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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 | DISCUSSION | 1 | 10 | [
"B18",
"B10",
"B23 B24 B25 B26 B27 B28 B29 B30 B31 B32 B33",
"B10"
] | 17,537,824 | pmid-15713734|pmid-16506242|pmid-3237687|pmid-9126848|pmid-15981261|pmid-16506242|pmid-15981273|pmid-15981272|pmid-15981271|pmid-15981270|pmid-15981266|pmid-15981262|pmid-15981258|pmid-15981255|pmid-15981251|pmid-15981249|pmid-15981246|pmid-16506242 | For a complete analysis of all models please see reference (10). | [
"18",
"10",
"23–33",
"10"
] | 64 | 1,100 | 1 | false | For a complete analysis of all models please see reference. | [
"10"
] | For a complete analysis of all models please see reference. | true | true | true | true | true | 190 |
2 | DISCUSSION | 1 | 23–33 | [
"B23 B24 B25 B26 B27 B28 B29 B30 B31 B32 B33",
"B10"
] | 17,537,824 | pmid-15981273|pmid-15981272|pmid-15981271|pmid-15981270|pmid-15981266|pmid-15981262|pmid-15981258|pmid-15981255|pmid-15981251|pmid-15981249|pmid-15981246|pmid-16506242 | Examples of ‘FastContact’ scoring for a subset of high quality docked models from eight groups for targets 8 and 12 of CAPRI rounds 3–5, from http://capri.ebi.ac.uk/. | [
"23–33",
"10"
] | 166 | 1,101 | 0 | false | Examples of ‘FastContact’ scoring for a subset of high quality docked models from eight groups for targets 8 and 12 of CAPRI rounds 3–5, from http://capri.ebi.ac.uk/. | [] | Examples of ‘FastContact’ scoring for a subset of high quality docked models from eight groups for targets 8 and 12 of CAPRI rounds 3–5, from http://capri.ebi.ac.uk/. | true | true | true | true | true | 191 |
2 | DISCUSSION | 1 | 23–33 | [
"B23 B24 B25 B26 B27 B28 B29 B30 B31 B32 B33",
"B10"
] | 17,537,824 | pmid-15981273|pmid-15981272|pmid-15981271|pmid-15981270|pmid-15981266|pmid-15981262|pmid-15981258|pmid-15981255|pmid-15981251|pmid-15981249|pmid-15981246|pmid-16506242 | For each of these targets, we run the models in our server and re-rank the models accordingly. | [
"23–33",
"10"
] | 94 | 1,102 | 0 | false | For each of these targets, we run the models in our server and re-rank the models accordingly. | [] | For each of these targets, we run the models in our server and re-rank the models accordingly. | true | true | true | true | true | 191 |
2 | DISCUSSION | 1 | 23–33 | [
"B23 B24 B25 B26 B27 B28 B29 B30 B31 B32 B33",
"B10"
] | 17,537,824 | pmid-15981273|pmid-15981272|pmid-15981271|pmid-15981270|pmid-15981266|pmid-15981262|pmid-15981258|pmid-15981255|pmid-15981251|pmid-15981249|pmid-15981246|pmid-16506242 | In all cases, the server was able to correctly rank a low RMSD model as the one with the lowest free energy score. | [
"23–33",
"10"
] | 114 | 1,103 | 0 | false | In all cases, the server was able to correctly rank a low RMSD model as the one with the lowest free energy score. | [] | In all cases, the server was able to correctly rank a low RMSD model as the one with the lowest free energy score. | true | true | true | true | true | 191 |
2 | DISCUSSION | 1 | 23–33 | [
"B23 B24 B25 B26 B27 B28 B29 B30 B31 B32 B33",
"B10"
] | 17,537,824 | pmid-15981273|pmid-15981272|pmid-15981271|pmid-15981270|pmid-15981266|pmid-15981262|pmid-15981258|pmid-15981255|pmid-15981251|pmid-15981249|pmid-15981246|pmid-16506242 | For comparison, we also marked with a diamond symbol the model ranked number 1 by the modeler (23–33). | [
"23–33",
"10"
] | 102 | 1,104 | 1 | false | For comparison, we also marked with a diamond symbol the model ranked number 1 by the modeler. | [
"23–33"
] | For comparison, we also marked with a diamond symbol the model ranked number 1 by the modeler. | true | true | true | true | true | 191 |
2 | DISCUSSION | 1 | 23–33 | [
"B23 B24 B25 B26 B27 B28 B29 B30 B31 B32 B33",
"B10"
] | 17,537,824 | pmid-15981273|pmid-15981272|pmid-15981271|pmid-15981270|pmid-15981266|pmid-15981262|pmid-15981258|pmid-15981255|pmid-15981251|pmid-15981249|pmid-15981246|pmid-16506242 | (A) target 8; (B) target 12. | [
"23–33",
"10"
] | 28 | 1,105 | 0 | false | (A) target 8; (B) target 12. | [] | (A) target 8; (B) target 12. | false | false | true | true | false | 191 |
2 | DISCUSSION | 1 | 10 | [
"B23 B24 B25 B26 B27 B28 B29 B30 B31 B32 B33",
"B10"
] | 17,537,824 | pmid-15981273|pmid-15981272|pmid-15981271|pmid-15981270|pmid-15981266|pmid-15981262|pmid-15981258|pmid-15981255|pmid-15981251|pmid-15981249|pmid-15981246|pmid-16506242 | For a complete analysis of all models please see reference (10). | [
"23–33",
"10"
] | 64 | 1,106 | 1 | false | For a complete analysis of all models please see reference. | [
"10"
] | For a complete analysis of all models please see reference. | true | true | true | true | true | 191 |
3 | DISCUSSION | 1 | 21 | [
"B21",
"B22"
] | 17,537,824 | pmid-10049302|pmid-14693807 | By splitting the free energy between electrostatics and desolvation, ‘Fastcontact’ also provides immediate insights into the nature of the binding interactions. | [
"21",
"22"
] | 160 | 1,107 | 0 | false | By splitting the free energy between electrostatics and desolvation, ‘Fastcontact’ also provides immediate insights into the nature of the binding interactions. | [] | By splitting the free energy between electrostatics and desolvation, ‘Fastcontact’ also provides immediate insights into the nature of the binding interactions. | true | true | true | true | true | 192 |
3 | DISCUSSION | 1 | 21 | [
"B21",
"B22"
] | 17,537,824 | pmid-10049302|pmid-14693807 | Namely, negative desolvation is associated with a hydrophobic pocket at the binding site, whereas positive desolvation characterizes mostly polar interfaces. | [
"21",
"22"
] | 157 | 1,108 | 0 | false | Namely, negative desolvation is associated with a hydrophobic pocket at the binding site, whereas positive desolvation characterizes mostly polar interfaces. | [] | Namely, negative desolvation is associated with a hydrophobic pocket at the binding site, whereas positive desolvation characterizes mostly polar interfaces. | true | true | true | true | true | 192 |
3 | DISCUSSION | 1 | 21 | [
"B21",
"B22"
] | 17,537,824 | pmid-10049302|pmid-14693807 | This is important since sometimes electrostatic or desolvation alone could lead to better discrimination than the combination of the two (21,22). | [
"21",
"22"
] | 145 | 1,109 | 0 | false | This is important since sometimes electrostatic or desolvation alone could lead to better discrimination than the combination of the two. | [
"21,22"
] | This is important since sometimes electrostatic or desolvation alone could lead to better discrimination than the combination of the two. | true | true | true | true | true | 192 |
3 | DISCUSSION | 1 | 21 | [
"B21",
"B22"
] | 17,537,824 | pmid-10049302|pmid-14693807 | The latter is, of course, due to the intrinsic limitations of empirical free energies. | [
"21",
"22"
] | 86 | 1,110 | 0 | false | The latter is, of course, due to the intrinsic limitations of empirical free energies. | [] | The latter is, of course, due to the intrinsic limitations of empirical free energies. | true | true | true | true | true | 192 |
3 | DISCUSSION | 1 | 21 | [
"B21",
"B22"
] | 17,537,824 | pmid-10049302|pmid-14693807 | In particular, reliable estimates for solvent and entropic interactions are not yet available. | [
"21",
"22"
] | 94 | 1,111 | 0 | false | In particular, reliable estimates for solvent and entropic interactions are not yet available. | [] | In particular, reliable estimates for solvent and entropic interactions are not yet available. | true | true | true | true | true | 192 |
0 | INTRODUCTION | 1 | 1 | [
"b1",
"b2",
"b3",
"b5",
"b6",
"b8"
] | 17,099,236 | pmid-8757721|pmid-12423780|pmid-1069283|pmid-9716496|pmid-4930244|pmid-4930243|pmid-10986462|pmid-11741540 | Colicins, which are produced by bacteria carrying the corresponding Col plasmids, kill sensitive Escherichia coli cells through activities involving the ion channels in the inner membranes, DNases or RNases (1,2). | [
"1",
"2",
"3",
"5",
"6",
"8"
] | 213 | 1,112 | 0 | false | Colicins, which are produced by bacteria carrying the corresponding Col plasmids, kill sensitive Escherichia coli cells through activities involving the ion channels in the inner membranes, DNases or RNases. | [
"1,2"
] | Colicins, which are produced by bacteria carrying the corresponding Col plasmids, kill sensitive Escherichia coli cells through activities involving the ion channels in the inner membranes, DNases or RNases. | true | true | true | true | true | 193 |
0 | INTRODUCTION | 1 | 1 | [
"b1",
"b2",
"b3",
"b5",
"b6",
"b8"
] | 17,099,236 | pmid-8757721|pmid-12423780|pmid-1069283|pmid-9716496|pmid-4930244|pmid-4930243|pmid-10986462|pmid-11741540 | The DNase-type colicins nonspecifically degrade the genomic DNAs of the sensitive cells (3–5), whereas those of the RNase type cleave 16S rRNA at the 49th phosphodiester bond from the 3′ end (6–8). | [
"1",
"2",
"3",
"5",
"6",
"8"
] | 197 | 1,113 | 0 | false | The DNase-type colicins nonspecifically degrade the genomic DNAs of the sensitive cells, whereas those of the RNase type cleave 16S rRNA at the 49th phosphodiester bond from the 3′ end. | [
"3–5",
"6–8"
] | The DNase-type colicins nonspecifically degrade the genomic DNAs of the sensitive cells, whereas those of the RNase type cleave 16S rRNA at the 49th phosphodiester bond from the 3′ end. | true | true | true | true | true | 193 |
0 | INTRODUCTION | 1 | 1 | [
"b1",
"b2",
"b3",
"b5",
"b6",
"b8"
] | 17,099,236 | pmid-8757721|pmid-12423780|pmid-1069283|pmid-9716496|pmid-4930244|pmid-4930243|pmid-10986462|pmid-11741540 | These colicins contain three domains—a membrane-translocating domain, a receptor-binding domain, and a catalytic domain—in their primary sequences. | [
"1",
"2",
"3",
"5",
"6",
"8"
] | 147 | 1,114 | 0 | false | These colicins contain three domains—a membrane-translocating domain, a receptor-binding domain, and a catalytic domain—in their primary sequences. | [] | These colicins contain three domains—a membrane-translocating domain, a receptor-binding domain, and a catalytic domain—in their primary sequences. | true | true | true | true | true | 193 |
0 | INTRODUCTION | 1 | 1 | [
"b1",
"b2",
"b3",
"b5",
"b6",
"b8"
] | 17,099,236 | pmid-8757721|pmid-12423780|pmid-1069283|pmid-9716496|pmid-4930244|pmid-4930243|pmid-10986462|pmid-11741540 | Colicinogenic cells also produce inhibitor proteins (Imm), the genes for which are located downstream of the col genes in the colicin operons that are under the control of the SOS-dependent promoters. | [
"1",
"2",
"3",
"5",
"6",
"8"
] | 200 | 1,115 | 0 | false | Colicinogenic cells also produce inhibitor proteins (Imm), the genes for which are located downstream of the col genes in the colicin operons that are under the control of the SOS-dependent promoters. | [] | Colicinogenic cells also produce inhibitor proteins (Imm), the genes for which are located downstream of the col genes in the colicin operons that are under the control of the SOS-dependent promoters. | true | true | true | true | true | 193 |
0 | INTRODUCTION | 1 | 1 | [
"b1",
"b2",
"b3",
"b5",
"b6",
"b8"
] | 17,099,236 | pmid-8757721|pmid-12423780|pmid-1069283|pmid-9716496|pmid-4930244|pmid-4930243|pmid-10986462|pmid-11741540 | Imms bind specifically to cognate colicins in order to protect their host cells. | [
"1",
"2",
"3",
"5",
"6",
"8"
] | 80 | 1,116 | 0 | false | Imms bind specifically to cognate colicins in order to protect their host cells. | [] | Imms bind specifically to cognate colicins in order to protect their host cells. | true | true | true | true | true | 193 |
1 | INTRODUCTION | 1 | 9 | [
"b9",
"b10",
"b11",
"b12"
] | 17,099,236 | pmid-388227|pmid-10092236|pmid-2549375|NA | In addition to the known RNase-type colicins, colicin E5 that has been recently characterized as a tRNase has a unique target for its toxicity. | [
"9",
"10",
"11",
"12"
] | 143 | 1,117 | 0 | false | In addition to the known RNase-type colicins, colicin E5 that has been recently characterized as a tRNase has a unique target for its toxicity. | [] | In addition to the known RNase-type colicins, colicin E5 that has been recently characterized as a tRNase has a unique target for its toxicity. | true | true | true | true | true | 194 |
1 | INTRODUCTION | 1 | 9 | [
"b9",
"b10",
"b11",
"b12"
] | 17,099,236 | pmid-388227|pmid-10092236|pmid-2549375|NA | It specifically cleaves the anticodons of E.coli tRNAs for Tyr, His, Asn and Asp. | [
"9",
"10",
"11",
"12"
] | 81 | 1,118 | 0 | false | It specifically cleaves the anticodons of E.coli tRNAs for Tyr, His, Asn and Asp. | [] | It specifically cleaves the anticodons of E.coli tRNAs for Tyr, His, Asn and Asp. | true | true | true | true | true | 194 |
1 | INTRODUCTION | 1 | 9 | [
"b9",
"b10",
"b11",
"b12"
] | 17,099,236 | pmid-388227|pmid-10092236|pmid-2549375|NA | These tRNAs decode NAY (N: any nucleotide, A: adenosine and Y: a pyrimidine nucleotide) codons by means of QUN anticodons, where queuosine (Q) is a 7-deazaguanosine with a cyclopentenediol side chain (9). | [
"9",
"10",
"11",
"12"
] | 204 | 1,119 | 1 | false | These tRNAs decode NAY (N: any nucleotide, A: adenosine and Y: a pyrimidine nucleotide) codons by means of QUN anticodons, where queuosine (Q) is a 7-deazaguanosine with a cyclopentenediol side chain. | [
"9"
] | These tRNAs decode NAY (N: any nucleotide, A: adenosine and Y: a pyrimidine nucleotide) codons by means of QUN anticodons, where queuosine (Q) is a 7-deazaguanosine with a cyclopentenediol side chain. | true | true | true | true | true | 194 |
1 | INTRODUCTION | 1 | 9 | [
"b9",
"b10",
"b11",
"b12"
] | 17,099,236 | pmid-388227|pmid-10092236|pmid-2549375|NA | Initially, colicin E5 was observed to cleave only the QU sequence of these tRNAs between positions 34 and 35, leaving a 2′,3′-cyclic phosphate on Q and a 5′-OH on U. | [
"9",
"10",
"11",
"12"
] | 165 | 1,120 | 0 | false | Initially, colicin E5 was observed to cleave only the QU sequence of these tRNAs between positions 34 and 35, leaving a 2′,3′-cyclic phosphate on Q and a 5′-OH on U. | [] | Initially, colicin E5 was observed to cleave only the QU sequence of these tRNAs between positions 34 and 35, leaving a 2′,3′-cyclic phosphate on Q and a 5′-OH on U. | true | true | true | true | true | 194 |
1 | INTRODUCTION | 1 | 9 | [
"b9",
"b10",
"b11",
"b12"
] | 17,099,236 | pmid-388227|pmid-10092236|pmid-2549375|NA | In tRNA-guanine transglycosylase-deficient strains the inherent G is not replaced with a precursor base of Q; this gives rise to tRNAs with GUN anticodons. | [
"9",
"10",
"11",
"12"
] | 155 | 1,121 | 0 | false | In tRNA-guanine transglycosylase-deficient strains the inherent G is not replaced with a precursor base of Q; this gives rise to tRNAs with GUN anticodons. | [] | In tRNA-guanine transglycosylase-deficient strains the inherent G is not replaced with a precursor base of Q; this gives rise to tRNAs with GUN anticodons. | true | true | true | true | true | 194 |
1 | INTRODUCTION | 1 | 10 | [
"b9",
"b10",
"b11",
"b12"
] | 17,099,236 | pmid-388227|pmid-10092236|pmid-2549375|NA | These strains were demonstrated to be sensitive to colicin E5; the tRNAs were still subjected to cleavage (10). | [
"9",
"10",
"11",
"12"
] | 111 | 1,122 | 1 | false | These strains were demonstrated to be sensitive to colicin E5; the tRNAs were still subjected to cleavage. | [
"10"
] | These strains were demonstrated to be sensitive to colicin E5; the tRNAs were still subjected to cleavage. | true | true | true | true | true | 194 |
1 | INTRODUCTION | 1 | 11 | [
"b9",
"b10",
"b11",
"b12"
] | 17,099,236 | pmid-388227|pmid-10092236|pmid-2549375|NA | It is assumed that colicin E5 consists of 556 amino acids (11). | [
"9",
"10",
"11",
"12"
] | 63 | 1,123 | 1 | false | It is assumed that colicin E5 consists of 556 amino acids. | [
"11"
] | It is assumed that colicin E5 consists of 556 amino acids. | true | true | true | true | true | 194 |
1 | INTRODUCTION | 1 | 9 | [
"b9",
"b10",
"b11",
"b12"
] | 17,099,236 | pmid-388227|pmid-10092236|pmid-2549375|NA | The ribonuclease activity of E5 resides solely within its C-terminal ribonuclease domain (E5-CRD; 115 amino acids), and this domain is responsible for its substrate specificity. | [
"9",
"10",
"11",
"12"
] | 177 | 1,124 | 0 | false | The ribonuclease activity of E5 resides solely within its C-terminal ribonuclease domain, and this domain is responsible for its substrate specificity. | [
"E5-CRD; 115 amino acids"
] | The ribonuclease activity of E5 resides solely within its C-terminal ribonuclease domain, and this domain is responsible for its substrate specificity. | true | true | true | true | true | 194 |
1 | INTRODUCTION | 1 | 12 | [
"b9",
"b10",
"b11",
"b12"
] | 17,099,236 | pmid-388227|pmid-10092236|pmid-2549375|NA | Furthermore, based on the results obtained from our assay using synthetic minihelices or linear oligoribonucleotides, E5-CRD can be referred to as an RNA restriction enzyme that specifically recognizes and cleaves single-stranded GU sequences (12). | [
"9",
"10",
"11",
"12"
] | 248 | 1,125 | 1 | false | Furthermore, based on the results obtained from our assay using synthetic minihelices or linear oligoribonucleotides, E5-CRD can be referred to as an RNA restriction enzyme that specifically recognizes and cleaves single-stranded GU sequences. | [
"12"
] | Furthermore, based on the results obtained from our assay using synthetic minihelices or linear oligoribonucleotides, E5-CRD can be referred to as an RNA restriction enzyme that specifically recognizes and cleaves single-stranded GU sequences. | true | true | true | true | true | 194 |
2 | INTRODUCTION | 1 | 13 | [
"b13",
"b14",
"b15",
"b16",
"b17"
] | 17,099,236 | pmid-10880568|pmid-10664586|pmid-16244131|pmid-15014439|pmid-15336558 | In addition to colicin E5, colicin D (13), PrrC (14) and zymocin (15) are also known to be tRNases. | [
"13",
"14",
"15",
"16",
"17"
] | 99 | 1,126 | 1 | false | In addition to colicin E5, colicin D, PrrC and zymocin are also known to be tRNases. | [
"13",
"14",
"15"
] | In addition to colicin E5, colicin D, PrrC and zymocin are also known to be tRNases. | true | true | true | true | true | 195 |
2 | INTRODUCTION | 1 | 13 | [
"b13",
"b14",
"b15",
"b16",
"b17"
] | 17,099,236 | pmid-10880568|pmid-10664586|pmid-16244131|pmid-15014439|pmid-15336558 | However, these enzymes are nonhomologous with each other and target tRNAs and cleavage sites that are different from those targeted by colicin E5. | [
"13",
"14",
"15",
"16",
"17"
] | 146 | 1,127 | 0 | false | However, these enzymes are nonhomologous with each other and target tRNAs and cleavage sites that are different from those targeted by colicin E5. | [] | However, these enzymes are nonhomologous with each other and target tRNAs and cleavage sites that are different from those targeted by colicin E5. | true | true | true | true | true | 195 |
2 | INTRODUCTION | 1 | 13 | [
"b13",
"b14",
"b15",
"b16",
"b17"
] | 17,099,236 | pmid-10880568|pmid-10664586|pmid-16244131|pmid-15014439|pmid-15336558 | Colicin D, which is produced by E.coli harboring a ColD plasmid, cleaves only four isoacceptors of tRNAArg between positions 38 and 39 at the 3′ junction of the anticodon stem and loop. | [
"13",
"14",
"15",
"16",
"17"
] | 185 | 1,128 | 0 | false | Colicin D, which is produced by E.coli harboring a ColD plasmid, cleaves only four isoacceptors of tRNAArg between positions 38 and 39 at the 3′ junction of the anticodon stem and loop. | [] | Colicin D, which is produced by E.coli harboring a ColD plasmid, cleaves only four isoacceptors of tRNAArg between positions 38 and 39 at the 3′ junction of the anticodon stem and loop. | true | true | true | true | true | 195 |
2 | INTRODUCTION | 1 | 13 | [
"b13",
"b14",
"b15",
"b16",
"b17"
] | 17,099,236 | pmid-10880568|pmid-10664586|pmid-16244131|pmid-15014439|pmid-15336558 | PrrC is induced in some E.coli isolates by T4 phage infection, and it only cleaves tRNALys between positions 33 and 34 at the 5′ side of the anticodon. | [
"13",
"14",
"15",
"16",
"17"
] | 151 | 1,129 | 0 | false | PrrC is induced in some E.coli isolates by T4 phage infection, and it only cleaves tRNALys between positions 33 and 34 at the 5′ side of the anticodon. | [] | PrrC is induced in some E.coli isolates by T4 phage infection, and it only cleaves tRNALys between positions 33 and 34 at the 5′ side of the anticodon. | true | true | true | true | true | 195 |
2 | INTRODUCTION | 1 | 13 | [
"b13",
"b14",
"b15",
"b16",
"b17"
] | 17,099,236 | pmid-10880568|pmid-10664586|pmid-16244131|pmid-15014439|pmid-15336558 | Zymocin, which is produced by Kluyveromyces lactis, was recently reported to cleave some yeast tRNAs at the 3′ side of the modified nucleotide U in the anticodons of 5-methoxycarbonylmethyl-2-thiouridine uridine cytosine (mcm5s2UUC), mcm5s2UUU | [
"13",
"14",
"15",
"16",
"17"
] | 243 | 1,130 | 0 | false | Zymocin, which is produced by Kluyveromyces lactis, was recently reported to cleave some yeast tRNAs at the 3′ side of the modified nucleotide U in the anticodons of 5-methoxycarbonylmethyl-2-thiouridine uridine cytosine (mcm5s2UUC), mcm5s2UUU | [] | Zymocin, which is produced by Kluyveromyces lactis, was recently reported to cleave some yeast tRNAs at the 3′ side of the modified nucleotide U in the anticodons of 5-methoxycarbonylmethyl-2-thiouridine uridine cytosine (mcm5s2UUC), mcm5s2UUU | true | true | false | true | false | 195 |
2 | INTRODUCTION | 1 | 13 | [
"b13",
"b14",
"b15",
"b16",
"b17"
] | 17,099,236 | pmid-10880568|pmid-10664586|pmid-16244131|pmid-15014439|pmid-15336558 | and mcm5s2UUG. | [
"13",
"14",
"15",
"16",
"17"
] | 14 | 1,131 | 0 | false | and mcm5s2UUG. | [] | and mcm5s2UUG. | false | true | true | true | false | 195 |
2 | INTRODUCTION | 1 | 13 | [
"b13",
"b14",
"b15",
"b16",
"b17"
] | 17,099,236 | pmid-10880568|pmid-10664586|pmid-16244131|pmid-15014439|pmid-15336558 | Among these tRNases, the crystal structure of the C-terminal catalytic domain of colicin D (D-CRD) has been solved (16,17); the structure revealed a curved row of basic residues on the molecular surface that could confer the tRNA recognition specificity. | [
"13",
"14",
"15",
"16",
"17"
] | 254 | 1,132 | 0 | false | Among these tRNases, the crystal structure of the C-terminal catalytic domain of colicin D (D-CRD) has been solved ; the structure revealed a curved row of basic residues on the molecular surface that could confer the tRNA recognition specificity. | [
"16,17"
] | Among these tRNases, the crystal structure of the C-terminal catalytic domain of colicin D (D-CRD) has been solved ; the structure revealed a curved row of basic residues on the molecular surface that could confer the tRNA recognition specificity. | true | true | true | true | true | 195 |
3 | INTRODUCTION | 1 | 18 | [
"b18",
"b19"
] | 17,099,236 | pmid-15537630|pmid-12526800 | ImmE5—a specific inhibitor protein of colicin E5—is expressed in host cells and binds to E5-CRD to prevent cell death. | [
"18",
"19"
] | 118 | 1,133 | 0 | false | ImmE5—a specific inhibitor protein of colicin E5—is expressed in host cells and binds to E5-CRD to prevent cell death. | [] | ImmE5—a specific inhibitor protein of colicin E5—is expressed in host cells and binds to E5-CRD to prevent cell death. | true | true | true | true | true | 196 |
3 | INTRODUCTION | 1 | 18 | [
"b18",
"b19"
] | 17,099,236 | pmid-15537630|pmid-12526800 | In addition to the nuclease-type colicin family, this type of proteinaceous toxin–antitoxin system (comprising addiction molecules), including MazE/F (18) and RelB/E (19) whose targets are considered to be the ACA sequences in mRNAs and stop codons of mRNAs in the ribosomal A site, respectively, has also been well studied. | [
"18",
"19"
] | 324 | 1,134 | 1 | false | In addition to the nuclease-type colicin family, this type of proteinaceous toxin–antitoxin system (comprising addiction molecules), including MazE/F and RelB/E whose targets are considered to be the ACA sequences in mRNAs and stop codons of mRNAs in the ribosomal A site, respectively, has also been well studied. | [
"18",
"19"
] | In addition to the nuclease-type colicin family, this type of proteinaceous toxin–antitoxin system (comprising addiction molecules), including MazE/F and RelB/E whose targets are considered to be the ACA sequences in mRNAs and stop codons of mRNAs in the ribosomal A site, respectively, has also been well studied. | true | true | true | true | true | 196 |
3 | INTRODUCTION | 1 | 18 | [
"b18",
"b19"
] | 17,099,236 | pmid-15537630|pmid-12526800 | The study of these molecules reveals the survival mechanism in bacteria; additionally, they serve as very good examples of protein–protein interactions. | [
"18",
"19"
] | 152 | 1,135 | 0 | false | The study of these molecules reveals the survival mechanism in bacteria; additionally, they serve as very good examples of protein–protein interactions. | [] | The study of these molecules reveals the survival mechanism in bacteria; additionally, they serve as very good examples of protein–protein interactions. | true | true | true | true | true | 196 |
3 | INTRODUCTION | 1 | 18 | [
"b18",
"b19"
] | 17,099,236 | pmid-15537630|pmid-12526800 | Furthermore, from the structural viewpoint, it is of special interest to determine whether ribonuclease inhibitors, i.e. | [
"18",
"19"
] | 120 | 1,136 | 0 | false | Furthermore, from the structural viewpoint, it is of special interest to determine whether ribonuclease inhibitors, i.e. | [] | Furthermore, from the structural viewpoint, it is of special interest to determine whether ribonuclease inhibitors, i.e. | true | true | true | true | true | 196 |
3 | INTRODUCTION | 1 | 18 | [
"b18",
"b19"
] | 17,099,236 | pmid-15537630|pmid-12526800 | inhibitors of toxins that target DNA or RNA, bind to the corresponding enzymes by mimicking the substrate RNAs/DNAs. | [
"18",
"19"
] | 116 | 1,137 | 0 | false | inhibitors of toxins that target DNA or RNA, bind to the corresponding enzymes by mimicking the substrate RNAs/DNAs. | [] | inhibitors of toxins that target DNA or RNA, bind to the corresponding enzymes by mimicking the substrate RNAs/DNAs. | false | true | true | true | false | 196 |
4 | INTRODUCTION | 0 | null | null | 17,099,236 | pmid-14580342|pmid-15901733|pmid-12718874 | Further, although E5-CRD exhibits ribonuclease activity, it lacks His that usually serves as a catalytic residue in all known ribonucleases. | null | 140 | 1,138 | 0 | false | null | null | Further, although E5-CRD exhibits ribonuclease activity, it lacks His that usually serves as a catalytic residue in all known ribonucleases. | true | true | true | true | true | 197 |
4 | INTRODUCTION | 0 | null | null | 17,099,236 | pmid-14580342|pmid-15901733|pmid-12718874 | Thus, E5-CRD must have an alternative mechanism that is responsible for its ribonuclease activity. | null | 98 | 1,139 | 0 | false | null | null | Thus, E5-CRD must have an alternative mechanism that is responsible for its ribonuclease activity. | true | true | true | true | true | 197 |
5 | INTRODUCTION | 1 | 20 | [
"b20",
"b21"
] | 17,099,236 | pmid-16060658|pmid-16524591|pmid-10092236 | Since E5-CRD shows no homology with any other proteins, we performed the structural analysis of E5-CRD in order to explore the novel features of colicin E5. | [
"20",
"21"
] | 156 | 1,140 | 0 | false | Since E5-CRD shows no homology with any other proteins, we performed the structural analysis of E5-CRD in order to explore the novel features of colicin E5. | [] | Since E5-CRD shows no homology with any other proteins, we performed the structural analysis of E5-CRD in order to explore the novel features of colicin E5. | true | true | true | true | true | 198 |
5 | INTRODUCTION | 1 | 20 | [
"b20",
"b21"
] | 17,099,236 | pmid-16060658|pmid-16524591|pmid-10092236 | Recently, Huang's group has reported the structures of E5-CRD (20) and E5-CRD complexed with ImmE5 (21) at a resolution of 1.5 and 1.15 Å, respectively; they also proposed a putative model of the interaction between E5-CRD and tRNA. | [
"20",
"21"
] | 232 | 1,141 | 1 | false | Recently, Huang's group has reported the structures of E5-CRD and E5-CRD complexed with ImmE5 at a resolution of 1.5 and 1.15 Å, respectively; they also proposed a putative model of the interaction between E5-CRD and tRNA. | [
"20",
"21"
] | Recently, Huang's group has reported the structures of E5-CRD and E5-CRD complexed with ImmE5 at a resolution of 1.5 and 1.15 Å, respectively; they also proposed a putative model of the interaction between E5-CRD and tRNA. | true | true | true | true | true | 198 |
5 | INTRODUCTION | 1 | 20 | [
"b20",
"b21"
] | 17,099,236 | pmid-16060658|pmid-16524591|pmid-10092236 | However, the precise structure of the active site in the pocket with catalytic residues remains unknown. | [
"20",
"21"
] | 104 | 1,142 | 0 | false | However, the precise structure of the active site in the pocket with catalytic residues remains unknown. | [] | However, the precise structure of the active site in the pocket with catalytic residues remains unknown. | true | true | true | true | true | 198 |
5 | INTRODUCTION | 1 | 20 | [
"b20",
"b21"
] | 17,099,236 | pmid-16060658|pmid-16524591|pmid-10092236 | Here, we report the crystal structures of E5-CRD complexed with its substrate analog and E5-CRD complexed with ImmE5. | [
"20",
"21"
] | 117 | 1,143 | 0 | false | Here, we report the crystal structures of E5-CRD complexed with its substrate analog and E5-CRD complexed with ImmE5. | [] | Here, we report the crystal structures of E5-CRD complexed with its substrate analog and E5-CRD complexed with ImmE5. | true | true | true | true | true | 198 |
5 | INTRODUCTION | 1 | 20 | [
"b20",
"b21"
] | 17,099,236 | pmid-16060658|pmid-16524591|pmid-10092236 | These structures clearly demonstrate the mechanism by which specific substrate recognition is achieved and reveal the residues that could play important roles for the catalytic activity in the absence of His. | [
"20",
"21"
] | 208 | 1,144 | 0 | false | These structures clearly demonstrate the mechanism by which specific substrate recognition is achieved and reveal the residues that could play important roles for the catalytic activity in the absence of His. | [] | These structures clearly demonstrate the mechanism by which specific substrate recognition is achieved and reveal the residues that could play important roles for the catalytic activity in the absence of His. | true | true | true | true | true | 198 |
5 | INTRODUCTION | 1 | 20 | [
"b20",
"b21"
] | 17,099,236 | pmid-16060658|pmid-16524591|pmid-10092236 | Based on these structures, we propose the double mimicry model to demonstrate the mechanism by which the protein–protein interaction replaces the RNA–RNA interaction. | [
"20",
"21"
] | 166 | 1,145 | 0 | false | Based on these structures, we propose the double mimicry model to demonstrate the mechanism by which the protein–protein interaction replaces the RNA–RNA interaction. | [] | Based on these structures, we propose the double mimicry model to demonstrate the mechanism by which the protein–protein interaction replaces the RNA–RNA interaction. | true | true | true | true | true | 198 |
0 | DISCUSSION | 1 | 27 | [
"b27",
"b28"
] | 17,099,236 | pmid-8757721|pmid-12423780|pmid-1069283|pmid-9716496|pmid-4930244|pmid-4930243|pmid-10986462|pmid-11741540 | Among the colicin family proteins, the crystal structure of RNase-type colicin E3 has been reported (27,28). | [
"27",
"28"
] | 108 | 1,146 | 0 | false | Among the colicin family proteins, the crystal structure of RNase-type colicin E3 has been reported. | [
"27,28"
] | Among the colicin family proteins, the crystal structure of RNase-type colicin E3 has been reported. | true | true | true | true | true | 199 |
0 | DISCUSSION | 1 | 27 | [
"b27",
"b28"
] | 17,099,236 | pmid-8757721|pmid-12423780|pmid-1069283|pmid-9716496|pmid-4930244|pmid-4930243|pmid-10986462|pmid-11741540 | Colicins E3 and E5 are homologous at the receptor-binding and membrane-translocating domains. | [
"27",
"28"
] | 93 | 1,147 | 0 | false | Colicins E3 and E5 are homologous at the receptor-binding and membrane-translocating domains. | [] | Colicins E3 and E5 are homologous at the receptor-binding and membrane-translocating domains. | true | true | true | true | true | 199 |
0 | DISCUSSION | 1 | 27 | [
"b27",
"b28"
] | 17,099,236 | pmid-8757721|pmid-12423780|pmid-1069283|pmid-9716496|pmid-4930244|pmid-4930243|pmid-10986462|pmid-11741540 | On the other hand, the catalytic domains of both these colicins showed no homology, reflecting completely different targets. | [
"27",
"28"
] | 124 | 1,148 | 0 | false | On the other hand, the catalytic domains of both these colicins showed no homology, reflecting completely different targets. | [] | On the other hand, the catalytic domains of both these colicins showed no homology, reflecting completely different targets. | true | true | true | true | true | 199 |
0 | DISCUSSION | 1 | 27 | [
"b27",
"b28"
] | 17,099,236 | pmid-8757721|pmid-12423780|pmid-1069283|pmid-9716496|pmid-4930244|pmid-4930243|pmid-10986462|pmid-11741540 | Colicin E5 is a tRNase that specifically targets the GU and QU sequences of the anticodons specifically. | [
"27",
"28"
] | 104 | 1,149 | 0 | false | Colicin E5 is a tRNase that specifically targets the GU and QU sequences of the anticodons specifically. | [] | Colicin E5 is a tRNase that specifically targets the GU and QU sequences of the anticodons specifically. | true | true | true | true | true | 199 |
0 | DISCUSSION | 1 | 27 | [
"b27",
"b28"
] | 17,099,236 | pmid-8757721|pmid-12423780|pmid-1069283|pmid-9716496|pmid-4930244|pmid-4930243|pmid-10986462|pmid-11741540 | In order to understand this specific recognition mechanism, we solved the crystal structure of the C-terminal tRNase domain of colicin E5 complexed with its substrate analog, dGpdUp. | [
"27",
"28"
] | 182 | 1,150 | 0 | false | In order to understand this specific recognition mechanism, we solved the crystal structure of the C-terminal tRNase domain of colicin E5 complexed with its substrate analog, dGpdUp. | [] | In order to understand this specific recognition mechanism, we solved the crystal structure of the C-terminal tRNase domain of colicin E5 complexed with its substrate analog, dGpdUp. | true | true | true | true | true | 199 |
0 | DISCUSSION | 1 | 27 | [
"b27",
"b28"
] | 17,099,236 | pmid-8757721|pmid-12423780|pmid-1069283|pmid-9716496|pmid-4930244|pmid-4930243|pmid-10986462|pmid-11741540 | The tight binding of dGpdUp to E5-CRD was achieved by ring–ring-interactions and the maximum possible hydrogen bonds, suggesting the mimicry of Watson–Crick-type interactions in both dG and dU (Figure 3A and C). | [
"27",
"28"
] | 211 | 1,151 | 0 | false | The tight binding of dGpdUp to E5-CRD was achieved by ring–ring-interactions and the maximum possible hydrogen bonds, suggesting the mimicry of Watson–Crick-type interactions in both dG and dU (Figure 3A and C). | [] | The tight binding of dGpdUp to E5-CRD was achieved by ring–ring-interactions and the maximum possible hydrogen bonds, suggesting the mimicry of Watson–Crick-type interactions in both dG and dU (Figure 3A and C). | true | true | true | true | true | 199 |
0 | DISCUSSION | 1 | 27 | [
"b27",
"b28"
] | 17,099,236 | pmid-8757721|pmid-12423780|pmid-1069283|pmid-9716496|pmid-4930244|pmid-4930243|pmid-10986462|pmid-11741540 | If the dG base were to be substituted by dA, none of these hydrogen bonds would be possible. | [
"27",
"28"
] | 92 | 1,152 | 0 | false | If the dG base were to be substituted by dA, none of these hydrogen bonds would be possible. | [] | If the dG base were to be substituted by dA, none of these hydrogen bonds would be possible. | true | true | true | true | true | 199 |
0 | DISCUSSION | 1 | 27 | [
"b27",
"b28"
] | 17,099,236 | pmid-8757721|pmid-12423780|pmid-1069283|pmid-9716496|pmid-4930244|pmid-4930243|pmid-10986462|pmid-11741540 | In contrast, if the same dG base was to be substituted by a Q base, all these hydrogen bonds would be retained, while the modification extending from the N7 position would easily extend into the solvent. | [
"27",
"28"
] | 203 | 1,153 | 0 | false | In contrast, if the same dG base was to be substituted by a Q base, all these hydrogen bonds would be retained, while the modification extending from the N7 position would easily extend into the solvent. | [] | In contrast, if the same dG base was to be substituted by a Q base, all these hydrogen bonds would be retained, while the modification extending from the N7 position would easily extend into the solvent. | true | true | true | true | true | 199 |
0 | DISCUSSION | 1 | 27 | [
"b27",
"b28"
] | 17,099,236 | pmid-8757721|pmid-12423780|pmid-1069283|pmid-9716496|pmid-4930244|pmid-4930243|pmid-10986462|pmid-11741540 | The above modeling consideration is consistent with the experimental observation that the tRNAs with Q as well as the corresponding molecules without Q are cleaved by E5-CRD. | [
"27",
"28"
] | 174 | 1,154 | 0 | false | The above modeling consideration is consistent with the experimental observation that the tRNAs with Q as well as the corresponding molecules without Q are cleaved by E5-CRD. | [] | The above modeling consideration is consistent with the experimental observation that the tRNAs with Q as well as the corresponding molecules without Q are cleaved by E5-CRD. | true | true | true | true | true | 199 |
1 | DISCUSSION | 0 | null | null | 17,099,236 | pmid-388227|pmid-10092236|pmid-2549375|NA | If the dU base were to be substituted by dC, only one hydrogen bond would be retained. | null | 86 | 1,155 | 0 | false | null | null | If the dU base were to be substituted by dC, only one hydrogen bond would be retained. | true | true | true | true | true | 200 |
1 | DISCUSSION | 0 | null | null | 17,099,236 | pmid-388227|pmid-10092236|pmid-2549375|NA | Thus, the nucleotide sequence G (or Q)-U appears to be favored by E5-CRD through the formation of maximum possible hydrogen bonds and aromatic ring (or pseudo ring) stacking interactions. | null | 187 | 1,156 | 0 | false | null | null | Thus, the nucleotide sequence G (or Q)-U appears to be favored by E5-CRD through the formation of maximum possible hydrogen bonds and aromatic ring (or pseudo ring) stacking interactions. | true | true | true | true | true | 200 |
1 | DISCUSSION | 0 | null | null | 17,099,236 | pmid-388227|pmid-10092236|pmid-2549375|NA | All the hydrogen bonds use the backbone amide N or carbonyl O of E5-CRD, except hydroxyl O of Ser52. | null | 100 | 1,157 | 0 | false | null | null | All the hydrogen bonds use the backbone amide N or carbonyl O of E5-CRD, except hydroxyl O of Ser52. | true | true | true | true | true | 200 |
2 | DISCUSSION | 0 | null | null | 17,099,236 | pmid-10880568|pmid-10664586|pmid-16244131|pmid-15014439|pmid-15336558 | In addition to the interactions of the bases by the hydrogen bonds and ring interactions, backbone phosphates are also retained by several hydrogen bonds. | null | 154 | 1,158 | 0 | false | null | null | In addition to the interactions of the bases by the hydrogen bonds and ring interactions, backbone phosphates are also retained by several hydrogen bonds. | true | true | true | true | true | 201 |
2 | DISCUSSION | 0 | null | null | 17,099,236 | pmid-10880568|pmid-10664586|pmid-16244131|pmid-15014439|pmid-15336558 | Thus, this observation also suggests that E5-CRD has less flexibility for substrate recognition; this results in binding to only the specific target. | null | 149 | 1,159 | 0 | false | null | null | Thus, this observation also suggests that E5-CRD has less flexibility for substrate recognition; this results in binding to only the specific target. | true | true | true | true | true | 201 |
3 | DISCUSSION | 0 | null | null | 17,099,236 | pmid-15537630|pmid-12526800 | These findings explain that the specific cleavage of the Q(G)UN anticodon sequence by E5-CRD is based on the GU-specific base recognition by E5-CRD. | null | 148 | 1,160 | 0 | false | null | null | These findings explain that the specific cleavage of the Q(G)UN anticodon sequence by E5-CRD is based on the GU-specific base recognition by E5-CRD. | true | true | true | true | true | 202 |
3 | DISCUSSION | 0 | null | null | 17,099,236 | pmid-15537630|pmid-12526800 | In addition, this specific recognition between the protein and the RNA is realized in a manner similar to the Watson–Crick-type interaction used in an RNA double strand. | null | 169 | 1,161 | 0 | false | null | null | In addition, this specific recognition between the protein and the RNA is realized in a manner similar to the Watson–Crick-type interaction used in an RNA double strand. | true | true | true | true | true | 202 |
4 | DISCUSSION | 1 | 29 | [
"b29",
"b30",
"b31"
] | 17,099,236 | pmid-14580342|pmid-15901733|pmid-12718874 | There are several examples of RNAs being processed in a site-specific manner. | [
"29",
"30",
"31"
] | 77 | 1,162 | 0 | false | There are several examples of RNAs being processed in a site-specific manner. | [] | There are several examples of RNAs being processed in a site-specific manner. | true | true | true | true | true | 203 |
4 | DISCUSSION | 1 | 29 | [
"b29",
"b30",
"b31"
] | 17,099,236 | pmid-14580342|pmid-15901733|pmid-12718874 | MazF and ChpBK cleave free RNAs at the ACA and ACY (Y: U, A or G) sequences, respectively (29,30). | [
"29",
"30",
"31"
] | 98 | 1,163 | 0 | false | MazF and ChpBK cleave free RNAs at the ACA and ACY (Y: U, A or G) sequences, respectively. | [
"29,30"
] | MazF and ChpBK cleave free RNAs at the ACA and ACY (Y: U, A or G) sequences, respectively. | true | true | true | true | true | 203 |
4 | DISCUSSION | 1 | 29 | [
"b29",
"b30",
"b31"
] | 17,099,236 | pmid-14580342|pmid-15901733|pmid-12718874 | Both proteins are E.coli chromosomal toxins and inhibit translation by cleaving mRNA. | [
"29",
"30",
"31"
] | 85 | 1,164 | 0 | false | Both proteins are E.coli chromosomal toxins and inhibit translation by cleaving mRNA. | [] | Both proteins are E.coli chromosomal toxins and inhibit translation by cleaving mRNA. | true | true | true | true | true | 203 |
4 | DISCUSSION | 1 | 31 | [
"b29",
"b30",
"b31"
] | 17,099,236 | pmid-14580342|pmid-15901733|pmid-12718874 | The crystal structure of MazF has been recently reported (31); however, no structural information on its substrate binding is available. | [
"29",
"30",
"31"
] | 136 | 1,165 | 1 | false | The crystal structure of MazF has been recently reported ; however, no structural information on its substrate binding is available. | [
"31"
] | The crystal structure of MazF has been recently reported ; however, no structural information on its substrate binding is available. | true | true | true | true | true | 203 |
5 | DISCUSSION | 1 | 10 | [
"b10"
] | 17,099,236 | pmid-16060658|pmid-16524591|pmid-10092236 | Although there should be a large number of GU sequences in cellular RNAs, E5 preferentially acts on tRNA anticodons in vivo (10). | [
"10"
] | 129 | 1,166 | 1 | false | Although there should be a large number of GU sequences in cellular RNAs, E5 preferentially acts on tRNA anticodons in vivo. | [
"10"
] | Although there should be a large number of GU sequences in cellular RNAs, E5 preferentially acts on tRNA anticodons in vivo. | true | true | true | true | true | 204 |
5 | DISCUSSION | 1 | 10 | [
"b10"
] | 17,099,236 | pmid-16060658|pmid-16524591|pmid-10092236 | When we docked E5-CRD and a tRNA molecule (tRNAAsp, PDB code 1ASY) manually by superimposing dGpdUp and GU of the tRNA, E5-CRD made contact only with the anticodon arm of tRNA (Figure 5). | [
"10"
] | 187 | 1,167 | 0 | false | When we docked E5-CRD and a tRNA molecule (tRNAAsp, PDB code 1ASY) manually by superimposing dGpdUp and GU of the tRNA, E5-CRD made contact only with the anticodon arm of tRNA (Figure 5). | [] | When we docked E5-CRD and a tRNA molecule manually by superimposing dGpdUp and GU of the tRNA, E5-CRD made contact only with the anticodon arm of tRNA (Figure 5). | true | true | true | true | true | 204 |
5 | DISCUSSION | 1 | 10 | [
"b10"
] | 17,099,236 | pmid-16060658|pmid-16524591|pmid-10092236 | Interestingly, the parallel helix of E5-CRD fits in the helix of the anticodon arm. | [
"10"
] | 83 | 1,168 | 0 | false | Interestingly, the parallel helix of E5-CRD fits in the helix of the anticodon arm. | [] | Interestingly, the parallel helix of E5-CRD fits in the helix of the anticodon arm. | true | true | true | true | true | 204 |
5 | DISCUSSION | 1 | 10 | [
"b10"
] | 17,099,236 | pmid-16060658|pmid-16524591|pmid-10092236 | This may explain the substrate specificity of tRNA, where E5-CRD tightly binds to tRNA thereby allowing the capture of G–U bases at the bottom of the binding pocket. | [
"10"
] | 165 | 1,169 | 0 | false | This may explain the substrate specificity of tRNA, where E5-CRD tightly binds to tRNA thereby allowing the capture of G–U bases at the bottom of the binding pocket. | [] | This may explain the substrate specificity of tRNA, where E5-CRD tightly binds to tRNA thereby allowing the capture of G–U bases at the bottom of the binding pocket. | true | true | true | true | true | 204 |
5 | DISCUSSION | 1 | 10 | [
"b10"
] | 17,099,236 | pmid-16060658|pmid-16524591|pmid-10092236 | Therefore, E5-CRD may prefer GU sequences embedded in specific secondary structures such as anticodon loops, and in fact, the enzyme kinetic study also demonstrated this GU preference by E5-CRD (12). | [
"10"
] | 199 | 1,170 | 0 | false | Therefore, E5-CRD may prefer GU sequences embedded in specific secondary structures such as anticodon loops, and in fact, the enzyme kinetic study also demonstrated this GU preference by E5-CRD (12). | [] | Therefore, E5-CRD may prefer GU sequences embedded in specific secondary structures such as anticodon loops, and in fact, the enzyme kinetic study also demonstrated this GU preference by E5-CRD. | true | true | true | true | true | 204 |
6 | DISCUSSION | 1 | 32 | [
"b32"
] | 17,099,236 | pmid-11848924 | If E5-CRD is a true ribonuclease that lacks His, which residues serve as the catalysts? | [
"32"
] | 87 | 1,171 | 0 | false | If E5-CRD is a true ribonuclease that lacks His, which residues serve as the catalysts? | [] | If E5-CRD is a true ribonuclease that lacks His, which residues serve as the catalysts? | true | true | true | true | true | 205 |
6 | DISCUSSION | 1 | 32 | [
"b32"
] | 17,099,236 | pmid-11848924 | Based on the crystal structure of the E5-CRD/dGpdUp complex, only Lys25, Lys60 and Arg33 were observed as charged residues with the proximity of the phosphates in the substrate (Figure 3B). | [
"32"
] | 189 | 1,172 | 0 | false | Based on the crystal structure of the E5-CRD/dGpdUp complex, only Lys25, Lys60 and Arg33 were observed as charged residues with the proximity of the phosphates in the substrate (Figure 3B). | [] | Based on the crystal structure of the E5-CRD/dGpdUp complex, only Lys25, Lys60 and Arg33 were observed as charged residues with the proximity of the phosphates in the substrate. | true | true | true | true | true | 205 |
6 | DISCUSSION | 1 | 32 | [
"b32"
] | 17,099,236 | pmid-11848924 | With reference to the well-studied case of pancreatic RNase A in which His12 is a general base located close to 2′-OH and His119 is a general acid located close to 5′-O in the 2′,3′-cyclizing step (32), Arg33 may position itself corresponding to that of His12, and Lys25 or Lys60 may position itself corresponding to that of His119. | [
"32"
] | 332 | 1,173 | 1 | false | With reference to the well-studied case of pancreatic RNase A in which His12 is a general base located close to 2′-OH and His119 is a general acid located close to 5′-O in the 2′,3′-cyclizing step, Arg33 may position itself corresponding to that of His12, and Lys25 or Lys60 may position itself corresponding to that of His119. | [
"32"
] | With reference to the well-studied case of pancreatic RNase A in which His12 is a general base located close to 2′-OH and His119 is a general acid located close to 5′-O in the 2′,3′-cyclizing step, Arg33 may position itself corresponding to that of His12, and Lys25 or Lys60 may position itself corresponding to that of His119. | true | true | true | true | true | 205 |
6 | DISCUSSION | 1 | 32 | [
"b32"
] | 17,099,236 | pmid-11848924 | The mutation analysis revealed that both R33Q and K25Q/K60Q mutants lost their killing activity, and either of the K25Q or the K60Q mutant exhibited a decreased activity. | [
"32"
] | 170 | 1,174 | 0 | false | The mutation analysis revealed that both R33Q and K25Q/K60Q mutants lost their killing activity, and either of the K25Q or the K60Q mutant exhibited a decreased activity. | [] | The mutation analysis revealed that both R33Q and K25Q/K60Q mutants lost their killing activity, and either of the K25Q or the K60Q mutant exhibited a decreased activity. | true | true | true | true | true | 205 |
6 | DISCUSSION | 1 | 32 | [
"b32"
] | 17,099,236 | pmid-11848924 | Thus, this result suggests that these three basic residues are important for the catalytic activity. | [
"32"
] | 100 | 1,175 | 0 | false | Thus, this result suggests that these three basic residues are important for the catalytic activity. | [] | Thus, this result suggests that these three basic residues are important for the catalytic activity. | true | true | true | true | true | 205 |
6 | DISCUSSION | 1 | 32 | [
"b32"
] | 17,099,236 | pmid-11848924 | Interestingly, E5-CRD preferred a very high pH to cleave a dinucleotide substrate (12). | [
"32"
] | 87 | 1,176 | 0 | false | Interestingly, E5-CRD preferred a very high pH to cleave a dinucleotide substrate (12). | [] | Interestingly, E5-CRD preferred a very high pH to cleave a dinucleotide substrate. | true | true | true | true | true | 205 |
6 | DISCUSSION | 1 | 32 | [
"b32"
] | 17,099,236 | pmid-11848924 | The normally accepted pKa values of the Arg and Lys side chains might explain this unusual pH preference. | [
"32"
] | 105 | 1,177 | 0 | false | The normally accepted pKa values of the Arg and Lys side chains might explain this unusual pH preference. | [] | The normally accepted pKa values of the Arg and Lys side chains might explain this unusual pH preference. | true | true | true | true | true | 205 |
6 | DISCUSSION | 1 | 32 | [
"b32"
] | 17,099,236 | pmid-11848924 | In addition, the carbonyl group of Ile94 is close to the guanidino group of Arg33, thereby forming a hydrogen bond; this possibly increases the basicity of the protonated guanidino group of Arg33. | [
"32"
] | 196 | 1,178 | 0 | false | In addition, the carbonyl group of Ile94 is close to the guanidino group of Arg33, thereby forming a hydrogen bond; this possibly increases the basicity of the protonated guanidino group of Arg33. | [] | In addition, the carbonyl group of Ile94 is close to the guanidino group of Arg33, thereby forming a hydrogen bond; this possibly increases the basicity of the protonated guanidino group of Arg33. | true | true | true | true | true | 205 |
6 | DISCUSSION | 1 | 32 | [
"b32"
] | 17,099,236 | pmid-11848924 | However, we could not thoroughly measure the activity at higher pH values due to RNA instability. | [
"32"
] | 97 | 1,179 | 0 | false | However, we could not thoroughly measure the activity at higher pH values due to RNA instability. | [] | However, we could not thoroughly measure the activity at higher pH values due to RNA instability. | true | true | true | true | true | 205 |
6 | DISCUSSION | 1 | 32 | [
"b32"
] | 17,099,236 | pmid-11848924 | On the other hand, in E.coli cells, in which it is difficult to achieve high pH values under physiological conditions, both Arg and Lys are assumed to be protonated. | [
"32"
] | 165 | 1,180 | 0 | false | On the other hand, in E.coli cells, in which it is difficult to achieve high pH values under physiological conditions, both Arg and Lys are assumed to be protonated. | [] | On the other hand, in E.coli cells, in which it is difficult to achieve high pH values under physiological conditions, both Arg and Lys are assumed to be protonated. | true | true | true | true | true | 205 |
6 | DISCUSSION | 1 | 32 | [
"b32"
] | 17,099,236 | pmid-11848924 | Thus, it is unlikely for these basic residues to function as general acid–base catalysts. | [
"32"
] | 89 | 1,181 | 0 | false | Thus, it is unlikely for these basic residues to function as general acid–base catalysts. | [] | Thus, it is unlikely for these basic residues to function as general acid–base catalysts. | true | true | true | true | true | 205 |
7 | DISCUSSION | 1 | 20 | [
"b20"
] | 17,099,236 | pmid-16060658 | have reported the crystal structure of the apo form of E5-CRD; they showed that Asp54, Arg56, Lys59, Asp105 and Arg107 (corresponding to their residue numbers Asp46, Arg48, Lys51, Asp97 and Asp99, respectively) affected its ribonuclease activity due to mutations (20). | [
"20"
] | 268 | 1,182 | 1 | false | have reported the crystal structure of the apo form of E5-CRD; they showed that Asp54, Arg56, Lys59, Asp105 and Arg107 (corresponding to their residue numbers Asp46, Arg48, Lys51, Asp97 and Asp99, respectively) affected its ribonuclease activity due to mutations. | [
"20"
] | have reported the crystal structure of the apo form of E5-CRD; they showed that Asp54, Arg56, Lys59, Asp105 and Arg107 (corresponding to their residue numbers Asp46, Arg48, Lys51, Asp97 and Asp99, respectively) affected its ribonuclease activity due to mutations. | false | true | true | true | false | 206 |
7 | DISCUSSION | 1 | 20 | [
"b20"
] | 17,099,236 | pmid-16060658 | Further, among these residues, Asp54 and Arg56 were suggested to be putative catalytic residues. | [
"20"
] | 96 | 1,183 | 0 | false | Further, among these residues, Asp54 and Arg56 were suggested to be putative catalytic residues. | [] | Further, among these residues, Asp54 and Arg56 were suggested to be putative catalytic residues. | true | true | true | true | true | 206 |
7 | DISCUSSION | 1 | 20 | [
"b20"
] | 17,099,236 | pmid-16060658 | Based on the structure of our complex, however, the Cα atoms of Asp54 and Arg56 were located approximately 14 and 11 Å, respectively, apart from the 2′-C atom of the deoxyguanosine of dGpdUp; in addition, the residues were blocked by uridine thereby preventing their contact with the 2′-C atom and the phosphate group between dG and dU. | [
"20"
] | 336 | 1,184 | 0 | false | Based on the structure of our complex, however, the Cα atoms of Asp54 and Arg56 were located approximately 14 and 11 Å, respectively, apart from the 2′-C atom of the deoxyguanosine of dGpdUp; in addition, the residues were blocked by uridine thereby preventing their contact with the 2′-C atom and the phosphate group between dG and dU. | [] | Based on the structure of our complex, however, the Cα atoms of Asp54 and Arg56 were located approximately 14 and 11 Å, respectively, apart from the 2′-C atom of the deoxyguanosine of dGpdUp; in addition, the residues were blocked by uridine thereby preventing their contact with the 2′-C atom and the phosphate group between dG and dU. | true | true | true | true | true | 206 |
7 | DISCUSSION | 1 | 20 | [
"b20"
] | 17,099,236 | pmid-16060658 | Furthermore, instead of playing a role in substrate binding, Asp54 and Arg56 formed a salt bridge, enabling the complex structure to maintain its conformation. | [
"20"
] | 159 | 1,185 | 0 | false | Furthermore, instead of playing a role in substrate binding, Asp54 and Arg56 formed a salt bridge, enabling the complex structure to maintain its conformation. | [] | Furthermore, instead of playing a role in substrate binding, Asp54 and Arg56 formed a salt bridge, enabling the complex structure to maintain its conformation. | true | true | true | true | true | 206 |
7 | DISCUSSION | 1 | 20 | [
"b20"
] | 17,099,236 | pmid-16060658 | In addition, Asp105–Arg107 also formed a salt bridge, thereby contributing to the interaction with the uracil base ring of the substrate. | [
"20"
] | 137 | 1,186 | 0 | false | In addition, Asp105–Arg107 also formed a salt bridge, thereby contributing to the interaction with the uracil base ring of the substrate. | [] | In addition, Asp105–Arg107 also formed a salt bridge, thereby contributing to the interaction with the uracil base ring of the substrate. | true | true | true | true | true | 206 |
7 | DISCUSSION | 1 | 20 | [
"b20"
] | 17,099,236 | pmid-16060658 | Thus, the loss of the ribonuclease activity due to mutations of these two residues demonstrates their importance with regard to the uridine binding revealed by our structure. | [
"20"
] | 174 | 1,187 | 0 | false | Thus, the loss of the ribonuclease activity due to mutations of these two residues demonstrates their importance with regard to the uridine binding revealed by our structure. | [] | Thus, the loss of the ribonuclease activity due to mutations of these two residues demonstrates their importance with regard to the uridine binding revealed by our structure. | true | true | true | true | true | 206 |
7 | DISCUSSION | 1 | 20 | [
"b20"
] | 17,099,236 | pmid-16060658 | Lys59 may also contribute to the substrate binding with the phosphate group. | [
"20"
] | 76 | 1,188 | 0 | false | Lys59 may also contribute to the substrate binding with the phosphate group. | [] | Lys59 may also contribute to the substrate binding with the phosphate group. | true | true | true | true | true | 206 |
8 | DISCUSSION | 0 | null | null | 17,099,236 | null | Therefore, the residues found in this study and by Lin et al. | null | 61 | 1,189 | 0 | false | null | null | Therefore, the residues found in this study and by Lin et al. | true | true | true | true | true | 207 |
8 | DISCUSSION | 0 | null | null | 17,099,236 | null | are crucial for the catalytic activity; however, none of these appear to be apparent catalytic residues, suggesting the existence of an alternative novel mechanism responsible for the E5 activity. | null | 196 | 1,190 | 0 | false | null | null | are crucial for the catalytic activity; however, none of these appear to be apparent catalytic residues, suggesting the existence of an alternative novel mechanism responsible for the E5 activity. | false | true | true | true | false | 207 |
9 | DISCUSSION | 0 | null | null | 17,099,236 | null | In deoxyribonucleases (DNases), a water molecule that is activated by divalent metal ions is involved in the catalytic reaction. | null | 128 | 1,191 | 0 | false | null | null | In deoxyribonucleases (DNases), a water molecule that is activated by divalent metal ions is involved in the catalytic reaction. | true | true | true | true | true | 208 |
9 | DISCUSSION | 0 | null | null | 17,099,236 | null | However, no metal ions were found to be associated with the E5-CRD/dGpdUp complex; in fact, the enzyme reaction was resistant to EDTA (data not shown). | null | 151 | 1,192 | 0 | false | null | null | However, no metal ions were found to be associated with the E5-CRD/dGpdUp complex; in fact, the enzyme reaction was resistant to EDTA (data not shown). | true | true | true | true | true | 208 |
9 | DISCUSSION | 0 | null | null | 17,099,236 | null | Although a water molecule was found to bind to O1P of the phosphate of dGpdUp in the active site, it may function to fix the substrate at the active site. | null | 154 | 1,193 | 0 | false | null | null | Although a water molecule was found to bind to O1P of the phosphate of dGpdUp in the active site, it may function to fix the substrate at the active site. | true | true | true | true | true | 208 |
10 | DISCUSSION | 1 | 21 | [
"b21",
"b33"
] | 17,099,236 | pmid-16524591|pmid-8043575 | Recently, Luna-Chávez et al. | [
"21",
"33"
] | 28 | 1,194 | 0 | false | Recently, Luna-Chávez et al. | [] | Recently, Luna-Chávez et al. | true | true | true | true | true | 209 |
10 | DISCUSSION | 1 | 21 | [
"b21",
"b33"
] | 17,099,236 | pmid-16524591|pmid-8043575 | have solved the crystal structure of E5-CRD complexed with its cognate inhibitor protein ImmE5 through a multiwavelength anomalous diffraction experiment (21). | [
"21",
"33"
] | 159 | 1,195 | 1 | false | have solved the crystal structure of E5-CRD complexed with its cognate inhibitor protein ImmE5 through a multiwavelength anomalous diffraction experiment. | [
"21"
] | have solved the crystal structure of E5-CRD complexed with its cognate inhibitor protein ImmE5 through a multiwavelength anomalous diffraction experiment. | false | true | true | true | false | 209 |
10 | DISCUSSION | 1 | 21 | [
"b21",
"b33"
] | 17,099,236 | pmid-16524591|pmid-8043575 | We have also been studying the same structure by using MIR. | [
"21",
"33"
] | 59 | 1,196 | 0 | false | We have also been studying the same structure by using MIR. | [] | We have also been studying the same structure by using MIR. | true | true | true | true | true | 209 |
10 | DISCUSSION | 1 | 21 | [
"b21",
"b33"
] | 17,099,236 | pmid-16524591|pmid-8043575 | As a result, when we superposed our E5-CRD/ImmE5 structure onto the structure obtained by Luna-Chávez et al., the r.m.s. | [
"21",
"33"
] | 120 | 1,197 | 0 | false | As a result, when we superposed our E5-CRD/ImmE5 structure onto the structure obtained by Luna-Chávez et al., the r.m.s. | [] | As a result, when we superposed our E5-CRD/ImmE5 structure onto the structure obtained by Luna-Chávez et al., the r.m.s. | true | true | true | true | true | 209 |
10 | DISCUSSION | 1 | 21 | [
"b21",
"b33"
] | 17,099,236 | pmid-16524591|pmid-8043575 | difference for the backbone atoms (Cα, C, O and N) was 0.18 Å. | [
"21",
"33"
] | 62 | 1,198 | 0 | false | difference for the backbone atoms (Cα, C, O and N) was 0.18 Å. | [] | difference for the backbone atoms (Cα, C, O and N) was 0.18 Å. | false | true | true | true | false | 209 |
10 | DISCUSSION | 1 | 21 | [
"b21",
"b33"
] | 17,099,236 | pmid-16524591|pmid-8043575 | The resolutions of our structure and their structures are 1.9 and 1.15 Å, respectively. | [
"21",
"33"
] | 87 | 1,199 | 0 | false | The resolutions of our structure and their structures are 1.9 and 1.15 Å, respectively. | [] | The resolutions of our structure and their structures are 1.9 and 1.15 Å, respectively. | true | true | true | true | true | 209 |
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