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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
2 | INTRODUCTION | 1 | 5 | [
"b5",
"b6",
"b7",
"b4",
"b8"
] | 17,130,147 | pmid-15103394|pmid-15860772|pmid-9521921|pmid-16914452|pmid-15273986 | We constructed this database exclusively using our unique dataset of completely sequenced and carefully annotated full-length cDNAs, which was produced by a human annotation meeting, H-Invitational (5,6). | [
"5",
"6",
"7",
"4",
"8"
] | 204 | 4,400 | 0 | false | We constructed this database exclusively using our unique dataset of completely sequenced and carefully annotated full-length cDNAs, which was produced by a human annotation meeting, H-Invitational. | [
"5,6"
] | We constructed this database exclusively using our unique dataset of completely sequenced and carefully annotated full-length cDNAs, which was produced by a human annotation meeting, H-Invitational. | true | true | true | true | true | 747 |
2 | INTRODUCTION | 1 | 5 | [
"b5",
"b6",
"b7",
"b4",
"b8"
] | 17,130,147 | pmid-15103394|pmid-15860772|pmid-9521921|pmid-16914452|pmid-15273986 | In H-Invitational, 56β419 cDNA sequences of human genes, which were fully sequenced with a sequence reliability higher than 99% [Phred values greater than 30; (7)] and whose potentially problematic sequences such as vectors and polyA tails were precisely trimmed, were subjected to manual annotation of AS variants. | [
"5",
"6",
"7",
"4",
"8"
] | 315 | 4,401 | 0 | false | In H-Invitational, 56 419 cDNA sequences of human genes, which were fully sequenced with a sequence reliability higher than 99% and whose potentially problematic sequences such as vectors and polyA tails were precisely trimmed, were subjected to manual annotation of AS variants. | [
"Phred values greater than 30; (7)"
] | In H-Invitational, 56 419 cDNA sequences of human genes, which were fully sequenced with a sequence reliability higher than 99% and whose potentially problematic sequences such as vectors and polyA tails were precisely trimmed, were subjected to manual annotation of AS variants. | true | true | true | true | true | 747 |
2 | INTRODUCTION | 1 | 4 | [
"b5",
"b6",
"b7",
"b4",
"b8"
] | 17,130,147 | pmid-15103394|pmid-15860772|pmid-9521921|pmid-16914452|pmid-15273986 | These cDNAs were clustered into 24β425 loci and of these, 6877 AS-containing loci, represented by 18β297 AS variants, were identified (4). | [
"5",
"6",
"7",
"4",
"8"
] | 138 | 4,402 | 1 | false | These cDNAs were clustered into 24 425 loci and of these, 6877 AS-containing loci, represented by 18 297 AS variants, were identified. | [
"4"
] | These cDNAs were clustered into 24 425 loci and of these, 6877 AS-containing loci, represented by 18 297 AS variants, were identified. | true | true | true | true | true | 747 |
2 | INTRODUCTION | 1 | 5 | [
"b5",
"b6",
"b7",
"b4",
"b8"
] | 17,130,147 | pmid-15103394|pmid-15860772|pmid-9521921|pmid-16914452|pmid-15273986 | As a specialized AS database, H-DBAS enables multifaceted analyses from various viewpoints, comprehensively aiming at elucidating functional consequences of widespread AS in human genes. | [
"5",
"6",
"7",
"4",
"8"
] | 186 | 4,403 | 0 | false | As a specialized AS database, H-DBAS enables multifaceted analyses from various viewpoints, comprehensively aiming at elucidating functional consequences of widespread AS in human genes. | [] | As a specialized AS database, H-DBAS enables multifaceted analyses from various viewpoints, comprehensively aiming at elucidating functional consequences of widespread AS in human genes. | true | true | true | true | true | 747 |
2 | INTRODUCTION | 1 | 5 | [
"b5",
"b6",
"b7",
"b4",
"b8"
] | 17,130,147 | pmid-15103394|pmid-15860772|pmid-9521921|pmid-16914452|pmid-15273986 | [Note: We will use the word, βlocusβ, for the transcript cluster for the purpose of simplicity. | [
"5",
"6",
"7",
"4",
"8"
] | 95 | 4,404 | 0 | false | [Note: We will use the word, βlocusβ, for the transcript cluster for the purpose of simplicity. | [] | [Note: We will use the word, βlocusβ, for the transcript cluster for the purpose of simplicity. | false | false | true | true | false | 747 |
2 | INTRODUCTION | 1 | 5 | [
"b5",
"b6",
"b7",
"b4",
"b8"
] | 17,130,147 | pmid-15103394|pmid-15860772|pmid-9521921|pmid-16914452|pmid-15273986 | However, the wording might be reconsidered, having observed highly diverse nature of the human transcriptome. | [
"5",
"6",
"7",
"4",
"8"
] | 109 | 4,405 | 0 | false | However, the wording might be reconsidered, having observed highly diverse nature of the human transcriptome. | [] | However, the wording might be reconsidered, having observed highly diverse nature of the human transcriptome. | true | true | true | true | true | 747 |
2 | INTRODUCTION | 1 | 8 | [
"b5",
"b6",
"b7",
"b4",
"b8"
] | 17,130,147 | pmid-15103394|pmid-15860772|pmid-9521921|pmid-16914452|pmid-15273986 | Also see the reference (8)]. | [
"5",
"6",
"7",
"4",
"8"
] | 28 | 4,406 | 1 | false | Also see the reference ]. | [
"8"
] | Also see the reference ]. | true | true | true | true | true | 747 |
0 | INTRODUCTION | 1 | 1β3 | [
"B1 B2 B3",
"B4",
"B5"
] | 17,631,616 | pmid-9361437|pmid-11243261|pmid-12571013|pmid-19719582|pmid-16957182 | Terminal restriction fragment length polymorphism (T-RFLP) analysis is a microbial fingerprinting technique capable of discriminating microbial communities quickly and relatively inexpensively (1β3). | [
"1β3",
"4",
"5"
] | 199 | 4,407 | 1 | false | Terminal restriction fragment length polymorphism (T-RFLP) analysis is a microbial fingerprinting technique capable of discriminating microbial communities quickly and relatively inexpensively. | [
"1β3"
] | Terminal restriction fragment length polymorphism (T-RFLP) analysis is a microbial fingerprinting technique capable of discriminating microbial communities quickly and relatively inexpensively. | true | true | true | true | true | 748 |
0 | INTRODUCTION | 1 | 1β3 | [
"B1 B2 B3",
"B4",
"B5"
] | 17,631,616 | pmid-9361437|pmid-11243261|pmid-12571013|pmid-19719582|pmid-16957182 | T-RFLP is increasingly used in high-throughput studies of microbial communities in combination with or even in lieu of clone library analysis (4,5). | [
"1β3",
"4",
"5"
] | 148 | 4,408 | 0 | false | T-RFLP is increasingly used in high-throughput studies of microbial communities in combination with or even in lieu of clone library analysis. | [
"4,5"
] | T-RFLP is increasingly used in high-throughput studies of microbial communities in combination with or even in lieu of clone library analysis. | true | true | true | true | true | 748 |
0 | INTRODUCTION | 1 | 1β3 | [
"B1 B2 B3",
"B4",
"B5"
] | 17,631,616 | pmid-9361437|pmid-11243261|pmid-12571013|pmid-19719582|pmid-16957182 | Briefly, the method involves PCR amplification of a gene of interest (often 16S rRNA genes) with fluorescent dye-labeled primers, followed by multiple single restriction digests done in parallel. | [
"1β3",
"4",
"5"
] | 195 | 4,409 | 0 | false | Briefly, the method involves PCR amplification of a gene of interest (often 16S rRNA genes) with fluorescent dye-labeled primers, followed by multiple single restriction digests done in parallel. | [] | Briefly, the method involves PCR amplification of a gene of interest with fluorescent dye-labeled primers, followed by multiple single restriction digests done in parallel. | true | true | true | true | true | 748 |
0 | INTRODUCTION | 1 | 1β3 | [
"B1 B2 B3",
"B4",
"B5"
] | 17,631,616 | pmid-9361437|pmid-11243261|pmid-12571013|pmid-19719582|pmid-16957182 | The resulting fragments are then separated by capillary electrophoresis with an internal size standard to determine the lengths of the terminal (fluorescently labeled) fragments. | [
"1β3",
"4",
"5"
] | 178 | 4,410 | 0 | false | The resulting fragments are then separated by capillary electrophoresis with an internal size standard to determine the lengths of the terminal (fluorescently labeled) fragments. | [] | The resulting fragments are then separated by capillary electrophoresis with an internal size standard to determine the lengths of the terminal (fluorescently labeled) fragments. | true | true | true | true | true | 748 |
0 | INTRODUCTION | 1 | 1β3 | [
"B1 B2 B3",
"B4",
"B5"
] | 17,631,616 | pmid-9361437|pmid-11243261|pmid-12571013|pmid-19719582|pmid-16957182 | Each distinct terminal restriction fragment is considered an operational taxonomic unit (OTU), thus the choice of restriction enzymes can impact the number of OTUs observed in each sample and the calculation of diversity statistics. | [
"1β3",
"4",
"5"
] | 232 | 4,411 | 0 | false | Each distinct terminal restriction fragment is considered an operational taxonomic unit (OTU), thus the choice of restriction enzymes can impact the number of OTUs observed in each sample and the calculation of diversity statistics. | [] | Each distinct terminal restriction fragment is considered an operational taxonomic unit (OTU), thus the choice of restriction enzymes can impact the number of OTUs observed in each sample and the calculation of diversity statistics. | true | true | true | true | true | 748 |
1 | INTRODUCTION | 1 | 6 | [
"B6",
"B1 B2 B3 B4 B5",
"B7 B8 B9 B10 B11 B12 B13 B14 B15 B16 B17 B18 B19 B20 B21 B22 B23 B24 B25 B26",
"B1",
"B2",
"B17"
] | 17,631,616 | pmid-12902276|pmid-9361437|pmid-11243261|pmid-12571013|pmid-19719582|pmid-16957182|pmid-10568840|pmid-10877790|pmid-11233162|NA|pmid-15880891|pmid-19712409|pmid-15767011|pmid-16269735|pmid-15746346|pmid-17064266|pmid-16957219|pmid-17142382|pmid-17041161|pmid-16944345|pmid-17023024|pmid-16957254|pmid-16461676|pmid-17196... | When analyzing uncharacterized and very diverse bacterial communities, sufficient community discrimination can often be accomplished with multiple randomly-chosen tetrameric restriction enzymes (6). | [
"6",
"1β5",
"7β26",
"1",
"2",
"17"
] | 198 | 4,412 | 1 | false | When analyzing uncharacterized and very diverse bacterial communities, sufficient community discrimination can often be accomplished with multiple randomly-chosen tetrameric restriction enzymes. | [
"6"
] | When analyzing uncharacterized and very diverse bacterial communities, sufficient community discrimination can often be accomplished with multiple randomly-chosen tetrameric restriction enzymes. | true | true | true | true | true | 749 |
1 | INTRODUCTION | 1 | 6 | [
"B6",
"B1 B2 B3 B4 B5",
"B7 B8 B9 B10 B11 B12 B13 B14 B15 B16 B17 B18 B19 B20 B21 B22 B23 B24 B25 B26",
"B1",
"B2",
"B17"
] | 17,631,616 | pmid-12902276|pmid-9361437|pmid-11243261|pmid-12571013|pmid-19719582|pmid-16957182|pmid-10568840|pmid-10877790|pmid-11233162|NA|pmid-15880891|pmid-19712409|pmid-15767011|pmid-16269735|pmid-15746346|pmid-17064266|pmid-16957219|pmid-17142382|pmid-17041161|pmid-16944345|pmid-17023024|pmid-16957254|pmid-16461676|pmid-17196... | However, a brief review of the literature indicates that there is still no standard in even this simplified case. | [
"6",
"1β5",
"7β26",
"1",
"2",
"17"
] | 113 | 4,413 | 0 | false | However, a brief review of the literature indicates that there is still no standard in even this simplified case. | [] | However, a brief review of the literature indicates that there is still no standard in even this simplified case. | true | true | true | true | true | 749 |
1 | INTRODUCTION | 1 | 6 | [
"B6",
"B1 B2 B3 B4 B5",
"B7 B8 B9 B10 B11 B12 B13 B14 B15 B16 B17 B18 B19 B20 B21 B22 B23 B24 B25 B26",
"B1",
"B2",
"B17"
] | 17,631,616 | pmid-12902276|pmid-9361437|pmid-11243261|pmid-12571013|pmid-19719582|pmid-16957182|pmid-10568840|pmid-10877790|pmid-11233162|NA|pmid-15880891|pmid-19712409|pmid-15767011|pmid-16269735|pmid-15746346|pmid-17064266|pmid-16957219|pmid-17142382|pmid-17041161|pmid-16944345|pmid-17023024|pmid-16957254|pmid-16461676|pmid-17196... | We examined 26 papers (1β5,7β26) that were published between 1997 and 2007 and used T-RFLP. | [
"6",
"1β5",
"7β26",
"1",
"2",
"17"
] | 91 | 4,414 | 0 | false | We examined 26 papers that were published between 1997 and 2007 and used T-RFLP. | [
"1β5,7β26"
] | We examined 26 papers that were published between 1997 and 2007 and used T-RFLP. | true | true | true | true | true | 749 |
1 | INTRODUCTION | 1 | 6 | [
"B6",
"B1 B2 B3 B4 B5",
"B7 B8 B9 B10 B11 B12 B13 B14 B15 B16 B17 B18 B19 B20 B21 B22 B23 B24 B25 B26",
"B1",
"B2",
"B17"
] | 17,631,616 | pmid-12902276|pmid-9361437|pmid-11243261|pmid-12571013|pmid-19719582|pmid-16957182|pmid-10568840|pmid-10877790|pmid-11233162|NA|pmid-15880891|pmid-19712409|pmid-15767011|pmid-16269735|pmid-15746346|pmid-17064266|pmid-16957219|pmid-17142382|pmid-17041161|pmid-16944345|pmid-17023024|pmid-16957254|pmid-16461676|pmid-17196... | Of those papers, 38% used universal bacterial primers combined with a single restriction enzyme, but the choice of enzyme was not consistent. | [
"6",
"1β5",
"7β26",
"1",
"2",
"17"
] | 141 | 4,415 | 0 | false | Of those papers, 38% used universal bacterial primers combined with a single restriction enzyme, but the choice of enzyme was not consistent. | [] | Of those papers, 38% used universal bacterial primers combined with a single restriction enzyme, but the choice of enzyme was not consistent. | true | true | true | true | true | 749 |
1 | INTRODUCTION | 1 | 6 | [
"B6",
"B1 B2 B3 B4 B5",
"B7 B8 B9 B10 B11 B12 B13 B14 B15 B16 B17 B18 B19 B20 B21 B22 B23 B24 B25 B26",
"B1",
"B2",
"B17"
] | 17,631,616 | pmid-12902276|pmid-9361437|pmid-11243261|pmid-12571013|pmid-19719582|pmid-16957182|pmid-10568840|pmid-10877790|pmid-11233162|NA|pmid-15880891|pmid-19712409|pmid-15767011|pmid-16269735|pmid-15746346|pmid-17064266|pmid-16957219|pmid-17142382|pmid-17041161|pmid-16944345|pmid-17023024|pmid-16957254|pmid-16461676|pmid-17196... | MspI was used most frequently (four studies), followed by TaqI (two studies), and one study each used AluI, CfoI, HhaI and HaeIII. | [
"6",
"1β5",
"7β26",
"1",
"2",
"17"
] | 130 | 4,416 | 0 | false | MspI was used most frequently (four studies), followed by TaqI (two studies), and one study each used AluI, CfoI, HhaI and HaeIII. | [] | MspI was used most frequently (four studies), followed by TaqI (two studies), and one study each used AluI, CfoI, HhaI and HaeIII. | true | true | true | true | true | 749 |
1 | INTRODUCTION | 1 | 6 | [
"B6",
"B1 B2 B3 B4 B5",
"B7 B8 B9 B10 B11 B12 B13 B14 B15 B16 B17 B18 B19 B20 B21 B22 B23 B24 B25 B26",
"B1",
"B2",
"B17"
] | 17,631,616 | pmid-12902276|pmid-9361437|pmid-11243261|pmid-12571013|pmid-19719582|pmid-16957182|pmid-10568840|pmid-10877790|pmid-11233162|NA|pmid-15880891|pmid-19712409|pmid-15767011|pmid-16269735|pmid-15746346|pmid-17064266|pmid-16957219|pmid-17142382|pmid-17041161|pmid-16944345|pmid-17023024|pmid-16957254|pmid-16461676|pmid-17196... | Overall, only three of the 26 papers included a rationalization of enzyme selection (1,2,17). | [
"6",
"1β5",
"7β26",
"1",
"2",
"17"
] | 93 | 4,417 | 0 | false | Overall, only three of the 26 papers included a rationalization of enzyme selection. | [
"1,2,17"
] | Overall, only three of the 26 papers included a rationalization of enzyme selection. | true | true | true | true | true | 749 |
2 | INTRODUCTION | 0 | null | null | 17,631,616 | null | An alternate approach to T-RFLP can be taken if the microbial community has been characterized (by clone library analysis or by prediction from previous studies) or if a particular taxonomic group is being targeted with specific primers. | null | 237 | 4,418 | 0 | false | null | null | An alternate approach to T-RFLP can be taken if the microbial community has been characterized (by clone library analysis or by prediction from previous studies) or if a particular taxonomic group is being targeted with specific primers. | true | true | true | true | true | 750 |
2 | INTRODUCTION | 0 | null | null | 17,631,616 | null | In this case, a more reasoned choice of restriction enzymes can be conducted. | null | 77 | 4,419 | 0 | false | null | null | In this case, a more reasoned choice of restriction enzymes can be conducted. | true | true | true | true | true | 750 |
2 | INTRODUCTION | 0 | null | null | 17,631,616 | null | In particular, specific species or microbial taxa of interest to the researcherβparticularly closely related taxa that may share some restriction sitesβcan often be differentiated if the proper restriction enzymes are selected. | null | 227 | 4,420 | 0 | false | null | null | In particular, specific species or microbial taxa of interest to the researcherβparticularly closely related taxa that may share some restriction sitesβcan often be differentiated if the proper restriction enzymes are selected. | true | true | true | true | true | 750 |
3 | INTRODUCTION | 1 | 27 | [
"B27",
"B28",
"B29",
"B30"
] | 17,631,616 | pmid-17202163|pmid-10919828|pmid-15746378|pmid-16787976 | There are, however, few resources available to narrow down the selection process. | [
"27",
"28",
"29",
"30"
] | 81 | 4,421 | 0 | false | There are, however, few resources available to narrow down the selection process. | [] | There are, however, few resources available to narrow down the selection process. | true | true | true | true | true | 751 |
3 | INTRODUCTION | 1 | 27 | [
"B27",
"B28",
"B29",
"B30"
] | 17,631,616 | pmid-17202163|pmid-10919828|pmid-15746378|pmid-16787976 | Over 600 Type II restriction enzymes are commercially available, accounting for 262 distinct specificities (27). | [
"27",
"28",
"29",
"30"
] | 112 | 4,422 | 1 | false | Over 600 Type II restriction enzymes are commercially available, accounting for 262 distinct specificities. | [
"27"
] | Over 600 Type II restriction enzymes are commercially available, accounting for 262 distinct specificities. | true | true | true | true | true | 751 |
3 | INTRODUCTION | 1 | 28 | [
"B27",
"B28",
"B29",
"B30"
] | 17,631,616 | pmid-17202163|pmid-10919828|pmid-15746378|pmid-16787976 | Existing computer programs for assisting in the choice of restriction enzymes include TAP-TRFLP (28), MiCA Enzyme Resolving Power Analysis (http://mica.ibest.uidaho.edu) and TRF-CUT (29). | [
"27",
"28",
"29",
"30"
] | 187 | 4,423 | 1 | false | Existing computer programs for assisting in the choice of restriction enzymes include TAP-TRFLP, MiCA Enzyme Resolving Power Analysis (http://mica.ibest.uidaho.edu) and TRF-CUT. | [
"28",
"29"
] | Existing computer programs for assisting in the choice of restriction enzymes include TAP-TRFLP, MiCA Enzyme Resolving Power Analysis (http://mica.ibest.uidaho.edu) and TRF-CUT. | true | true | true | true | true | 751 |
3 | INTRODUCTION | 1 | 27 | [
"B27",
"B28",
"B29",
"B30"
] | 17,631,616 | pmid-17202163|pmid-10919828|pmid-15746378|pmid-16787976 | These programs perform in silico restriction digestions of a predefined sequence database or user-provided sequences, but these results must still be manually examined to determine which enzymes are best suited to discriminate that set of sequences. | [
"27",
"28",
"29",
"30"
] | 249 | 4,424 | 0 | false | These programs perform in silico restriction digestions of a predefined sequence database or user-provided sequences, but these results must still be manually examined to determine which enzymes are best suited to discriminate that set of sequences. | [] | These programs perform in silico restriction digestions of a predefined sequence database or user-provided sequences, but these results must still be manually examined to determine which enzymes are best suited to discriminate that set of sequences. | true | true | true | true | true | 751 |
3 | INTRODUCTION | 1 | 30 | [
"B27",
"B28",
"B29",
"B30"
] | 17,631,616 | pmid-17202163|pmid-10919828|pmid-15746378|pmid-16787976 | CLEAVER (30), a stand alone program, provides the above features as well as the ability to assign sequences to taxonomic groups at multiple levels and to search for enzymes that cut one group but not another group. | [
"27",
"28",
"29",
"30"
] | 214 | 4,425 | 1 | false | CLEAVER, a stand alone program, provides the above features as well as the ability to assign sequences to taxonomic groups at multiple levels and to search for enzymes that cut one group but not another group. | [
"30"
] | CLEAVER, a stand alone program, provides the above features as well as the ability to assign sequences to taxonomic groups at multiple levels and to search for enzymes that cut one group but not another group. | true | true | true | true | true | 751 |
3 | INTRODUCTION | 1 | 27 | [
"B27",
"B28",
"B29",
"B30"
] | 17,631,616 | pmid-17202163|pmid-10919828|pmid-15746378|pmid-16787976 | However, it is limited to comparing only two groups at once. | [
"27",
"28",
"29",
"30"
] | 60 | 4,426 | 0 | false | However, it is limited to comparing only two groups at once. | [] | However, it is limited to comparing only two groups at once. | true | true | true | true | true | 751 |
3 | INTRODUCTION | 1 | 27 | [
"B27",
"B28",
"B29",
"B30"
] | 17,631,616 | pmid-17202163|pmid-10919828|pmid-15746378|pmid-16787976 | Restriction Endonuclease Picker (REPK) addresses this gap by finding enzymes that are able to discriminate an unlimited number of user-designated sequence groups on the basis of their terminal restriction fragment lengths. | [
"27",
"28",
"29",
"30"
] | 222 | 4,427 | 0 | false | Restriction Endonuclease Picker (REPK) addresses this gap by finding enzymes that are able to discriminate an unlimited number of user-designated sequence groups on the basis of their terminal restriction fragment lengths. | [] | Restriction Endonuclease Picker (REPK) addresses this gap by finding enzymes that are able to discriminate an unlimited number of user-designated sequence groups on the basis of their terminal restriction fragment lengths. | true | true | true | true | true | 751 |
3 | INTRODUCTION | 1 | 27 | [
"B27",
"B28",
"B29",
"B30"
] | 17,631,616 | pmid-17202163|pmid-10919828|pmid-15746378|pmid-16787976 | If no single enzyme can discriminate all groups, REPK reports sets of four restriction enzymes that together are able to differentiate the groups of interest. | [
"27",
"28",
"29",
"30"
] | 158 | 4,428 | 0 | false | If no single enzyme can discriminate all groups, REPK reports sets of four restriction enzymes that together are able to differentiate the groups of interest. | [] | If no single enzyme can discriminate all groups, REPK reports sets of four restriction enzymes that together are able to differentiate the groups of interest. | true | true | true | true | true | 751 |
3 | INTRODUCTION | 1 | 27 | [
"B27",
"B28",
"B29",
"B30"
] | 17,631,616 | pmid-17202163|pmid-10919828|pmid-15746378|pmid-16787976 | An important component of REPK is this ability to specify the taxonomic rank of sequences to be differentiated, which is particularly useful in the case where a diverse microbial community has been characterized by clone library analysis or there is an existing database of several subgroups of sequences that amplify wi... | [
"27",
"28",
"29",
"30"
] | 349 | 4,429 | 0 | false | An important component of REPK is this ability to specify the taxonomic rank of sequences to be differentiated, which is particularly useful in the case where a diverse microbial community has been characterized by clone library analysis or there is an existing database of several subgroups of sequences that amplify wi... | [] | An important component of REPK is this ability to specify the taxonomic rank of sequences to be differentiated, which is particularly useful in the case where a diverse microbial community has been characterized by clone library analysis or there is an existing database of several subgroups of sequences that amplify wi... | true | true | true | true | true | 751 |
0 | INTRODUCTION | 1 | 3 | [
"B1",
"B2",
"B3",
"B4",
"B5",
"B6",
"B7",
"B8",
"B9",
"B10",
"B11"
] | 17,567,602 | pmid-6297745|pmid-6197186|NA|pmid-7521014|pmid-16274247|pmid-11459506|pmid-7723823|pmid-8849775|pmid-9288965|pmid-16125106|pmid-12910259 | The discovery of naturally occurring RNA enzymes (ribozymes) (1,2) has postulated so-called the RNA world where RNAs could have served both genetic and catalytic roles (3). | [
"1",
"2",
"3",
"4",
"5",
"6",
"7",
"8",
"9",
"10",
"11"
] | 172 | 4,430 | 1 | false | The discovery of naturally occurring RNA enzymes (ribozymes) has postulated so-called the RNA world where RNAs could have served both genetic and catalytic roles. | [
"1,2",
"3"
] | The discovery of naturally occurring RNA enzymes (ribozymes) has postulated so-called the RNA world where RNAs could have served both genetic and catalytic roles. | true | true | true | true | true | 752 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5",
"B6",
"B7",
"B8",
"B9",
"B10",
"B11"
] | 17,567,602 | pmid-6297745|pmid-6197186|NA|pmid-7521014|pmid-16274247|pmid-11459506|pmid-7723823|pmid-8849775|pmid-9288965|pmid-16125106|pmid-12910259 | This notion has motivated us to not only search more ribozymes from nature (in vivo) but also artificially generate ribozymes in vitro with a wide variety of catalytic functions. | [
"1",
"2",
"3",
"4",
"5",
"6",
"7",
"8",
"9",
"10",
"11"
] | 178 | 4,431 | 0 | false | This notion has motivated us to not only search more ribozymes from nature (in vivo) but also artificially generate ribozymes in vitro with a wide variety of catalytic functions. | [] | This notion has motivated us to not only search more ribozymes from nature (in vivo) but also artificially generate ribozymes in vitro with a wide variety of catalytic functions. | true | true | true | true | true | 752 |
0 | INTRODUCTION | 1 | 6 | [
"B1",
"B2",
"B3",
"B4",
"B5",
"B6",
"B7",
"B8",
"B9",
"B10",
"B11"
] | 17,567,602 | pmid-6297745|pmid-6197186|NA|pmid-7521014|pmid-16274247|pmid-11459506|pmid-7723823|pmid-8849775|pmid-9288965|pmid-16125106|pmid-12910259 | Representative examples include phosphoryl transfer (4,5), acylation (6), alkylation (7,8), Diels-Alder (9), aldol (10) and redox (11) reactions. | [
"1",
"2",
"3",
"4",
"5",
"6",
"7",
"8",
"9",
"10",
"11"
] | 145 | 4,432 | 1 | false | Representative examples include phosphoryl transfer, acylation, alkylation, Diels-Alder, aldol and redox reactions. | [
"4,5",
"6",
"7,8",
"9",
"10",
"11"
] | Representative examples include phosphoryl transfer, acylation, alkylation, Diels-Alder, aldol and redox reactions. | true | true | true | true | true | 752 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5",
"B6",
"B7",
"B8",
"B9",
"B10",
"B11"
] | 17,567,602 | pmid-6297745|pmid-6197186|NA|pmid-7521014|pmid-16274247|pmid-11459506|pmid-7723823|pmid-8849775|pmid-9288965|pmid-16125106|pmid-12910259 | Among them, in vitro selection of ribozymes that utilize nucleotide triphosphates (NTPs) has been of great interest since NTPs are playing diverse but essential roles in biological systems. | [
"1",
"2",
"3",
"4",
"5",
"6",
"7",
"8",
"9",
"10",
"11"
] | 189 | 4,433 | 0 | false | Among them, in vitro selection of ribozymes that utilize nucleotide triphosphates (NTPs) has been of great interest since NTPs are playing diverse but essential roles in biological systems. | [] | Among them, in vitro selection of ribozymes that utilize nucleotide triphosphates (NTPs) has been of great interest since NTPs are playing diverse but essential roles in biological systems. | true | true | true | true | true | 752 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5",
"B6",
"B7",
"B8",
"B9",
"B10",
"B11"
] | 17,567,602 | pmid-6297745|pmid-6197186|NA|pmid-7521014|pmid-16274247|pmid-11459506|pmid-7723823|pmid-8849775|pmid-9288965|pmid-16125106|pmid-12910259 | ATP, for example, is one of the building blocks of RNA and at the same time serves an energy or a phosphate source as well as in cofactors. | [
"1",
"2",
"3",
"4",
"5",
"6",
"7",
"8",
"9",
"10",
"11"
] | 139 | 4,434 | 0 | false | ATP, for example, is one of the building blocks of RNA and at the same time serves an energy or a phosphate source as well as in cofactors. | [] | ATP, for example, is one of the building blocks of RNA and at the same time serves an energy or a phosphate source as well as in cofactors. | true | true | true | true | true | 752 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5",
"B6",
"B7",
"B8",
"B9",
"B10",
"B11"
] | 17,567,602 | pmid-6297745|pmid-6197186|NA|pmid-7521014|pmid-16274247|pmid-11459506|pmid-7723823|pmid-8849775|pmid-9288965|pmid-16125106|pmid-12910259 | Because of their potential biological significance, tremendous efforts have been made to evolve NTP-utilizing ribozymes from an RNA pool of random sequences. | [
"1",
"2",
"3",
"4",
"5",
"6",
"7",
"8",
"9",
"10",
"11"
] | 157 | 4,435 | 0 | false | Because of their potential biological significance, tremendous efforts have been made to evolve NTP-utilizing ribozymes from an RNA pool of random sequences. | [] | Because of their potential biological significance, tremendous efforts have been made to evolve NTP-utilizing ribozymes from an RNA pool of random sequences. | true | true | true | true | true | 752 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5",
"B6",
"B7",
"B8",
"B9",
"B10",
"B11"
] | 17,567,602 | pmid-6297745|pmid-6197186|NA|pmid-7521014|pmid-16274247|pmid-11459506|pmid-7723823|pmid-8849775|pmid-9288965|pmid-16125106|pmid-12910259 | Indeed, it has been thus far reported that ribozymes catalyze three types of chemistry with nucleotide substrates. | [
"1",
"2",
"3",
"4",
"5",
"6",
"7",
"8",
"9",
"10",
"11"
] | 114 | 4,436 | 0 | false | Indeed, it has been thus far reported that ribozymes catalyze three types of chemistry with nucleotide substrates. | [] | Indeed, it has been thus far reported that ribozymes catalyze three types of chemistry with nucleotide substrates. | true | true | true | true | true | 752 |
1 | INTRODUCTION | 1 | 4 | [
"B4",
"B12",
"B13 B14 B15",
"B16",
"B17",
"B16"
] | 17,567,602 | pmid-7521014|pmid-7578148|pmid-9184134|pmid-17044717|pmid-16973893|pmid-11358999|pmid-12031665|pmid-11358999|pmid-12031665 | The first example is ribozymes that use ATP as a phosphate source. | [
"4",
"12",
"13β15",
"16",
"17",
"16"
] | 66 | 4,437 | 0 | false | The first example is ribozymes that use ATP as a phosphate source. | [] | The first example is ribozymes that use ATP as a phosphate source. | true | true | true | true | true | 753 |
1 | INTRODUCTION | 1 | 4 | [
"B4",
"B12",
"B13 B14 B15",
"B16",
"B17",
"B16"
] | 17,567,602 | pmid-7521014|pmid-7578148|pmid-9184134|pmid-17044717|pmid-16973893|pmid-11358999|pmid-12031665|pmid-11358999|pmid-12031665 | Polynucleotide kinase ribozymes (4,12) are capable of catalyzing 5β²- or 2β²-phosphoryl transfer reaction. | [
"4",
"12",
"13β15",
"16",
"17",
"16"
] | 104 | 4,438 | 0 | false | Polynucleotide kinase ribozymes are capable of catalyzing 5β²- or 2β²-phosphoryl transfer reaction. | [
"4,12"
] | Polynucleotide kinase ribozymes are capable of catalyzing 5β²- or 2β²-phosphoryl transfer reaction. | true | true | true | true | true | 753 |
1 | INTRODUCTION | 1 | 13β15 | [
"B4",
"B12",
"B13 B14 B15",
"B16",
"B17",
"B16"
] | 17,567,602 | pmid-7521014|pmid-7578148|pmid-9184134|pmid-17044717|pmid-16973893|pmid-11358999|pmid-12031665|pmid-11358999|pmid-12031665 | The second example is a 5β²-capping ribozyme (13β15), which utilizes GDP (as well as GMP or GTP) to form a 5β²β5β² phosphoanhydride bond that is analogous to the 5β²-cap structure of mRNA. | [
"4",
"12",
"13β15",
"16",
"17",
"16"
] | 184 | 4,439 | 1 | false | The second example is a 5β²-capping ribozyme, which utilizes GDP (as well as GMP or GTP) to form a 5β²β5β² phosphoanhydride bond that is analogous to the 5β²-cap structure of mRNA. | [
"13β15"
] | The second example is a 5β²-capping ribozyme, which utilizes GDP (as well as GMP or GTP) to form a 5β²β5β² phosphoanhydride bond that is analogous to the 5β²-cap structure of mRNA. | true | true | true | true | true | 753 |
1 | INTRODUCTION | 1 | 4 | [
"B4",
"B12",
"B13 B14 B15",
"B16",
"B17",
"B16"
] | 17,567,602 | pmid-7521014|pmid-7578148|pmid-9184134|pmid-17044717|pmid-16973893|pmid-11358999|pmid-12031665|pmid-11358999|pmid-12031665 | The third example is those that can elongate their own or other oligonucleotide chain by NTPs (16,17). | [
"4",
"12",
"13β15",
"16",
"17",
"16"
] | 102 | 4,440 | 0 | false | The third example is those that can elongate their own or other oligonucleotide chain by NTPs. | [
"16,17"
] | The third example is those that can elongate their own or other oligonucleotide chain by NTPs. | true | true | true | true | true | 753 |
1 | INTRODUCTION | 1 | 4 | [
"B4",
"B12",
"B13 B14 B15",
"B16",
"B17",
"B16"
] | 17,567,602 | pmid-7521014|pmid-7578148|pmid-9184134|pmid-17044717|pmid-16973893|pmid-11358999|pmid-12031665|pmid-11358999|pmid-12031665 | Earlier ribozymes of this kind were isolated as those capable of ligating an oligonucleotide to its own 5β²-end. | [
"4",
"12",
"13β15",
"16",
"17",
"16"
] | 111 | 4,441 | 0 | false | Earlier ribozymes of this kind were isolated as those capable of ligating an oligonucleotide to its own 5β²-end. | [] | Earlier ribozymes of this kind were isolated as those capable of ligating an oligonucleotide to its own 5β²-end. | true | true | true | true | true | 753 |
1 | INTRODUCTION | 1 | 16 | [
"B4",
"B12",
"B13 B14 B15",
"B16",
"B17",
"B16"
] | 17,567,602 | pmid-7521014|pmid-7578148|pmid-9184134|pmid-17044717|pmid-16973893|pmid-11358999|pmid-12031665|pmid-11358999|pmid-12031665 | One of these ribozymes, called Class I ligase ribozyme, was further evolved using various ingenious strategies and successfully turned into an RNA polymerase ribozyme (16). | [
"4",
"12",
"13β15",
"16",
"17",
"16"
] | 172 | 4,442 | 1 | false | One of these ribozymes, called Class I ligase ribozyme, was further evolved using various ingenious strategies and successfully turned into an RNA polymerase ribozyme. | [
"16"
] | One of these ribozymes, called Class I ligase ribozyme, was further evolved using various ingenious strategies and successfully turned into an RNA polymerase ribozyme. | true | true | true | true | true | 753 |
1 | INTRODUCTION | 1 | 4 | [
"B4",
"B12",
"B13 B14 B15",
"B16",
"B17",
"B16"
] | 17,567,602 | pmid-7521014|pmid-7578148|pmid-9184134|pmid-17044717|pmid-16973893|pmid-11358999|pmid-12031665|pmid-11358999|pmid-12031665 | Significantly, this ribozyme is able to add multiple nucleotides to the 3β²-end of a substrate RNA according to the external template sequence in trans; thus, its 5β²β3β² polymerization function is analogous to the naturally occurring counterparts. | [
"4",
"12",
"13β15",
"16",
"17",
"16"
] | 245 | 4,443 | 0 | false | Significantly, this ribozyme is able to add multiple nucleotides to the 3β²-end of a substrate RNA according to the external template sequence in trans; thus, its 5β²β3β² polymerization function is analogous to the naturally occurring counterparts. | [] | Significantly, this ribozyme is able to add multiple nucleotides to the 3β²-end of a substrate RNA according to the external template sequence in trans; thus, its 5β²β3β² polymerization function is analogous to the naturally occurring counterparts. | true | true | true | true | true | 753 |
2 | INTRODUCTION | 1 | 4 | [
"B4",
"B5",
"B12",
"B18"
] | 17,567,602 | pmid-7521014|pmid-16274247|pmid-7578148|pmid-16790565 | Most of earlier demonstrations described above have dealt with chemistry where the selection strategy could be rather easily devised; i.e. | [
"4",
"5",
"12",
"18"
] | 138 | 4,444 | 0 | false | Most of earlier demonstrations described above have dealt with chemistry where the selection strategy could be rather easily devised; i.e. | [] | Most of earlier demonstrations described above have dealt with chemistry where the selection strategy could be rather easily devised; i.e. | true | true | true | true | true | 754 |
2 | INTRODUCTION | 1 | 4 | [
"B4",
"B5",
"B12",
"B18"
] | 17,567,602 | pmid-7521014|pmid-16274247|pmid-7578148|pmid-16790565 | a selection method allowed ones to fish out desired ribozymes with only one possible function or with a dominant function competing with other potential reactions to occur. | [
"4",
"5",
"12",
"18"
] | 172 | 4,445 | 0 | false | a selection method allowed ones to fish out desired ribozymes with only one possible function or with a dominant function competing with other potential reactions to occur. | [] | a selection method allowed ones to fish out desired ribozymes with only one possible function or with a dominant function competing with other potential reactions to occur. | false | true | true | true | false | 754 |
2 | INTRODUCTION | 1 | 4 | [
"B4",
"B5",
"B12",
"B18"
] | 17,567,602 | pmid-7521014|pmid-16274247|pmid-7578148|pmid-16790565 | However, this does not mean that the ribozyme chemistry using NTPs or other nucleotide phosphates is limited to these reactions. | [
"4",
"5",
"12",
"18"
] | 128 | 4,446 | 0 | false | However, this does not mean that the ribozyme chemistry using NTPs or other nucleotide phosphates is limited to these reactions. | [] | However, this does not mean that the ribozyme chemistry using NTPs or other nucleotide phosphates is limited to these reactions. | true | true | true | true | true | 754 |
2 | INTRODUCTION | 1 | 4 | [
"B4",
"B5",
"B12",
"B18"
] | 17,567,602 | pmid-7521014|pmid-16274247|pmid-7578148|pmid-16790565 | For example, phosphoryl transfer to the 3β²-hydroxyl or 5β²-triphosphate (5β²-ppp), and the 5β²-nucleotidyl transfer (3β²β5β² extension) could be catalyzed by RNA using ATP (or other NTPs) as a substrate. | [
"4",
"5",
"12",
"18"
] | 198 | 4,447 | 0 | false | For example, phosphoryl transfer to the 3β²-hydroxyl or 5β²-triphosphate, and the 5β²-nucleotidyl transfer could be catalyzed by RNA using ATP (or other NTPs) as a substrate. | [
"5β²-ppp",
"3β²β5β² extension"
] | For example, phosphoryl transfer to the 3β²-hydroxyl or 5β²-triphosphate, and the 5β²-nucleotidyl transfer could be catalyzed by RNA using ATP (or other NTPs) as a substrate. | true | true | true | true | true | 754 |
2 | INTRODUCTION | 1 | 4 | [
"B4",
"B5",
"B12",
"B18"
] | 17,567,602 | pmid-7521014|pmid-16274247|pmid-7578148|pmid-16790565 | In principle, RNA sequences that catalyze one of these reactions can be selected by a conventional strategy that yielded kinase ribozymes using ATP-Ξ³S as a substrate (4,5,12,18); yet, no ribozyme with such functions has been reported. | [
"4",
"5",
"12",
"18"
] | 234 | 4,448 | 0 | false | In principle, RNA sequences that catalyze one of these reactions can be selected by a conventional strategy that yielded kinase ribozymes using ATP-Ξ³S as a substrate ; yet, no ribozyme with such functions has been reported. | [
"4,5,12,18"
] | In principle, RNA sequences that catalyze one of these reactions can be selected by a conventional strategy that yielded kinase ribozymes using ATP-Ξ³S as a substrate ; yet, no ribozyme with such functions has been reported. | true | true | true | true | true | 754 |
2 | INTRODUCTION | 1 | 4 | [
"B4",
"B5",
"B12",
"B18"
] | 17,567,602 | pmid-7521014|pmid-16274247|pmid-7578148|pmid-16790565 | Therefore, a challenge is how ribozymes that catalyze unreported reactions are isolated and identified from a random RNA pool competing with those catalyzing other reactions reported previously. | [
"4",
"5",
"12",
"18"
] | 194 | 4,449 | 0 | false | Therefore, a challenge is how ribozymes that catalyze unreported reactions are isolated and identified from a random RNA pool competing with those catalyzing other reactions reported previously. | [] | Therefore, a challenge is how ribozymes that catalyze unreported reactions are isolated and identified from a random RNA pool competing with those catalyzing other reactions reported previously. | true | true | true | true | true | 754 |
2 | INTRODUCTION | 1 | 4 | [
"B4",
"B5",
"B12",
"B18"
] | 17,567,602 | pmid-7521014|pmid-16274247|pmid-7578148|pmid-16790565 | Accordingly, the selection strategy should be the most critical factor toward the success. | [
"4",
"5",
"12",
"18"
] | 90 | 4,450 | 0 | false | Accordingly, the selection strategy should be the most critical factor toward the success. | [] | Accordingly, the selection strategy should be the most critical factor toward the success. | true | true | true | true | true | 754 |
3 | INTRODUCTION | 0 | null | null | 17,567,602 | pmid-6301484|pmid-8524303|pmid-8524303|NA|pmid-14700631 | To isolate ribozymes capable of catalyzing the above reactions, we developed a strategy involving three layers of selection constraints to enrich 5β²-ppp-dependent catalytic species in a random RNA pool. | null | 202 | 4,451 | 0 | false | null | null | To isolate ribozymes capable of catalyzing the above reactions, we developed a strategy involving three layers of selection constraints to enrich 5β²-ppp-dependent catalytic species in a random RNA pool. | true | true | true | true | true | 755 |
3 | INTRODUCTION | 0 | null | null | 17,567,602 | pmid-6301484|pmid-8524303|pmid-8524303|NA|pmid-14700631 | Executing this selection indeed yielded a novel RNA sequence that catalyzes one of the above reactions: 3β²β5β² nucleotide extension. | null | 131 | 4,452 | 0 | false | null | null | Executing this selection indeed yielded a novel RNA sequence that catalyzes one of the above reactions: 3β²β5β² nucleotide extension. | true | true | true | true | true | 755 |
3 | INTRODUCTION | 0 | null | null | 17,567,602 | pmid-6301484|pmid-8524303|pmid-8524303|NA|pmid-14700631 | We report here selection and characterization of this ribozyme that shows intriguing promiscuous recognition to purine nucleotides. | null | 131 | 4,453 | 0 | false | null | null | We report here selection and characterization of this ribozyme that shows intriguing promiscuous recognition to purine nucleotides. | true | true | true | true | true | 755 |
0 | DISCUSSION | 0 | null | null | 17,567,602 | pmid-6297745|pmid-6197186|NA|pmid-7521014|pmid-16274247|pmid-11459506|pmid-7723823|pmid-8849775|pmid-9288965|pmid-16125106|pmid-12910259 | Here we have shown in vitro selection of a novel ribozyme C06 that catalyzes the 5β²-nucleotidyl transfer reaction forming the 2β²β5β² phosphodiester bond (Figure 4E). | null | 164 | 4,454 | 0 | false | null | null | Here we have shown in vitro selection of a novel ribozyme C06 that catalyzes the 5β²-nucleotidyl transfer reaction forming the 2β²β5β² phosphodiester bond (Figure 4E). | true | true | true | true | true | 756 |
0 | DISCUSSION | 0 | null | null | 17,567,602 | pmid-6297745|pmid-6197186|NA|pmid-7521014|pmid-16274247|pmid-11459506|pmid-7723823|pmid-8849775|pmid-9288965|pmid-16125106|pmid-12910259 | The C06 sequence was found in pool 14-I as a minor population compared to possible internal kinases (Figure 2B). | null | 112 | 4,455 | 0 | false | null | null | The C06 sequence was found in pool 14-I as a minor population compared to possible internal kinases (Figure 2B). | true | true | true | true | true | 756 |
0 | DISCUSSION | 0 | null | null | 17,567,602 | pmid-6297745|pmid-6197186|NA|pmid-7521014|pmid-16274247|pmid-11459506|pmid-7723823|pmid-8849775|pmid-9288965|pmid-16125106|pmid-12910259 | Finding of such a sequence was made possible by executing selection under the layers of selection criteria and the careful sequence comparison in two pools at the round 14 generated by the procedures involving 5β²-ppp or 5β²-OH RNA for the selection. | null | 248 | 4,456 | 0 | false | null | null | Finding of such a sequence was made possible by executing selection under the layers of selection criteria and the careful sequence comparison in two pools at the round 14 generated by the procedures involving 5β²-ppp or 5β²-OH RNA for the selection. | true | true | true | true | true | 756 |
0 | DISCUSSION | 0 | null | null | 17,567,602 | pmid-6297745|pmid-6197186|NA|pmid-7521014|pmid-16274247|pmid-11459506|pmid-7723823|pmid-8849775|pmid-9288965|pmid-16125106|pmid-12910259 | Especially, the latter counterselection strategy facilitated the confirmation of the desired activity without checking all clones for their activities. | null | 151 | 4,457 | 0 | false | null | null | Especially, the latter counterselection strategy facilitated the confirmation of the desired activity without checking all clones for their activities. | true | true | true | true | true | 756 |
0 | DISCUSSION | 0 | null | null | 17,567,602 | pmid-6297745|pmid-6197186|NA|pmid-7521014|pmid-16274247|pmid-11459506|pmid-7723823|pmid-8849775|pmid-9288965|pmid-16125106|pmid-12910259 | The 5β²-nucleotidyl transfer reaction is considered as a 3β²β5β² mononucleotide extension, and thus no natural counterpart is known to exist in the present enzyme world. | null | 166 | 4,458 | 0 | false | null | null | The 5β²-nucleotidyl transfer reaction is considered as a 3β²β5β² mononucleotide extension, and thus no natural counterpart is known to exist in the present enzyme world. | true | true | true | true | true | 756 |
0 | DISCUSSION | 0 | null | null | 17,567,602 | pmid-6297745|pmid-6197186|NA|pmid-7521014|pmid-16274247|pmid-11459506|pmid-7723823|pmid-8849775|pmid-9288965|pmid-16125106|pmid-12910259 | Nonetheless, an RNA molecule reported here is able to perform such a unique chemistry in cis as well as in trans. | null | 113 | 4,459 | 0 | false | null | null | Nonetheless, an RNA molecule reported here is able to perform such a unique chemistry in cis as well as in trans. | true | true | true | true | true | 756 |
1 | DISCUSSION | 1 | 17 | [
"B17"
] | 17,567,602 | pmid-7521014|pmid-7578148|pmid-9184134|pmid-17044717|pmid-16973893|pmid-11358999|pmid-12031665|pmid-11358999|pmid-12031665 | Joyce et al. | [
"17"
] | 12 | 4,460 | 0 | false | Joyce et al. | [] | Joyce et al. | true | true | true | true | true | 757 |
1 | DISCUSSION | 1 | 17 | [
"B17"
] | 17,567,602 | pmid-7521014|pmid-7578148|pmid-9184134|pmid-17044717|pmid-16973893|pmid-11358999|pmid-12031665|pmid-11358999|pmid-12031665 | have reported a ribozyme capable of catalyzing both 5β²- and 3β²-nucleotidyl transfer reactions (17). | [
"17"
] | 99 | 4,461 | 1 | false | have reported a ribozyme capable of catalyzing both 5β²- and 3β²-nucleotidyl transfer reactions. | [
"17"
] | have reported a ribozyme capable of catalyzing both 5β²- and 3β²-nucleotidyl transfer reactions. | false | true | true | true | false | 757 |
1 | DISCUSSION | 1 | 17 | [
"B17"
] | 17,567,602 | pmid-7521014|pmid-7578148|pmid-9184134|pmid-17044717|pmid-16973893|pmid-11358999|pmid-12031665|pmid-11358999|pmid-12031665 | This ribozyme, called E278-19, is a variant of Class | [
"17"
] | 52 | 4,462 | 0 | false | This ribozyme, called E278-19, is a variant of Class | [] | This ribozyme, called E278-19, is a variant of Class | true | true | false | true | false | 757 |
1 | DISCUSSION | 1 | 17 | [
"B17"
] | 17,567,602 | pmid-7521014|pmid-7578148|pmid-9184134|pmid-17044717|pmid-16973893|pmid-11358999|pmid-12031665|pmid-11358999|pmid-12031665 | I ligase ribozyme isolated by a continuous in vitro evolution procedure aimed at evolving 5β²β3β² mono- or di-nucleotide extension. | [
"17"
] | 129 | 4,463 | 0 | false | I ligase ribozyme isolated by a continuous in vitro evolution procedure aimed at evolving 5β²β3β² mono- or di-nucleotide extension. | [] | I ligase ribozyme isolated by a continuous in vitro evolution procedure aimed at evolving 5β²β3β² mono- or di-nucleotide extension. | true | true | true | true | true | 757 |
1 | DISCUSSION | 1 | 17 | [
"B17"
] | 17,567,602 | pmid-7521014|pmid-7578148|pmid-9184134|pmid-17044717|pmid-16973893|pmid-11358999|pmid-12031665|pmid-11358999|pmid-12031665 | Thus, the 3β²β5β² nucleotidyl transfer activity was coincidently discovered in the collection of ligase or polymerase ribozymes, but it certainly kept the same signatures as the parental class I ligase ribozyme, where the incoming nucleotide formed a base pair with the template nucleotide and the 3β²β5β² phosphodiester lin... | [
"17"
] | 339 | 4,464 | 0 | false | Thus, the 3β²β5β² nucleotidyl transfer activity was coincidently discovered in the collection of ligase or polymerase ribozymes, but it certainly kept the same signatures as the parental class I ligase ribozyme, where the incoming nucleotide formed a base pair with the template nucleotide and the 3β²β5β² phosphodiester lin... | [] | Thus, the 3β²β5β² nucleotidyl transfer activity was coincidently discovered in the collection of ligase or polymerase ribozymes, but it certainly kept the same signatures as the parental class I ligase ribozyme, where the incoming nucleotide formed a base pair with the template nucleotide and the 3β²β5β² phosphodiester lin... | true | true | true | true | true | 757 |
2 | DISCUSSION | 0 | null | null | 17,567,602 | pmid-7521014|pmid-16274247|pmid-7578148|pmid-16790565 | In contrast, C06 and its miniaturized variant M4 promiscuously recognize the incoming purine nucleotides for the 3β²β5β² extension (Figure 5). | null | 140 | 4,465 | 0 | false | null | null | In contrast, C06 and its miniaturized variant M4 promiscuously recognize the incoming purine nucleotides for the 3β²β5β² extension (Figure 5). | true | true | true | true | true | 758 |
2 | DISCUSSION | 0 | null | null | 17,567,602 | pmid-7521014|pmid-16274247|pmid-7578148|pmid-16790565 | Although it has not been ruled out if a nucleotide templating to the incoming purine nucleotide resides in the active site, the observed promiscuous activity toward various purine bases suggests that specific hydrogen bonding to purine bases is very unlikely. | null | 259 | 4,466 | 0 | false | null | null | Although it has not been ruled out if a nucleotide templating to the incoming purine nucleotide resides in the active site, the observed promiscuous activity toward various purine bases suggests that specific hydrogen bonding to purine bases is very unlikely. | true | true | true | true | true | 758 |
2 | DISCUSSION | 0 | null | null | 17,567,602 | pmid-7521014|pmid-16274247|pmid-7578148|pmid-16790565 | We rather think that the incoming substrate is guided by base-stacking interactions to the active site of ribozyme and somehow the ribozyme 5β²-Ξ±-phosphate is projected to the 2β²-OH of the incoming nucleotide for the nucleophilic attack. | null | 236 | 4,467 | 0 | false | null | null | We rather think that the incoming substrate is guided by base-stacking interactions to the active site of ribozyme and somehow the ribozyme 5β²-Ξ±-phosphate is projected to the 2β²-OH of the incoming nucleotide for the nucleophilic attack. | true | true | true | true | true | 758 |
3 | DISCUSSION | 1 | 22 | [
"B22",
"B23",
"B23",
"B3",
"B24"
] | 17,567,602 | pmid-6301484|pmid-8524303|pmid-8524303|NA|pmid-14700631 | Even though we cannot identify a direct counterpart enzyme in the contemporary protein world, terminal deoxyribonucleotide transferase (TdT) catalyzes a similar reaction. | [
"22",
"23",
"23",
"3",
"24"
] | 170 | 4,468 | 0 | false | Even though we cannot identify a direct counterpart enzyme in the contemporary protein world, terminal deoxyribonucleotide transferase (TdT) catalyzes a similar reaction. | [] | Even though we cannot identify a direct counterpart enzyme in the contemporary protein world, terminal deoxyribonucleotide transferase (TdT) catalyzes a similar reaction. | true | true | true | true | true | 759 |
3 | DISCUSSION | 1 | 22 | [
"B22",
"B23",
"B23",
"B3",
"B24"
] | 17,567,602 | pmid-6301484|pmid-8524303|pmid-8524303|NA|pmid-14700631 | This enzyme can add nucleotide(s) to the 3β²-end of DNA in a template-independent manner. | [
"22",
"23",
"23",
"3",
"24"
] | 88 | 4,469 | 0 | false | This enzyme can add nucleotide(s) to the 3β²-end of DNA in a template-independent manner. | [] | This enzyme can add nucleotide(s) to the 3β²-end of DNA in a template-independent manner. | true | true | true | true | true | 759 |
3 | DISCUSSION | 1 | 22 | [
"B22",
"B23",
"B23",
"B3",
"B24"
] | 17,567,602 | pmid-6301484|pmid-8524303|pmid-8524303|NA|pmid-14700631 | Also TdT is well-known to have a preference to dG over other deoxyribonucleotides even though it basically has a promiscuous ability to accept nucleotide substrates (22). | [
"22",
"23",
"23",
"3",
"24"
] | 170 | 4,470 | 1 | false | Also TdT is well-known to have a preference to dG over other deoxyribonucleotides even though it basically has a promiscuous ability to accept nucleotide substrates. | [
"22"
] | Also TdT is well-known to have a preference to dG over other deoxyribonucleotides even though it basically has a promiscuous ability to accept nucleotide substrates. | true | true | true | true | true | 759 |
3 | DISCUSSION | 1 | 23 | [
"B22",
"B23",
"B23",
"B3",
"B24"
] | 17,567,602 | pmid-6301484|pmid-8524303|pmid-8524303|NA|pmid-14700631 | TdT apparently uses base-stacking interaction at least for its second nucleotidyl transfer step (23). | [
"22",
"23",
"23",
"3",
"24"
] | 101 | 4,471 | 1 | false | TdT apparently uses base-stacking interaction at least for its second nucleotidyl transfer step. | [
"23"
] | TdT apparently uses base-stacking interaction at least for its second nucleotidyl transfer step. | true | true | true | true | true | 759 |
3 | DISCUSSION | 1 | 22 | [
"B22",
"B23",
"B23",
"B3",
"B24"
] | 17,567,602 | pmid-6301484|pmid-8524303|pmid-8524303|NA|pmid-14700631 | Although TdT shares some of key features of M4, distinct differences exist regarding directionality and substrate specificity of the nucleotidyl transfer event. | [
"22",
"23",
"23",
"3",
"24"
] | 160 | 4,472 | 0 | false | Although TdT shares some of key features of M4, distinct differences exist regarding directionality and substrate specificity of the nucleotidyl transfer event. | [] | Although TdT shares some of key features of M4, distinct differences exist regarding directionality and substrate specificity of the nucleotidyl transfer event. | true | true | true | true | true | 759 |
3 | DISCUSSION | 1 | 23 | [
"B22",
"B23",
"B23",
"B3",
"B24"
] | 17,567,602 | pmid-6301484|pmid-8524303|pmid-8524303|NA|pmid-14700631 | As TdT plays an indispensable role in enhancing the diversity of the immunoglobulin repertoire (23), we can imagine a beneficial role of terminal nucleotide transfer at either end of RNA in the RNA world with regard to a genetic diversity, where the recombination could have been the primary source to achieve an evoluti... | [
"22",
"23",
"23",
"3",
"24"
] | 344 | 4,473 | 1 | false | As TdT plays an indispensable role in enhancing the diversity of the immunoglobulin repertoire, we can imagine a beneficial role of terminal nucleotide transfer at either end of RNA in the RNA world with regard to a genetic diversity, where the recombination could have been the primary source to achieve an evolution or... | [
"23",
"3,24"
] | As TdT plays an indispensable role in enhancing the diversity of the immunoglobulin repertoire, we can imagine a beneficial role of terminal nucleotide transfer at either end of RNA in the RNA world with regard to a genetic diversity, where the recombination could have been the primary source to achieve an evolution or... | true | true | true | true | true | 759 |
4 | DISCUSSION | 1 | 25β28 | [
"B25 B26 B27 B28",
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | During the course of mutation studies, we found that indispensable motifs in M4 reside in the regions of the 5β²-overhang, P2βP3 junction and L3 loop (Figures 3 and 6A). | [
"25β28",
"25",
"26",
"27",
"28",
"30"
] | 168 | 4,474 | 0 | false | During the course of mutation studies, we found that indispensable motifs in M4 reside in the regions of the 5β²-overhang, P2βP3 junction and L3 loop (Figures 3 and 6A). | [] | During the course of mutation studies, we found that indispensable motifs in M4 reside in the regions of the 5β²-overhang, P2βP3 junction and L3 loop (Figures 3 and 6A). | true | true | true | true | true | 760 |
4 | DISCUSSION | 1 | 25β28 | [
"B25 B26 B27 B28",
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | Since M4 catalyzes essentially the same chemistry as RNA ligase ribozymes except for the directionality of extension, it is of interest to compare the secondary structure of M4 with those of reported ligase ribozymes. | [
"25β28",
"25",
"26",
"27",
"28",
"30"
] | 217 | 4,475 | 0 | false | Since M4 catalyzes essentially the same chemistry as RNA ligase ribozymes except for the directionality of extension, it is of interest to compare the secondary structure of M4 with those of reported ligase ribozymes. | [] | Since M4 catalyzes essentially the same chemistry as RNA ligase ribozymes except for the directionality of extension, it is of interest to compare the secondary structure of M4 with those of reported ligase ribozymes. | true | true | true | true | true | 760 |
4 | DISCUSSION | 1 | 25β28 | [
"B25 B26 B27 B28",
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | Four representative ligases are selected for comparison; Bartel's class II ligase, Ellington's L1 ligase, Joyce's R3C and cytidine-free ligases (Figure 6BβE) (25β28), all of which form a 2β²β5β² phosphodiester linkages like M4 ribozyme. | [
"25β28",
"25",
"26",
"27",
"28",
"30"
] | 234 | 4,476 | 1 | false | Four representative ligases are selected for comparison; Bartel's class II ligase, Ellington's L1 ligase, Joyce's R3C and cytidine-free ligases (Figure 6BβE), all of which form a 2β²β5β² phosphodiester linkages like M4 ribozyme. | [
"25β28"
] | Four representative ligases are selected for comparison; Bartel's class II ligase, Ellington's L1 ligase, Joyce's R3C and cytidine-free ligases, all of which form a 2β²β5β² phosphodiester linkages like M4 ribozyme. | true | true | true | true | true | 760 |
4 | DISCUSSION | 1 | 25β28 | [
"B25 B26 B27 B28",
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | These four ligases share the structural features of 5β²-overhang and internal guide sequence for the incoming oligonucleotide. | [
"25β28",
"25",
"26",
"27",
"28",
"30"
] | 125 | 4,477 | 0 | false | These four ligases share the structural features of 5β²-overhang and internal guide sequence for the incoming oligonucleotide. | [] | These four ligases share the structural features of 5β²-overhang and internal guide sequence for the incoming oligonucleotide. | true | true | true | true | true | 760 |
4 | DISCUSSION | 1 | 25β28 | [
"B25 B26 B27 B28",
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | An obvious similarity found in all ribozymes including M4 is that the junction domain likely consisting of a part of catalytic core is dominated with A and G, occasionally containing U (note that G is dominated at the 5β²-end because the consecutive Gs generally give higher transcription efficiency and therefore such RN... | [
"25β28",
"25",
"26",
"27",
"28",
"30"
] | 364 | 4,478 | 0 | false | An obvious similarity found in all ribozymes including M4 is that the junction domain likely consisting of a part of catalytic core is dominated with A and G, occasionally containing U (note that G is dominated at the 5β²-end because the consecutive Gs generally give higher transcription efficiency and therefore such RN... | [] | An obvious similarity found in all ribozymes including M4 is that the junction domain likely consisting of a part of catalytic core is dominated with A and G, occasionally containing U. | true | true | true | true | true | 760 |
4 | DISCUSSION | 1 | 25β28 | [
"B25 B26 B27 B28",
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | This suggests that such AG-rich motifs are suitable for composing the tertiary space where 5β²-Ξ±-phosphate is positioned to the 2β²-OH of the incoming nucleotide. | [
"25β28",
"25",
"26",
"27",
"28",
"30"
] | 160 | 4,479 | 0 | false | This suggests that such AG-rich motifs are suitable for composing the tertiary space where 5β²-Ξ±-phosphate is positioned to the 2β²-OH of the incoming nucleotide. | [] | This suggests that such AG-rich motifs are suitable for composing the tertiary space where 5β²-Ξ±-phosphate is positioned to the 2β²-OH of the incoming nucleotide. | true | true | true | true | true | 760 |
4 | DISCUSSION | 1 | 25β28 | [
"B25 B26 B27 B28",
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | On the other hand, a significant difference between M4 and these ribozymes is that M4 lacks the internal guide sequence for specific base pairing. | [
"25β28",
"25",
"26",
"27",
"28",
"30"
] | 146 | 4,480 | 0 | false | On the other hand, a significant difference between M4 and these ribozymes is that M4 lacks the internal guide sequence for specific base pairing. | [] | On the other hand, a significant difference between M4 and these ribozymes is that M4 lacks the internal guide sequence for specific base pairing. | true | true | true | true | true | 760 |
4 | DISCUSSION | 1 | 25β28 | [
"B25 B26 B27 B28",
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | Probably, the P2βP3 junction and L3 region would be located in close proximity, creating a 3D space for bringing the incoming purine nucleotides to the active site via base-stacking interactions. | [
"25β28",
"25",
"26",
"27",
"28",
"30"
] | 195 | 4,481 | 0 | false | Probably, the P2βP3 junction and L3 region would be located in close proximity, creating a 3D space for bringing the incoming purine nucleotides to the active site via base-stacking interactions. | [] | Probably, the P2βP3 junction and L3 region would be located in close proximity, creating a 3D space for bringing the incoming purine nucleotides to the active site via base-stacking interactions. | true | true | true | true | true | 760 |
4 | DISCUSSION | 1 | 25β28 | [
"B25 B26 B27 B28",
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | Figure 6.Proposed secondary structures of M4 ribozyme and ligases. | [
"25β28",
"25",
"26",
"27",
"28",
"30"
] | 66 | 4,482 | 0 | false | Figure 6.Proposed secondary structures of M4 ribozyme and ligases. | [] | Figure 6.Proposed secondary structures of M4 ribozyme and ligases. | true | true | true | true | true | 760 |
4 | DISCUSSION | 1 | 25β28 | [
"B25 B26 B27 B28",
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | (A) M4 from this study. | [
"25β28",
"25",
"26",
"27",
"28",
"30"
] | 23 | 4,483 | 0 | false | (A) M4 from this study. | [] | (A) M4 from this study. | false | false | true | true | false | 760 |
4 | DISCUSSION | 1 | 25 | [
"B25 B26 B27 B28",
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | (B) Bartel's class II ligase ribozyme (25). | [
"25β28",
"25",
"26",
"27",
"28",
"30"
] | 43 | 4,484 | 1 | false | (B) Bartel's class II ligase ribozyme. | [
"25"
] | (B) Bartel's class II ligase ribozyme. | false | false | true | true | false | 760 |
4 | DISCUSSION | 1 | 26 | [
"B25 B26 B27 B28",
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | (C) Ellington's L1 ligase ribozyme (26). | [
"25β28",
"25",
"26",
"27",
"28",
"30"
] | 40 | 4,485 | 1 | false | (C) Ellington's L1 ligase ribozyme. | [
"26"
] | (C) Ellington's L1 ligase ribozyme. | false | false | true | true | false | 760 |
4 | DISCUSSION | 1 | 25β28 | [
"B25 B26 B27 B28",
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | (D) and (E) Joyce's R3C and cytidine-free ligase ribozyme, respectively (27,28). | [
"25β28",
"25",
"26",
"27",
"28",
"30"
] | 80 | 4,486 | 0 | false | (D) and (E) Joyce's R3C and cytidine-free ligase ribozyme, respectively. | [
"27,28"
] | (D) and (E) Joyce's R3C and cytidine-free ligase ribozyme, respectively. | false | false | true | true | false | 760 |
4 | DISCUSSION | 1 | 30 | [
"B25 B26 B27 B28",
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | (F) Siverman's 7S11 RNA ligase DNA enzyme (30). | [
"25β28",
"25",
"26",
"27",
"28",
"30"
] | 47 | 4,487 | 1 | false | (F) Siverman's 7S11 RNA ligase DNA enzyme. | [
"30"
] | (F) Siverman's 7S11 RNA ligase DNA enzyme. | false | false | true | true | false | 760 |
4 | DISCUSSION | 1 | 25β28 | [
"B25 B26 B27 B28",
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | Bases likely involved in catalysis are shown. | [
"25β28",
"25",
"26",
"27",
"28",
"30"
] | 45 | 4,488 | 0 | false | Bases likely involved in catalysis are shown. | [] | Bases likely involved in catalysis are shown. | true | true | true | true | true | 760 |
4 | DISCUSSION | 1 | 25β28 | [
"B25 B26 B27 B28",
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | Other parts of ribozyme sequences are shown in solid line; DNA parts are shown in thicker solid line. | [
"25β28",
"25",
"26",
"27",
"28",
"30"
] | 101 | 4,489 | 0 | false | Other parts of ribozyme sequences are shown in solid line; DNA parts are shown in thicker solid line. | [] | Other parts of ribozyme sequences are shown in solid line; DNA parts are shown in thicker solid line. | true | true | true | true | true | 760 |
4 | DISCUSSION | 1 | 25β28 | [
"B25 B26 B27 B28",
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | The hydroxyl nucleophile of incoming purine (R) or oligonucleotide substrate (dashed lines) attacks the Ξ±-phosphate on the ribozyme. | [
"25β28",
"25",
"26",
"27",
"28",
"30"
] | 132 | 4,490 | 0 | false | The hydroxyl nucleophile of incoming purine (R) or oligonucleotide substrate (dashed lines) attacks the Ξ±-phosphate on the ribozyme. | [] | The hydroxyl nucleophile of incoming purine (R) or oligonucleotide substrate (dashed lines) attacks the Ξ±-phosphate on the ribozyme. | true | true | true | true | true | 760 |
5 | DISCUSSION | 1 | 25 | [
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | Proposed secondary structures of M4 ribozyme and ligases. | [
"25",
"26",
"27",
"28",
"30"
] | 57 | 4,491 | 0 | false | Proposed secondary structures of M4 ribozyme and ligases. | [] | Proposed secondary structures of M4 ribozyme and ligases. | true | true | true | true | true | 761 |
5 | DISCUSSION | 1 | 25 | [
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | (A) M4 from this study. | [
"25",
"26",
"27",
"28",
"30"
] | 23 | 4,492 | 0 | false | (A) M4 from this study. | [] | (A) M4 from this study. | false | false | true | true | false | 761 |
5 | DISCUSSION | 1 | 25 | [
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | (B) Bartel's class II ligase ribozyme (25). | [
"25",
"26",
"27",
"28",
"30"
] | 43 | 4,493 | 1 | false | (B) Bartel's class II ligase ribozyme. | [
"25"
] | (B) Bartel's class II ligase ribozyme. | false | false | true | true | false | 761 |
5 | DISCUSSION | 1 | 26 | [
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | (C) Ellington's L1 ligase ribozyme (26). | [
"25",
"26",
"27",
"28",
"30"
] | 40 | 4,494 | 1 | false | (C) Ellington's L1 ligase ribozyme. | [
"26"
] | (C) Ellington's L1 ligase ribozyme. | false | false | true | true | false | 761 |
5 | DISCUSSION | 1 | 25 | [
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | (D) and (E) Joyce's R3C and cytidine-free ligase ribozyme, respectively (27,28). | [
"25",
"26",
"27",
"28",
"30"
] | 80 | 4,495 | 0 | false | (D) and (E) Joyce's R3C and cytidine-free ligase ribozyme, respectively. | [
"27,28"
] | (D) and (E) Joyce's R3C and cytidine-free ligase ribozyme, respectively. | false | false | true | true | false | 761 |
5 | DISCUSSION | 1 | 30 | [
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | (F) Siverman's 7S11 RNA ligase DNA enzyme (30). | [
"25",
"26",
"27",
"28",
"30"
] | 47 | 4,496 | 1 | false | (F) Siverman's 7S11 RNA ligase DNA enzyme. | [
"30"
] | (F) Siverman's 7S11 RNA ligase DNA enzyme. | false | false | true | true | false | 761 |
5 | DISCUSSION | 1 | 25 | [
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | Bases likely involved in catalysis are shown. | [
"25",
"26",
"27",
"28",
"30"
] | 45 | 4,497 | 0 | false | Bases likely involved in catalysis are shown. | [] | Bases likely involved in catalysis are shown. | true | true | true | true | true | 761 |
5 | DISCUSSION | 1 | 25 | [
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | Other parts of ribozyme sequences are shown in solid line; DNA parts are shown in thicker solid line. | [
"25",
"26",
"27",
"28",
"30"
] | 101 | 4,498 | 0 | false | Other parts of ribozyme sequences are shown in solid line; DNA parts are shown in thicker solid line. | [] | Other parts of ribozyme sequences are shown in solid line; DNA parts are shown in thicker solid line. | true | true | true | true | true | 761 |
5 | DISCUSSION | 1 | 25 | [
"B25",
"B26",
"B27",
"B28",
"B30"
] | 17,567,602 | pmid-7618102|pmid-11345430|pmid-11333020|pmid-10580507|pmid-14758353 | The hydroxyl nucleophile of incoming purine (R) or oligonucleotide substrate (dashed lines) attacks the Ξ±-phosphate on the ribozyme. | [
"25",
"26",
"27",
"28",
"30"
] | 132 | 4,499 | 0 | false | The hydroxyl nucleophile of incoming purine (R) or oligonucleotide substrate (dashed lines) attacks the Ξ±-phosphate on the ribozyme. | [] | The hydroxyl nucleophile of incoming purine (R) or oligonucleotide substrate (dashed lines) attacks the Ξ±-phosphate on the ribozyme. | true | true | true | true | true | 761 |
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