paragraph_index int64 | sec string | p_has_citation int64 | cites string | citeids list | pmid int64 | cited_id string | sentences string | all_sent_cites list | sent_len int64 | sentence_batch_index int64 | sent_has_citation float64 | qc_fail bool | cited_sentence string | cites_in_sentence list | cln_sentence string | is_cap bool | is_alpha bool | ends_wp bool | cit_qc bool | lgtm bool | __index_level_0__ int64 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4"
] | 17,670,797 | pmid-10807004|pmid-1962210|pmid-12691534|pmid-15025524|pmid-17226957 | Figure 1.Structures of PMO and (RX)8− PMO conjugate. | [
"1",
"2",
"3",
"4"
] | 52 | 8,200 | 0 | false | Figure 1.Structures of PMO and (RX)8− PMO conjugate. | [] | Figure 1.Structures of PMO and (RX)8− PMO conjugate. | true | true | true | true | true | 1,326 |
1 | INTRODUCTION | 0 | null | null | 17,670,797 | pmid-17097177|pmid-17097177 | Structures of PMO and (RX)8− PMO conjugate. | null | 43 | 8,201 | 0 | false | null | null | Structures of PMO and (RX)8− PMO conjugate. | true | true | true | true | true | 1,327 |
2 | INTRODUCTION | 1 | 5 | [
"B5",
"B5",
"B6",
"B7",
"B8",
"B9",
"B7",
"B11 B12 B13",
"B7",
"B13"
] | 17,670,797 | pmid-17226957|pmid-17226957|pmid-17097177|pmid-17344287|pmid-16724091|pmid-16919955|pmid-17344287|pmid-15795246|pmid-16966399|pmid-16987987|pmid-17344287|pmid-16987987 | Important considerations in the design of effective CPPs include the ability to deliver AO efficiently, stability in living systems and toxicity. | [
"5",
"5",
"6",
"7",
"8",
"9",
"7",
"11–13",
"7",
"13"
] | 145 | 8,202 | 0 | false | Important considerations in the design of effective CPPs include the ability to deliver AO efficiently, stability in living systems and toxicity. | [] | Important considerations in the design of effective CPPs include the ability to deliver AO efficiently, stability in living systems and toxicity. | true | true | true | true | true | 1,328 |
2 | INTRODUCTION | 1 | 5 | [
"B5",
"B5",
"B6",
"B7",
"B8",
"B9",
"B7",
"B11 B12 B13",
"B7",
"B13"
] | 17,670,797 | pmid-17226957|pmid-17226957|pmid-17097177|pmid-17344287|pmid-16724091|pmid-16919955|pmid-17344287|pmid-15795246|pmid-16966399|pmid-16987987|pmid-17344287|pmid-16987987 | We have reported that Tat and oligoarginine peptides are not stable in human serum (5), and are therefore ill-suited for in vivo applications. | [
"5",
"5",
"6",
"7",
"8",
"9",
"7",
"11–13",
"7",
"13"
] | 142 | 8,203 | 1 | false | We have reported that Tat and oligoarginine peptides are not stable in human serum, and are therefore ill-suited for in vivo applications. | [
"5"
] | We have reported that Tat and oligoarginine peptides are not stable in human serum, and are therefore ill-suited for in vivo applications. | true | true | true | true | true | 1,328 |
2 | INTRODUCTION | 1 | 5 | [
"B5",
"B5",
"B6",
"B7",
"B8",
"B9",
"B7",
"B11 B12 B13",
"B7",
"B13"
] | 17,670,797 | pmid-17226957|pmid-17226957|pmid-17097177|pmid-17344287|pmid-16724091|pmid-16919955|pmid-17344287|pmid-15795246|pmid-16966399|pmid-16987987|pmid-17344287|pmid-16987987 | Oligoarginine peptides incorporating non-α amino acids have been proven superior to oligoarginine alone. | [
"5",
"5",
"6",
"7",
"8",
"9",
"7",
"11–13",
"7",
"13"
] | 104 | 8,204 | 0 | false | Oligoarginine peptides incorporating non-α amino acids have been proven superior to oligoarginine alone. | [] | Oligoarginine peptides incorporating non-α amino acids have been proven superior to oligoarginine alone. | true | true | true | true | true | 1,328 |
2 | INTRODUCTION | 1 | 5 | [
"B5",
"B5",
"B6",
"B7",
"B8",
"B9",
"B7",
"B11 B12 B13",
"B7",
"B13"
] | 17,670,797 | pmid-17226957|pmid-17226957|pmid-17097177|pmid-17344287|pmid-16724091|pmid-16919955|pmid-17344287|pmid-15795246|pmid-16966399|pmid-16987987|pmid-17344287|pmid-16987987 | CPPs containing 6-aminohexanoic acid (X) and β-alanine (B) were more stable in human serum than Tat or oligoarginine peptides (5). | [
"5",
"5",
"6",
"7",
"8",
"9",
"7",
"11–13",
"7",
"13"
] | 130 | 8,205 | 1 | false | CPPs containing 6-aminohexanoic acid (X) and β-alanine (B) were more stable in human serum than Tat or oligoarginine peptides. | [
"5"
] | CPPs containing 6-aminohexanoic acid (X) and β-alanine (B) were more stable in human serum than Tat or oligoarginine peptides. | true | true | true | true | true | 1,328 |
2 | INTRODUCTION | 1 | 6 | [
"B5",
"B5",
"B6",
"B7",
"B8",
"B9",
"B7",
"B11 B12 B13",
"B7",
"B13"
] | 17,670,797 | pmid-17226957|pmid-17226957|pmid-17097177|pmid-17344287|pmid-16724091|pmid-16919955|pmid-17344287|pmid-15795246|pmid-16966399|pmid-16987987|pmid-17344287|pmid-16987987 | A CPP−PMO conjugate, (RXR)4−PMO, has been shown to be more efficient in the correction of pre-mRNA mis-splicing (6) and in inhibition of the replication of mouse hepatitis virus in vivo (7) than an oligoarginine peptide. | [
"5",
"5",
"6",
"7",
"8",
"9",
"7",
"11–13",
"7",
"13"
] | 220 | 8,206 | 1 | false | A CPP−PMO conjugate, (RXR)4−PMO, has been shown to be more efficient in the correction of pre-mRNA mis-splicing and in inhibition of the replication of mouse hepatitis virus in vivo than an oligoarginine peptide. | [
"6",
"7"
] | A CPP−PMO conjugate, (RXR)4−PMO, has been shown to be more efficient in the correction of pre-mRNA mis-splicing and in inhibition of the replication of mouse hepatitis virus in vivo than an oligoarginine peptide. | true | true | true | true | true | 1,328 |
2 | INTRODUCTION | 1 | 8 | [
"B5",
"B5",
"B6",
"B7",
"B8",
"B9",
"B7",
"B11 B12 B13",
"B7",
"B13"
] | 17,670,797 | pmid-17226957|pmid-17226957|pmid-17097177|pmid-17344287|pmid-16724091|pmid-16919955|pmid-17344287|pmid-15795246|pmid-16966399|pmid-16987987|pmid-17344287|pmid-16987987 | In addition, (RXR)4−PMO conjugates have been shown to cause effective exon skipping in muscle cells from DMD dogs (8), in human muscle explants (9) and in mdx mice (10), as well as inhibiting the replication of various viruses in cell cultures (7,11–13) and in mice (7,13). | [
"5",
"5",
"6",
"7",
"8",
"9",
"7",
"11–13",
"7",
"13"
] | 273 | 8,207 | 1 | false | In addition, (RXR)4−PMO conjugates have been shown to cause effective exon skipping in muscle cells from DMD dogs, in human muscle explants and in mdx mice (10), as well as inhibiting the replication of various viruses in cell cultures and in mice. | [
"8",
"9",
"7,11–13",
"7,13"
] | In addition, (RXR)4−PMO conjugates have been shown to cause effective exon skipping in muscle cells from DMD dogs, in human muscle explants and in mdx mice (10), as well as inhibiting the replication of various viruses in cell cultures and in mice. | true | true | true | true | true | 1,328 |
3 | INTRODUCTION | 1 | 5 | [
"B5",
"B13"
] | 17,670,797 | pmid-17226957|pmid-16987987|pmid-12411431|pmid-12166934 | The above studies have helped make it clear that unnatural amino acids can confer enhanced stability and activity, and therefore improve the potential of CPPs to deliver therapeutic PMO. | [
"5",
"13"
] | 186 | 8,208 | 0 | false | The above studies have helped make it clear that unnatural amino acids can confer enhanced stability and activity, and therefore improve the potential of CPPs to deliver therapeutic PMO. | [] | The above studies have helped make it clear that unnatural amino acids can confer enhanced stability and activity, and therefore improve the potential of CPPs to deliver therapeutic PMO. | true | true | true | true | true | 1,329 |
3 | INTRODUCTION | 1 | 5 | [
"B5",
"B13"
] | 17,670,797 | pmid-17226957|pmid-16987987|pmid-12411431|pmid-12166934 | In pursuit of CPPs with improved characteristics, we have carried out a structure–activity relationship study to investigate the effects of unnatural amino acid insertions in oligoarginine peptides on cellular delivery, nuclear antisense activity, toxicity and serum-binding characteristics of the resulting CPP−PMO conj... | [
"5",
"13"
] | 327 | 8,209 | 0 | false | In pursuit of CPPs with improved characteristics, we have carried out a structure–activity relationship study to investigate the effects of unnatural amino acid insertions in oligoarginine peptides on cellular delivery, nuclear antisense activity, toxicity and serum-binding characteristics of the resulting CPP−PMO conj... | [] | In pursuit of CPPs with improved characteristics, we have carried out a structure–activity relationship study to investigate the effects of unnatural amino acid insertions in oligoarginine peptides on cellular delivery, nuclear antisense activity, toxicity and serum-binding characteristics of the resulting CPP−PMO conj... | true | true | true | true | true | 1,329 |
3 | INTRODUCTION | 1 | 5 | [
"B5",
"B13"
] | 17,670,797 | pmid-17226957|pmid-16987987|pmid-12411431|pmid-12166934 | The unnatural amino acids studied here are X, B and D-arginine (r). | [
"5",
"13"
] | 67 | 8,210 | 0 | false | The unnatural amino acids studied here are X, B and D-arginine (r). | [] | The unnatural amino acids studied here are X, B and D-arginine (r). | true | true | true | true | true | 1,329 |
3 | INTRODUCTION | 1 | 5 | [
"B5",
"B13"
] | 17,670,797 | pmid-17226957|pmid-16987987|pmid-12411431|pmid-12166934 | We chose to study the X amino acid based on the successes of the (RXR)4 CPP in several studies as shown in the previous paragraph. | [
"5",
"13"
] | 130 | 8,211 | 0 | false | We chose to study the X amino acid based on the successes of the (RXR)4 CPP in several studies as shown in the previous paragraph. | [] | We chose to study the X amino acid based on the successes of the (RXR)4 CPP in several studies as shown in the previous paragraph. | true | true | true | true | true | 1,329 |
3 | INTRODUCTION | 1 | 5 | [
"B5",
"B13"
] | 17,670,797 | pmid-17226957|pmid-16987987|pmid-12411431|pmid-12166934 | B and r amino acids were chosen because they have good enzymatic stability (5). | [
"5",
"13"
] | 79 | 8,212 | 1 | false | B and r amino acids were chosen because they have good enzymatic stability. | [
"5"
] | B and r amino acids were chosen because they have good enzymatic stability. | true | true | true | true | true | 1,329 |
3 | INTRODUCTION | 1 | 5 | [
"B5",
"B13"
] | 17,670,797 | pmid-17226957|pmid-16987987|pmid-12411431|pmid-12166934 | The CPPs are (i) the oligoarginine sequences, R8 and R9, (ii) sequences with RXR, RX and RB repeats, as well as various combinations thereof, and (iii) sequences containing D-arginine, r8, (rX)8 (rXR)4, (rXr)4 and (rB)8. | [
"5",
"13"
] | 220 | 8,213 | 0 | false | The CPPs are (i) the oligoarginine sequences, R8 and R9, (ii) sequences with RXR, RX and RB repeats, as well as various combinations thereof, and (iii) sequences containing D-arginine, r8, (rX)8 (rXR)4, (rXr)4 and (rB)8. | [] | The CPPs are (i) the oligoarginine sequences, R8 and R9, (ii) sequences with RXR, RX and RB repeats, as well as various combinations thereof, and (iii) sequences containing D-arginine, r8, (rX)8 (rXR)4, (rXr)4 and (rB)8. | true | true | true | true | true | 1,329 |
3 | INTRODUCTION | 1 | 13 | [
"B5",
"B13"
] | 17,670,797 | pmid-17226957|pmid-16987987|pmid-12411431|pmid-12166934 | The CPP−PMO conjugates were evaluated for their relative (a) cellular uptake, as determined by flow cytometry, (b) antisense activity, as determined by a splice correction assay (13) and (c) cellular toxicity, as determined by MTT cell viability, propidium iodide membrane integrity and hemolysis assays, as well as by m... | [
"5",
"13"
] | 339 | 8,214 | 1 | false | The CPP−PMO conjugates were evaluated for their relative (a) cellular uptake, as determined by flow cytometry, (b) antisense activity, as determined by a splice correction assay and (c) cellular toxicity, as determined by MTT cell viability, propidium iodide membrane integrity and hemolysis assays, as well as by micros... | [
"13"
] | The CPP−PMO conjugates were evaluated for their relative (a) cellular uptake, as determined by flow cytometry, (b) antisense activity, as determined by a splice correction assay and (c) cellular toxicity, as determined by MTT cell viability, propidium iodide membrane integrity and hemolysis assays, as well as by micros... | true | true | true | true | true | 1,329 |
0 | DISCUSSION | 1 | 5 | [
"B5"
] | 17,670,797 | pmid-10807004|pmid-1962210|pmid-12691534|pmid-15025524|pmid-17226957 | The naturally occurring CPPs such as Tat peptide are not stable in blood and neither are oligolysine/oligoarginine (5), rendering these CPPs unfavorable as transporters for therapeutic AOs. | [
"5"
] | 189 | 8,215 | 1 | false | The naturally occurring CPPs such as Tat peptide are not stable in blood and neither are oligolysine/oligoarginine, rendering these CPPs unfavorable as transporters for therapeutic AOs. | [
"5"
] | The naturally occurring CPPs such as Tat peptide are not stable in blood and neither are oligolysine/oligoarginine, rendering these CPPs unfavorable as transporters for therapeutic AOs. | true | true | true | true | true | 1,330 |
0 | DISCUSSION | 1 | 5 | [
"B5"
] | 17,670,797 | pmid-10807004|pmid-1962210|pmid-12691534|pmid-15025524|pmid-17226957 | We reasoned that one approach to improve stability would be to use non-α amino acids or D-amino acids. | [
"5"
] | 102 | 8,216 | 0 | false | We reasoned that one approach to improve stability would be to use non-α amino acids or D-amino acids. | [] | We reasoned that one approach to improve stability would be to use non-α amino acids or D-amino acids. | true | true | true | true | true | 1,330 |
0 | DISCUSSION | 1 | 5 | [
"B5"
] | 17,670,797 | pmid-10807004|pmid-1962210|pmid-12691534|pmid-15025524|pmid-17226957 | In this study, we investigated whether incorporation of 6-aminohexanoic acid (X), β-alanine (B) and D-arginine (r) amino acids into the CPP would affect cellular delivery, antisense activity, toxicity and serum binding of the resulting CPP−PMO conjugates. | [
"5"
] | 255 | 8,217 | 0 | false | In this study, we investigated whether incorporation of 6-aminohexanoic acid (X), β-alanine (B) and D-arginine (r) amino acids into the CPP would affect cellular delivery, antisense activity, toxicity and serum binding of the resulting CPP−PMO conjugates. | [] | In this study, we investigated whether incorporation of 6-aminohexanoic acid (X), β-alanine (B) and D-arginine (r) amino acids into the CPP would affect cellular delivery, antisense activity, toxicity and serum binding of the resulting CPP−PMO conjugates. | true | true | true | true | true | 1,330 |
1 | DISCUSSION | 1 | 6 | [
"B6",
"B6"
] | 17,670,797 | pmid-17097177|pmid-17097177 | We found that CPP−PMOF conjugates containing X/B residues did not enter cells as efficiently as R8− and R9−PMO conjugates. | [
"6",
"6"
] | 122 | 8,218 | 0 | false | We found that CPP−PMOF conjugates containing X/B residues did not enter cells as efficiently as R8− and R9−PMO conjugates. | [] | We found that CPP−PMOF conjugates containing X/B residues did not enter cells as efficiently as R8− and R9−PMO conjugates. | true | true | true | true | true | 1,331 |
1 | DISCUSSION | 1 | 6 | [
"B6",
"B6"
] | 17,670,797 | pmid-17097177|pmid-17097177 | This is consistent with our previous finding for the (RXR)4 conjugate (6). | [
"6",
"6"
] | 74 | 8,219 | 1 | false | This is consistent with our previous finding for the (RXR)4 conjugate. | [
"6"
] | This is consistent with our previous finding for the (RXR)4 conjugate. | true | true | true | true | true | 1,331 |
1 | DISCUSSION | 1 | 6 | [
"B6",
"B6"
] | 17,670,797 | pmid-17097177|pmid-17097177 | We have found that cell surface proteoglycans were involved with binding of the Tat−, R9F2− and (RXR)4−PMO conjugates with the (RXR)4 conjugate having the lowest binding affinity. | [
"6",
"6"
] | 179 | 8,220 | 0 | false | We have found that cell surface proteoglycans were involved with binding of the Tat−, R9F2− and (RXR)4−PMO conjugates with the (RXR)4 conjugate having the lowest binding affinity. | [] | We have found that cell surface proteoglycans were involved with binding of the Tat−, R9F2− and (RXR)4−PMO conjugates with the (RXR)4 conjugate having the lowest binding affinity. | true | true | true | true | true | 1,331 |
1 | DISCUSSION | 1 | 6 | [
"B6",
"B6"
] | 17,670,797 | pmid-17097177|pmid-17097177 | Insertion of X into an oligoarginine CPP reduces the charge density and may lead to decreased binding affinity for proteoglycans. | [
"6",
"6"
] | 129 | 8,221 | 0 | false | Insertion of X into an oligoarginine CPP reduces the charge density and may lead to decreased binding affinity for proteoglycans. | [] | Insertion of X into an oligoarginine CPP reduces the charge density and may lead to decreased binding affinity for proteoglycans. | true | true | true | true | true | 1,331 |
1 | DISCUSSION | 1 | 6 | [
"B6",
"B6"
] | 17,670,797 | pmid-17097177|pmid-17097177 | Despite the lower cellular uptake of X/B-containing CPP–PMO, they generated higher antisense activities in the cell nucleus than oligoarginine−PMO. | [
"6",
"6"
] | 147 | 8,222 | 0 | false | Despite the lower cellular uptake of X/B-containing CPP–PMO, they generated higher antisense activities in the cell nucleus than oligoarginine−PMO. | [] | Despite the lower cellular uptake of X/B-containing CPP–PMO, they generated higher antisense activities in the cell nucleus than oligoarginine−PMO. | true | true | true | true | true | 1,331 |
1 | DISCUSSION | 1 | 6 | [
"B6",
"B6"
] | 17,670,797 | pmid-17097177|pmid-17097177 | We have found that endocytosis was the internalization mechanism (at least primarily) for oligoarginine- and (RXR)4−PMO conjugates. | [
"6",
"6"
] | 131 | 8,223 | 0 | false | We have found that endocytosis was the internalization mechanism (at least primarily) for oligoarginine- and (RXR)4−PMO conjugates. | [] | We have found that endocytosis was the internalization mechanism (at least primarily) for oligoarginine- and (RXR)4−PMO conjugates. | true | true | true | true | true | 1,331 |
1 | DISCUSSION | 1 | 6 | [
"B6",
"B6"
] | 17,670,797 | pmid-17097177|pmid-17097177 | Indication of different uptake mechanisms was not found among these conjugates (6). | [
"6",
"6"
] | 83 | 8,224 | 1 | false | Indication of different uptake mechanisms was not found among these conjugates. | [
"6"
] | Indication of different uptake mechanisms was not found among these conjugates. | true | true | true | true | true | 1,331 |
1 | DISCUSSION | 1 | 6 | [
"B6",
"B6"
] | 17,670,797 | pmid-17097177|pmid-17097177 | Therefore we hypothesize that X/B-containing conjugates have a greater ability to escape from endosomes/lysosomes than oligoarginine conjugates by a mechanism as yet to be studied. | [
"6",
"6"
] | 180 | 8,225 | 0 | false | Therefore we hypothesize that X/B-containing conjugates have a greater ability to escape from endosomes/lysosomes than oligoarginine conjugates by a mechanism as yet to be studied. | [] | Therefore we hypothesize that X/B-containing conjugates have a greater ability to escape from endosomes/lysosomes than oligoarginine conjugates by a mechanism as yet to be studied. | true | true | true | true | true | 1,331 |
2 | DISCUSSION | 0 | null | null | 17,670,797 | pmid-17226957|pmid-17226957|pmid-17097177|pmid-17344287|pmid-16724091|pmid-16919955|pmid-17344287|pmid-15795246|pmid-16966399|pmid-16987987|pmid-17344287|pmid-16987987 | The number of X residues affects both the nuclear antisense activity and the toxicity of conjugates. | null | 100 | 8,226 | 0 | false | null | null | The number of X residues affects both the nuclear antisense activity and the toxicity of conjugates. | true | true | true | true | true | 1,332 |
2 | DISCUSSION | 0 | null | null | 17,670,797 | pmid-17226957|pmid-17226957|pmid-17097177|pmid-17344287|pmid-16724091|pmid-16919955|pmid-17344287|pmid-15795246|pmid-16966399|pmid-16987987|pmid-17344287|pmid-16987987 | The CPP−PMO conjugate with 8 X residues [(RX)8−PMO] had the highest activity followed by one with 5 Xs | null | 102 | 8,227 | 0 | false | null | null | The CPP−PMO conjugate with 8 X residues [(RX)8−PMO] had the highest activity followed by one with 5 Xs | true | true | false | true | false | 1,332 |
2 | DISCUSSION | 0 | null | null | 17,670,797 | pmid-17226957|pmid-17226957|pmid-17097177|pmid-17344287|pmid-16724091|pmid-16919955|pmid-17344287|pmid-15795246|pmid-16966399|pmid-16987987|pmid-17344287|pmid-16987987 | [(RXR)4−PMO] (Figures 1 and 4). | null | 31 | 8,228 | 0 | false | null | null | [(RXR)4−PMO] (Figures 1 and 4). | false | false | true | true | false | 1,332 |
2 | DISCUSSION | 0 | null | null | 17,670,797 | pmid-17226957|pmid-17226957|pmid-17097177|pmid-17344287|pmid-16724091|pmid-16919955|pmid-17344287|pmid-15795246|pmid-16966399|pmid-16987987|pmid-17344287|pmid-16987987 | However, these conjugates were toxic to cells at higher concentrations, which may be a concern when considering potential applications for in vivo delivery of PMO. | null | 163 | 8,229 | 0 | false | null | null | However, these conjugates were toxic to cells at higher concentrations, which may be a concern when considering potential applications for in vivo delivery of PMO. | true | true | true | true | true | 1,332 |
2 | DISCUSSION | 0 | null | null | 17,670,797 | pmid-17226957|pmid-17226957|pmid-17097177|pmid-17344287|pmid-16724091|pmid-16919955|pmid-17344287|pmid-15795246|pmid-16966399|pmid-16987987|pmid-17344287|pmid-16987987 | Replacement of all 8 Xs with Bs decreased both toxicity and antisense activity. | null | 79 | 8,230 | 0 | false | null | null | Replacement of all 8 Xs with Bs decreased both toxicity and antisense activity. | true | true | true | true | true | 1,332 |
2 | DISCUSSION | 0 | null | null | 17,670,797 | pmid-17226957|pmid-17226957|pmid-17097177|pmid-17344287|pmid-16724091|pmid-16919955|pmid-17344287|pmid-15795246|pmid-16966399|pmid-16987987|pmid-17344287|pmid-16987987 | The combination of 3–4 Xs with several B residues yielded CPPs with no detectable toxicity, and at some concentrations several of them had similar antisense activity as (RX)8−PMO. | null | 179 | 8,231 | 0 | false | null | null | The combination of 3–4 Xs with several B residues yielded CPPs with no detectable toxicity, and at some concentrations several of them had similar antisense activity as (RX)8−PMO. | true | true | true | true | true | 1,332 |
2 | DISCUSSION | 0 | null | null | 17,670,797 | pmid-17226957|pmid-17226957|pmid-17097177|pmid-17344287|pmid-16724091|pmid-16919955|pmid-17344287|pmid-15795246|pmid-16966399|pmid-16987987|pmid-17344287|pmid-16987987 | We think this type of CPP, having Bs and fewer than 5 Xs, will offer balanced activity and low toxicity as well as the stability, and have considerable potential for delivery of therapeutic AOs. | null | 194 | 8,232 | 0 | false | null | null | We think this type of CPP, having Bs and fewer than 5 Xs, will offer balanced activity and low toxicity as well as the stability, and have considerable potential for delivery of therapeutic AOs. | true | true | true | true | true | 1,332 |
2 | DISCUSSION | 0 | null | null | 17,670,797 | pmid-17226957|pmid-17226957|pmid-17097177|pmid-17344287|pmid-16724091|pmid-16919955|pmid-17344287|pmid-15795246|pmid-16966399|pmid-16987987|pmid-17344287|pmid-16987987 | Further investigation into the toxicity and activity versus dosing levels of these CPPs in vivo is warranted. | null | 109 | 8,233 | 0 | false | null | null | Further investigation into the toxicity and activity versus dosing levels of these CPPs in vivo is warranted. | true | true | true | true | true | 1,332 |
3 | DISCUSSION | 1 | 20 | [
"B19",
"B20"
] | 17,670,797 | pmid-17226957|pmid-16987987|pmid-12411431|pmid-12166934 | Surprisingly, the replacement of L-arginine with D-arginine enhanced neither uptake nor antisense activity for oligoarginine, or X- and B-containing conjugates. | [
"20",
"21"
] | 160 | 8,234 | 0 | false | Surprisingly, the replacement of L-arginine with D-arginine enhanced neither uptake nor antisense activity for oligoarginine, or X- and B-containing conjugates. | [] | Surprisingly, the replacement of L-arginine with D-arginine enhanced neither uptake nor antisense activity for oligoarginine, or X- and B-containing conjugates. | true | true | true | true | true | 1,333 |
3 | DISCUSSION | 1 | 20 | [
"B19",
"B20"
] | 17,670,797 | pmid-17226957|pmid-16987987|pmid-12411431|pmid-12166934 | In the case of (RX)8−PMO, the replacement actually caused a small but statistically significant decrease in activity. | [
"20",
"21"
] | 117 | 8,235 | 0 | false | In the case of (RX)8−PMO, the replacement actually caused a small but statistically significant decrease in activity. | [] | In the case of (RX)8−PMO, the replacement actually caused a small but statistically significant decrease in activity. | true | true | true | true | true | 1,333 |
3 | DISCUSSION | 1 | 20 | [
"B19",
"B20"
] | 17,670,797 | pmid-17226957|pmid-16987987|pmid-12411431|pmid-12166934 | Our observation is different from the results reported by others (20,21) who found that D-CPPs had higher cellular uptake than L-CPPs, although no biological functional cargo was used in their study. | [
"20",
"21"
] | 199 | 8,236 | 0 | false | Our observation is different from the results reported by others who found that D-CPPs had higher cellular uptake than L-CPPs, although no biological functional cargo was used in their study. | [
"20,21"
] | Our observation is different from the results reported by others who found that D-CPPs had higher cellular uptake than L-CPPs, although no biological functional cargo was used in their study. | true | true | true | true | true | 1,333 |
3 | DISCUSSION | 1 | 20 | [
"B19",
"B20"
] | 17,670,797 | pmid-17226957|pmid-16987987|pmid-12411431|pmid-12166934 | The difference between results may be due to the type and size of cargos and the cell lines used for the assays. | [
"20",
"21"
] | 112 | 8,237 | 0 | false | The difference between results may be due to the type and size of cargos and the cell lines used for the assays. | [] | The difference between results may be due to the type and size of cargos and the cell lines used for the assays. | true | true | true | true | true | 1,333 |
3 | DISCUSSION | 1 | 20 | [
"B19",
"B20"
] | 17,670,797 | pmid-17226957|pmid-16987987|pmid-12411431|pmid-12166934 | Whether the use of D-arginine-containing peptides results in superior CPP−PMO functional activity in vivo remains to be tested. | [
"20",
"21"
] | 127 | 8,238 | 0 | false | Whether the use of D-arginine-containing peptides results in superior CPP−PMO functional activity in vivo remains to be tested. | [] | Whether the use of D-arginine-containing peptides results in superior CPP−PMO functional activity in vivo remains to be tested. | true | true | true | true | true | 1,333 |
4 | DISCUSSION | 1 | 5 | [
"B5",
"B5"
] | 17,670,797 | pmid-17226957|pmid-17226957 | We attempted to understand the nature of (RX)8− and (RXR)4−PMO toxicity. | [
"5",
"5"
] | 72 | 8,239 | 0 | false | We attempted to understand the nature of (RX)8− and (RXR)4−PMO toxicity. | [] | We attempted to understand the nature of (RX)8− and (RXR)4−PMO toxicity. | true | true | true | true | true | 1,334 |
4 | DISCUSSION | 1 | 5 | [
"B5",
"B5"
] | 17,670,797 | pmid-17226957|pmid-17226957 | It is apparent that these two conjugates caused little immediate membrane damage with 0.5 or 5 h treatment at concentrations as high as 60 μM (Figure 8). | [
"5",
"5"
] | 153 | 8,240 | 0 | false | It is apparent that these two conjugates caused little immediate membrane damage with 0.5 or 5 h treatment at concentrations as high as 60 μM (Figure 8). | [] | It is apparent that these two conjugates caused little immediate membrane damage with 0.5 or 5 h treatment at concentrations as high as 60 μM (Figure 8). | true | true | true | true | true | 1,334 |
4 | DISCUSSION | 1 | 5 | [
"B5",
"B5"
] | 17,670,797 | pmid-17226957|pmid-17226957 | However, these two conjugates had dose-dependent toxicity with 24 hr treatment as shown by the leaky cell membranes and fewer cells compared to controls (Figure 6C&D, Figure 8). | [
"5",
"5"
] | 177 | 8,241 | 0 | false | However, these two conjugates had dose-dependent toxicity with 24 hr treatment as shown by the leaky cell membranes and fewer cells compared to controls (Figure 6C&D, Figure 8). | [] | However, these two conjugates had dose-dependent toxicity with 24 hr treatment as shown by the leaky cell membranes and fewer cells compared to controls (Figure 6C&D, Figure 8). | true | true | true | true | true | 1,334 |
4 | DISCUSSION | 1 | 5 | [
"B5",
"B5"
] | 17,670,797 | pmid-17226957|pmid-17226957 | Interestingly, the replacement of Xs with Bs in (RX)8−PMO abolished the toxicity, and the replacement of L-arginine with D-arginine reduced the toxicity of (RX)8−PMO (Figure 6). | [
"5",
"5"
] | 177 | 8,242 | 0 | false | Interestingly, the replacement of Xs with Bs in (RX)8−PMO abolished the toxicity, and the replacement of L-arginine with D-arginine reduced the toxicity of (RX)8−PMO (Figure 6). | [] | Interestingly, the replacement of Xs with Bs in (RX)8−PMO abolished the toxicity, and the replacement of L-arginine with D-arginine reduced the toxicity of (RX)8−PMO (Figure 6). | true | true | true | true | true | 1,334 |
4 | DISCUSSION | 1 | 5 | [
"B5",
"B5"
] | 17,670,797 | pmid-17226957|pmid-17226957 | We have found that (rX)8−PMO was completely stable and the peptide portion of (RB)8−PMO was only partially degraded, whereas the peptide portion of (RX)8−PMO was completely degraded in cells (5). | [
"5",
"5"
] | 195 | 8,243 | 1 | false | We have found that (rX)8−PMO was completely stable and the peptide portion of (RB)8−PMO was only partially degraded, whereas the peptide portion of (RX)8−PMO was completely degraded in cells. | [
"5"
] | We have found that (rX)8−PMO was completely stable and the peptide portion of (RB)8−PMO was only partially degraded, whereas the peptide portion of (RX)8−PMO was completely degraded in cells. | true | true | true | true | true | 1,334 |
4 | DISCUSSION | 1 | 5 | [
"B5",
"B5"
] | 17,670,797 | pmid-17226957|pmid-17226957 | We wondered whether the difference in toxicity among (RX)8, (RB)8 and (rX)8−PMO conjugates was caused by differences in intracellular stability, resulting in the metabolized products of (RX)8−PMO producing toxicity. | [
"5",
"5"
] | 215 | 8,244 | 0 | false | We wondered whether the difference in toxicity among (RX)8, (RB)8 and (rX)8−PMO conjugates was caused by differences in intracellular stability, resulting in the metabolized products of (RX)8−PMO producing toxicity. | [] | We wondered whether the difference in toxicity among (RX)8, (RB)8 and (rX)8−PMO conjugates was caused by differences in intracellular stability, resulting in the metabolized products of (RX)8−PMO producing toxicity. | true | true | true | true | true | 1,334 |
4 | DISCUSSION | 1 | 5 | [
"B5",
"B5"
] | 17,670,797 | pmid-17226957|pmid-17226957 | The identifiable metabolized products of (RX)8−PMO were XRXB−PMO and XB−PMO (5) but neither product had any detectable toxicity as measured by MTT assay (data not shown). | [
"5",
"5"
] | 170 | 8,245 | 1 | false | The identifiable metabolized products of (RX)8−PMO were XRXB−PMO and XB−PMO but neither product had any detectable toxicity as measured by MTT assay (data not shown). | [
"5"
] | The identifiable metabolized products of (RX)8−PMO were XRXB−PMO and XB−PMO but neither product had any detectable toxicity as measured by MTT assay (data not shown). | true | true | true | true | true | 1,334 |
4 | DISCUSSION | 1 | 5 | [
"B5",
"B5"
] | 17,670,797 | pmid-17226957|pmid-17226957 | It is possible that the CPP portion was degraded into free amino acids and/or smaller peptide fragments which were toxic. | [
"5",
"5"
] | 121 | 8,246 | 0 | false | It is possible that the CPP portion was degraded into free amino acids and/or smaller peptide fragments which were toxic. | [] | It is possible that the CPP portion was degraded into free amino acids and/or smaller peptide fragments which were toxic. | true | true | true | true | true | 1,334 |
4 | DISCUSSION | 1 | 5 | [
"B5",
"B5"
] | 17,670,797 | pmid-17226957|pmid-17226957 | However, our investigation revealed that neither free R nor X, alone or in combination, caused cellular toxicity. | [
"5",
"5"
] | 113 | 8,247 | 0 | false | However, our investigation revealed that neither free R nor X, alone or in combination, caused cellular toxicity. | [] | However, our investigation revealed that neither free R nor X, alone or in combination, caused cellular toxicity. | true | true | true | true | true | 1,334 |
4 | DISCUSSION | 1 | 5 | [
"B5",
"B5"
] | 17,670,797 | pmid-17226957|pmid-17226957 | Another possibility is that because of the high hydrophobicity of X compared to B, X in combination with positively charged arginine residues leads to toxicity not generated by B residue combinations. | [
"5",
"5"
] | 200 | 8,248 | 0 | false | Another possibility is that because of the high hydrophobicity of X compared to B, X in combination with positively charged arginine residues leads to toxicity not generated by B residue combinations. | [] | Another possibility is that because of the high hydrophobicity of X compared to B, X in combination with positively charged arginine residues leads to toxicity not generated by B residue combinations. | true | true | true | true | true | 1,334 |
4 | DISCUSSION | 1 | 5 | [
"B5",
"B5"
] | 17,670,797 | pmid-17226957|pmid-17226957 | However, this explanation does not account for the difference in toxicity observed between (RX)8−PMO and (rX)8−PMO, which have the same hydrophobicity. | [
"5",
"5"
] | 151 | 8,249 | 0 | false | However, this explanation does not account for the difference in toxicity observed between (RX)8−PMO and (rX)8−PMO, which have the same hydrophobicity. | [] | However, this explanation does not account for the difference in toxicity observed between (RX)8−PMO and (rX)8−PMO, which have the same hydrophobicity. | true | true | true | true | true | 1,334 |
4 | DISCUSSION | 1 | 5 | [
"B5",
"B5"
] | 17,670,797 | pmid-17226957|pmid-17226957 | Perhaps the toxicity of (RXR)4−PMO and (RX)8−PMO was caused by the peptide fragments that we could not identify by mass spectrometry. | [
"5",
"5"
] | 133 | 8,250 | 0 | false | Perhaps the toxicity of (RXR)4−PMO and (RX)8−PMO was caused by the peptide fragments that we could not identify by mass spectrometry. | [] | Perhaps the toxicity of (RXR)4−PMO and (RX)8−PMO was caused by the peptide fragments that we could not identify by mass spectrometry. | true | true | true | true | true | 1,334 |
5 | DISCUSSION | 0 | null | null | 17,670,797 | null | Unlike the toxicity difference between (RX)8− and (rX)8−PMO, the L→D replacement did not change the toxicity of (RXR)4−PMO (Figure 6). | null | 134 | 8,251 | 0 | false | null | null | Unlike the toxicity difference between (RX)8− and (rX)8−PMO, the L→D replacement did not change the toxicity of (RXR)4−PMO (Figure 6). | true | true | true | true | true | 1,335 |
5 | DISCUSSION | 0 | null | null | 17,670,797 | null | Substitution of either one R (rXR) or two R (rXr) from the RXR repeat neither reduced nor increased the toxicity profile of (RXR)4−PMO. | null | 135 | 8,252 | 0 | false | null | null | Substitution of either one R (rXR) or two R (rXr) from the RXR repeat neither reduced nor increased the toxicity profile of (RXR)4−PMO. | true | true | true | true | true | 1,335 |
5 | DISCUSSION | 0 | null | null | 17,670,797 | null | At this point, we do not fully understand the mechanisms of (RXR)4− and (RX)8−PMO conjugate toxicity, but look forward to studying this topic further. | null | 150 | 8,253 | 0 | false | null | null | At this point, we do not fully understand the mechanisms of (RXR)4− and (RX)8−PMO conjugate toxicity, but look forward to studying this topic further. | true | true | true | true | true | 1,335 |
6 | DISCUSSION | 0 | null | null | 17,670,797 | null | Serum effect on the activity of a CPP−AO conjugates is an important issue when considering potential in vivo applications. | null | 122 | 8,254 | 0 | false | null | null | Serum effect on the activity of a CPP−AO conjugates is an important issue when considering potential in vivo applications. | true | true | true | true | true | 1,336 |
6 | DISCUSSION | 0 | null | null | 17,670,797 | null | X/B-containing conjugates were still active in 60% serum while oligoarginine conjugates were not. | null | 97 | 8,255 | 0 | false | null | null | X/B-containing conjugates were still active in 60% serum while oligoarginine conjugates were not. | true | true | true | true | true | 1,336 |
6 | DISCUSSION | 0 | null | null | 17,670,797 | null | The greater stability of the X/B-containing conjugates to serum enzymes is likely a factor contributing to their high activity. | null | 127 | 8,256 | 0 | false | null | null | The greater stability of the X/B-containing conjugates to serum enzymes is likely a factor contributing to their high activity. | true | true | true | true | true | 1,336 |
6 | DISCUSSION | 0 | null | null | 17,670,797 | null | The loss of activity in high serum concentrations makes oligoarginine CPPs undesirable as potential therapeutic AO carriers. | null | 124 | 8,257 | 0 | false | null | null | The loss of activity in high serum concentrations makes oligoarginine CPPs undesirable as potential therapeutic AO carriers. | true | true | true | true | true | 1,336 |
7 | DISCUSSION | 1 | 5 | [
"B5"
] | 17,670,797 | pmid-17226957 | In summary, we have found that the X/B-containing CPP−PMO conjugates are superior to oligoarginine−PMO conjugates for the following reasons: they display higher activity in cell nuclei, are less affected by serum and are more stable in blood (5). | [
"5"
] | 246 | 8,258 | 1 | false | In summary, we have found that the X/B-containing CPP−PMO conjugates are superior to oligoarginine−PMO conjugates for the following reasons: they display higher activity in cell nuclei, are less affected by serum and are more stable in blood. | [
"5"
] | In summary, we have found that the X/B-containing CPP−PMO conjugates are superior to oligoarginine−PMO conjugates for the following reasons: they display higher activity in cell nuclei, are less affected by serum and are more stable in blood. | true | true | true | true | true | 1,337 |
7 | DISCUSSION | 1 | 5 | [
"B5"
] | 17,670,797 | pmid-17226957 | The toxicity of the X/B-containing CPPs can be reduced by keeping the number of X residues below 5 while still maintaining a reasonable delivery efficacy and stability. | [
"5"
] | 168 | 8,259 | 0 | false | The toxicity of the X/B-containing CPPs can be reduced by keeping the number of X residues below 5 while still maintaining a reasonable delivery efficacy and stability. | [] | The toxicity of the X/B-containing CPPs can be reduced by keeping the number of X residues below 5 while still maintaining a reasonable delivery efficacy and stability. | true | true | true | true | true | 1,337 |
7 | DISCUSSION | 1 | 5 | [
"B5"
] | 17,670,797 | pmid-17226957 | This study provides a basis for further optimization of CPP sequence using R, r, X and B residues in the interest of further reducing toxicity and increasing antisense activity, which will likely lead to more effective AO transporters for potential therapeutic applications. | [
"5"
] | 274 | 8,260 | 0 | false | This study provides a basis for further optimization of CPP sequence using R, r, X and B residues in the interest of further reducing toxicity and increasing antisense activity, which will likely lead to more effective AO transporters for potential therapeutic applications. | [] | This study provides a basis for further optimization of CPP sequence using R, r, X and B residues in the interest of further reducing toxicity and increasing antisense activity, which will likely lead to more effective AO transporters for potential therapeutic applications. | true | true | true | true | true | 1,337 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5"
] | 17,392,345 | pmid-16164997|pmid-7524073|pmid-10393194|pmid-10445873|pmid-11101533 | Protein synthesis requires quality control systems to ensure accuracy between the genetic information carried by messenger RNAs (mRNAs) and the sequence of the corresponding proteins. | [
"1",
"2",
"3",
"4",
"5"
] | 183 | 8,261 | 0 | false | Protein synthesis requires quality control systems to ensure accuracy between the genetic information carried by messenger RNAs (mRNAs) and the sequence of the corresponding proteins. | [] | Protein synthesis requires quality control systems to ensure accuracy between the genetic information carried by messenger RNAs (mRNAs) and the sequence of the corresponding proteins. | true | true | true | true | true | 1,338 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5"
] | 17,392,345 | pmid-16164997|pmid-7524073|pmid-10393194|pmid-10445873|pmid-11101533 | In bacteria, when translation proceeds on a truncated mRNA, ribosomes carry on the elongation process until the mRNA 3′-end is reached. | [
"1",
"2",
"3",
"4",
"5"
] | 135 | 8,262 | 0 | false | In bacteria, when translation proceeds on a truncated mRNA, ribosomes carry on the elongation process until the mRNA 3′-end is reached. | [] | In bacteria, when translation proceeds on a truncated mRNA, ribosomes carry on the elongation process until the mRNA 3′-end is reached. | true | true | true | true | true | 1,338 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5"
] | 17,392,345 | pmid-16164997|pmid-7524073|pmid-10393194|pmid-10445873|pmid-11101533 | There, translation termination is inefficient and ribosomes stall with the nascent polypeptide chain on the peptidyl-tRNA site (P-site), whereas the aminoacyl-tRNA site (A-site) is empty or only partially filled with the incomplete mRNA (Figure 1A). | [
"1",
"2",
"3",
"4",
"5"
] | 249 | 8,263 | 0 | false | There, translation termination is inefficient and ribosomes stall with the nascent polypeptide chain on the peptidyl-tRNA site (P-site), whereas the aminoacyl-tRNA site (A-site) is empty or only partially filled with the incomplete mRNA. | [
"Figure 1A"
] | There, translation termination is inefficient and ribosomes stall with the nascent polypeptide chain on the peptidyl-tRNA site (P-site), whereas the aminoacyl-tRNA site (A-site) is empty or only partially filled with the incomplete mRNA. | true | true | true | true | true | 1,338 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5"
] | 17,392,345 | pmid-16164997|pmid-7524073|pmid-10393194|pmid-10445873|pmid-11101533 | A quality-control mechanism, referred as trans-translation, rescues and recycles the stalled ribosomes and targets the incomplete protein for degradation. | [
"1",
"2",
"3",
"4",
"5"
] | 154 | 8,264 | 0 | false | A quality-control mechanism, referred as trans-translation, rescues and recycles the stalled ribosomes and targets the incomplete protein for degradation. | [] | A quality-control mechanism, referred as trans-translation, rescues and recycles the stalled ribosomes and targets the incomplete protein for degradation. | true | true | true | true | true | 1,338 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5"
] | 17,392,345 | pmid-16164997|pmid-7524073|pmid-10393194|pmid-10445873|pmid-11101533 | This process requires a specific RNA acting as both a transfer and a messenger RNA (tmRNA, ssrA or 10Sa RNA). | [
"1",
"2",
"3",
"4",
"5"
] | 109 | 8,265 | 0 | false | This process requires a specific RNA acting as both a transfer and a messenger RNA. | [
"tmRNA, ssrA or 10Sa RNA"
] | This process requires a specific RNA acting as both a transfer and a messenger RNA. | true | true | true | true | true | 1,338 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5"
] | 17,392,345 | pmid-16164997|pmid-7524073|pmid-10393194|pmid-10445873|pmid-11101533 | TmRNA has a tRNA (TLD) and a mRNA (MLD)-like domains. | [
"1",
"2",
"3",
"4",
"5"
] | 53 | 8,266 | 0 | false | TmRNA has a tRNA (TLD) and a mRNA (MLD)-like domains. | [] | TmRNA has a tRNA (TLD) and a mRNA (MLD)-like domains. | true | true | true | true | true | 1,338 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5"
] | 17,392,345 | pmid-16164997|pmid-7524073|pmid-10393194|pmid-10445873|pmid-11101533 | The TLD is aminoacylated with alanine (Ala) by alanyl-tRNA synthetase (AlaRS) and the MLD is a short (27–105 nt-long) internal open reading frame (ORF). | [
"1",
"2",
"3",
"4",
"5"
] | 152 | 8,267 | 0 | false | The TLD is aminoacylated with alanine (Ala) by alanyl-tRNA synthetase (AlaRS) and the MLD is a short internal open reading frame (ORF). | [
"27–105 nt-long"
] | The TLD is aminoacylated with alanine (Ala) by alanyl-tRNA synthetase (AlaRS) and the MLD is a short internal open reading frame (ORF). | true | true | true | true | true | 1,338 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5"
] | 17,392,345 | pmid-16164997|pmid-7524073|pmid-10393194|pmid-10445873|pmid-11101533 | During trans-translation, alanyl-tmRNA enters the A-site and, despite the lack of codon–anticodon interaction, the incomplete peptide chain is transferred to its alanine. | [
"1",
"2",
"3",
"4",
"5"
] | 170 | 8,268 | 0 | false | During trans-translation, alanyl-tmRNA enters the A-site and, despite the lack of codon–anticodon interaction, the incomplete peptide chain is transferred to its alanine. | [] | During trans-translation, alanyl-tmRNA enters the A-site and, despite the lack of codon–anticodon interaction, the incomplete peptide chain is transferred to its alanine. | true | true | true | true | true | 1,338 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5"
] | 17,392,345 | pmid-16164997|pmid-7524073|pmid-10393194|pmid-10445873|pmid-11101533 | Translation then switches to the MLD, which encodes a tag that targets the incomplete protein to degradation. | [
"1",
"2",
"3",
"4",
"5"
] | 109 | 8,269 | 0 | false | Translation then switches to the MLD, which encodes a tag that targets the incomplete protein to degradation. | [] | Translation then switches to the MLD, which encodes a tag that targets the incomplete protein to degradation. | true | true | true | true | true | 1,338 |
0 | INTRODUCTION | 1 | 2 | [
"B1",
"B2",
"B3",
"B4",
"B5"
] | 17,392,345 | pmid-16164997|pmid-7524073|pmid-10393194|pmid-10445873|pmid-11101533 | During trans-translation, tmRNA acts in concert with specific ligands [for a recent review, see (1)] including 70S ribosomes, AlaRS (2), small protein B (SmpB) (3), elongation factor Tu (EF-Tu) (4) and ribosomal protein S1 (5). | [
"1",
"2",
"3",
"4",
"5"
] | 227 | 8,270 | 1 | false | During trans-translation, tmRNA acts in concert with specific ligands including 70S ribosomes, AlaRS, small protein B (SmpB), elongation factor Tu (EF-Tu) and ribosomal protein S1. | [
"for a recent review, see (1)",
"2",
"3",
"4",
"5"
] | During trans-translation, tmRNA acts in concert with specific ligands including 70S ribosomes, AlaRS, small protein B (SmpB), elongation factor Tu (EF-Tu) and ribosomal protein S1. | true | true | true | true | true | 1,338 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5"
] | 17,392,345 | pmid-16164997|pmid-7524073|pmid-10393194|pmid-10445873|pmid-11101533 | Figure 1.Ribosomal protein S1 is dispensable for the tRNA-like function of tmRNA. | [
"1",
"2",
"3",
"4",
"5"
] | 81 | 8,271 | 0 | false | Figure 1.Ribosomal protein S1 is dispensable for the tRNA-like function of tmRNA. | [] | Figure 1.Ribosomal protein S1 is dispensable for the tRNA-like function of tmRNA. | true | true | true | true | true | 1,338 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5"
] | 17,392,345 | pmid-16164997|pmid-7524073|pmid-10393194|pmid-10445873|pmid-11101533 | (A) Schematic representation of the first step of trans-translation (trans-peptidation) on polyU mRNAs. | [
"1",
"2",
"3",
"4",
"5"
] | 103 | 8,272 | 0 | false | (A) Schematic representation of the first step of trans-translation (trans-peptidation) on polyU mRNAs. | [] | (A) Schematic representation of the first step of trans-translation (trans-peptidation) on polyU mRNAs. | false | false | true | true | false | 1,338 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5"
] | 17,392,345 | pmid-16164997|pmid-7524073|pmid-10393194|pmid-10445873|pmid-11101533 | The light gray ovals are the ribosomal subunits (the larger for the 50S and the smaller for the 30S). | [
"1",
"2",
"3",
"4",
"5"
] | 101 | 8,273 | 0 | false | The light gray ovals are the ribosomal subunits. | [
"the larger for the 50S and the smaller for the 30S"
] | The light gray ovals are the ribosomal subunits. | true | true | true | true | true | 1,338 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5"
] | 17,392,345 | pmid-16164997|pmid-7524073|pmid-10393194|pmid-10445873|pmid-11101533 | The white ovals are, from right to left, the decoding site (A); the transpeptidyl-site (P) and the exit site (E). | [
"1",
"2",
"3",
"4",
"5"
] | 113 | 8,274 | 0 | false | The white ovals are, from right to left, the decoding site (A); the transpeptidyl-site (P) and the exit site (E). | [] | The white ovals are, from right to left, the decoding site (A); the transpeptidyl-site (P) and the exit site (E). | true | true | true | true | true | 1,338 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5"
] | 17,392,345 | pmid-16164997|pmid-7524073|pmid-10393194|pmid-10445873|pmid-11101533 | tRNAs and tmRNA are depicted as hooks and as a lasso, respectively (for further insights see (1)). | [
"1",
"2",
"3",
"4",
"5"
] | 98 | 8,275 | 0 | false | tRNAs and tmRNA are depicted as hooks and as a lasso, respectively ). | [
"for further insights see (1"
] | tRNAs and tmRNA are depicted as hooks and as a lasso, respectively ). | false | true | true | true | false | 1,338 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5"
] | 17,392,345 | pmid-16164997|pmid-7524073|pmid-10393194|pmid-10445873|pmid-11101533 | (B) Western blots showing the quasi-absence of S1 in purified ‘S1-free’ 70S ribosomes compared to genuine 70S ribosomes. | [
"1",
"2",
"3",
"4",
"5"
] | 120 | 8,276 | 0 | false | (B) Western blots showing the quasi-absence of S1 in purified ‘S1-free’ 70S ribosomes compared to genuine 70S ribosomes. | [] | (B) Western blots showing the quasi-absence of S1 in purified ‘S1-free’ 70S ribosomes compared to genuine 70S ribosomes. | false | false | true | true | false | 1,338 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5"
] | 17,392,345 | pmid-16164997|pmid-7524073|pmid-10393194|pmid-10445873|pmid-11101533 | The trans-translation in vitro assay is inactive in the absence of SmpB. | [
"1",
"2",
"3",
"4",
"5"
] | 72 | 8,277 | 0 | false | The trans-translation in vitro assay is inactive in the absence of SmpB. | [] | The trans-translation in vitro assay is inactive in the absence of SmpB. | true | true | true | true | true | 1,338 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5"
] | 17,392,345 | pmid-16164997|pmid-7524073|pmid-10393194|pmid-10445873|pmid-11101533 | (D) Assay of alanine trans-peptidation (asterisk in A), using S1-free 70S ribosomes and increasing amounts of exogenous S1. | [
"1",
"2",
"3",
"4",
"5"
] | 123 | 8,278 | 0 | false | (D) Assay of alanine trans-peptidation (asterisk in A), using S1-free 70S ribosomes and increasing amounts of exogenous S1. | [] | (D) Assay of alanine trans-peptidation (asterisk in A), using S1-free 70S ribosomes and increasing amounts of exogenous S1. | false | false | true | true | false | 1,338 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5"
] | 17,392,345 | pmid-16164997|pmid-7524073|pmid-10393194|pmid-10445873|pmid-11101533 | Trans-peptidation is monitored by the incorporation of 3H-Ala from alanyl-tmRNA into polyPhe and is normalized to the level of translation, measured in parallel by the incorporation of 14C-Phe (section ‘Experimental procedures’). | [
"1",
"2",
"3",
"4",
"5"
] | 229 | 8,279 | 0 | false | Trans-peptidation is monitored by the incorporation of 3H-Ala from alanyl-tmRNA into polyPhe and is normalized to the level of translation, measured in parallel by the incorporation of 14C-Phe (section ‘Experimental procedures’). | [] | Trans-peptidation is monitored by the incorporation of 3H-Ala from alanyl-tmRNA into polyPhe and is normalized to the level of translation, measured in parallel by the incorporation of 14C-Phe (section ‘Experimental procedures’). | true | true | true | true | true | 1,338 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2",
"B3",
"B4",
"B5"
] | 17,392,345 | pmid-16164997|pmid-7524073|pmid-10393194|pmid-10445873|pmid-11101533 | The Y-axis represents the quantities (number of pmoles) of 3H alanine incorporated per assay. | [
"1",
"2",
"3",
"4",
"5"
] | 93 | 8,280 | 0 | false | The Y-axis represents the quantities (number of pmoles) of 3H alanine incorporated per assay. | [] | The Y-axis represents the quantities (number of pmoles) of 3H alanine incorporated per assay. | true | true | true | true | true | 1,338 |
1 | INTRODUCTION | 0 | null | null | 17,392,345 | null | Ribosomal protein S1 is dispensable for the tRNA-like function of tmRNA. | null | 72 | 8,281 | 0 | false | null | null | Ribosomal protein S1 is dispensable for the tRNA-like function of tmRNA. | true | true | true | true | true | 1,339 |
1 | INTRODUCTION | 0 | null | null | 17,392,345 | null | (A) Schematic representation of the first step of trans-translation (trans-peptidation) on polyU mRNAs. | null | 103 | 8,282 | 0 | false | null | null | (A) Schematic representation of the first step of trans-translation (trans-peptidation) on polyU mRNAs. | false | false | true | true | false | 1,339 |
1 | INTRODUCTION | 0 | null | null | 17,392,345 | null | The light gray ovals are the ribosomal subunits (the larger for the 50S and the smaller for the 30S). | null | 101 | 8,283 | 0 | false | null | null | The light gray ovals are the ribosomal subunits (the larger for the 50S and the smaller for the 30S). | true | true | true | true | true | 1,339 |
1 | INTRODUCTION | 0 | null | null | 17,392,345 | null | The white ovals are, from right to left, the decoding site (A); the transpeptidyl-site (P) and the exit site (E). | null | 113 | 8,284 | 0 | false | null | null | The white ovals are, from right to left, the decoding site (A); the transpeptidyl-site (P) and the exit site (E). | true | true | true | true | true | 1,339 |
1 | INTRODUCTION | 0 | null | null | 17,392,345 | null | tRNAs and tmRNA are depicted as hooks and as a lasso, respectively (for further insights see (1)). | null | 98 | 8,285 | 0 | false | null | null | tRNAs and tmRNA are depicted as hooks and as a lasso, respectively (for further insights see (1)). | false | true | true | true | false | 1,339 |
1 | INTRODUCTION | 0 | null | null | 17,392,345 | null | (B) Western blots showing the quasi-absence of S1 in purified ‘S1-free’ 70S ribosomes compared to genuine 70S ribosomes. | null | 120 | 8,286 | 0 | false | null | null | (B) Western blots showing the quasi-absence of S1 in purified ‘S1-free’ 70S ribosomes compared to genuine 70S ribosomes. | false | false | true | true | false | 1,339 |
1 | INTRODUCTION | 0 | null | null | 17,392,345 | null | The trans-translation in vitro assay is inactive in the absence of SmpB. | null | 72 | 8,287 | 0 | false | null | null | The trans-translation in vitro assay is inactive in the absence of SmpB. | true | true | true | true | true | 1,339 |
1 | INTRODUCTION | 0 | null | null | 17,392,345 | null | (D) Assay of alanine trans-peptidation (asterisk in A), using S1-free 70S ribosomes and increasing amounts of exogenous S1. | null | 123 | 8,288 | 0 | false | null | null | (D) Assay of alanine trans-peptidation (asterisk in A), using S1-free 70S ribosomes and increasing amounts of exogenous S1. | false | false | true | true | false | 1,339 |
1 | INTRODUCTION | 0 | null | null | 17,392,345 | null | Trans-peptidation is monitored by the incorporation of 3H-Ala from alanyl-tmRNA into polyPhe and is normalized to the level of translation, measured in parallel by the incorporation of 14C-Phe (section ‘Experimental procedures’). | null | 229 | 8,289 | 0 | false | null | null | Trans-peptidation is monitored by the incorporation of 3H-Ala from alanyl-tmRNA into polyPhe and is normalized to the level of translation, measured in parallel by the incorporation of 14C-Phe (section ‘Experimental procedures’). | true | true | true | true | true | 1,339 |
1 | INTRODUCTION | 0 | null | null | 17,392,345 | null | The Y-axis represents the quantities (number of pmoles) of 3H alanine incorporated per assay. | null | 93 | 8,290 | 0 | false | null | null | The Y-axis represents the quantities (number of pmoles) of 3H alanine incorporated per assay. | true | true | true | true | true | 1,339 |
2 | INTRODUCTION | 1 | 6 | [
"B6",
"B7",
"B8",
"B9"
] | 17,392,345 | pmid-6348874|pmid-375222|pmid-9008164|pmid-7003157 | S1, the largest ribosomal protein, binds weakly and reversibly to the head of the 30S ribosomal subunit (6), with an apparent binding constant of 20 nM | [
"6",
"7",
"8",
"9"
] | 151 | 8,291 | 1 | false | S1, the largest ribosomal protein, binds weakly and reversibly to the head of the 30S ribosomal subunit, with an apparent binding constant of 20 nM | [
"6"
] | S1, the largest ribosomal protein, binds weakly and reversibly to the head of the 30S ribosomal subunit, with an apparent binding constant of 20 nM | true | true | false | true | false | 1,340 |
2 | INTRODUCTION | 1 | 6 | [
"B6",
"B7",
"B8",
"B9"
] | 17,392,345 | pmid-6348874|pmid-375222|pmid-9008164|pmid-7003157 | [(7), and M. Hallier, unpublished Surface Plasmon Resonance data]. | [
"6",
"7",
"8",
"9"
] | 66 | 8,292 | 0 | false | . | [
"(7), and M. Hallier, unpublished Surface Plasmon Resonance data"
] | . | false | false | true | true | false | 1,340 |
2 | INTRODUCTION | 1 | 8 | [
"B6",
"B7",
"B8",
"B9"
] | 17,392,345 | pmid-6348874|pmid-375222|pmid-9008164|pmid-7003157 | S1 consists of six imperfectly repeated motifs, each organized in an oligonucleotide/oligosaccharide binding (OB) fold (8). | [
"6",
"7",
"8",
"9"
] | 123 | 8,293 | 1 | false | S1 consists of six imperfectly repeated motifs, each organized in an oligonucleotide/oligosaccharide binding (OB) fold. | [
"8"
] | S1 consists of six imperfectly repeated motifs, each organized in an oligonucleotide/oligosaccharide binding (OB) fold. | true | true | true | true | true | 1,340 |
2 | INTRODUCTION | 1 | 9 | [
"B6",
"B7",
"B8",
"B9"
] | 17,392,345 | pmid-6348874|pmid-375222|pmid-9008164|pmid-7003157 | Whereas the first two N-terminal motifs are required for anchoring S1 to the head of the ribosomal small subunit, the four C-terminal motifs face the solvent side (9). | [
"6",
"7",
"8",
"9"
] | 167 | 8,294 | 1 | false | Whereas the first two N-terminal motifs are required for anchoring S1 to the head of the ribosomal small subunit, the four C-terminal motifs face the solvent side. | [
"9"
] | Whereas the first two N-terminal motifs are required for anchoring S1 to the head of the ribosomal small subunit, the four C-terminal motifs face the solvent side. | true | true | true | true | true | 1,340 |
3 | INTRODUCTION | 1 | 10 | [
"B10",
"B5",
"B11 B12 B13",
"B14",
"B15",
"B16"
] | 17,392,345 | pmid-11248028|pmid-11101533|pmid-12457560|pmid-15340139|pmid-15564671|pmid-11593008|pmid-12677067|NA | Protein S1 co- | [
"10",
"5",
"11–13",
"14",
"15",
"16"
] | 14 | 8,295 | 0 | false | Protein S1 co- | [] | Protein S1 co- | true | true | false | true | false | 1,341 |
3 | INTRODUCTION | 1 | 10 | [
"B10",
"B5",
"B11 B12 B13",
"B14",
"B15",
"B16"
] | 17,392,345 | pmid-11248028|pmid-11101533|pmid-12457560|pmid-15340139|pmid-15564671|pmid-11593008|pmid-12677067|NA | purifies in vivo with an over-expressed tmRNA–SmpB complex (10) and the protein binds tmRNA in vitro with a 10–100 nM apparent binding constant (5,11–13). | [
"10",
"5",
"11–13",
"14",
"15",
"16"
] | 154 | 8,296 | 1 | false | purifies in vivo with an over-expressed tmRNA–SmpB complex and the protein binds tmRNA in vitro with a 10–100 nM apparent binding constant. | [
"10",
"5,11–13"
] | purifies in vivo with an over-expressed tmRNA–SmpB complex and the protein binds tmRNA in vitro with a 10–100 nM apparent binding constant. | false | true | true | true | false | 1,341 |
3 | INTRODUCTION | 1 | 10 | [
"B10",
"B5",
"B11 B12 B13",
"B14",
"B15",
"B16"
] | 17,392,345 | pmid-11248028|pmid-11101533|pmid-12457560|pmid-15340139|pmid-15564671|pmid-11593008|pmid-12677067|NA | Its exact role during trans-translation is unclear. | [
"10",
"5",
"11–13",
"14",
"15",
"16"
] | 51 | 8,297 | 0 | false | Its exact role during trans-translation is unclear. | [] | Its exact role during trans-translation is unclear. | true | true | true | true | true | 1,341 |
3 | INTRODUCTION | 1 | 10 | [
"B10",
"B5",
"B11 B12 B13",
"B14",
"B15",
"B16"
] | 17,392,345 | pmid-11248028|pmid-11101533|pmid-12457560|pmid-15340139|pmid-15564671|pmid-11593008|pmid-12677067|NA | Conceivably, S1 could prevent degradation of the tmRNA in the cytoplasm before it is loaded onto the ribosome and/or it could be involved in translation resumption onto tmRNA internal ORF, especially since the latter lacks a Shine Dalgarno element (SD) or an initiation codon (in most species, translation resumes onto a... | [
"10",
"5",
"11–13",
"14",
"15",
"16"
] | 337 | 8,298 | 0 | false | Conceivably, S1 could prevent degradation of the tmRNA in the cytoplasm before it is loaded onto the ribosome and/or it could be involved in translation resumption onto tmRNA internal ORF, especially since the latter lacks a Shine Dalgarno element (SD) or an initiation codon (in most species, translation resumes onto a... | [] | Conceivably, S1 could prevent degradation of the tmRNA in the cytoplasm before it is loaded onto the ribosome and/or it could be involved in translation resumption onto tmRNA internal ORF, especially since the latter lacks a Shine Dalgarno element (SD) or an initiation codon (in most species, translation resumes onto a... | true | true | true | true | true | 1,341 |
3 | INTRODUCTION | 1 | 14 | [
"B10",
"B5",
"B11 B12 B13",
"B14",
"B15",
"B16"
] | 17,392,345 | pmid-11248028|pmid-11101533|pmid-12457560|pmid-15340139|pmid-15564671|pmid-11593008|pmid-12677067|NA | However, S1 stands at the junction of the head, platform and main body of the 30S subunit, at the opposite side of the decoding site (14). | [
"10",
"5",
"11–13",
"14",
"15",
"16"
] | 138 | 8,299 | 1 | false | However, S1 stands at the junction of the head, platform and main body of the 30S subunit, at the opposite side of the decoding site. | [
"14"
] | However, S1 stands at the junction of the head, platform and main body of the 30S subunit, at the opposite side of the decoding site. | true | true | true | true | true | 1,341 |
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