VDR–RXR heterodimer to the nVDRE is not a direct binding to DNA, but occurs via the transcription factor VDIR. | true | true | true | true | true | 394 |
2 | DISCUSSION | 1 | 4 | [
"B4",
"B10 B11 B12"
] | 17,426,122 | pmid-10322133|pmid-7566127|pmid-7566114|pmid-10877839|pmid-16094445|pmid-11559745|pmid-15934135|pmid-1325645|pmid-8776727|pmid-8663213 | We found that in vitro-translated VDR–RXR heterodimers cannot bind to the nVDRE although in vitro-translated VDIR can (Figure 3). | [
"4",
"10–12"
] | 129 | 2,292 | 0 | false | We found that in vitro-translated VDR–RXR heterodimers cannot bind to the nVDRE although in vitro-translated VDIR can (Figure 3). | [] | We found that in vitro-translated VDR–RXR heterodimers cannot bind to the nVDRE although in vitro-translated VDIR can (Figure 3). | true | true | true | true | true | 394 |
2 | DISCUSSION | 1 | 4 | [
"B4",
"B10 B11 B12"
] | 17,426,122 | pmid-10322133|pmid-7566127|pmid-7566114|pmid-10877839|pmid-16094445|pmid-11559745|pmid-15934135|pmid-1325645|pmid-8776727|pmid-8663213 | Interestingly, with the distal VDREs, reasonable VDR–RXR heterodimer association could be observed with VDRE1 and VDRE2 from regions 7 and 9, respectively. | [
"4",
"10–12"
] | 155 | 2,293 | 0 | false | Interestingly, with the distal VDREs, reasonable VDR–RXR heterodimer association could be observed with VDRE1 and VDRE2 from regions 7 and 9, respectively. | [] | Interestingly, with the distal VDREs, reasonable VDR–RXR heterodimer association could be observed with VDRE1 and VDRE2 from regions 7 and 9, respectively. | true | true | true | true | true | 394 |
2 | DISCUSSION | 1 | 4 | [
"B4",
"B10 B11 B12"
] | 17,426,122 | pmid-10322133|pmid-7566127|pmid-7566114|pmid-10877839|pmid-16094445|pmid-11559745|pmid-15934135|pmid-1325645|pmid-8776727|pmid-8663213 | This did not apply to the neighboring VDRE3, suggesting that VDR is associated only with VDRE2 within region 9. | [
"4",
"10–12"
] | 111 | 2,294 | 0 | false | This did not apply to the neighboring VDRE3, suggesting that VDR is associated only with VDRE2 within region 9. | [] | This did not apply to the neighboring VDRE3, suggesting that VDR is associated only with VDRE2 within region 9. | true | true | true | true | true | 394 |
2 | DISCUSSION | 1 | 4 | [
"B4",
"B10 B11 B12"
] | 17,426,122 | pmid-10322133|pmid-7566127|pmid-7566114|pmid-10877839|pmid-16094445|pmid-11559745|pmid-15934135|pmid-1325645|pmid-8776727|pmid-8663213 | The binding of the VDR–RXR complex to VDRE1 and VDRE2 was ligand dependent, but contrary to that of nVDRE, the binding may involve direct interactions with DNA sequences. | [
"4",
"10–12"
] | 170 | 2,295 | 0 | false | The binding of the VDR–RXR complex to VDRE1 and VDRE2 was ligand dependent, but contrary to that of nVDRE, the binding may involve direct interactions with DNA sequences. | [] | The binding of the VDR–RXR complex to VDRE1 and VDRE2 was ligand dependent, but contrary to that of nVDRE, the binding may involve direct interactions with DNA sequences. | true | true | true | true | true | 394 |
2 | DISCUSSION | 1 | 10–12 | [
"B4",
"B10 B11 B12"
] | 17,426,122 | pmid-10322133|pmid-7566127|pmid-7566114|pmid-10877839|pmid-16094445|pmid-11559745|pmid-15934135|pmid-1325645|pmid-8776727|pmid-8663213 | Therefore, the new distal VDREs resemble positive VDREs, as has been previously described for most of the negative VDREs identified so far (10–12). | [
"4",
"10–12"
] | 147 | 2,296 | 1 | false | Therefore, the new distal VDREs resemble positive VDREs, as has been previously described for most of the negative VDREs identified so far. | [
"10–12"
] | Therefore, the new distal VDREs resemble positive VDREs, as has been previously described for most of the negative VDREs identified so far. | true | true | true | true | true | 394 |
3 | DISCUSSION | 0 | null | null | 17,426,122 | pmid-7632726|pmid-8036172|pmid-8060315|pmid-7829502|pmid-15863722|pmid-15919092|pmid-16186133|pmid-16497728|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | A reporter gene analysis of different CYP27B1 promoter fragments (Figure 4) showed that both the regions containing the nVDRE and VDRE2/3 were able to repress gene activity in HEK-293 cells, but not in MCF-7 cells. | null | 214 | 2,297 | 0 | false | null | null | A reporter gene analysis of different CYP27B1 promoter fragments (Figure 4) showed that both the regions containing the nVDRE and VDRE2/3 were able to repress gene activity in HEK-293 cells, but not in MCF-7 cells. | true | true | true | true | true | 395 |
3 | DISCUSSION | 0 | null | null | 17,426,122 | pmid-7632726|pmid-8036172|pmid-8060315|pmid-7829502|pmid-15863722|pmid-15919092|pmid-16186133|pmid-16497728|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | In addition, a longer promoter fragment including both the nVDRE and VDRE2/3, an even more significant repression was achieved. | null | 127 | 2,298 | 0 | false | null | null | In addition, a longer promoter fragment including both the nVDRE and VDRE2/3, an even more significant repression was achieved. | true | true | true | true | true | 395 |
3 | DISCUSSION | 0 | null | null | 17,426,122 | pmid-7632726|pmid-8036172|pmid-8060315|pmid-7829502|pmid-15863722|pmid-15919092|pmid-16186133|pmid-16497728|pmid-15934135|pmid-15691891|pmid-15243130|pmid-9465024 | Therefore, our results suggest that both nVDRE and VDRE2/3 are efficient negative regulators of the CYP27B1 promoter and work in HEK-293 cells together in the repression of CYP27B1 gene expression. | null | 197 | 2,299 | 0 | false | null | null | Therefore, our results suggest that both nVDRE and VDRE2/3 are efficient negative regulators of the CYP27B1 promoter and work in HEK-293 cells together in the repression of CYP27B1 gene expression. | true | true | true | true | true | 395 |
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