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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
4 | DISCUSSION | 0 | null | null | 17,202,157 | null | Inhibition of DNA methylation by AZAdC results in modest activation of CAII expression as compared to hormone-induced activation (Figure 7A). | null | 141 | 1,500 | 0 | false | null | null | Inhibition of DNA methylation by AZAdC results in modest activation of CAII expression as compared to hormone-induced activation (Figure 7A). | true | true | true | true | true | 255 |
4 | DISCUSSION | 0 | null | null | 17,202,157 | null | Although a significant decrease in CpG methylation is induced at the upstream part of the CpG island (Figure 6D), AZAdC treatment does not cause a positional change of the active histone marks. | null | 193 | 1,501 | 0 | false | null | null | Although a significant decrease in CpG methylation is induced at the upstream part of the CpG island (Figure 6D), AZAdC treatment does not cause a positional change of the active histone marks. | true | true | true | true | true | 255 |
4 | DISCUSSION | 0 | null | null | 17,202,157 | null | Instead, a moderate local increase in H3K9 acetylation and H3K4 tri-methylation is evident. | null | 91 | 1,502 | 0 | false | null | null | Instead, a moderate local increase in H3K9 acetylation and H3K4 tri-methylation is evident. | true | true | true | true | true | 255 |
4 | DISCUSSION | 0 | null | null | 17,202,157 | null | The increase in H3K9 acetylation could be the result of the dislodgement of MeCP2-complexed HDACs immediately upstream from the active histone marks. | null | 149 | 1,503 | 0 | false | null | null | The increase in H3K9 acetylation could be the result of the dislodgement of MeCP2-complexed HDACs immediately upstream from the active histone marks. | true | true | true | true | true | 255 |
4 | DISCUSSION | 0 | null | null | 17,202,157 | null | Intrusion of the active epigenetic code into the distal part of the CpG island does not occur, reinforcing the notion of the presence of a boundary or an activity that targets and maintains the active histone marks to a particular position. | null | 240 | 1,504 | 0 | false | null | null | Intrusion of the active epigenetic code into the distal part of the CpG island does not occur, reinforcing the notion of the presence of a boundary or an activity that targets and maintains the active histone marks to a particular position. | true | true | true | true | true | 255 |
5 | DISCUSSION | 1 | 12 | [
"b12",
"b30"
] | 17,202,157 | pmid-11782440|pmid-14716017 | In the T2EC erythrocytic progenitor cells the CAII gene is transcribed, the active histone marks are associated with the CAII promoter, but DNA methylation is absent. | [
"12",
"30"
] | 166 | 1,505 | 0 | false | In the T2EC erythrocytic progenitor cells the CAII gene is transcribed, the active histone marks are associated with the CAII promoter, but DNA methylation is absent. | [] | In the T2EC erythrocytic progenitor cells the CAII gene is transcribed, the active histone marks are associated with the CAII promoter, but DNA methylation is absent. | true | true | true | true | true | 256 |
5 | DISCUSSION | 1 | 12 | [
"b12",
"b30"
] | 17,202,157 | pmid-11782440|pmid-14716017 | DNA methylation has apparently occurred later during differentiation, although it is currently unclear whether this also occurs in the animal or whether DNA methylation is due to AEV-induced transformation and/or culturing. | [
"12",
"30"
] | 223 | 1,506 | 0 | false | DNA methylation has apparently occurred later during differentiation, although it is currently unclear whether this also occurs in the animal or whether DNA methylation is due to AEV-induced transformation and/or culturing. | [] | DNA methylation has apparently occurred later during differentiation, although it is currently unclear whether this also occurs in the animal or whether DNA methylation is due to AEV-induced transformation and/or culturing. | true | true | true | true | true | 256 |
5 | DISCUSSION | 1 | 12 | [
"b12",
"b30"
] | 17,202,157 | pmid-11782440|pmid-14716017 | DNA methylation has been postulated to be a secondary event that occurs after initial silencing events involving other mechanisms (12). | [
"12",
"30"
] | 135 | 1,507 | 1 | false | DNA methylation has been postulated to be a secondary event that occurs after initial silencing events involving other mechanisms. | [
"12"
] | DNA methylation has been postulated to be a secondary event that occurs after initial silencing events involving other mechanisms. | true | true | true | true | true | 256 |
5 | DISCUSSION | 1 | 12 | [
"b12",
"b30"
] | 17,202,157 | pmid-11782440|pmid-14716017 | A possible scenario for CAII repression would involve the initial AEV-mediated delivery of a dominant negative v-ErbA that is not responsive to T3. | [
"12",
"30"
] | 147 | 1,508 | 0 | false | A possible scenario for CAII repression would involve the initial AEV-mediated delivery of a dominant negative v-ErbA that is not responsive to T3. | [] | A possible scenario for CAII repression would involve the initial AEV-mediated delivery of a dominant negative v-ErbA that is not responsive to T3. | true | true | true | true | true | 256 |
5 | DISCUSSION | 1 | 12 | [
"b12",
"b30"
] | 17,202,157 | pmid-11782440|pmid-14716017 | Although this subsequently repressed transcription by inhibiting PIC assembly, it did not lead to histone deacetylation at the promoter. | [
"12",
"30"
] | 136 | 1,509 | 0 | false | Although this subsequently repressed transcription by inhibiting PIC assembly, it did not lead to histone deacetylation at the promoter. | [] | Although this subsequently repressed transcription by inhibiting PIC assembly, it did not lead to histone deacetylation at the promoter. | true | true | true | true | true | 256 |
5 | DISCUSSION | 1 | 12 | [
"b12",
"b30"
] | 17,202,157 | pmid-11782440|pmid-14716017 | Subsequently, DNA methylation evoked by this repressed state could have progressed towards the CAII promoter, but halted because of the presence of a putative boundary which may involve the active histone marks in addition to other factors. | [
"12",
"30"
] | 240 | 1,510 | 0 | false | Subsequently, DNA methylation evoked by this repressed state could have progressed towards the CAII promoter, but halted because of the presence of a putative boundary which may involve the active histone marks in addition to other factors. | [] | Subsequently, DNA methylation evoked by this repressed state could have progressed towards the CAII promoter, but halted because of the presence of a putative boundary which may involve the active histone marks in addition to other factors. | true | true | true | true | true | 256 |
5 | DISCUSSION | 1 | 30 | [
"b12",
"b30"
] | 17,202,157 | pmid-11782440|pmid-14716017 | Such factors may include CTCF, which has been shown to protect DNA against de novo DNA methylation during imprinting (30), and the combinatorial presence of CTCF and active histone modifications hints to the possibility that they establish a chromatin state that does not permit DNA methylation to spread. | [
"12",
"30"
] | 305 | 1,511 | 1 | false | Such factors may include CTCF, which has been shown to protect DNA against de novo DNA methylation during imprinting, and the combinatorial presence of CTCF and active histone modifications hints to the possibility that they establish a chromatin state that does not permit DNA methylation to spread. | [
"30"
] | Such factors may include CTCF, which has been shown to protect DNA against de novo DNA methylation during imprinting, and the combinatorial presence of CTCF and active histone modifications hints to the possibility that they establish a chromatin state that does not permit DNA methylation to spread. | true | true | true | true | true | 256 |
6 | DISCUSSION | 1 | 31 | [
"b31"
] | 17,202,157 | pmid-11454739 | We present here the first example of a bipartite CpG island code, but such codes may be a general phenomenon. | [
"31"
] | 109 | 1,512 | 0 | false | We present here the first example of a bipartite CpG island code, but such codes may be a general phenomenon. | [] | We present here the first example of a bipartite CpG island code, but such codes may be a general phenomenon. | true | true | true | true | true | 257 |
6 | DISCUSSION | 1 | 31 | [
"b31"
] | 17,202,157 | pmid-11454739 | Similar local CpG methylation patterns have been described for promoter-containing CpG islands of the mouse and human APRT, ADA and telomerase genes (31), but histone modifications have not been analyzed in these promoters. | [
"31"
] | 223 | 1,513 | 1 | false | Similar local CpG methylation patterns have been described for promoter-containing CpG islands of the mouse and human APRT, ADA and telomerase genes, but histone modifications have not been analyzed in these promoters. | [
"31"
] | Similar local CpG methylation patterns have been described for promoter-containing CpG islands of the mouse and human APRT, ADA and telomerase genes, but histone modifications have not been analyzed in these promoters. | true | true | true | true | true | 257 |
6 | DISCUSSION | 1 | 31 | [
"b31"
] | 17,202,157 | pmid-11454739 | Whether a bipartite CpG island code is linked to genes that are actively repressed like CAII remains to be elucidated. | [
"31"
] | 118 | 1,514 | 0 | false | Whether a bipartite CpG island code is linked to genes that are actively repressed like CAII remains to be elucidated. | [] | Whether a bipartite CpG island code is linked to genes that are actively repressed like CAII remains to be elucidated. | true | true | true | true | true | 257 |
6 | DISCUSSION | 1 | 31 | [
"b31"
] | 17,202,157 | pmid-11454739 | Silencing by CpG methylation is believed to involve progressive spreading of DNA methylation, eventually covering entire CpG islands. | [
"31"
] | 133 | 1,515 | 0 | false | Silencing by CpG methylation is believed to involve progressive spreading of DNA methylation, eventually covering entire CpG islands. | [] | Silencing by CpG methylation is believed to involve progressive spreading of DNA methylation, eventually covering entire CpG islands. | true | true | true | true | true | 257 |
6 | DISCUSSION | 1 | 31 | [
"b31"
] | 17,202,157 | pmid-11454739 | Our data suggest that boundary elements function as crucial antagonists against such gene silencing events. | [
"31"
] | 107 | 1,516 | 0 | false | Our data suggest that boundary elements function as crucial antagonists against such gene silencing events. | [] | Our data suggest that boundary elements function as crucial antagonists against such gene silencing events. | true | true | true | true | true | 257 |
6 | DISCUSSION | 1 | 31 | [
"b31"
] | 17,202,157 | pmid-11454739 | Whatever the molecular mechanism, the bipartite code within the promoter does not preclude gene activity, and as such it challenges the paradigm that methylation of promoter-containing CpG islands invariantly causes gene silencing. | [
"31"
] | 231 | 1,517 | 0 | false | Whatever the molecular mechanism, the bipartite code within the promoter does not preclude gene activity, and as such it challenges the paradigm that methylation of promoter-containing CpG islands invariantly causes gene silencing. | [] | Whatever the molecular mechanism, the bipartite code within the promoter does not preclude gene activity, and as such it challenges the paradigm that methylation of promoter-containing CpG islands invariantly causes gene silencing. | true | true | true | true | true | 257 |
0 | INTRODUCTION | 1 | 1–4 | [
"B1 B2 B3 B4",
"B5",
"B6",
"B7",
"B8"
] | 17,389,642 | pmid-4508150|pmid-2866795|pmid-1373237|pmid-1985896|NA|pmid-8386773|pmid-5416897|pmid-9931000 | The major challenges in the development of artificial ribonucleases (aRNases) are the achievement of sequence specificity of RNA cleavage and high cleavage efficiency. | [
"1–4",
"5",
"6",
"7",
"8"
] | 167 | 1,518 | 0 | false | The major challenges in the development of artificial ribonucleases (aRNases) are the achievement of sequence specificity of RNA cleavage and high cleavage efficiency. | [] | The major challenges in the development of artificial ribonucleases (aRNases) are the achievement of sequence specificity of RNA cleavage and high cleavage efficiency. | true | true | true | true | true | 258 |
0 | INTRODUCTION | 1 | 1–4 | [
"B1 B2 B3 B4",
"B5",
"B6",
"B7",
"B8"
] | 17,389,642 | pmid-4508150|pmid-2866795|pmid-1373237|pmid-1985896|NA|pmid-8386773|pmid-5416897|pmid-9931000 | Natural ribonucleases of RNase A family (1–4) exhibit pyrimidine-X specificity. | [
"1–4",
"5",
"6",
"7",
"8"
] | 79 | 1,519 | 1 | false | Natural ribonucleases of RNase A family exhibit pyrimidine-X specificity. | [
"1–4"
] | Natural ribonucleases of RNase A family exhibit pyrimidine-X specificity. | true | true | true | true | true | 258 |
0 | INTRODUCTION | 1 | 6 | [
"B1 B2 B3 B4",
"B5",
"B6",
"B7",
"B8"
] | 17,389,642 | pmid-4508150|pmid-2866795|pmid-1373237|pmid-1985896|NA|pmid-8386773|pmid-5416897|pmid-9931000 | Ribonucleases of T1 family (RNase T1 from Aspergillus oryzae (5) and RNase F1 from Fusarium moniliforme (6) exhibit guanine-X specificity, and RNase U2 from Ustilago sphaerogena (7) exhibit adenine-X specificity. | [
"1–4",
"5",
"6",
"7",
"8"
] | 212 | 1,520 | 1 | false | Ribonucleases of T1 family and RNase F1 from Fusarium moniliforme exhibit guanine-X specificity, and RNase U2 from Ustilago sphaerogena exhibit adenine-X specificity. | [
"RNase T1 from Aspergillus oryzae (5",
"6",
"7"
] | Ribonucleases of T1 family and RNase F1 from Fusarium moniliforme exhibit guanine-X specificity, and RNase U2 from Ustilago sphaerogena exhibit adenine-X specificity. | true | true | true | true | true | 258 |
0 | INTRODUCTION | 1 | 8 | [
"B1 B2 B3 B4",
"B5",
"B6",
"B7",
"B8"
] | 17,389,642 | pmid-4508150|pmid-2866795|pmid-1373237|pmid-1985896|NA|pmid-8386773|pmid-5416897|pmid-9931000 | Attempts have been made to alter the specificity of ribonuclease T1 by protein engineering methods (8), but this goal has not been achieved till date. | [
"1–4",
"5",
"6",
"7",
"8"
] | 150 | 1,521 | 1 | false | Attempts have been made to alter the specificity of ribonuclease T1 by protein engineering methods, but this goal has not been achieved till date. | [
"8"
] | Attempts have been made to alter the specificity of ribonuclease T1 by protein engineering methods, but this goal has not been achieved till date. | true | true | true | true | true | 258 |
1 | INTRODUCTION | 1 | 9–11 | [
"B9 B10 B11",
"B12",
"B13",
"B14"
] | 17,389,642 | pmid-9528657|NA|pmid-8604321|NA|NA|pmid-3331337|pmid-15047859|NA | One approach to the design of aRNases consists of mimicking active sites of natural enzymes by conjugates bearing the functional groups of amino acids that form the catalytic centre of the enzyme and catalysing the transesterification reaction [for example, imidazole (9–11), aminogroups (12), guanidinium groups (13)]. | [
"9–11",
"12",
"13",
"14"
] | 319 | 1,522 | 0 | false | One approach to the design of aRNases consists of mimicking active sites of natural enzymes by conjugates bearing the functional groups of amino acids that form the catalytic centre of the enzyme and catalysing the transesterification reaction. | [
"for example, imidazole (9–11), aminogroups (12), guanidinium groups (13)"
] | One approach to the design of aRNases consists of mimicking active sites of natural enzymes by conjugates bearing the functional groups of amino acids that form the catalytic centre of the enzyme and catalysing the transesterification reaction. | true | true | true | true | true | 259 |
1 | INTRODUCTION | 1 | 14 | [
"B9 B10 B11",
"B12",
"B13",
"B14"
] | 17,389,642 | pmid-9528657|NA|pmid-8604321|NA|NA|pmid-3331337|pmid-15047859|NA | aRNases designed using this approach usually display cleavage specificity similar to that of RNase A: they cleave RNA predominantly at linkages within Pyr-A motifs, which are known to be highly sensitive towards various cleaving agents (14). | [
"9–11",
"12",
"13",
"14"
] | 241 | 1,523 | 1 | false | aRNases designed using this approach usually display cleavage specificity similar to that of RNase A: they cleave RNA predominantly at linkages within Pyr-A motifs, which are known to be highly sensitive towards various cleaving agents. | [
"14"
] | aRNases designed using this approach usually display cleavage specificity similar to that of RNase A: they cleave RNA predominantly at linkages within Pyr-A motifs, which are known to be highly sensitive towards various cleaving agents. | false | true | true | true | false | 259 |
1 | INTRODUCTION | 1 | 9–11 | [
"B9 B10 B11",
"B12",
"B13",
"B14"
] | 17,389,642 | pmid-9528657|NA|pmid-8604321|NA|NA|pmid-3331337|pmid-15047859|NA | These aRNases accelerate cleavage at the most sensitive sites within RNA. | [
"9–11",
"12",
"13",
"14"
] | 73 | 1,524 | 0 | false | These aRNases accelerate cleavage at the most sensitive sites within RNA. | [] | These aRNases accelerate cleavage at the most sensitive sites within RNA. | true | true | true | true | true | 259 |
2 | INTRODUCTION | 0 | null | null | 17,389,642 | pmid-16615805 | The sequence specificity of natural RNases is determined by the substrate recognition centre in which the specific interaction of amino acids with RNA provides for the specific binding and placement of a particular heterocyclic base, thus resulting in the optimal conformation of internucleotide phosphodiester bonds, which are subjected to cleavage. | null | 350 | 1,525 | 0 | false | null | null | The sequence specificity of natural RNases is determined by the substrate recognition centre in which the specific interaction of amino acids with RNA provides for the specific binding and placement of a particular heterocyclic base, thus resulting in the optimal conformation of internucleotide phosphodiester bonds, which are subjected to cleavage. | true | true | true | true | true | 260 |
2 | INTRODUCTION | 0 | null | null | 17,389,642 | pmid-16615805 | Accurate mimicking of ribonuclease active centres is a difficult task because of their complex spatial structure providing for multipoint contacts within the enzyme–substrate complex, and specific and dynamic nature of the centres that undergo conformational changes. | null | 267 | 1,526 | 0 | false | null | null | Accurate mimicking of ribonuclease active centres is a difficult task because of their complex spatial structure providing for multipoint contacts within the enzyme–substrate complex, and specific and dynamic nature of the centres that undergo conformational changes. | true | true | true | true | true | 260 |
3 | INTRODUCTION | 1 | 15 | [
"B15",
"B13",
"B16 B17 B18 B19 B20 B21"
] | 17,389,642 | pmid-1379732|NA|NA|pmid-15047859|pmid-16615805|NA|pmid-12462971|NA|pmid-11433033|pmid-11433033|pmid-12654263 | Attempts were made to stabilize the RNA heterocyclic bases optimally for cleavage conformations via stacking interactions with aromatic amino acids [for example, phenylalanine (15)], which were introduced into the structure of conjugates mimicking RNase active centres. | [
"15",
"13",
"16–21"
] | 269 | 1,527 | 0 | false | Attempts were made to stabilize the RNA heterocyclic bases optimally for cleavage conformations via stacking interactions with aromatic amino acids, which were introduced into the structure of conjugates mimicking RNase active centres. | [
"for example, phenylalanine (15)"
] | Attempts were made to stabilize the RNA heterocyclic bases optimally for cleavage conformations via stacking interactions with aromatic amino acids, which were introduced into the structure of conjugates mimicking RNase active centres. | true | true | true | true | true | 261 |
3 | INTRODUCTION | 1 | 15 | [
"B15",
"B13",
"B16 B17 B18 B19 B20 B21"
] | 17,389,642 | pmid-1379732|NA|NA|pmid-15047859|pmid-16615805|NA|pmid-12462971|NA|pmid-11433033|pmid-11433033|pmid-12654263 | However, these conjugates did not exhibit any cleavage specificity other than Pyr-A. | [
"15",
"13",
"16–21"
] | 84 | 1,528 | 0 | false | However, these conjugates did not exhibit any cleavage specificity other than Pyr-A. | [] | However, these conjugates did not exhibit any cleavage specificity other than Pyr-A. | true | true | true | true | true | 261 |
3 | INTRODUCTION | 1 | 13 | [
"B15",
"B13",
"B16 B17 B18 B19 B20 B21"
] | 17,389,642 | pmid-1379732|NA|NA|pmid-15047859|pmid-16615805|NA|pmid-12462971|NA|pmid-11433033|pmid-11433033|pmid-12654263 | aRNases displaying other specificity were developed by introducing guanidinium groups and arginine residues into the structure of aRNases: some G–X cleavage activity was reported for conjugates of anthraquinone and imidodiacetate bearing carboxylic and ammonium ions (13) and conjugates of oligodeoxyribonucleotides and peptide (LR)4-G-amide (16–21). | [
"15",
"13",
"16–21"
] | 350 | 1,529 | 1 | false | aRNases displaying other specificity were developed by introducing guanidinium groups and arginine residues into the structure of aRNases: some G–X cleavage activity was reported for conjugates of anthraquinone and imidodiacetate bearing carboxylic and ammonium ions and conjugates of oligodeoxyribonucleotides and peptide (LR)4-G-amide. | [
"13",
"16–21"
] | aRNases displaying other specificity were developed by introducing guanidinium groups and arginine residues into the structure of aRNases: some G–X cleavage activity was reported for conjugates of anthraquinone and imidodiacetate bearing carboxylic and ammonium ions and conjugates of oligodeoxyribonucleotides and peptide (LR)4-G-amide. | false | true | true | true | false | 261 |
4 | INTRODUCTION | 1 | 16 | [
"B16",
"B19",
"B16",
"B19",
"B17",
"B20"
] | 17,389,642 | NA|NA|NA|NA|pmid-15047859|pmid-12462971 | Recently, the conjugates of peptide (LR)4-G-NH2 attached to 5′-terminal phosphate of antisense oligonucleotides were obtained (16,19). | [
"16",
"19",
"16",
"19",
"17",
"20"
] | 134 | 1,530 | 0 | false | Recently, the conjugates of peptide (LR)4-G-NH2 attached to 5′-terminal phosphate of antisense oligonucleotides were obtained. | [
"16,19"
] | Recently, the conjugates of peptide (LR)4-G-NH2 attached to 5′-terminal phosphate of antisense oligonucleotides were obtained. | true | true | true | true | true | 262 |
4 | INTRODUCTION | 1 | 16 | [
"B16",
"B19",
"B16",
"B19",
"B17",
"B20"
] | 17,389,642 | NA|NA|NA|NA|pmid-15047859|pmid-12462971 | These conjugates were found to cleave RNA both in the vicinity of oligonucleotide complementary sequence and in a random manner at Pyr-A and G–X linkages (16,19). | [
"16",
"19",
"16",
"19",
"17",
"20"
] | 162 | 1,531 | 0 | false | These conjugates were found to cleave RNA both in the vicinity of oligonucleotide complementary sequence and in a random manner at Pyr-A and G–X linkages. | [
"16,19"
] | These conjugates were found to cleave RNA both in the vicinity of oligonucleotide complementary sequence and in a random manner at Pyr-A and G–X linkages. | true | true | true | true | true | 262 |
4 | INTRODUCTION | 1 | 16 | [
"B16",
"B19",
"B16",
"B19",
"B17",
"B20"
] | 17,389,642 | NA|NA|NA|NA|pmid-15047859|pmid-12462971 | We found that the oligonucleotide in the conjugates plays an unusual role: it promotes formation of an ‘active’ peptide conformation because the peptide itself exhibits no ribonuclease activity (17,20). | [
"16",
"19",
"16",
"19",
"17",
"20"
] | 202 | 1,532 | 0 | false | We found that the oligonucleotide in the conjugates plays an unusual role: it promotes formation of an ‘active’ peptide conformation because the peptide itself exhibits no ribonuclease activity. | [
"17,20"
] | We found that the oligonucleotide in the conjugates plays an unusual role: it promotes formation of an ‘active’ peptide conformation because the peptide itself exhibits no ribonuclease activity. | true | true | true | true | true | 262 |
4 | INTRODUCTION | 1 | 16 | [
"B16",
"B19",
"B16",
"B19",
"B17",
"B20"
] | 17,389,642 | NA|NA|NA|NA|pmid-15047859|pmid-12462971 | All designed oligonucleotide–peptide conjugates displayed either G–X > Pyr-A or G–X < Pyr-A activity, but both activities were observed simultaneously. | [
"16",
"19",
"16",
"19",
"17",
"20"
] | 151 | 1,533 | 0 | false | All designed oligonucleotide–peptide conjugates displayed either G–X > Pyr-A or G–X < Pyr-A activity, but both activities were observed simultaneously. | [] | All designed oligonucleotide–peptide conjugates displayed either G–X > Pyr-A or G–X < Pyr-A activity, but both activities were observed simultaneously. | true | true | true | true | true | 262 |
4 | INTRODUCTION | 1 | 16 | [
"B16",
"B19",
"B16",
"B19",
"B17",
"B20"
] | 17,389,642 | NA|NA|NA|NA|pmid-15047859|pmid-12462971 | The main task of this work was to design the conjugate(s) exhibiting G–X cleavage activity similar only to RNase T1. | [
"16",
"19",
"16",
"19",
"17",
"20"
] | 116 | 1,534 | 0 | false | The main task of this work was to design the conjugate(s) exhibiting G–X cleavage activity similar only to RNase T1. | [] | The main task of this work was to design the conjugate(s) exhibiting G–X cleavage activity similar only to RNase T1. | true | true | true | true | true | 262 |
5 | INTRODUCTION | 0 | null | null | 17,389,642 | NA|pmid-15250719|NA | In this article, we solve this problem and describe the first single-stranded guanine-specific aRNase—conjugate of nonadeoxyribonucleotide GGATCTCTT and peptide (RL)4-G-amide connected by the linker of three deoxyribose residues (pep-9), which display only G–X cleavage activity under various conditions. | null | 304 | 1,535 | 0 | false | null | null | In this article, we solve this problem and describe the first single-stranded guanine-specific aRNase—conjugate of nonadeoxyribonucleotide GGATCTCTT and peptide (RL)4-G-amide connected by the linker of three deoxyribose residues (pep-9), which display only G–X cleavage activity under various conditions. | true | true | true | true | true | 263 |
5 | INTRODUCTION | 0 | null | null | 17,389,642 | NA|pmid-15250719|NA | Rate enhancement of RNA cleavage at G–X linkages catalysed by pep-9 is 108, as compared to non-catalysed reactions; pep-9 cleaves G–X linkages only 105-fold less rapidly than RNase T1 (kcat_RNase T1/kcat_pep-9 = 105). | null | 217 | 1,536 | 0 | false | null | null | Rate enhancement of RNA cleavage at G–X linkages catalysed by pep-9 is 108, as compared to non-catalysed reactions; pep-9 cleaves G–X linkages only 105-fold less rapidly than RNase T1 (kcat_RNase T1/kcat_pep-9 = 105). | true | true | true | true | true | 263 |
0 | DISCUSSION | 0 | null | null | 17,389,642 | pmid-4508150|pmid-2866795|pmid-1373237|pmid-1985896|NA|pmid-8386773|pmid-5416897|pmid-9931000 | The data obtained show that oligonucleotide–peptide conjugate pep-9 is the first aRNase exhibiting RNase T1-like cleavage activity under a wide range of conditions. | null | 164 | 1,537 | 0 | false | null | null | The data obtained show that oligonucleotide–peptide conjugate pep-9 is the first aRNase exhibiting RNase T1-like cleavage activity under a wide range of conditions. | true | true | true | true | true | 264 |
0 | DISCUSSION | 0 | null | null | 17,389,642 | pmid-4508150|pmid-2866795|pmid-1373237|pmid-1985896|NA|pmid-8386773|pmid-5416897|pmid-9931000 | The low molecular weight catalyst (pep-9) discovered is 105-fold less active as compared to RNase T1, but it accelerates cleavage at G–X linkages in RNA 107–108-fold as compared to spontaneous hydrolysis. | null | 204 | 1,538 | 0 | false | null | null | The low molecular weight catalyst (pep-9) discovered is 105-fold less active as compared to RNase T1, but it accelerates cleavage at G–X linkages in RNA 107–108-fold as compared to spontaneous hydrolysis. | true | true | true | true | true | 264 |
0 | DISCUSSION | 0 | null | null | 17,389,642 | pmid-4508150|pmid-2866795|pmid-1373237|pmid-1985896|NA|pmid-8386773|pmid-5416897|pmid-9931000 | The unique specificity found is a surprising fact per se and requires explanations on which factors (oligonucleotide or/and peptide sequence, conjugate structure, etc.) | null | 168 | 1,539 | 0 | false | null | null | The unique specificity found is a surprising fact per se and requires explanations on which factors (oligonucleotide or/and peptide sequence, conjugate structure, etc.) | true | true | false | true | false | 264 |
0 | DISCUSSION | 0 | null | null | 17,389,642 | pmid-4508150|pmid-2866795|pmid-1373237|pmid-1985896|NA|pmid-8386773|pmid-5416897|pmid-9931000 | provide for this specificity. | null | 29 | 1,540 | 0 | false | null | null | provide for this specificity. | false | true | true | true | false | 264 |
1 | DISCUSSION | 1 | 17 | [
"B17",
"B30"
] | 17,389,642 | pmid-9528657|NA|pmid-8604321|NA|NA|pmid-3331337|pmid-15047859|NA | The conjugate pep-9 functionally mimics RNase T1. | [
"17",
"30"
] | 49 | 1,541 | 0 | false | The conjugate pep-9 functionally mimics RNase T1. | [] | The conjugate pep-9 functionally mimics RNase T1. | true | true | true | true | true | 265 |
1 | DISCUSSION | 1 | 17 | [
"B17",
"B30"
] | 17,389,642 | pmid-9528657|NA|pmid-8604321|NA|NA|pmid-3331337|pmid-15047859|NA | The conjugate pep-9 is a single-stranded guanine-specific ribonuclease exhibiting multiple reaction turnover and yielding cleavage products similar to the products of RNase T1 (17). | [
"17",
"30"
] | 181 | 1,542 | 1 | false | The conjugate pep-9 is a single-stranded guanine-specific ribonuclease exhibiting multiple reaction turnover and yielding cleavage products similar to the products of RNase T1. | [
"17"
] | The conjugate pep-9 is a single-stranded guanine-specific ribonuclease exhibiting multiple reaction turnover and yielding cleavage products similar to the products of RNase T1. | true | true | true | true | true | 265 |
1 | DISCUSSION | 1 | 30 | [
"B17",
"B30"
] | 17,389,642 | pmid-9528657|NA|pmid-8604321|NA|NA|pmid-3331337|pmid-15047859|NA | Cleavage of RNA by the conjugate as well as by RNase T1 displays only moderate temperature dependence (30). | [
"17",
"30"
] | 107 | 1,543 | 1 | false | Cleavage of RNA by the conjugate as well as by RNase T1 displays only moderate temperature dependence. | [
"30"
] | Cleavage of RNA by the conjugate as well as by RNase T1 displays only moderate temperature dependence. | true | true | true | true | true | 265 |
1 | DISCUSSION | 1 | 17 | [
"B17",
"B30"
] | 17,389,642 | pmid-9528657|NA|pmid-8604321|NA|NA|pmid-3331337|pmid-15047859|NA | This fact as well as the saturation curve of the concentration profile of pep-9 are evidences for the cleavage reaction proceeding within the complex RNA/pep-9. | [
"17",
"30"
] | 160 | 1,544 | 0 | false | This fact as well as the saturation curve of the concentration profile of pep-9 are evidences for the cleavage reaction proceeding within the complex RNA/pep-9. | [] | This fact as well as the saturation curve of the concentration profile of pep-9 are evidences for the cleavage reaction proceeding within the complex RNA/pep-9. | true | true | true | true | true | 265 |
1 | DISCUSSION | 1 | 17 | [
"B17",
"B30"
] | 17,389,642 | pmid-9528657|NA|pmid-8604321|NA|NA|pmid-3331337|pmid-15047859|NA | The affinity of the conjugate to RNA is provided by the peptide moiety and oligonucleotide, which is not complementary to RNA substrate, is not involved in binding with RNA. | [
"17",
"30"
] | 173 | 1,545 | 0 | false | The affinity of the conjugate to RNA is provided by the peptide moiety and oligonucleotide, which is not complementary to RNA substrate, is not involved in binding with RNA. | [] | The affinity of the conjugate to RNA is provided by the peptide moiety and oligonucleotide, which is not complementary to RNA substrate, is not involved in binding with RNA. | true | true | true | true | true | 265 |
1 | DISCUSSION | 1 | 17 | [
"B17",
"B30"
] | 17,389,642 | pmid-9528657|NA|pmid-8604321|NA|NA|pmid-3331337|pmid-15047859|NA | This allows us to postulate pep-9 as an artificial enzyme with aptamer-like peculiarities. | [
"17",
"30"
] | 90 | 1,546 | 0 | false | This allows us to postulate pep-9 as an artificial enzyme with aptamer-like peculiarities. | [] | This allows us to postulate pep-9 as an artificial enzyme with aptamer-like peculiarities. | true | true | true | true | true | 265 |
2 | DISCUSSION | 1 | 18 | [
"B18"
] | 17,389,642 | pmid-16615805 | Analysis of structure–function relationships in the conjugate pep-9 clearly shows that any alterations of oligonucleotide sequence and length in pep-9 and deletion of the linker group result in the loss of ribonuclease activity and the appearance of Pyr-A cleavage specificity; thus, the sequence of nonadeoxyribonucleotide GGATCTCTT is obligatory for the conjugate to exhibit G–X specificity. | [
"18"
] | 393 | 1,547 | 0 | false | Analysis of structure–function relationships in the conjugate pep-9 clearly shows that any alterations of oligonucleotide sequence and length in pep-9 and deletion of the linker group result in the loss of ribonuclease activity and the appearance of Pyr-A cleavage specificity; thus, the sequence of nonadeoxyribonucleotide GGATCTCTT is obligatory for the conjugate to exhibit G–X specificity. | [] | Analysis of structure–function relationships in the conjugate pep-9 clearly shows that any alterations of oligonucleotide sequence and length in pep-9 and deletion of the linker group result in the loss of ribonuclease activity and the appearance of Pyr-A cleavage specificity; thus, the sequence of nonadeoxyribonucleotide GGATCTCTT is obligatory for the conjugate to exhibit G–X specificity. | true | true | true | true | true | 266 |
2 | DISCUSSION | 1 | 18 | [
"B18"
] | 17,389,642 | pmid-16615805 | The importance of the linker group between oligonucleotide and peptide parts of the conjugate correlate with the data published in (18). | [
"18"
] | 136 | 1,548 | 1 | false | The importance of the linker group between oligonucleotide and peptide parts of the conjugate correlate with the data published in. | [
"18"
] | The importance of the linker group between oligonucleotide and peptide parts of the conjugate correlate with the data published in. | true | true | true | true | true | 266 |
2 | DISCUSSION | 1 | 18 | [
"B18"
] | 17,389,642 | pmid-16615805 | It was found that two or three nucleotides adjacent to the peptide serve as a linker, providing a turn of oligonucleotide around the peptide and facilitating intramolecular oligonucleotide and peptide interactions. | [
"18"
] | 214 | 1,549 | 0 | false | It was found that two or three nucleotides adjacent to the peptide serve as a linker, providing a turn of oligonucleotide around the peptide and facilitating intramolecular oligonucleotide and peptide interactions. | [] | It was found that two or three nucleotides adjacent to the peptide serve as a linker, providing a turn of oligonucleotide around the peptide and facilitating intramolecular oligonucleotide and peptide interactions. | true | true | true | true | true | 266 |
3 | DISCUSSION | 1 | 31 | [
"B31",
"B31",
"B32"
] | 17,389,642 | pmid-1379732|NA|NA|pmid-15047859|pmid-16615805|NA|pmid-12462971|NA|pmid-11433033|pmid-11433033|pmid-12654263 | It is known that arginine is a multiple-donor amino acid that can form a number of specific hydrogen bonds with nucleotides (31). | [
"31",
"31",
"32"
] | 129 | 1,550 | 1 | false | It is known that arginine is a multiple-donor amino acid that can form a number of specific hydrogen bonds with nucleotides. | [
"31"
] | It is known that arginine is a multiple-donor amino acid that can form a number of specific hydrogen bonds with nucleotides. | true | true | true | true | true | 267 |
3 | DISCUSSION | 1 | 31 | [
"B31",
"B31",
"B32"
] | 17,389,642 | pmid-1379732|NA|NA|pmid-15047859|pmid-16615805|NA|pmid-12462971|NA|pmid-11433033|pmid-11433033|pmid-12654263 | The ability of arginine to form hydrogen bonds with DNA/RNA nucleobases within DNA(RNA)–protein complexes decreases in order G > T > | [
"31",
"31",
"32"
] | 132 | 1,551 | 0 | false | The ability of arginine to form hydrogen bonds with DNA/RNA nucleobases within DNA(RNA)–protein complexes decreases in order G > T > | [] | The ability of arginine to form hydrogen bonds with DNA/RNA nucleobases within DNA(RNA)–protein complexes decreases in order G > T > | true | true | false | true | false | 267 |
3 | DISCUSSION | 1 | 31 | [
"B31",
"B31",
"B32"
] | 17,389,642 | pmid-1379732|NA|NA|pmid-15047859|pmid-16615805|NA|pmid-12462971|NA|pmid-11433033|pmid-11433033|pmid-12654263 | A > C (31,32). | [
"31",
"31",
"32"
] | 14 | 1,552 | 0 | false | A > C. | [
"31,32"
] | A > C. | true | true | true | true | true | 267 |
3 | DISCUSSION | 1 | 31 | [
"B31",
"B31",
"B32"
] | 17,389,642 | pmid-1379732|NA|NA|pmid-15047859|pmid-16615805|NA|pmid-12462971|NA|pmid-11433033|pmid-11433033|pmid-12654263 | These properties can be important not only for the interaction of the peptide (LR)4-G with guanine residues in RNA, but also for the specific intramolecular binding of arginine with guanine residues presented in the conjugate. | [
"31",
"31",
"32"
] | 226 | 1,553 | 0 | false | These properties can be important not only for the interaction of the peptide (LR)4-G with guanine residues in RNA, but also for the specific intramolecular binding of arginine with guanine residues presented in the conjugate. | [] | These properties can be important not only for the interaction of the peptide (LR)4-G with guanine residues in RNA, but also for the specific intramolecular binding of arginine with guanine residues presented in the conjugate. | true | true | true | true | true | 267 |
4 | DISCUSSION | 0 | null | null | 17,389,642 | NA|NA|NA|NA|pmid-15047859|pmid-12462971 | Thus, the obtained data let us to suppose existence of some active conformation of the conjugate, which is formed as the result of a set of intermolecular contacts between the oligonucleotide and the peptide parts. | null | 214 | 1,554 | 0 | false | null | null | Thus, the obtained data let us to suppose existence of some active conformation of the conjugate, which is formed as the result of a set of intermolecular contacts between the oligonucleotide and the peptide parts. | true | true | true | true | true | 268 |
4 | DISCUSSION | 0 | null | null | 17,389,642 | NA|NA|NA|NA|pmid-15047859|pmid-12462971 | Electrostatic contacts play an important role in G–X activity of pep-9, either by stabilization of an ‘active’ conjugate conformation and/or by stabilization of RNA (G–X motif)/pep-9 reactive complex. | null | 200 | 1,555 | 0 | false | null | null | Electrostatic contacts play an important role in G–X activity of pep-9, either by stabilization of an ‘active’ conjugate conformation and/or by stabilization of RNA (G–X motif)/pep-9 reactive complex. | true | true | true | true | true | 268 |
4 | DISCUSSION | 0 | null | null | 17,389,642 | NA|NA|NA|NA|pmid-15047859|pmid-12462971 | This is suggested by the high activity of pep-9 in the absence of mono- and divalent cations and inhibition of its activity in their presence. | null | 142 | 1,556 | 0 | false | null | null | This is suggested by the high activity of pep-9 in the absence of mono- and divalent cations and inhibition of its activity in their presence. | true | true | true | true | true | 268 |
4 | DISCUSSION | 0 | null | null | 17,389,642 | NA|NA|NA|NA|pmid-15047859|pmid-12462971 | High ribonuclease activity of pep-9 under the salt-free conditions is an apparent result of the removal of electrostatic shielding of RNA, which facilitates RNA–pep-9 interaction. | null | 179 | 1,557 | 0 | false | null | null | High ribonuclease activity of pep-9 under the salt-free conditions is an apparent result of the removal of electrostatic shielding of RNA, which facilitates RNA–pep-9 interaction. | true | true | true | true | true | 268 |
5 | DISCUSSION | 1 | 33 | [
"B33",
"B34",
"B35"
] | 17,389,642 | NA|pmid-15250719|NA | The main question is: how does pep-9 cleave G–X linkages? | [
"33",
"34",
"35"
] | 57 | 1,558 | 0 | false | The main question is: how does pep-9 cleave G–X linkages? | [] | The main question is: how does pep-9 cleave G–X linkages? | true | true | true | true | true | 269 |
5 | DISCUSSION | 1 | 33 | [
"B33",
"B34",
"B35"
] | 17,389,642 | NA|pmid-15250719|NA | pH profile did not shed light on the possible mechanism of RNA cleavage by pep-9. | [
"33",
"34",
"35"
] | 81 | 1,559 | 0 | false | pH profile did not shed light on the possible mechanism of RNA cleavage by pep-9. | [] | pH profile did not shed light on the possible mechanism of RNA cleavage by pep-9. | false | true | true | true | false | 269 |
5 | DISCUSSION | 1 | 33 | [
"B33",
"B34",
"B35"
] | 17,389,642 | NA|pmid-15250719|NA | Strong decrease of activity could not be attributed to the pKa values of amino acids and heterocyclic bases because, in this range of pH, charges of arginine and glycine amide remain constant (pKa are 12.48 and ∼9.7 for guanidinium group and for Gly-amide, respectively) (33), and pKa values of heterocyclic bases (G, C, A and T) lies in the range 9.4–11.2, depending on sequence (34) and microenvironments (35). | [
"33",
"34",
"35"
] | 412 | 1,560 | 1 | false | Strong decrease of activity could not be attributed to the pKa values of amino acids and heterocyclic bases because, in this range of pH, charges of arginine and glycine amide remain constant (pKa are 12.48 and ∼9.7 for guanidinium group and for Gly-amide, respectively), and pKa values of heterocyclic bases (G, C, A and T) lies in the range 9.4–11.2, depending on sequence and microenvironments. | [
"33",
"34",
"35"
] | Strong decrease of activity could not be attributed to the pKa values of amino acids and heterocyclic bases because, in this range of pH, charges of arginine and glycine amide remain constant (pKa are 12.48 and ∼9.7 for guanidinium group and for Gly-amide, respectively), and pKa values of heterocyclic bases (G, C, A and T) lies in the range 9.4–11.2, depending on sequence and microenvironments. | true | true | true | true | true | 269 |
5 | DISCUSSION | 1 | 33 | [
"B33",
"B34",
"B35"
] | 17,389,642 | NA|pmid-15250719|NA | The data presented allow us to assume that multipoint contacts formed between pep-9 and guanine residue disrupt its stacking with adjacent nucleobases in RNA chain and change conformation to close to the ‘in-line’ one. | [
"33",
"34",
"35"
] | 218 | 1,561 | 0 | false | The data presented allow us to assume that multipoint contacts formed between pep-9 and guanine residue disrupt its stacking with adjacent nucleobases in RNA chain and change conformation to close to the ‘in-line’ one. | [] | The data presented allow us to assume that multipoint contacts formed between pep-9 and guanine residue disrupt its stacking with adjacent nucleobases in RNA chain and change conformation to close to the ‘in-line’ one. | true | true | true | true | true | 269 |
5 | DISCUSSION | 1 | 33 | [
"B33",
"B34",
"B35"
] | 17,389,642 | NA|pmid-15250719|NA | Thus, by a set of hydrogen bonds formed with guanine residue, pep-9 causes conformational changes to ribose phosphate of the guanine residue, followed by self-cleavage of the phosphodiester bond. | [
"33",
"34",
"35"
] | 195 | 1,562 | 0 | false | Thus, by a set of hydrogen bonds formed with guanine residue, pep-9 causes conformational changes to ribose phosphate of the guanine residue, followed by self-cleavage of the phosphodiester bond. | [] | Thus, by a set of hydrogen bonds formed with guanine residue, pep-9 causes conformational changes to ribose phosphate of the guanine residue, followed by self-cleavage of the phosphodiester bond. | true | true | true | true | true | 269 |
5 | DISCUSSION | 1 | 33 | [
"B33",
"B34",
"B35"
] | 17,389,642 | NA|pmid-15250719|NA | It worth noting that this type of interaction was never described for guanine nucleotides to date, while this reaction is typical for uridine and cytosine nucleotides. | [
"33",
"34",
"35"
] | 167 | 1,563 | 0 | false | It worth noting that this type of interaction was never described for guanine nucleotides to date, while this reaction is typical for uridine and cytosine nucleotides. | [] | It worth noting that this type of interaction was never described for guanine nucleotides to date, while this reaction is typical for uridine and cytosine nucleotides. | true | true | true | true | true | 269 |
6 | DISCUSSION | 0 | null | null | 17,389,642 | null | Thus, we developed aRNase displaying G–X cleavage specificity with a unique structure: a chimeric biopolymer built of nonadeoxyribonucleotide and peptide connected by a linker of three deoxyribose residues. | null | 206 | 1,564 | 0 | false | null | null | Thus, we developed aRNase displaying G–X cleavage specificity with a unique structure: a chimeric biopolymer built of nonadeoxyribonucleotide and peptide connected by a linker of three deoxyribose residues. | true | true | true | true | true | 270 |
6 | DISCUSSION | 0 | null | null | 17,389,642 | null | Identification of such a unique catalytic structure capable of specific cleaving at G–X linkages is an evidence for the existence of catalysts with aptamer-like peculiarities displaying other specificities. | null | 206 | 1,565 | 0 | false | null | null | Identification of such a unique catalytic structure capable of specific cleaving at G–X linkages is an evidence for the existence of catalysts with aptamer-like peculiarities displaying other specificities. | true | true | true | true | true | 270 |
6 | DISCUSSION | 0 | null | null | 17,389,642 | null | The study of interactions that provide for the activity of this structure can lead to the elucidation of the principles of recognition topology that can be used to design other molecules with unique properties. | null | 210 | 1,566 | 0 | false | null | null | The study of interactions that provide for the activity of this structure can lead to the elucidation of the principles of recognition topology that can be used to design other molecules with unique properties. | true | true | true | true | true | 270 |
0 | INTRODUCTION | 1 | 1–3 | [
"B1 B2 B3",
"B3",
"B4 B5 B6 B7 B8 B9 B10",
"B11",
"B12",
"B3",
"B13 B14 B15 B16",
"B16 B17 B18 B19 B20 B21 B22 B23 B24 B25 B26 B27 B28 B29 B30 B31 B32"
] | 17,553,835 | pmid-7500330|pmid-9757830|pmid-16164976|pmid-16164976|pmid-8443588|pmid-9430589|pmid-9499042|pmid-9769215|pmid-10606514|pmid-10924101|pmid-16434700|pmid-8057466|pmid-7545662|pmid-16164976|pmid-9057495|pmid-9465785|pmid-12954779|pmid-15854648|pmid-15854648|pmid-10982342|pmid-11344257|pmid-11922672|pmid-11932404|pmid-12054820|pmid-12084921|pmid-12581633|pmid-12684000|pmid-15099739|pmid-15454467|pmid-15033363|pmid-15271979|pmid-16077025|pmid-16997322|pmid-17029416|pmid-16962137|pmid-15271979|pmid-15271979 | Human immunodeficiency virus type 1 (HIV-1) nucleocapsid protein (NC) is a small, basic, nucleic-acid-binding protein having two zinc fingers connected by a short, basic amino acid linker. | [
"1–3",
"3",
"4–10",
"11",
"12",
"3",
"13–16",
"16–32"
] | 188 | 1,567 | 0 | false | Human immunodeficiency virus type 1 (HIV-1) nucleocapsid protein (NC) is a small, basic, nucleic-acid-binding protein having two zinc fingers connected by a short, basic amino acid linker. | [] | Human immunodeficiency virus type 1 nucleocapsid protein (NC) is a small, basic, nucleic-acid-binding protein having two zinc fingers connected by a short, basic amino acid linker. | true | true | true | true | true | 271 |
0 | INTRODUCTION | 1 | 1–3 | [
"B1 B2 B3",
"B3",
"B4 B5 B6 B7 B8 B9 B10",
"B11",
"B12",
"B3",
"B13 B14 B15 B16",
"B16 B17 B18 B19 B20 B21 B22 B23 B24 B25 B26 B27 B28 B29 B30 B31 B32"
] | 17,553,835 | pmid-7500330|pmid-9757830|pmid-16164976|pmid-16164976|pmid-8443588|pmid-9430589|pmid-9499042|pmid-9769215|pmid-10606514|pmid-10924101|pmid-16434700|pmid-8057466|pmid-7545662|pmid-16164976|pmid-9057495|pmid-9465785|pmid-12954779|pmid-15854648|pmid-15854648|pmid-10982342|pmid-11344257|pmid-11922672|pmid-11932404|pmid-12054820|pmid-12084921|pmid-12581633|pmid-12684000|pmid-15099739|pmid-15454467|pmid-15033363|pmid-15271979|pmid-16077025|pmid-16997322|pmid-17029416|pmid-16962137|pmid-15271979|pmid-15271979 | Each finger contains the invariant CCHC metal-ion-binding motif (1–3). | [
"1–3",
"3",
"4–10",
"11",
"12",
"3",
"13–16",
"16–32"
] | 70 | 1,568 | 1 | false | Each finger contains the invariant CCHC metal-ion-binding motif. | [
"1–3"
] | Each finger contains the invariant CCHC metal-ion-binding motif. | true | true | true | true | true | 271 |
0 | INTRODUCTION | 1 | 3 | [
"B1 B2 B3",
"B3",
"B4 B5 B6 B7 B8 B9 B10",
"B11",
"B12",
"B3",
"B13 B14 B15 B16",
"B16 B17 B18 B19 B20 B21 B22 B23 B24 B25 B26 B27 B28 B29 B30 B31 B32"
] | 17,553,835 | pmid-7500330|pmid-9757830|pmid-16164976|pmid-16164976|pmid-8443588|pmid-9430589|pmid-9499042|pmid-9769215|pmid-10606514|pmid-10924101|pmid-16434700|pmid-8057466|pmid-7545662|pmid-16164976|pmid-9057495|pmid-9465785|pmid-12954779|pmid-15854648|pmid-15854648|pmid-10982342|pmid-11344257|pmid-11922672|pmid-11932404|pmid-12054820|pmid-12084921|pmid-12581633|pmid-12684000|pmid-15099739|pmid-15454467|pmid-15033363|pmid-15271979|pmid-16077025|pmid-16997322|pmid-17029416|pmid-16962137|pmid-15271979|pmid-15271979 | NC binds non-specifically to the phosphodiester backbone of nucleic acids (3), but also exhibits sequence-specific binding at sites with runs of Gs or T/UGs (4–10). | [
"1–3",
"3",
"4–10",
"11",
"12",
"3",
"13–16",
"16–32"
] | 164 | 1,569 | 1 | false | NC binds non-specifically to the phosphodiester backbone of nucleic acids, but also exhibits sequence-specific binding at sites with runs of Gs or T/UGs. | [
"3",
"4–10"
] | NC binds non-specifically to the phosphodiester backbone of nucleic acids, but also exhibits sequence-specific binding at sites with runs of Gs or T/UGs. | true | true | true | true | true | 271 |
0 | INTRODUCTION | 1 | 11 | [
"B1 B2 B3",
"B3",
"B4 B5 B6 B7 B8 B9 B10",
"B11",
"B12",
"B3",
"B13 B14 B15 B16",
"B16 B17 B18 B19 B20 B21 B22 B23 B24 B25 B26 B27 B28 B29 B30 B31 B32"
] | 17,553,835 | pmid-7500330|pmid-9757830|pmid-16164976|pmid-16164976|pmid-8443588|pmid-9430589|pmid-9499042|pmid-9769215|pmid-10606514|pmid-10924101|pmid-16434700|pmid-8057466|pmid-7545662|pmid-16164976|pmid-9057495|pmid-9465785|pmid-12954779|pmid-15854648|pmid-15854648|pmid-10982342|pmid-11344257|pmid-11922672|pmid-11932404|pmid-12054820|pmid-12084921|pmid-12581633|pmid-12684000|pmid-15099739|pmid-15454467|pmid-15033363|pmid-15271979|pmid-16077025|pmid-16997322|pmid-17029416|pmid-16962137|pmid-15271979|pmid-15271979 | In addition, NC is a nucleic acid chaperone and is able to catalyze nucleic acid conformational rearrangements that lead to formation of the most thermodynamically stable structures (11) (reviewed in 1–3,12). | [
"1–3",
"3",
"4–10",
"11",
"12",
"3",
"13–16",
"16–32"
] | 208 | 1,570 | 1 | false | In addition, NC is a nucleic acid chaperone and is able to catalyze nucleic acid conformational rearrangements that lead to formation of the most thermodynamically stable structures. | [
"11",
"reviewed in 1–3,12"
] | In addition, NC is a nucleic acid chaperone and is able to catalyze nucleic acid conformational rearrangements that lead to formation of the most thermodynamically stable structures. | true | true | true | true | true | 271 |
0 | INTRODUCTION | 1 | 3 | [
"B1 B2 B3",
"B3",
"B4 B5 B6 B7 B8 B9 B10",
"B11",
"B12",
"B3",
"B13 B14 B15 B16",
"B16 B17 B18 B19 B20 B21 B22 B23 B24 B25 B26 B27 B28 B29 B30 B31 B32"
] | 17,553,835 | pmid-7500330|pmid-9757830|pmid-16164976|pmid-16164976|pmid-8443588|pmid-9430589|pmid-9499042|pmid-9769215|pmid-10606514|pmid-10924101|pmid-16434700|pmid-8057466|pmid-7545662|pmid-16164976|pmid-9057495|pmid-9465785|pmid-12954779|pmid-15854648|pmid-15854648|pmid-10982342|pmid-11344257|pmid-11922672|pmid-11932404|pmid-12054820|pmid-12084921|pmid-12581633|pmid-12684000|pmid-15099739|pmid-15454467|pmid-15033363|pmid-15271979|pmid-16077025|pmid-16997322|pmid-17029416|pmid-16962137|pmid-15271979|pmid-15271979 | The chaperone function has two independent activities (3): aggregation of nucleic acids, localized primarily to the N-terminal basic residues (13–16); and weak destabilization of duplex molecules, associated with the zinc fingers (16–32). | [
"1–3",
"3",
"4–10",
"11",
"12",
"3",
"13–16",
"16–32"
] | 238 | 1,571 | 1 | false | The chaperone function has two independent activities : aggregation of nucleic acids, localized primarily to the N-terminal basic residues ; and weak destabilization of duplex molecules, associated with the zinc fingers. | [
"3",
"13–16",
"16–32"
] | The chaperone function has two independent activities : aggregation of nucleic acids, localized primarily to the N-terminal basic residues ; and weak destabilization of duplex molecules, associated with the zinc fingers. | true | true | true | true | true | 271 |
1 | INTRODUCTION | 1 | 2 | [
"B2",
"B3",
"B33",
"B9",
"B34 B35 B36 B37 B38",
"B3",
"B39"
] | 17,553,835 | pmid-9757830|pmid-16164976|pmid-12206453|pmid-10924101|pmid-9933645|pmid-10233940|pmid-11786014|pmid-15327946|pmid-16314282|pmid-16164976|NA|pmid-15033363|pmid-15542863|pmid-15218022|pmid-16291743 | The nucleic acid chaperone activity of NC is required for efficient and highly specific DNA synthesis. | [
"2",
"3",
"33",
"9",
"34–38",
"3",
"39"
] | 102 | 1,572 | 0 | false | The nucleic acid chaperone activity of NC is required for efficient and highly specific DNA synthesis. | [] | The nucleic acid chaperone activity of NC is required for efficient and highly specific DNA synthesis. | true | true | true | true | true | 272 |
1 | INTRODUCTION | 1 | 2 | [
"B2",
"B3",
"B33",
"B9",
"B34 B35 B36 B37 B38",
"B3",
"B39"
] | 17,553,835 | pmid-9757830|pmid-16164976|pmid-12206453|pmid-10924101|pmid-9933645|pmid-10233940|pmid-11786014|pmid-15327946|pmid-16314282|pmid-16164976|NA|pmid-15033363|pmid-15542863|pmid-15218022|pmid-16291743 | Indeed, NC plays an important role in almost every step in reverse transcription including the minus-strand (2,3,33) and plus-strand (9,34–38) transfer events that are mandatory for synthesis of full-length minus- and plus-strand DNAs and formation of the long-terminal repeats present at the ends of proviral DNA. | [
"2",
"3",
"33",
"9",
"34–38",
"3",
"39"
] | 314 | 1,573 | 0 | false | Indeed, NC plays an important role in almost every step in reverse transcription including the minus-strand and plus-strand transfer events that are mandatory for synthesis of full-length minus- and plus-strand DNAs and formation of the long-terminal repeats present at the ends of proviral DNA. | [
"2,3,33",
"9,34–38"
] | Indeed, NC plays an important role in almost every step in reverse transcription including the minus-strand and plus-strand transfer events that are mandatory for synthesis of full-length minus- and plus-strand DNAs and formation of the long-terminal repeats present at the ends of proviral DNA. | true | true | true | true | true | 272 |
1 | INTRODUCTION | 1 | 2 | [
"B2",
"B3",
"B33",
"B9",
"B34 B35 B36 B37 B38",
"B3",
"B39"
] | 17,553,835 | pmid-9757830|pmid-16164976|pmid-12206453|pmid-10924101|pmid-9933645|pmid-10233940|pmid-11786014|pmid-15327946|pmid-16314282|pmid-16164976|NA|pmid-15033363|pmid-15542863|pmid-15218022|pmid-16291743 | In minus-strand transfer, the initial DNA product of reverse transcription, known as (−) strong-stop DNA [(−) SSDNA], is translocated to the 3′ end of the viral genome (acceptor RNA) in a reaction mediated by base pairing of the complementary repeat (R) regions at the 3′ ends of the DNA and RNA molecules (3,39). | [
"2",
"3",
"33",
"9",
"34–38",
"3",
"39"
] | 313 | 1,574 | 0 | false | In minus-strand transfer, the initial DNA product of reverse transcription, known as (−) strong-stop DNA [(−) SSDNA], is translocated to the 3′ end of the viral genome (acceptor RNA) in a reaction mediated by base pairing of the complementary repeat (R) regions at the 3′ ends of the DNA and RNA molecules. | [
"3,39"
] | In minus-strand transfer, the initial DNA product of reverse transcription, known as (−) strong-stop DNA [(−) SSDNA], is translocated to the 3′ end of the viral genome (acceptor RNA) in a reaction mediated by base pairing of the complementary repeat (R) regions at the 3′ ends of the DNA and RNA molecules. | true | true | true | true | true | 272 |
2 | INTRODUCTION | 1 | 16 | [
"B16",
"B19",
"B23 B24 B25 B26",
"B40 B41 B42",
"B17",
"B20",
"B32",
"B41",
"B43 B44 B45 B46 B47 B48",
"B3"
] | 17,553,835 | pmid-15854648|pmid-11922672|pmid-12581633|pmid-12684000|pmid-15099739|pmid-15454467|pmid-9188585|pmid-12473448|pmid-16471833|pmid-10982342|pmid-11932404|pmid-16962137|pmid-12473448|pmid-7989315|pmid-7543198|pmid-9760259|pmid-9658119|pmid-12846564|pmid-16406407|pmid-16164976|pmid-11497429|pmid-15854644|pmid-16406407|pmid-16962137|pmid-16100256|pmid-17372205 | For HIV-1, R consists of 97 nucleotides (nt). | [
"16",
"19",
"23–26",
"40–42",
"17",
"20",
"32",
"41",
"43–48",
"3"
] | 45 | 1,575 | 0 | false | For HIV-1, R consists of 97 nucleotides (nt). | [] | For HIV-1, R consists of 97 nucleotides (nt). | true | true | true | true | true | 273 |
2 | INTRODUCTION | 1 | 16 | [
"B16",
"B19",
"B23 B24 B25 B26",
"B40 B41 B42",
"B17",
"B20",
"B32",
"B41",
"B43 B44 B45 B46 B47 B48",
"B3"
] | 17,553,835 | pmid-15854648|pmid-11922672|pmid-12581633|pmid-12684000|pmid-15099739|pmid-15454467|pmid-9188585|pmid-12473448|pmid-16471833|pmid-10982342|pmid-11932404|pmid-16962137|pmid-12473448|pmid-7989315|pmid-7543198|pmid-9760259|pmid-9658119|pmid-12846564|pmid-16406407|pmid-16164976|pmid-11497429|pmid-15854644|pmid-16406407|pmid-16962137|pmid-16100256|pmid-17372205 | The first 59 nt in acceptor RNA and (−) SSDNA form highly stable, complementary stem-loop structures, which are referred to as transactivation response elements (TAR) RNA and TAR DNA, respectively. | [
"16",
"19",
"23–26",
"40–42",
"17",
"20",
"32",
"41",
"43–48",
"3"
] | 197 | 1,576 | 0 | false | The first 59 nt in acceptor RNA and (−) SSDNA form highly stable, complementary stem-loop structures, which are referred to as transactivation response elements (TAR) RNA and TAR DNA, respectively. | [] | The first 59 nt in acceptor RNA and (−) SSDNA form highly stable, complementary stem-loop structures, which are referred to as transactivation response elements (TAR) RNA and TAR DNA, respectively. | true | true | true | true | true | 273 |
2 | INTRODUCTION | 1 | 16 | [
"B16",
"B19",
"B23 B24 B25 B26",
"B40 B41 B42",
"B17",
"B20",
"B32",
"B41",
"B43 B44 B45 B46 B47 B48",
"B3"
] | 17,553,835 | pmid-15854648|pmid-11922672|pmid-12581633|pmid-12684000|pmid-15099739|pmid-15454467|pmid-9188585|pmid-12473448|pmid-16471833|pmid-10982342|pmid-11932404|pmid-16962137|pmid-12473448|pmid-7989315|pmid-7543198|pmid-9760259|pmid-9658119|pmid-12846564|pmid-16406407|pmid-16164976|pmid-11497429|pmid-15854644|pmid-16406407|pmid-16962137|pmid-16100256|pmid-17372205 | NC stimulates HIV-1 minus-strand transfer (3 and references therein) by transiently destabilizing the TAR structures (16,19,23–26,40–42). | [
"16",
"19",
"23–26",
"40–42",
"17",
"20",
"32",
"41",
"43–48",
"3"
] | 137 | 1,577 | 0 | false | NC stimulates HIV-1 minus-strand transfer by transiently destabilizing the TAR structures. | [
"3 and references therein",
"16,19,23–26,40–42"
] | NC stimulates HIV-1 minus-strand transfer by transiently destabilizing the TAR structures. | true | true | true | true | true | 273 |
2 | INTRODUCTION | 1 | 3 | [
"B16",
"B19",
"B23 B24 B25 B26",
"B40 B41 B42",
"B17",
"B20",
"B32",
"B41",
"B43 B44 B45 B46 B47 B48",
"B3"
] | 17,553,835 | pmid-15854648|pmid-11922672|pmid-12581633|pmid-12684000|pmid-15099739|pmid-15454467|pmid-9188585|pmid-12473448|pmid-16471833|pmid-10982342|pmid-11932404|pmid-16962137|pmid-12473448|pmid-7989315|pmid-7543198|pmid-9760259|pmid-9658119|pmid-12846564|pmid-16406407|pmid-16164976|pmid-11497429|pmid-15854644|pmid-16406407|pmid-16962137|pmid-16100256|pmid-17372205 | Destabilization of these structures promotes annealing of TAR RNA to TAR DNA (17,20,32,41,43–48) and inhibits a competing self-priming reaction at the 3′ end of (−) SSDNA (3). | [
"16",
"19",
"23–26",
"40–42",
"17",
"20",
"32",
"41",
"43–48",
"3"
] | 175 | 1,578 | 1 | false | Destabilization of these structures promotes annealing of TAR RNA to TAR DNA and inhibits a competing self-priming reaction at the 3′ end of (−) SSDNA. | [
"17,20,32,41,43–48",
"3"
] | Destabilization of these structures promotes annealing of TAR RNA to TAR DNA and inhibits a competing self-priming reaction at the 3′ end of (−) SSDNA. | true | true | true | true | true | 273 |
3 | INTRODUCTION | 1 | 49–51 | [
"B49 B50 B51",
"B52 B53 B54 B55",
"B56",
"B57",
"B48",
"B58",
"B32",
"B59"
] | 17,553,835 | pmid-15152202|pmid-15345057|pmid-16064056|pmid-8078946|pmid-10212256|pmid-10954609|pmid-10756194|pmid-11497429|pmid-15854644|pmid-16406407|pmid-16100256|pmid-16962137|pmid-17372205|pmid-11497429|pmid-10931958|pmid-17043221 | Loop–loop interactions have been shown to be critical for dimerization and packaging of retroviral RNA (49–51) as well as for the formation of kissing complexes containing TAR RNA (52–55). | [
"49–51",
"52–55",
"56",
"57",
"48",
"58",
"32",
"59"
] | 188 | 1,579 | 1 | false | Loop–loop interactions have been shown to be critical for dimerization and packaging of retroviral RNA as well as for the formation of kissing complexes containing TAR RNA. | [
"49–51",
"52–55"
] | Loop–loop interactions have been shown to be critical for dimerization and packaging of retroviral RNA as well as for the formation of kissing complexes containing TAR RNA. | true | true | true | true | true | 274 |
3 | INTRODUCTION | 1 | 49–51 | [
"B49 B50 B51",
"B52 B53 B54 B55",
"B56",
"B57",
"B48",
"B58",
"B32",
"B59"
] | 17,553,835 | pmid-15152202|pmid-15345057|pmid-16064056|pmid-8078946|pmid-10212256|pmid-10954609|pmid-10756194|pmid-11497429|pmid-15854644|pmid-16406407|pmid-16100256|pmid-16962137|pmid-17372205|pmid-11497429|pmid-10931958|pmid-17043221 | Indeed, nucleation of the NC-catalyzed annealing step in minus-strand transfer was proposed to occur through interaction between the apical loops of TAR RNA and TAR DNA (56,57). | [
"49–51",
"52–55",
"56",
"57",
"48",
"58",
"32",
"59"
] | 177 | 1,580 | 0 | false | Indeed, nucleation of the NC-catalyzed annealing step in minus-strand transfer was proposed to occur through interaction between the apical loops of TAR RNA and TAR DNA. | [
"56,57"
] | Indeed, nucleation of the NC-catalyzed annealing step in minus-strand transfer was proposed to occur through interaction between the apical loops of TAR RNA and TAR DNA. | true | true | true | true | true | 274 |
3 | INTRODUCTION | 1 | 48 | [
"B49 B50 B51",
"B52 B53 B54 B55",
"B56",
"B57",
"B48",
"B58",
"B32",
"B59"
] | 17,553,835 | pmid-15152202|pmid-15345057|pmid-16064056|pmid-8078946|pmid-10212256|pmid-10954609|pmid-10756194|pmid-11497429|pmid-15854644|pmid-16406407|pmid-16100256|pmid-16962137|pmid-17372205|pmid-11497429|pmid-10931958|pmid-17043221 | However, an alternative proposal suggested that nucleation proceeds through destabilization of the 3′ and 5′ stem termini (48). | [
"49–51",
"52–55",
"56",
"57",
"48",
"58",
"32",
"59"
] | 127 | 1,581 | 1 | false | However, an alternative proposal suggested that nucleation proceeds through destabilization of the 3′ and 5′ stem termini. | [
"48"
] | However, an alternative proposal suggested that nucleation proceeds through destabilization of the 3′ and 5′ stem termini. | true | true | true | true | true | 274 |
3 | INTRODUCTION | 1 | 58 | [
"B49 B50 B51",
"B52 B53 B54 B55",
"B56",
"B57",
"B48",
"B58",
"B32",
"B59"
] | 17,553,835 | pmid-15152202|pmid-15345057|pmid-16064056|pmid-8078946|pmid-10212256|pmid-10954609|pmid-10756194|pmid-11497429|pmid-15854644|pmid-16406407|pmid-16100256|pmid-16962137|pmid-17372205|pmid-11497429|pmid-10931958|pmid-17043221 | Based on single-molecule FRET experiments (58) and a detailed kinetic study of NC-promoted annealing of mini-TAR constructs (32), it was also proposed that multiple pathways might be involved. | [
"49–51",
"52–55",
"56",
"57",
"48",
"58",
"32",
"59"
] | 192 | 1,582 | 1 | false | Based on single-molecule FRET experiments and a detailed kinetic study of NC-promoted annealing of mini-TAR constructs, it was also proposed that multiple pathways might be involved. | [
"58",
"32"
] | Based on single-molecule FRET experiments and a detailed kinetic study of NC-promoted annealing of mini-TAR constructs, it was also proposed that multiple pathways might be involved. | true | true | true | true | true | 274 |
3 | INTRODUCTION | 1 | 59 | [
"B49 B50 B51",
"B52 B53 B54 B55",
"B56",
"B57",
"B48",
"B58",
"B32",
"B59"
] | 17,553,835 | pmid-15152202|pmid-15345057|pmid-16064056|pmid-8078946|pmid-10212256|pmid-10954609|pmid-10756194|pmid-11497429|pmid-15854644|pmid-16406407|pmid-16100256|pmid-16962137|pmid-17372205|pmid-11497429|pmid-10931958|pmid-17043221 | More recent studies with full-length TAR suggest that a zipper mechanism involving the lower stems and bulges is the major nucleation pathway for TAR annealing in the presence of NC (59) (Vo, M.-N., Rouzina, I. and Musier-Forsyth, K., in preparation). | [
"49–51",
"52–55",
"56",
"57",
"48",
"58",
"32",
"59"
] | 251 | 1,583 | 1 | false | More recent studies with full-length TAR suggest that a zipper mechanism involving the lower stems and bulges is the major nucleation pathway for TAR annealing in the presence of NC (Vo, M.-N., Rouzina, I. and Musier-Forsyth, K., in preparation). | [
"59"
] | More recent studies with full-length TAR suggest that a zipper mechanism involving the lower stems and bulges is the major nucleation pathway for TAR annealing in the presence of NC (Vo, M.-N., Rouzina, I. and Musier-Forsyth, K., in preparation). | true | true | true | true | true | 274 |
4 | INTRODUCTION | 1 | 24–26 | [
"B24 B25 B26",
"B59 B60 B61",
"B28",
"B32",
"B62 B63 B64 B65 B66 B67 B68 B69 B70 B71 B72 B73 B74",
"B19",
"B28",
"B28"
] | 17,553,835 | pmid-12684000|pmid-15099739|pmid-15454467|pmid-17372205|pmid-10982320|pmid-15542863|pmid-15271979|pmid-16962137|pmid-7666433|pmid-12097560|pmid-12595541|pmid-12783894|pmid-12595540|pmid-12801926|pmid-15342633|pmid-15218022|pmid-16092503|pmid-16216274|pmid-15751967|pmid-16291743|pmid-16782713|pmid-11922672|pmid-15271979|pmid-15271979 | The structure and thermostability of the nucleic acid intermediates are major determinants for NC-facilitated minus-strand transfer. | [
"24–26",
"59–61",
"28",
"32",
"62–74",
"19",
"28",
"28"
] | 132 | 1,584 | 0 | false | The structure and thermostability of the nucleic acid intermediates are major determinants for NC-facilitated minus-strand transfer. | [] | The structure and thermostability of the nucleic acid intermediates are major determinants for NC-facilitated minus-strand transfer. | true | true | true | true | true | 275 |
4 | INTRODUCTION | 1 | 24–26 | [
"B24 B25 B26",
"B59 B60 B61",
"B28",
"B32",
"B62 B63 B64 B65 B66 B67 B68 B69 B70 B71 B72 B73 B74",
"B19",
"B28",
"B28"
] | 17,553,835 | pmid-12684000|pmid-15099739|pmid-15454467|pmid-17372205|pmid-10982320|pmid-15542863|pmid-15271979|pmid-16962137|pmid-7666433|pmid-12097560|pmid-12595541|pmid-12783894|pmid-12595540|pmid-12801926|pmid-15342633|pmid-15218022|pmid-16092503|pmid-16216274|pmid-15751967|pmid-16291743|pmid-16782713|pmid-11922672|pmid-15271979|pmid-15271979 | A number of studies have emphasized the importance of maintaining the bulges in the TAR DNA structure of (−) SSDNA (24–26,59–61) as well as the critical role of acceptor RNA structure (28,32,62–74). | [
"24–26",
"59–61",
"28",
"32",
"62–74",
"19",
"28",
"28"
] | 198 | 1,585 | 0 | false | A number of studies have emphasized the importance of maintaining the bulges in the TAR DNA structure of (−) SSDNA as well as the critical role of acceptor RNA structure. | [
"24–26,59–61",
"28,32,62–74"
] | A number of studies have emphasized the importance of maintaining the bulges in the TAR DNA structure of (−) SSDNA as well as the critical role of acceptor RNA structure. | true | true | true | true | true | 275 |
4 | INTRODUCTION | 1 | 24–26 | [
"B24 B25 B26",
"B59 B60 B61",
"B28",
"B32",
"B62 B63 B64 B65 B66 B67 B68 B69 B70 B71 B72 B73 B74",
"B19",
"B28",
"B28"
] | 17,553,835 | pmid-12684000|pmid-15099739|pmid-15454467|pmid-17372205|pmid-10982320|pmid-15542863|pmid-15271979|pmid-16962137|pmid-7666433|pmid-12097560|pmid-12595541|pmid-12783894|pmid-12595540|pmid-12801926|pmid-15342633|pmid-15218022|pmid-16092503|pmid-16216274|pmid-15751967|pmid-16291743|pmid-16782713|pmid-11922672|pmid-15271979|pmid-15271979 | Interestingly, minus-strand transfer is more sensitive to the thermostability of acceptor RNA than to the stability and structure of (−) SSDNA (19,28). | [
"24–26",
"59–61",
"28",
"32",
"62–74",
"19",
"28",
"28"
] | 151 | 1,586 | 0 | false | Interestingly, minus-strand transfer is more sensitive to the thermostability of acceptor RNA than to the stability and structure of (−) SSDNA. | [
"19,28"
] | Interestingly, minus-strand transfer is more sensitive to the thermostability of acceptor RNA than to the stability and structure of (−) SSDNA. | true | true | true | true | true | 275 |
4 | INTRODUCTION | 1 | 28 | [
"B24 B25 B26",
"B59 B60 B61",
"B28",
"B32",
"B62 B63 B64 B65 B66 B67 B68 B69 B70 B71 B72 B73 B74",
"B19",
"B28",
"B28"
] | 17,553,835 | pmid-12684000|pmid-15099739|pmid-15454467|pmid-17372205|pmid-10982320|pmid-15542863|pmid-15271979|pmid-16962137|pmid-7666433|pmid-12097560|pmid-12595541|pmid-12783894|pmid-12595540|pmid-12801926|pmid-15342633|pmid-15218022|pmid-16092503|pmid-16216274|pmid-15751967|pmid-16291743|pmid-16782713|pmid-11922672|pmid-15271979|pmid-15271979 | These findings are consistent with NC's weak destabilizing activity (see above) and led to the conclusion that efficient minus-strand transfer requires a delicate thermodynamic balance between the structures of (−) SSDNA and acceptor RNA and the stability of the annealed RNA–DNA hybrid (28). | [
"24–26",
"59–61",
"28",
"32",
"62–74",
"19",
"28",
"28"
] | 292 | 1,587 | 1 | false | These findings are consistent with NC's weak destabilizing activity (see above) and led to the conclusion that efficient minus-strand transfer requires a delicate thermodynamic balance between the structures of (−) SSDNA and acceptor RNA and the stability of the annealed RNA–DNA hybrid. | [
"28"
] | These findings are consistent with NC's weak destabilizing activity (see above) and led to the conclusion that efficient minus-strand transfer requires a delicate thermodynamic balance between the structures of (−) SSDNA and acceptor RNA and the stability of the annealed RNA–DNA hybrid. | true | true | true | true | true | 275 |
5 | INTRODUCTION | 1 | 28 | [
"B28"
] | 17,553,835 | pmid-15271979|pmid-16164976|pmid-10233940 | In the present study, we have elucidated the paradoxical activity of two acceptor RNAs (RNA 70 and RNA 50) in minus-strand transfer: Despite the fact that RNA 70 has a higher predicted overall free energy of folding (ΔG) than RNA 50, more transfer product is synthesized with the RNA 70 acceptor than with RNA 50 in assays with the same (−) SSDNA (28). | [
"28"
] | 352 | 1,588 | 1 | false | In the present study, we have elucidated the paradoxical activity of two acceptor RNAs (RNA 70 and RNA 50) in minus-strand transfer: Despite the fact that RNA 70 has a higher predicted overall free energy of folding (ΔG) than RNA 50, more transfer product is synthesized with the RNA 70 acceptor than with RNA 50 in assays with the same (−) SSDNA. | [
"28"
] | In the present study, we have elucidated the paradoxical activity of two acceptor RNAs (RNA 70 and RNA 50) in minus-strand transfer: Despite the fact that RNA 70 has a higher predicted overall free energy of folding (ΔG) than RNA 50, more transfer product is synthesized with the RNA 70 acceptor than with RNA 50 in assays with the same (−) SSDNA. | true | true | true | true | true | 276 |
5 | INTRODUCTION | 1 | 28 | [
"B28"
] | 17,553,835 | pmid-15271979|pmid-16164976|pmid-10233940 | Based on extensive mutational analysis, we demonstrate for the first time that the local structure of acceptor RNA at potential nucleation sites, rather than overall thermodynamic stability, is a crucial determinant for NC chaperone activity during the minus-strand transfer step of reverse transcription. | [
"28"
] | 305 | 1,589 | 0 | false | Based on extensive mutational analysis, we demonstrate for the first time that the local structure of acceptor RNA at potential nucleation sites, rather than overall thermodynamic stability, is a crucial determinant for NC chaperone activity during the minus-strand transfer step of reverse transcription. | [] | Based on extensive mutational analysis, we demonstrate for the first time that the local structure of acceptor RNA at potential nucleation sites, rather than overall thermodynamic stability, is a crucial determinant for NC chaperone activity during the minus-strand transfer step of reverse transcription. | true | true | true | true | true | 276 |
6 | INTRODUCTION | 1 | 75 | [
"B75"
] | 17,553,835 | pmid-16394022|pmid-10982342|pmid-11932404 | We also show that in our reconstituted system, NC-mediated annealing is more efficient than strand transfer (i.e. | [
"75"
] | 113 | 1,590 | 0 | false | We also show that in our reconstituted system, NC-mediated annealing is more efficient than strand transfer (i.e. | [] | We also show that in our reconstituted system, NC-mediated annealing is more efficient than strand transfer (i.e. | true | true | true | true | true | 277 |
6 | INTRODUCTION | 1 | 75 | [
"B75"
] | 17,553,835 | pmid-16394022|pmid-10982342|pmid-11932404 | annealing plus reverse transcriptase (RT)-catalyzed elongation of minus-strand DNA). | [
"75"
] | 84 | 1,591 | 0 | false | annealing plus reverse transcriptase (RT)-catalyzed elongation of minus-strand DNA). | [] | annealing plus reverse transcriptase (RT)-catalyzed elongation of minus-strand DNA). | false | true | true | true | false | 277 |
6 | INTRODUCTION | 1 | 75 | [
"B75"
] | 17,553,835 | pmid-16394022|pmid-10982342|pmid-11932404 | Since RT activity (but not annealing) requires Mg2+ (75), it seemed likely that the lower values for strand transfer might be due to the presence of a high concentration of Mg2+ in strand transfer reactions. | [
"75"
] | 207 | 1,592 | 1 | false | Since RT activity (but not annealing) requires Mg2+, it seemed likely that the lower values for strand transfer might be due to the presence of a high concentration of Mg2+ in strand transfer reactions. | [
"75"
] | Since RT activity (but not annealing) requires Mg2+, it seemed likely that the lower values for strand transfer might be due to the presence of a high concentration of Mg2+ in strand transfer reactions. | true | true | true | true | true | 277 |
6 | INTRODUCTION | 1 | 75 | [
"B75"
] | 17,553,835 | pmid-16394022|pmid-10982342|pmid-11932404 | In fact, experiments presented below strongly suggest that Mg2+ competes with NC for binding to the negatively charged phosphodiester backbone in (−) SSDNA and acceptor RNA. | [
"75"
] | 173 | 1,593 | 0 | false | In fact, experiments presented below strongly suggest that Mg2+ competes with NC for binding to the negatively charged phosphodiester backbone in (−) SSDNA and acceptor RNA. | [] | In fact, experiments presented below strongly suggest that Mg2+ competes with NC for binding to the negatively charged phosphodiester backbone in (−) SSDNA and acceptor RNA. | true | true | true | true | true | 277 |
6 | INTRODUCTION | 1 | 75 | [
"B75"
] | 17,553,835 | pmid-16394022|pmid-10982342|pmid-11932404 | Finally, we present data indicating that for our system, destabilization of a secondary structure formed by the 5′ TAR RNA sequence and to a lesser extent, loop–loop interactions between TAR RNA and TAR DNA contribute to efficient minus-strand transfer. | [
"75"
] | 253 | 1,594 | 0 | false | Finally, we present data indicating that for our system, destabilization of a secondary structure formed by the 5′ TAR RNA sequence and to a lesser extent, loop–loop interactions between TAR RNA and TAR DNA contribute to efficient minus-strand transfer. | [] | Finally, we present data indicating that for our system, destabilization of a secondary structure formed by the 5′ TAR RNA sequence and to a lesser extent, loop–loop interactions between TAR RNA and TAR DNA contribute to efficient minus-strand transfer. | true | true | true | true | true | 277 |
0 | DISCUSSION | 1 | 28 | [
"B28",
"B28"
] | 17,553,835 | pmid-7500330|pmid-9757830|pmid-16164976|pmid-16164976|pmid-8443588|pmid-9430589|pmid-9499042|pmid-9769215|pmid-10606514|pmid-10924101|pmid-16434700|pmid-8057466|pmid-7545662|pmid-16164976|pmid-9057495|pmid-9465785|pmid-12954779|pmid-15854648|pmid-15854648|pmid-10982342|pmid-11344257|pmid-11922672|pmid-11932404|pmid-12054820|pmid-12084921|pmid-12581633|pmid-12684000|pmid-15099739|pmid-15454467|pmid-15033363|pmid-15271979|pmid-16077025|pmid-16997322|pmid-17029416|pmid-16962137|pmid-15271979|pmid-15271979 | The goal of the present study was to provide new insights into the mechanism of HIV-1 NC nucleic acid chaperone activity in the minus-strand transfer step of reverse transcription. | [
"28",
"28"
] | 180 | 1,595 | 0 | false | The goal of the present study was to provide new insights into the mechanism of HIV-1 NC nucleic acid chaperone activity in the minus-strand transfer step of reverse transcription. | [] | The goal of the present study was to provide new insights into the mechanism of HIV-1 NC nucleic acid chaperone activity in the minus-strand transfer step of reverse transcription. | true | true | true | true | true | 278 |
0 | DISCUSSION | 1 | 28 | [
"B28",
"B28"
] | 17,553,835 | pmid-7500330|pmid-9757830|pmid-16164976|pmid-16164976|pmid-8443588|pmid-9430589|pmid-9499042|pmid-9769215|pmid-10606514|pmid-10924101|pmid-16434700|pmid-8057466|pmid-7545662|pmid-16164976|pmid-9057495|pmid-9465785|pmid-12954779|pmid-15854648|pmid-15854648|pmid-10982342|pmid-11344257|pmid-11922672|pmid-11932404|pmid-12054820|pmid-12084921|pmid-12581633|pmid-12684000|pmid-15099739|pmid-15454467|pmid-15033363|pmid-15271979|pmid-16077025|pmid-16997322|pmid-17029416|pmid-16962137|pmid-15271979|pmid-15271979 | Our approach was to use a reconstituted system with model substrates described in an earlier report (28), since their structures are not overly complex and are therefore especially suitable for mutagenic analysis (Figure 2). | [
"28",
"28"
] | 224 | 1,596 | 1 | false | Our approach was to use a reconstituted system with model substrates described in an earlier report, since their structures are not overly complex and are therefore especially suitable for mutagenic analysis (Figure 2). | [
"28"
] | Our approach was to use a reconstituted system with model substrates described in an earlier report, since their structures are not overly complex and are therefore especially suitable for mutagenic analysis. | true | true | true | true | true | 278 |
0 | DISCUSSION | 1 | 28 | [
"B28",
"B28"
] | 17,553,835 | pmid-7500330|pmid-9757830|pmid-16164976|pmid-16164976|pmid-8443588|pmid-9430589|pmid-9499042|pmid-9769215|pmid-10606514|pmid-10924101|pmid-16434700|pmid-8057466|pmid-7545662|pmid-16164976|pmid-9057495|pmid-9465785|pmid-12954779|pmid-15854648|pmid-15854648|pmid-10982342|pmid-11344257|pmid-11922672|pmid-11932404|pmid-12054820|pmid-12084921|pmid-12581633|pmid-12684000|pmid-15099739|pmid-15454467|pmid-15033363|pmid-15271979|pmid-16077025|pmid-16997322|pmid-17029416|pmid-16962137|pmid-15271979|pmid-15271979 | We initially focused on the question of whether efficient strand transfer is determined by the overall thermodynamic stability and structure of acceptor RNA or more directly, by local structure at the nucleation site. | [
"28",
"28"
] | 217 | 1,597 | 0 | false | We initially focused on the question of whether efficient strand transfer is determined by the overall thermodynamic stability and structure of acceptor RNA or more directly, by local structure at the nucleation site. | [] | We initially focused on the question of whether efficient strand transfer is determined by the overall thermodynamic stability and structure of acceptor RNA or more directly, by local structure at the nucleation site. | true | true | true | true | true | 278 |
0 | DISCUSSION | 1 | 28 | [
"B28",
"B28"
] | 17,553,835 | pmid-7500330|pmid-9757830|pmid-16164976|pmid-16164976|pmid-8443588|pmid-9430589|pmid-9499042|pmid-9769215|pmid-10606514|pmid-10924101|pmid-16434700|pmid-8057466|pmid-7545662|pmid-16164976|pmid-9057495|pmid-9465785|pmid-12954779|pmid-15854648|pmid-15854648|pmid-10982342|pmid-11344257|pmid-11922672|pmid-11932404|pmid-12054820|pmid-12084921|pmid-12581633|pmid-12684000|pmid-15099739|pmid-15454467|pmid-15033363|pmid-15271979|pmid-16077025|pmid-16997322|pmid-17029416|pmid-16962137|pmid-15271979|pmid-15271979 | In assays with RNA 70 and RNA 50, we found that the higher strand transfer activity exhibited by RNA 70 is correlated with the local stem-loop structure at the 5′ end of the TAR sequence, which contains 11 bases complementary to an 11-nt single-stranded region in DNA 50 (Figure 2), and not with RNA 70's predicted overall thermodynamic stability, which is actually considerably higher than that of RNA 50 (Figure 2A) (28). | [
"28",
"28"
] | 423 | 1,598 | 1 | false | In assays with RNA 70 and RNA 50, we found that the higher strand transfer activity exhibited by RNA 70 is correlated with the local stem-loop structure at the 5′ end of the TAR sequence, which contains 11 bases complementary to an 11-nt single-stranded region in DNA 50 (Figure 2), and not with RNA 70's predicted overall thermodynamic stability, which is actually considerably higher than that of RNA 50 (Figure 2A). | [
"28"
] | In assays with RNA 70 and RNA 50, we found that the higher strand transfer activity exhibited by RNA 70 is correlated with the local stem-loop structure at the 5′ end of the TAR sequence, which contains 11 bases complementary to an 11-nt single-stranded region in DNA 50, and not with RNA 70's predicted overall thermodynamic stability, which is actually considerably higher than that of RNA 50. | true | true | true | true | true | 278 |
1 | DISCUSSION | 1 | 27 | [
"B27",
"B61",
"B69",
"B73"
] | 17,553,835 | pmid-9757830|pmid-16164976|pmid-12206453|pmid-10924101|pmid-9933645|pmid-10233940|pmid-11786014|pmid-15327946|pmid-16314282|pmid-16164976|NA|pmid-15033363|pmid-15542863|pmid-15218022|pmid-16291743 | In further support of our ideas, the data clearly demonstrated that stabilizing mutations in the relevant local structure dramatically reduce the rate and extent of strand transfer and increase dependence on NC (Figures 3 and 4), whereas destabilizing mutations lead to a marked increase in strand transfer efficiency and loss of the NC requirement (Figure 3). | [
"27",
"61",
"69",
"73"
] | 360 | 1,599 | 0 | false | In further support of our ideas, the data clearly demonstrated that stabilizing mutations in the relevant local structure dramatically reduce the rate and extent of strand transfer and increase dependence on NC (Figures 3 and 4), whereas destabilizing mutations lead to a marked increase in strand transfer efficiency and loss of the NC requirement (Figure 3). | [] | In further support of our ideas, the data clearly demonstrated that stabilizing mutations in the relevant local structure dramatically reduce the rate and extent of strand transfer and increase dependence on NC (Figures 3 and 4), whereas destabilizing mutations lead to a marked increase in strand transfer efficiency and loss of the NC requirement (Figure 3). | true | true | true | true | true | 279 |
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