paragraph_index int64 | sec string | p_has_citation int64 | cites string | citeids list | pmid int64 | cited_id string | sentences string | all_sent_cites list | sent_len int64 | sentence_batch_index int64 | sent_has_citation float64 | qc_fail bool | cited_sentence string | cites_in_sentence list | cln_sentence string | is_cap bool | is_alpha bool | ends_wp bool | cit_qc bool | lgtm bool | __index_level_0__ int64 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
2 | INTRODUCTION | 1 | 2 | [
"b2",
"b4"
] | 17,142,240 | pmid-14980014|pmid-10890390 | This ability can be estimated by a method that we term ‘knowledge based cross-validation’ by which we determine how the a priori known subtypes (e.g. | [
"2",
"4"
] | 149 | 800 | 0 | false | This ability can be estimated by a method that we term ‘knowledge based cross-validation’ by which we determine how the a priori known subtypes (e.g. | [] | This ability can be estimated by a method that we term ‘knowledge based cross-validation’ by which we determine how the a priori known subtypes (e.g. | true | true | true | true | true | 139 |
2 | INTRODUCTION | 1 | 2 | [
"b2",
"b4"
] | 17,142,240 | pmid-14980014|pmid-10890390 | protein families within a superfamily) can be recognized, based on other known subtypes (2–4). | [
"2",
"4"
] | 94 | 801 | 0 | false | protein families within a superfamily) can be recognized, based on other known subtypes. | [
"2–4"
] | protein families within a superfamily) can be recognized, based on other known subtypes. | false | true | true | true | false | 139 |
3 | INTRODUCTION | 0 | null | null | 17,142,240 | null | In view of the above difficulties and the number of new genomes sequenced, it is critically important to define benchmark datasets for assessing the accuracy of classification algorithms. | null | 187 | 802 | 0 | false | null | null | In view of the above difficulties and the number of new genomes sequenced, it is critically important to define benchmark datasets for assessing the accuracy of classification algorithms. | true | true | true | true | true | 140 |
3 | INTRODUCTION | 0 | null | null | 17,142,240 | null | The goal of the Protein Classification Benchmark collection is to provide a standardized set of protein data and procedures that makes it easier to compare new methods with the established ones. | null | 194 | 803 | 0 | false | null | null | The goal of the Protein Classification Benchmark collection is to provide a standardized set of protein data and procedures that makes it easier to compare new methods with the established ones. | true | true | true | true | true | 140 |
3 | INTRODUCTION | 0 | null | null | 17,142,240 | null | The collection is based on two general ideas: (i) since protein groups are highly variable, the performance of an algorithm has to be tested on a wide range of classification tasks, such as the recognition of all the protein families in a given database; (ii) the utility of a classifier is determined by its ability to recognize novel subtypes of the existing proteins. | null | 370 | 804 | 0 | false | null | null | The collection is based on two general ideas: (i) since protein groups are highly variable, the performance of an algorithm has to be tested on a wide range of classification tasks, such as the recognition of all the protein families in a given database; (ii) the utility of a classifier is determined by its ability to recognize novel subtypes of the existing proteins. | true | true | true | true | true | 140 |
3 | INTRODUCTION | 0 | null | null | 17,142,240 | null | The collection is primarily meant for those interested in developing sequence or structure comparison algorithms and/or machine learning methods for protein classification. | null | 172 | 805 | 0 | false | null | null | The collection is primarily meant for those interested in developing sequence or structure comparison algorithms and/or machine learning methods for protein classification. | true | true | true | true | true | 140 |
0 | INTRODUCTION | 1 | 1 | [
"b1",
"b2",
"b3"
] | 17,012,281 | pmid-15568970|pmid-10946107|pmid-12955455|pmid-16242989|pmid-10562560|pmid-15037779|pmid-16379013|pmid-10556512|pmid-16115062|pmid-14706817 | Group II introns have been detected in eukaryotic organelles as well as in eubacterial genomes as intervening sequences of protein, tRNA or rRNA coding genes. | [
"1",
"2",
"3"
] | 158 | 806 | 0 | false | Group II introns have been detected in eukaryotic organelles as well as in eubacterial genomes as intervening sequences of protein, tRNA or rRNA coding genes. | [] | Group II introns have been detected in eukaryotic organelles as well as in eubacterial genomes as intervening sequences of protein, tRNA or rRNA coding genes. | true | true | true | true | true | 141 |
0 | INTRODUCTION | 1 | 1 | [
"b1",
"b2",
"b3"
] | 17,012,281 | pmid-15568970|pmid-10946107|pmid-12955455|pmid-16242989|pmid-10562560|pmid-15037779|pmid-16379013|pmid-10556512|pmid-16115062|pmid-14706817 | Common to all group II introns is a conserved secondary structure that consists of six double-helical domains (DI-DVI) radiating from a central wheel (1). | [
"1",
"2",
"3"
] | 154 | 807 | 1 | false | Common to all group II introns is a conserved secondary structure that consists of six double-helical domains (DI-DVI) radiating from a central wheel. | [
"1"
] | Common to all group II introns is a conserved secondary structure that consists of six double-helical domains (DI-DVI) radiating from a central wheel. | true | true | true | true | true | 141 |
0 | INTRODUCTION | 1 | 1 | [
"b1",
"b2",
"b3"
] | 17,012,281 | pmid-15568970|pmid-10946107|pmid-12955455|pmid-16242989|pmid-10562560|pmid-15037779|pmid-16379013|pmid-10556512|pmid-16115062|pmid-14706817 | Group II introns splice via two sequential transesterifications that in vitro occur in some cases autocatalytically. | [
"1",
"2",
"3"
] | 116 | 808 | 0 | false | Group II introns splice via two sequential transesterifications that in vitro occur in some cases autocatalytically. | [] | Group II introns splice via two sequential transesterifications that in vitro occur in some cases autocatalytically. | true | true | true | true | true | 141 |
0 | INTRODUCTION | 1 | 1 | [
"b1",
"b2",
"b3"
] | 17,012,281 | pmid-15568970|pmid-10946107|pmid-12955455|pmid-16242989|pmid-10562560|pmid-15037779|pmid-16379013|pmid-10556512|pmid-16115062|pmid-14706817 | In vivo, however, splicing is dependent on protein co-factors as was shown by mutant analyses (2,3). | [
"1",
"2",
"3"
] | 100 | 809 | 0 | false | In vivo, however, splicing is dependent on protein co-factors as was shown by mutant analyses. | [
"2,3"
] | In vivo, however, splicing is dependent on protein co-factors as was shown by mutant analyses. | true | true | true | true | true | 141 |
1 | INTRODUCTION | 1 | 4 | [
"b4",
"b5",
"b6"
] | 17,012,281 | pmid-16453785|pmid-3280139|pmid-1707343|pmid-8382803|pmid-8117737|pmid-11406270|NA|NA | In Chlamydomonas reinhardtii chloroplasts, two trans-splicing introns were found in the psaA gene encoding the major P700 chlorophyll a/b-binding protein (4). | [
"4",
"5",
"6"
] | 158 | 810 | 1 | false | In Chlamydomonas reinhardtii chloroplasts, two trans-splicing introns were found in the psaA gene encoding the major P700 chlorophyll a/b-binding protein. | [
"4"
] | In Chlamydomonas reinhardtii chloroplasts, two trans-splicing introns were found in the psaA gene encoding the major P700 chlorophyll a/b-binding protein. | true | true | true | true | true | 142 |
1 | INTRODUCTION | 1 | 5 | [
"b4",
"b5",
"b6"
] | 17,012,281 | pmid-16453785|pmid-3280139|pmid-1707343|pmid-8382803|pmid-8117737|pmid-11406270|NA|NA | In the case of the first intron of the psaA gene, three independently transcribed RNAs associate via tertiary interactions to form a functional group II intron, resulting in trans-splicing of the flanking exon 1 and exon 2 (5). | [
"4",
"5",
"6"
] | 227 | 811 | 1 | false | In the case of the first intron of the psaA gene, three independently transcribed RNAs associate via tertiary interactions to form a functional group II intron, resulting in trans-splicing of the flanking exon 1 and exon 2. | [
"5"
] | In the case of the first intron of the psaA gene, three independently transcribed RNAs associate via tertiary interactions to form a functional group II intron, resulting in trans-splicing of the flanking exon 1 and exon 2. | true | true | true | true | true | 142 |
1 | INTRODUCTION | 1 | 4 | [
"b4",
"b5",
"b6"
] | 17,012,281 | pmid-16453785|pmid-3280139|pmid-1707343|pmid-8382803|pmid-8117737|pmid-11406270|NA|NA | Part of this tripartite group II intron is the tscA RNA that is processed from a chloroplast-encoded precursor RNA. | [
"4",
"5",
"6"
] | 115 | 812 | 0 | false | Part of this tripartite group II intron is the tscA RNA that is processed from a chloroplast-encoded precursor RNA. | [] | Part of this tripartite group II intron is the tscA RNA that is processed from a chloroplast-encoded precursor RNA. | true | true | true | true | true | 142 |
1 | INTRODUCTION | 1 | 6 | [
"b4",
"b5",
"b6"
] | 17,012,281 | pmid-16453785|pmid-3280139|pmid-1707343|pmid-8382803|pmid-8117737|pmid-11406270|NA|NA | Secondary structure predictions revealed that tscA contains domain DII and DIII as well as partial domains DI and DIV of the conserved secondary group II intron structure (6). | [
"4",
"5",
"6"
] | 175 | 813 | 1 | false | Secondary structure predictions revealed that tscA contains domain DII and DIII as well as partial domains DI and DIV of the conserved secondary group II intron structure. | [
"6"
] | Secondary structure predictions revealed that tscA contains domain DII and DIII as well as partial domains DI and DIV of the conserved secondary group II intron structure. | true | true | true | true | true | 142 |
2 | INTRODUCTION | 1 | 7 | [
"b7",
"b8",
"b9",
"b11"
] | 17,012,281 | pmid-10562560|pmid-16115062|pmid-16407333|pmid-15037779|pmid-11437228|pmid-15980199|NA|pmid-12569397|pmid-9077453|pmid-11073993|pmid-10921904|pmid-7565770|pmid-14992573 | Mutant work in C.reinhardtii has shown that >14 nuclear genes affect the chloroplast trans-splicing reaction, and complementation of some of the characterized mutants led to the identification of the molecular determinants. | [
"7",
"8",
"9",
"11"
] | 223 | 814 | 0 | false | Mutant work in C.reinhardtii has shown that >14 nuclear genes affect the chloroplast trans-splicing reaction, and complementation of some of the characterized mutants led to the identification of the molecular determinants. | [] | Mutant work in C.reinhardtii has shown that >14 nuclear genes affect the chloroplast trans-splicing reaction, and complementation of some of the characterized mutants led to the identification of the molecular determinants. | true | true | true | true | true | 143 |
2 | INTRODUCTION | 1 | 7 | [
"b7",
"b8",
"b9",
"b11"
] | 17,012,281 | pmid-10562560|pmid-16115062|pmid-16407333|pmid-15037779|pmid-11437228|pmid-15980199|NA|pmid-12569397|pmid-9077453|pmid-11073993|pmid-10921904|pmid-7565770|pmid-14992573 | Although some of the identified polypeptides are related to proteins involved in nucleic acid metabolisms, this function seems to be non-essential for intron splicing (7,8). | [
"7",
"8",
"9",
"11"
] | 173 | 815 | 0 | false | Although some of the identified polypeptides are related to proteins involved in nucleic acid metabolisms, this function seems to be non-essential for intron splicing. | [
"7,8"
] | Although some of the identified polypeptides are related to proteins involved in nucleic acid metabolisms, this function seems to be non-essential for intron splicing. | true | true | true | true | true | 143 |
2 | INTRODUCTION | 1 | 7 | [
"b7",
"b8",
"b9",
"b11"
] | 17,012,281 | pmid-10562560|pmid-16115062|pmid-16407333|pmid-15037779|pmid-11437228|pmid-15980199|NA|pmid-12569397|pmid-9077453|pmid-11073993|pmid-10921904|pmid-7565770|pmid-14992573 | Similar to nuclear mRNA splicing, these protein components might be part of a chloroplast splicing complex, because they were found in large stromal or membrane-bound RNA-containing complexes (9–11). | [
"7",
"8",
"9",
"11"
] | 199 | 816 | 0 | false | Similar to nuclear mRNA splicing, these protein components might be part of a chloroplast splicing complex, because they were found in large stromal or membrane-bound RNA-containing complexes. | [
"9–11"
] | Similar to nuclear mRNA splicing, these protein components might be part of a chloroplast splicing complex, because they were found in large stromal or membrane-bound RNA-containing complexes. | true | true | true | true | true | 143 |
3 | INTRODUCTION | 1 | 12 | [
"b12",
"b13",
"b14"
] | 17,012,281 | pmid-11437228|pmid-10921904|pmid-14735123 | To define further components of a putative ‘chloroplast spliceosome’ in C.reinhardtii, we used the tscA RNA as bait to identify novel intron RNA-binding proteins. | [
"12",
"13",
"14"
] | 162 | 817 | 0 | false | To define further components of a putative ‘chloroplast spliceosome’ in C.reinhardtii, we used the tscA RNA as bait to identify novel intron RNA-binding proteins. | [] | To define further components of a putative ‘chloroplast spliceosome’ in C.reinhardtii, we used the tscA RNA as bait to identify novel intron RNA-binding proteins. | true | true | true | true | true | 144 |
3 | INTRODUCTION | 1 | 12 | [
"b12",
"b13",
"b14"
] | 17,012,281 | pmid-11437228|pmid-10921904|pmid-14735123 | Using the yeast three-hybrid system, we isolated a polypeptide that seems to be a novel member of the multifunctional nucleosome assembly protein (NAP) family. | [
"12",
"13",
"14"
] | 159 | 818 | 0 | false | Using the yeast three-hybrid system, we isolated a polypeptide that seems to be a novel member of the multifunctional nucleosome assembly protein (NAP) family. | [] | Using the yeast three-hybrid system, we isolated a polypeptide that seems to be a novel member of the multifunctional nucleosome assembly protein (NAP) family. | true | true | true | true | true | 144 |
3 | INTRODUCTION | 1 | 12 | [
"b12",
"b13",
"b14"
] | 17,012,281 | pmid-11437228|pmid-10921904|pmid-14735123 | These well-conserved eukaryotic histone chaperones facilitate, for example, the nucleosome assembly and remodelling of chromatin, and are implicated in transcriptional regulation and cell cycle regulation (12,13). | [
"12",
"13",
"14"
] | 213 | 819 | 0 | false | These well-conserved eukaryotic histone chaperones facilitate, for example, the nucleosome assembly and remodelling of chromatin, and are implicated in transcriptional regulation and cell cycle regulation. | [
"12,13"
] | These well-conserved eukaryotic histone chaperones facilitate, for example, the nucleosome assembly and remodelling of chromatin, and are implicated in transcriptional regulation and cell cycle regulation. | true | true | true | true | true | 144 |
3 | INTRODUCTION | 1 | 12 | [
"b12",
"b13",
"b14"
] | 17,012,281 | pmid-11437228|pmid-10921904|pmid-14735123 | Here, we assign a novel function to a NAP-like protein. | [
"12",
"13",
"14"
] | 55 | 820 | 0 | false | Here, we assign a novel function to a NAP-like protein. | [] | Here, we assign a novel function to a NAP-like protein. | true | true | true | true | true | 144 |
3 | INTRODUCTION | 1 | 12 | [
"b12",
"b13",
"b14"
] | 17,012,281 | pmid-11437228|pmid-10921904|pmid-14735123 | Laser scanning confocal fluorescence microscopy (LSCFM) and in vitro binding assays demonstrate that chloroplasts of C.reinhardtii contain a NAP-like protein that specifically binds to organellar group II intron RNA and U-rich chloroplast transcripts. | [
"12",
"13",
"14"
] | 251 | 821 | 0 | false | Laser scanning confocal fluorescence microscopy (LSCFM) and in vitro binding assays demonstrate that chloroplasts of C.reinhardtii contain a NAP-like protein that specifically binds to organellar group II intron RNA and U-rich chloroplast transcripts. | [] | Laser scanning confocal fluorescence microscopy (LSCFM) and in vitro binding assays demonstrate that chloroplasts of C.reinhardtii contain a NAP-like protein that specifically binds to organellar group II intron RNA and U-rich chloroplast transcripts. | true | true | true | true | true | 144 |
3 | INTRODUCTION | 1 | 14 | [
"b12",
"b13",
"b14"
] | 17,012,281 | pmid-11437228|pmid-10921904|pmid-14735123 | Our data further support the view that during evolution, chloroplasts have acquired novel nuclear components that most probably were not delivered by endosymbiont gene transfer (14). | [
"12",
"13",
"14"
] | 182 | 822 | 1 | false | Our data further support the view that during evolution, chloroplasts have acquired novel nuclear components that most probably were not delivered by endosymbiont gene transfer. | [
"14"
] | Our data further support the view that during evolution, chloroplasts have acquired novel nuclear components that most probably were not delivered by endosymbiont gene transfer. | true | true | true | true | true | 144 |
0 | DISCUSSION | 1 | 53 | [
"b53",
"b7",
"b11",
"b54",
"b55",
"b8",
"b56"
] | 17,012,281 | pmid-15568970|pmid-10946107|pmid-12955455|pmid-16242989|pmid-10562560|pmid-15037779|pmid-16379013|pmid-10556512|pmid-16115062|pmid-14706817 | The splicing chemistry and RNA structures of self-splicing group II introns and nuclear pre-mRNA introns are strikingly similar. | [
"53",
"7",
"11",
"54",
"55",
"8",
"56"
] | 128 | 823 | 0 | false | The splicing chemistry and RNA structures of self-splicing group II introns and nuclear pre-mRNA introns are strikingly similar. | [] | The splicing chemistry and RNA structures of self-splicing group II introns and nuclear pre-mRNA introns are strikingly similar. | true | true | true | true | true | 145 |
0 | DISCUSSION | 1 | 53 | [
"b53",
"b7",
"b11",
"b54",
"b55",
"b8",
"b56"
] | 17,012,281 | pmid-15568970|pmid-10946107|pmid-12955455|pmid-16242989|pmid-10562560|pmid-15037779|pmid-16379013|pmid-10556512|pmid-16115062|pmid-14706817 | Thereby, suggesting some evolutionary relationship between group II introns and the nuclear spliceosomal intron (53). | [
"53",
"7",
"11",
"54",
"55",
"8",
"56"
] | 117 | 824 | 1 | false | Thereby, suggesting some evolutionary relationship between group II introns and the nuclear spliceosomal intron. | [
"53"
] | Thereby, suggesting some evolutionary relationship between group II introns and the nuclear spliceosomal intron. | true | true | true | true | true | 145 |
0 | DISCUSSION | 1 | 53 | [
"b53",
"b7",
"b11",
"b54",
"b55",
"b8",
"b56"
] | 17,012,281 | pmid-15568970|pmid-10946107|pmid-12955455|pmid-16242989|pmid-10562560|pmid-15037779|pmid-16379013|pmid-10556512|pmid-16115062|pmid-14706817 | Moreover, there is compelling evidence to suggest that chloroplast spliceosomes catalyse intron splicing using a similar mechanism to that reported for nuclear spliceosomes. | [
"53",
"7",
"11",
"54",
"55",
"8",
"56"
] | 173 | 825 | 0 | false | Moreover, there is compelling evidence to suggest that chloroplast spliceosomes catalyse intron splicing using a similar mechanism to that reported for nuclear spliceosomes. | [] | Moreover, there is compelling evidence to suggest that chloroplast spliceosomes catalyse intron splicing using a similar mechanism to that reported for nuclear spliceosomes. | true | true | true | true | true | 145 |
0 | DISCUSSION | 1 | 54 | [
"b53",
"b7",
"b11",
"b54",
"b55",
"b8",
"b56"
] | 17,012,281 | pmid-15568970|pmid-10946107|pmid-12955455|pmid-16242989|pmid-10562560|pmid-15037779|pmid-16379013|pmid-10556512|pmid-16115062|pmid-14706817 | This suggestion is the result of data obtained form a combination of different experimental approaches that have identified components of a putative chloroplast spliceosome in C.reinhardtii (7–11) and higher plants (54). | [
"53",
"7",
"11",
"54",
"55",
"8",
"56"
] | 220 | 826 | 1 | false | This suggestion is the result of data obtained form a combination of different experimental approaches that have identified components of a putative chloroplast spliceosome in C.reinhardtii and higher plants. | [
"7–11",
"54"
] | This suggestion is the result of data obtained form a combination of different experimental approaches that have identified components of a putative chloroplast spliceosome in C.reinhardtii and higher plants. | true | true | true | true | true | 145 |
0 | DISCUSSION | 1 | 53 | [
"b53",
"b7",
"b11",
"b54",
"b55",
"b8",
"b56"
] | 17,012,281 | pmid-15568970|pmid-10946107|pmid-12955455|pmid-16242989|pmid-10562560|pmid-15037779|pmid-16379013|pmid-10556512|pmid-16115062|pmid-14706817 | Additional support comes from studies with tobacco chloroplasts. | [
"53",
"7",
"11",
"54",
"55",
"8",
"56"
] | 64 | 827 | 0 | false | Additional support comes from studies with tobacco chloroplasts. | [] | Additional support comes from studies with tobacco chloroplasts. | true | true | true | true | true | 145 |
0 | DISCUSSION | 1 | 55 | [
"b53",
"b7",
"b11",
"b54",
"b55",
"b8",
"b56"
] | 17,012,281 | pmid-15568970|pmid-10946107|pmid-12955455|pmid-16242989|pmid-10562560|pmid-15037779|pmid-16379013|pmid-10556512|pmid-16115062|pmid-14706817 | Nakamura and co-workers (55) identified chloroplast ribonucleoproteins (cpRNPs) that are associated in vivo with various species of chloroplast mRNAs and intron-containing precursor tRNAs. | [
"53",
"7",
"11",
"54",
"55",
"8",
"56"
] | 188 | 828 | 1 | false | Nakamura and co-workers identified chloroplast ribonucleoproteins (cpRNPs) that are associated in vivo with various species of chloroplast mRNAs and intron-containing precursor tRNAs. | [
"55"
] | Nakamura and co-workers identified chloroplast ribonucleoproteins (cpRNPs) that are associated in vivo with various species of chloroplast mRNAs and intron-containing precursor tRNAs. | true | true | true | true | true | 145 |
0 | DISCUSSION | 1 | 53 | [
"b53",
"b7",
"b11",
"b54",
"b55",
"b8",
"b56"
] | 17,012,281 | pmid-15568970|pmid-10946107|pmid-12955455|pmid-16242989|pmid-10562560|pmid-15037779|pmid-16379013|pmid-10556512|pmid-16115062|pmid-14706817 | They suggested that these stromal RNA–protein complexes promote, for example, RNA splicing, processing or editing. | [
"53",
"7",
"11",
"54",
"55",
"8",
"56"
] | 114 | 829 | 0 | false | They suggested that these stromal RNA–protein complexes promote, for example, RNA splicing, processing or editing. | [] | They suggested that these stromal RNA–protein complexes promote, for example, RNA splicing, processing or editing. | true | true | true | true | true | 145 |
0 | DISCUSSION | 1 | 53 | [
"b53",
"b7",
"b11",
"b54",
"b55",
"b8",
"b56"
] | 17,012,281 | pmid-15568970|pmid-10946107|pmid-12955455|pmid-16242989|pmid-10562560|pmid-15037779|pmid-16379013|pmid-10556512|pmid-16115062|pmid-14706817 | Previously, the yeast three-hybrid system was used to demonstrate specific binding of proteins to organellar intron RNA (8,56). | [
"53",
"7",
"11",
"54",
"55",
"8",
"56"
] | 127 | 830 | 0 | false | Previously, the yeast three-hybrid system was used to demonstrate specific binding of proteins to organellar intron RNA. | [
"8,56"
] | Previously, the yeast three-hybrid system was used to demonstrate specific binding of proteins to organellar intron RNA. | true | true | true | true | true | 145 |
0 | DISCUSSION | 1 | 53 | [
"b53",
"b7",
"b11",
"b54",
"b55",
"b8",
"b56"
] | 17,012,281 | pmid-15568970|pmid-10946107|pmid-12955455|pmid-16242989|pmid-10562560|pmid-15037779|pmid-16379013|pmid-10556512|pmid-16115062|pmid-14706817 | In this work, we used the yeast three-hybrid system successfully to screen a C.reinhardtii cDNA library and we were able to detect the novel organellar protein cNAPL that specifically binds to the first psaA group II intron. | [
"53",
"7",
"11",
"54",
"55",
"8",
"56"
] | 224 | 831 | 0 | false | In this work, we used the yeast three-hybrid system successfully to screen a C.reinhardtii cDNA library and we were able to detect the novel organellar protein cNAPL that specifically binds to the first psaA group II intron. | [] | In this work, we used the yeast three-hybrid system successfully to screen a C.reinhardtii cDNA library and we were able to detect the novel organellar protein cNAPL that specifically binds to the first psaA group II intron. | true | true | true | true | true | 145 |
0 | DISCUSSION | 1 | 53 | [
"b53",
"b7",
"b11",
"b54",
"b55",
"b8",
"b56"
] | 17,012,281 | pmid-15568970|pmid-10946107|pmid-12955455|pmid-16242989|pmid-10562560|pmid-15037779|pmid-16379013|pmid-10556512|pmid-16115062|pmid-14706817 | The binding of cNAPL to domains DII+III and DV+VI of the first psaA intron was further shown in electromobility shift assays. | [
"53",
"7",
"11",
"54",
"55",
"8",
"56"
] | 125 | 832 | 0 | false | The binding of cNAPL to domains DII+III and DV+VI of the first psaA intron was further shown in electromobility shift assays. | [] | The binding of cNAPL to domains DII+III and DV+VI of the first psaA intron was further shown in electromobility shift assays. | true | true | true | true | true | 145 |
1 | DISCUSSION | 1 | 57 | [
"b57",
"b58",
"b22",
"b59",
"b60"
] | 17,012,281 | pmid-16453785|pmid-3280139|pmid-1707343|pmid-8382803|pmid-8117737|pmid-11406270|NA|NA | In several other studies using defined intron domains, separated molecules were found to fold into a structure corresponding to their conformation in the complete active intronic RNA (57,58). | [
"57",
"58",
"22",
"59",
"60"
] | 191 | 833 | 0 | false | In several other studies using defined intron domains, separated molecules were found to fold into a structure corresponding to their conformation in the complete active intronic RNA. | [
"57,58"
] | In several other studies using defined intron domains, separated molecules were found to fold into a structure corresponding to their conformation in the complete active intronic RNA. | true | true | true | true | true | 146 |
1 | DISCUSSION | 1 | 22 | [
"b57",
"b58",
"b22",
"b59",
"b60"
] | 17,012,281 | pmid-16453785|pmid-3280139|pmid-1707343|pmid-8382803|pmid-8117737|pmid-11406270|NA|NA | Recent studies have demonstrated that fragmented intron molecules are appropriate targets for gel retardation assays (22). | [
"57",
"58",
"22",
"59",
"60"
] | 122 | 834 | 1 | false | Recent studies have demonstrated that fragmented intron molecules are appropriate targets for gel retardation assays. | [
"22"
] | Recent studies have demonstrated that fragmented intron molecules are appropriate targets for gel retardation assays. | true | true | true | true | true | 146 |
1 | DISCUSSION | 1 | 57 | [
"b57",
"b58",
"b22",
"b59",
"b60"
] | 17,012,281 | pmid-16453785|pmid-3280139|pmid-1707343|pmid-8382803|pmid-8117737|pmid-11406270|NA|NA | In EMSA, we observed multiple shifted bands after incubating domains DII+III of tscA RNA with increasing amounts of cNAPL. | [
"57",
"58",
"22",
"59",
"60"
] | 122 | 835 | 0 | false | In EMSA, we observed multiple shifted bands after incubating domains DII+III of tscA RNA with increasing amounts of cNAPL. | [] | In EMSA, we observed multiple shifted bands after incubating domains DII+III of tscA RNA with increasing amounts of cNAPL. | true | true | true | true | true | 146 |
1 | DISCUSSION | 1 | 59 | [
"b57",
"b58",
"b22",
"b59",
"b60"
] | 17,012,281 | pmid-16453785|pmid-3280139|pmid-1707343|pmid-8382803|pmid-8117737|pmid-11406270|NA|NA | As was shown for example for the mutated SxlN1 protein of Drosophila, multiple shifted bands probably correspond to the sequential filling of binding sites when protein concentration is increased (59). | [
"57",
"58",
"22",
"59",
"60"
] | 201 | 836 | 1 | false | As was shown for example for the mutated SxlN1 protein of Drosophila, multiple shifted bands probably correspond to the sequential filling of binding sites when protein concentration is increased. | [
"59"
] | As was shown for example for the mutated SxlN1 protein of Drosophila, multiple shifted bands probably correspond to the sequential filling of binding sites when protein concentration is increased. | true | true | true | true | true | 146 |
1 | DISCUSSION | 1 | 57 | [
"b57",
"b58",
"b22",
"b59",
"b60"
] | 17,012,281 | pmid-16453785|pmid-3280139|pmid-1707343|pmid-8382803|pmid-8117737|pmid-11406270|NA|NA | Hence, the two shifted bands observed in Figure 2b–d shows non-cooperative binding of cNAPL to domains DII and DIII, thus indicating at least two binding sites. | [
"57",
"58",
"22",
"59",
"60"
] | 160 | 837 | 0 | false | Hence, the two shifted bands observed in Figure 2b–d shows non-cooperative binding of cNAPL to domains DII and DIII, thus indicating at least two binding sites. | [] | Hence, the two shifted bands observed in Figure 2b–d shows non-cooperative binding of cNAPL to domains DII and DIII, thus indicating at least two binding sites. | true | true | true | true | true | 146 |
1 | DISCUSSION | 1 | 57 | [
"b57",
"b58",
"b22",
"b59",
"b60"
] | 17,012,281 | pmid-16453785|pmid-3280139|pmid-1707343|pmid-8382803|pmid-8117737|pmid-11406270|NA|NA | However, we were not able to detect a known RNA-binding motif [, (60)] in cNAPL, such as the RNP motif, the K homology motif (KH) or the RGG (Arg-Gly-Gly) box. | [
"57",
"58",
"22",
"59",
"60"
] | 159 | 838 | 0 | false | However, we were not able to detect a known RNA-binding motif in cNAPL, such as the RNP motif, the K homology motif (KH) or the RGG (Arg-Gly-Gly) box. | [
", (60)"
] | However, we were not able to detect a known RNA-binding motif in cNAPL, such as the RNP motif, the K homology motif (KH) or the RGG (Arg-Gly-Gly) box. | true | true | true | true | true | 146 |
1 | DISCUSSION | 1 | 57 | [
"b57",
"b58",
"b22",
"b59",
"b60"
] | 17,012,281 | pmid-16453785|pmid-3280139|pmid-1707343|pmid-8382803|pmid-8117737|pmid-11406270|NA|NA | Further binding studies with truncated cNAPL constructs could help to determine the exact RNA-binding domain. | [
"57",
"58",
"22",
"59",
"60"
] | 109 | 839 | 0 | false | Further binding studies with truncated cNAPL constructs could help to determine the exact RNA-binding domain. | [] | Further binding studies with truncated cNAPL constructs could help to determine the exact RNA-binding domain. | true | true | true | true | true | 146 |
2 | DISCUSSION | 1 | 12 | [
"b12",
"b42",
"b61",
"b45",
"b62",
"b63",
"b13",
"b64",
"b65"
] | 17,012,281 | pmid-10562560|pmid-16115062|pmid-16407333|pmid-15037779|pmid-11437228|pmid-15980199|NA|pmid-12569397|pmid-9077453|pmid-11073993|pmid-10921904|pmid-7565770|pmid-14992573 | cNAPL is a member of the multifunctional family of NAPs that are involved in processes which normally take place in the nucleus or the cytoplasm of various eukaryotes (12,42,61). | [
"12",
"42",
"61",
"45",
"62",
"63",
"13",
"64",
"65"
] | 178 | 840 | 0 | false | cNAPL is a member of the multifunctional family of NAPs that are involved in processes which normally take place in the nucleus or the cytoplasm of various eukaryotes. | [
"12,42,61"
] | cNAPL is a member of the multifunctional family of NAPs that are involved in processes which normally take place in the nucleus or the cytoplasm of various eukaryotes. | false | true | true | true | false | 147 |
2 | DISCUSSION | 1 | 12 | [
"b12",
"b42",
"b61",
"b45",
"b62",
"b63",
"b13",
"b64",
"b65"
] | 17,012,281 | pmid-10562560|pmid-16115062|pmid-16407333|pmid-15037779|pmid-11437228|pmid-15980199|NA|pmid-12569397|pmid-9077453|pmid-11073993|pmid-10921904|pmid-7565770|pmid-14992573 | Besides their distinct functions in mitotic events and cytokinesis, NAPs act as histone chaperones, binding to all core histones with a preference for H2A and H2B and working as a deposition factor by transferring NAP1-bound histones to double-stranded DNA. | [
"12",
"42",
"61",
"45",
"62",
"63",
"13",
"64",
"65"
] | 257 | 841 | 0 | false | Besides their distinct functions in mitotic events and cytokinesis, NAPs act as histone chaperones, binding to all core histones with a preference for H2A and H2B and working as a deposition factor by transferring NAP1-bound histones to double-stranded DNA. | [] | Besides their distinct functions in mitotic events and cytokinesis, NAPs act as histone chaperones, binding to all core histones with a preference for H2A and H2B and working as a deposition factor by transferring NAP1-bound histones to double-stranded DNA. | true | true | true | true | true | 147 |
2 | DISCUSSION | 1 | 12 | [
"b12",
"b42",
"b61",
"b45",
"b62",
"b63",
"b13",
"b64",
"b65"
] | 17,012,281 | pmid-10562560|pmid-16115062|pmid-16407333|pmid-15037779|pmid-11437228|pmid-15980199|NA|pmid-12569397|pmid-9077453|pmid-11073993|pmid-10921904|pmid-7565770|pmid-14992573 | In addition to its nucleosome assembly and histone-binding activity, NAP1 as well as plant NAP1-like proteins may be involved in regulating gene expression and therefore cellular differentiation (45,62,63). | [
"12",
"42",
"61",
"45",
"62",
"63",
"13",
"64",
"65"
] | 206 | 842 | 0 | false | In addition to its nucleosome assembly and histone-binding activity, NAP1 as well as plant NAP1-like proteins may be involved in regulating gene expression and therefore cellular differentiation. | [
"45,62,63"
] | In addition to its nucleosome assembly and histone-binding activity, NAP1 as well as plant NAP1-like proteins may be involved in regulating gene expression and therefore cellular differentiation. | true | true | true | true | true | 147 |
2 | DISCUSSION | 1 | 12 | [
"b12",
"b42",
"b61",
"b45",
"b62",
"b63",
"b13",
"b64",
"b65"
] | 17,012,281 | pmid-10562560|pmid-16115062|pmid-16407333|pmid-15037779|pmid-11437228|pmid-15980199|NA|pmid-12569397|pmid-9077453|pmid-11073993|pmid-10921904|pmid-7565770|pmid-14992573 | NAP1 has also been shown to facilitate transcription factor binding by disruption of the histone octamer through the binding of H2A and H2B (13,64). | [
"12",
"42",
"61",
"45",
"62",
"63",
"13",
"64",
"65"
] | 148 | 843 | 0 | false | NAP1 has also been shown to facilitate transcription factor binding by disruption of the histone octamer through the binding of H2A and H2B. | [
"13,64"
] | NAP1 has also been shown to facilitate transcription factor binding by disruption of the histone octamer through the binding of H2A and H2B. | true | true | true | true | true | 147 |
2 | DISCUSSION | 1 | 65 | [
"b12",
"b42",
"b61",
"b45",
"b62",
"b63",
"b13",
"b64",
"b65"
] | 17,012,281 | pmid-10562560|pmid-16115062|pmid-16407333|pmid-15037779|pmid-11437228|pmid-15980199|NA|pmid-12569397|pmid-9077453|pmid-11073993|pmid-10921904|pmid-7565770|pmid-14992573 | NAP1 also shuttles histones H2A and H2B as well as a complex of H2A, H2B, H3 and H4 between the template DNA and nascent RNA during transcription (65). | [
"12",
"42",
"61",
"45",
"62",
"63",
"13",
"64",
"65"
] | 151 | 844 | 1 | false | NAP1 also shuttles histones H2A and H2B as well as a complex of H2A, H2B, H3 and H4 between the template DNA and nascent RNA during transcription. | [
"65"
] | NAP1 also shuttles histones H2A and H2B as well as a complex of H2A, H2B, H3 and H4 between the template DNA and nascent RNA during transcription. | true | true | true | true | true | 147 |
2 | DISCUSSION | 1 | 12 | [
"b12",
"b42",
"b61",
"b45",
"b62",
"b63",
"b13",
"b64",
"b65"
] | 17,012,281 | pmid-10562560|pmid-16115062|pmid-16407333|pmid-15037779|pmid-11437228|pmid-15980199|NA|pmid-12569397|pmid-9077453|pmid-11073993|pmid-10921904|pmid-7565770|pmid-14992573 | To date, however, it is still unknown whether NAP1 interacts directly also with RNA. | [
"12",
"42",
"61",
"45",
"62",
"63",
"13",
"64",
"65"
] | 84 | 845 | 0 | false | To date, however, it is still unknown whether NAP1 interacts directly also with RNA. | [] | To date, however, it is still unknown whether NAP1 interacts directly also with RNA. | true | true | true | true | true | 147 |
3 | DISCUSSION | 0 | null | null | 17,012,281 | pmid-11437228|pmid-10921904|pmid-14735123 | Phylogenetic analysis indicates that cNAPL is related to nuclear localized NAP polypeptides. | null | 92 | 846 | 0 | false | null | null | Phylogenetic analysis indicates that cNAPL is related to nuclear localized NAP polypeptides. | true | true | true | true | true | 148 |
3 | DISCUSSION | 0 | null | null | 17,012,281 | pmid-11437228|pmid-10921904|pmid-14735123 | The clustering of cNAPL with algal NAPs and not with NAPs of higher plants could be explained by its chloroplast targeting signal. | null | 130 | 847 | 0 | false | null | null | The clustering of cNAPL with algal NAPs and not with NAPs of higher plants could be explained by its chloroplast targeting signal. | true | true | true | true | true | 148 |
3 | DISCUSSION | 0 | null | null | 17,012,281 | pmid-11437228|pmid-10921904|pmid-14735123 | In the case of Thalassiosira NAP, TargetP predicted a 69 amino acid signal sequence, which could not be assigned clearly to any organelle. | null | 138 | 848 | 0 | false | null | null | In the case of Thalassiosira NAP, TargetP predicted a 69 amino acid signal sequence, which could not be assigned clearly to any organelle. | true | true | true | true | true | 148 |
3 | DISCUSSION | 0 | null | null | 17,012,281 | pmid-11437228|pmid-10921904|pmid-14735123 | Diatoms, such as T.pseudonana, possess so-called ‘complex plastids’ delineated by four distinct membranes. | null | 106 | 849 | 0 | false | null | null | Diatoms, such as T.pseudonana, possess so-called ‘complex plastids’ delineated by four distinct membranes. | true | true | true | true | true | 148 |
3 | DISCUSSION | 0 | null | null | 17,012,281 | pmid-11437228|pmid-10921904|pmid-14735123 | For a nuclear-encoded plastid polypeptide to be directed to the plastids, multiple targeting signals are necessary. | null | 115 | 850 | 0 | false | null | null | For a nuclear-encoded plastid polypeptide to be directed to the plastids, multiple targeting signals are necessary. | true | true | true | true | true | 148 |
3 | DISCUSSION | 0 | null | null | 17,012,281 | pmid-11437228|pmid-10921904|pmid-14735123 | Thus, determining a protein's localization in diatoms using today's prediction programs is difficult. | null | 101 | 851 | 0 | false | null | null | Thus, determining a protein's localization in diatoms using today's prediction programs is difficult. | true | true | true | true | true | 148 |
4 | DISCUSSION | 1 | 14 | [
"b14",
"b66",
"b14"
] | 17,012,281 | pmid-14735123|pmid-12493248|pmid-14735123 | It is now generally accepted that double-membrane-bound chloroplasts are the result of an endosymbiotic event involving a cyanobacterial-like organism early on in evolution. | [
"14",
"66",
"14"
] | 173 | 852 | 0 | false | It is now generally accepted that double-membrane-bound chloroplasts are the result of an endosymbiotic event involving a cyanobacterial-like organism early on in evolution. | [] | It is now generally accepted that double-membrane-bound chloroplasts are the result of an endosymbiotic event involving a cyanobacterial-like organism early on in evolution. | true | true | true | true | true | 149 |
4 | DISCUSSION | 1 | 14 | [
"b14",
"b66",
"b14"
] | 17,012,281 | pmid-14735123|pmid-12493248|pmid-14735123 | During evolution, the cyanobacterial endosymbiont has lost its autonomy, and this has been accompanied by significant changes of the chloroplast proteome (14,66). | [
"14",
"66",
"14"
] | 162 | 853 | 0 | false | During evolution, the cyanobacterial endosymbiont has lost its autonomy, and this has been accompanied by significant changes of the chloroplast proteome. | [
"14,66"
] | During evolution, the cyanobacterial endosymbiont has lost its autonomy, and this has been accompanied by significant changes of the chloroplast proteome. | true | true | true | true | true | 149 |
4 | DISCUSSION | 1 | 14 | [
"b14",
"b66",
"b14"
] | 17,012,281 | pmid-14735123|pmid-12493248|pmid-14735123 | A key factor in this process of adoption was the loss of genetic material resulting from gene transfer to the cell nucleus. | [
"14",
"66",
"14"
] | 123 | 854 | 0 | false | A key factor in this process of adoption was the loss of genetic material resulting from gene transfer to the cell nucleus. | [] | A key factor in this process of adoption was the loss of genetic material resulting from gene transfer to the cell nucleus. | true | true | true | true | true | 149 |
4 | DISCUSSION | 1 | 14 | [
"b14",
"b66",
"b14"
] | 17,012,281 | pmid-14735123|pmid-12493248|pmid-14735123 | The vast majority of proteins in present day chloroplasts are encoded by the host nucleus and require N-terminal presequences that target them back to the chloroplast. | [
"14",
"66",
"14"
] | 167 | 855 | 0 | false | The vast majority of proteins in present day chloroplasts are encoded by the host nucleus and require N-terminal presequences that target them back to the chloroplast. | [] | The vast majority of proteins in present day chloroplasts are encoded by the host nucleus and require N-terminal presequences that target them back to the chloroplast. | true | true | true | true | true | 149 |
4 | DISCUSSION | 1 | 14 | [
"b14",
"b66",
"b14"
] | 17,012,281 | pmid-14735123|pmid-12493248|pmid-14735123 | Therefore, in order to establish a functional organelle–nucleus interaction, chloroplasts have had to import a set of new proteins to adapt their metabolism to the new conditions. | [
"14",
"66",
"14"
] | 179 | 856 | 0 | false | Therefore, in order to establish a functional organelle–nucleus interaction, chloroplasts have had to import a set of new proteins to adapt their metabolism to the new conditions. | [] | Therefore, in order to establish a functional organelle–nucleus interaction, chloroplasts have had to import a set of new proteins to adapt their metabolism to the new conditions. | true | true | true | true | true | 149 |
4 | DISCUSSION | 1 | 14 | [
"b14",
"b66",
"b14"
] | 17,012,281 | pmid-14735123|pmid-12493248|pmid-14735123 | Interestingly, a proportion of these proteins do not seem to have been acquired from cyanobacteria (14). | [
"14",
"66",
"14"
] | 104 | 857 | 1 | false | Interestingly, a proportion of these proteins do not seem to have been acquired from cyanobacteria. | [
"14"
] | Interestingly, a proportion of these proteins do not seem to have been acquired from cyanobacteria. | true | true | true | true | true | 149 |
4 | DISCUSSION | 1 | 14 | [
"b14",
"b66",
"b14"
] | 17,012,281 | pmid-14735123|pmid-12493248|pmid-14735123 | Phylogenetic analysis and database research revealed that no NAP homologues could be identified in prokaryotic organisms. | [
"14",
"66",
"14"
] | 121 | 858 | 0 | false | Phylogenetic analysis and database research revealed that no NAP homologues could be identified in prokaryotic organisms. | [] | Phylogenetic analysis and database research revealed that no NAP homologues could be identified in prokaryotic organisms. | true | true | true | true | true | 149 |
4 | DISCUSSION | 1 | 14 | [
"b14",
"b66",
"b14"
] | 17,012,281 | pmid-14735123|pmid-12493248|pmid-14735123 | We therefore suggest that cNAPL does not originate from an endosymbiotic gene transfer event and that the chloroplast of C.reinhardtii has gained cNAPL as a novel nuclear-encoded factor. | [
"14",
"66",
"14"
] | 186 | 859 | 0 | false | We therefore suggest that cNAPL does not originate from an endosymbiotic gene transfer event and that the chloroplast of C.reinhardtii has gained cNAPL as a novel nuclear-encoded factor. | [] | We therefore suggest that cNAPL does not originate from an endosymbiotic gene transfer event and that the chloroplast of C.reinhardtii has gained cNAPL as a novel nuclear-encoded factor. | true | true | true | true | true | 149 |
4 | DISCUSSION | 1 | 14 | [
"b14",
"b66",
"b14"
] | 17,012,281 | pmid-14735123|pmid-12493248|pmid-14735123 | The phylogenetic analysis suggests that cNapl originate from a nuclear Nap gene, and is probably the result of a gene duplication event that occurred after separation of higher plants from green algae. | [
"14",
"66",
"14"
] | 201 | 860 | 0 | false | The phylogenetic analysis suggests that cNapl originate from a nuclear Nap gene, and is probably the result of a gene duplication event that occurred after separation of higher plants from green algae. | [] | The phylogenetic analysis suggests that cNapl originate from a nuclear Nap gene, and is probably the result of a gene duplication event that occurred after separation of higher plants from green algae. | true | true | true | true | true | 149 |
4 | DISCUSSION | 1 | 14 | [
"b14",
"b66",
"b14"
] | 17,012,281 | pmid-14735123|pmid-12493248|pmid-14735123 | We thus propose that cNAPL with its chloroplast transit peptide represents a new type of NAP-like polypeptide. | [
"14",
"66",
"14"
] | 110 | 861 | 0 | false | We thus propose that cNAPL with its chloroplast transit peptide represents a new type of NAP-like polypeptide. | [] | We thus propose that cNAPL with its chloroplast transit peptide represents a new type of NAP-like polypeptide. | true | true | true | true | true | 149 |
5 | DISCUSSION | 1 | 1 | [
"b1",
"b67",
"b7",
"b68",
"b69",
"b1",
"b8",
"b9",
"b70"
] | 17,012,281 | pmid-15568970|NA|pmid-10562560|pmid-16505350|NA|pmid-15568970|pmid-16115062|pmid-16407333|NA | Many group II introns of plants have lost their self-splicing activity during evolution and thus, recruited host-encoded proteins as splicing factors (1,67). | [
"1",
"67",
"7",
"68",
"69",
"1",
"8",
"9",
"70"
] | 157 | 862 | 0 | false | Many group II introns of plants have lost their self-splicing activity during evolution and thus, recruited host-encoded proteins as splicing factors. | [
"1,67"
] | Many group II introns of plants have lost their self-splicing activity during evolution and thus, recruited host-encoded proteins as splicing factors. | true | true | true | true | true | 150 |
5 | DISCUSSION | 1 | 1 | [
"b1",
"b67",
"b7",
"b68",
"b69",
"b1",
"b8",
"b9",
"b70"
] | 17,012,281 | pmid-15568970|NA|pmid-10562560|pmid-16505350|NA|pmid-15568970|pmid-16115062|pmid-16407333|NA | The participation of nuclear-encoded proteins in chloroplast splicing could provide a means to control the biogenesis of the photosynthetic apparatus. | [
"1",
"67",
"7",
"68",
"69",
"1",
"8",
"9",
"70"
] | 150 | 863 | 0 | false | The participation of nuclear-encoded proteins in chloroplast splicing could provide a means to control the biogenesis of the photosynthetic apparatus. | [] | The participation of nuclear-encoded proteins in chloroplast splicing could provide a means to control the biogenesis of the photosynthetic apparatus. | true | true | true | true | true | 150 |
5 | DISCUSSION | 1 | 1 | [
"b1",
"b67",
"b7",
"b68",
"b69",
"b1",
"b8",
"b9",
"b70"
] | 17,012,281 | pmid-15568970|NA|pmid-10562560|pmid-16505350|NA|pmid-15568970|pmid-16115062|pmid-16407333|NA | It has been suggested that these recruited host-encoded proteins probably had other functions in the cell. | [
"1",
"67",
"7",
"68",
"69",
"1",
"8",
"9",
"70"
] | 106 | 864 | 0 | false | It has been suggested that these recruited host-encoded proteins probably had other functions in the cell. | [] | It has been suggested that these recruited host-encoded proteins probably had other functions in the cell. | true | true | true | true | true | 150 |
5 | DISCUSSION | 1 | 1 | [
"b1",
"b67",
"b7",
"b68",
"b69",
"b1",
"b8",
"b9",
"b70"
] | 17,012,281 | pmid-15568970|NA|pmid-10562560|pmid-16505350|NA|pmid-15568970|pmid-16115062|pmid-16407333|NA | Many of these proteins show some degree of homology to proteins involved in RNA metabolism. | [
"1",
"67",
"7",
"68",
"69",
"1",
"8",
"9",
"70"
] | 91 | 865 | 0 | false | Many of these proteins show some degree of homology to proteins involved in RNA metabolism. | [] | Many of these proteins show some degree of homology to proteins involved in RNA metabolism. | true | true | true | true | true | 150 |
5 | DISCUSSION | 1 | 7 | [
"b1",
"b67",
"b7",
"b68",
"b69",
"b1",
"b8",
"b9",
"b70"
] | 17,012,281 | pmid-15568970|NA|pmid-10562560|pmid-16505350|NA|pmid-15568970|pmid-16115062|pmid-16407333|NA | For example, Raa2 of C.reinhardtii shows homology to pseudouridine synthetase; however, such enzymatic activity is not required for trans-splicing of psaA RNA (7). | [
"1",
"67",
"7",
"68",
"69",
"1",
"8",
"9",
"70"
] | 163 | 866 | 1 | false | For example, Raa2 of C.reinhardtii shows homology to pseudouridine synthetase; however, such enzymatic activity is not required for trans-splicing of psaA RNA. | [
"7"
] | For example, Raa2 of C.reinhardtii shows homology to pseudouridine synthetase; however, such enzymatic activity is not required for trans-splicing of psaA RNA. | true | true | true | true | true | 150 |
5 | DISCUSSION | 1 | 68 | [
"b1",
"b67",
"b7",
"b68",
"b69",
"b1",
"b8",
"b9",
"b70"
] | 17,012,281 | pmid-15568970|NA|pmid-10562560|pmid-16505350|NA|pmid-15568970|pmid-16115062|pmid-16407333|NA | Another example is Mss116p of Saccharomyces cerevisiae, which influences the splicing of all nine group I and all four group II introns in mitochondria (68). | [
"1",
"67",
"7",
"68",
"69",
"1",
"8",
"9",
"70"
] | 157 | 867 | 1 | false | Another example is Mss116p of Saccharomyces cerevisiae, which influences the splicing of all nine group I and all four group II introns in mitochondria. | [
"68"
] | Another example is Mss116p of Saccharomyces cerevisiae, which influences the splicing of all nine group I and all four group II introns in mitochondria. | true | true | true | true | true | 150 |
5 | DISCUSSION | 1 | 1 | [
"b1",
"b67",
"b7",
"b68",
"b69",
"b1",
"b8",
"b9",
"b70"
] | 17,012,281 | pmid-15568970|NA|pmid-10562560|pmid-16505350|NA|pmid-15568970|pmid-16115062|pmid-16407333|NA | Mss116p is related to DEAD-box proteins with RNA chaperone function and may facilitate splicing by resolving misfolded introns. | [
"1",
"67",
"7",
"68",
"69",
"1",
"8",
"9",
"70"
] | 127 | 868 | 0 | false | Mss116p is related to DEAD-box proteins with RNA chaperone function and may facilitate splicing by resolving misfolded introns. | [] | Mss116p is related to DEAD-box proteins with RNA chaperone function and may facilitate splicing by resolving misfolded introns. | true | true | true | true | true | 150 |
5 | DISCUSSION | 1 | 69 | [
"b1",
"b67",
"b7",
"b68",
"b69",
"b1",
"b8",
"b9",
"b70"
] | 17,012,281 | pmid-15568970|NA|pmid-10562560|pmid-16505350|NA|pmid-15568970|pmid-16115062|pmid-16407333|NA | However, it is generally discussed that proteins involved in splicing and interacting with intron RNAs seem to support RNA folding or to stabilize the active conformation, whereas the catalytic potential is clearly located in the RNA itself (69). | [
"1",
"67",
"7",
"68",
"69",
"1",
"8",
"9",
"70"
] | 246 | 869 | 1 | false | However, it is generally discussed that proteins involved in splicing and interacting with intron RNAs seem to support RNA folding or to stabilize the active conformation, whereas the catalytic potential is clearly located in the RNA itself. | [
"69"
] | However, it is generally discussed that proteins involved in splicing and interacting with intron RNAs seem to support RNA folding or to stabilize the active conformation, whereas the catalytic potential is clearly located in the RNA itself. | true | true | true | true | true | 150 |
5 | DISCUSSION | 1 | 1 | [
"b1",
"b67",
"b7",
"b68",
"b69",
"b1",
"b8",
"b9",
"b70"
] | 17,012,281 | pmid-15568970|NA|pmid-10562560|pmid-16505350|NA|pmid-15568970|pmid-16115062|pmid-16407333|NA | Furthermore, Mss116p is a bifunctional protein that influences, in addition to splicing of group I and group II introns, some RNA end-processing reactions and translation of a subset of mitochondrial mRNAs. | [
"1",
"67",
"7",
"68",
"69",
"1",
"8",
"9",
"70"
] | 206 | 870 | 0 | false | Furthermore, Mss116p is a bifunctional protein that influences, in addition to splicing of group I and group II introns, some RNA end-processing reactions and translation of a subset of mitochondrial mRNAs. | [] | Furthermore, Mss116p is a bifunctional protein that influences, in addition to splicing of group I and group II introns, some RNA end-processing reactions and translation of a subset of mitochondrial mRNAs. | true | true | true | true | true | 150 |
5 | DISCUSSION | 1 | 1 | [
"b1",
"b67",
"b7",
"b68",
"b69",
"b1",
"b8",
"b9",
"b70"
] | 17,012,281 | pmid-15568970|NA|pmid-10562560|pmid-16505350|NA|pmid-15568970|pmid-16115062|pmid-16407333|NA | Indeed, for several nuclear-encoded host proteins, it is known that they have additional cellular functions and seem to have been recruited for splicing during evolution (1). | [
"1",
"67",
"7",
"68",
"69",
"1",
"8",
"9",
"70"
] | 174 | 871 | 1 | false | Indeed, for several nuclear-encoded host proteins, it is known that they have additional cellular functions and seem to have been recruited for splicing during evolution. | [
"1"
] | Indeed, for several nuclear-encoded host proteins, it is known that they have additional cellular functions and seem to have been recruited for splicing during evolution. | true | true | true | true | true | 150 |
5 | DISCUSSION | 1 | 1 | [
"b1",
"b67",
"b7",
"b68",
"b69",
"b1",
"b8",
"b9",
"b70"
] | 17,012,281 | pmid-15568970|NA|pmid-10562560|pmid-16505350|NA|pmid-15568970|pmid-16115062|pmid-16407333|NA | Therefore, it has been questioned whether cNAPL is also a multifunctional protein. | [
"1",
"67",
"7",
"68",
"69",
"1",
"8",
"9",
"70"
] | 82 | 872 | 0 | false | Therefore, it has been questioned whether cNAPL is also a multifunctional protein. | [] | Therefore, it has been questioned whether cNAPL is also a multifunctional protein. | true | true | true | true | true | 150 |
5 | DISCUSSION | 1 | 1 | [
"b1",
"b67",
"b7",
"b68",
"b69",
"b1",
"b8",
"b9",
"b70"
] | 17,012,281 | pmid-15568970|NA|pmid-10562560|pmid-16505350|NA|pmid-15568970|pmid-16115062|pmid-16407333|NA | The analysed interactions of cNAPL with tscA RNA and domains DV and DVI of the first psaA intron implicate a role for cNAPL as a potential tscA RNA processing factor and also as a splicing factor of the first psaA intron. | [
"1",
"67",
"7",
"68",
"69",
"1",
"8",
"9",
"70"
] | 221 | 873 | 0 | false | The analysed interactions of cNAPL with tscA RNA and domains DV and DVI of the first psaA intron implicate a role for cNAPL as a potential tscA RNA processing factor and also as a splicing factor of the first psaA intron. | [] | The analysed interactions of cNAPL with tscA RNA and domains DV and DVI of the first psaA intron implicate a role for cNAPL as a potential tscA RNA processing factor and also as a splicing factor of the first psaA intron. | true | true | true | true | true | 150 |
5 | DISCUSSION | 1 | 8 | [
"b1",
"b67",
"b7",
"b68",
"b69",
"b1",
"b8",
"b9",
"b70"
] | 17,012,281 | pmid-15568970|NA|pmid-10562560|pmid-16505350|NA|pmid-15568970|pmid-16115062|pmid-16407333|NA | An example for such a bifunctional protein comes from recent work where Rat1 is required for both processing of tscA RNA as well as for splicing of the first psaA intron (8). | [
"1",
"67",
"7",
"68",
"69",
"1",
"8",
"9",
"70"
] | 174 | 874 | 1 | false | An example for such a bifunctional protein comes from recent work where Rat1 is required for both processing of tscA RNA as well as for splicing of the first psaA intron. | [
"8"
] | An example for such a bifunctional protein comes from recent work where Rat1 is required for both processing of tscA RNA as well as for splicing of the first psaA intron. | true | true | true | true | true | 150 |
5 | DISCUSSION | 1 | 9 | [
"b1",
"b67",
"b7",
"b68",
"b69",
"b1",
"b8",
"b9",
"b70"
] | 17,012,281 | pmid-15568970|NA|pmid-10562560|pmid-16505350|NA|pmid-15568970|pmid-16115062|pmid-16407333|NA | Another factor involved in tscA RNA processing and splicing of both introns is Raa1-L137H (9), allelic to HN31 (70). | [
"1",
"67",
"7",
"68",
"69",
"1",
"8",
"9",
"70"
] | 116 | 875 | 1 | false | Another factor involved in tscA RNA processing and splicing of both introns is Raa1-L137H, allelic to HN31. | [
"9",
"70"
] | Another factor involved in tscA RNA processing and splicing of both introns is Raa1-L137H, allelic to HN31. | true | true | true | true | true | 150 |
6 | DISCUSSION | 1 | 71 | [
"b71",
"b72",
"b69"
] | 17,012,281 | pmid-2684776|pmid-8670849|NA | cNAPL binds specifically to domains DII and DVI of the first psaA intron. | [
"71",
"72",
"69"
] | 73 | 876 | 0 | false | cNAPL binds specifically to domains DII and DVI of the first psaA intron. | [] | cNAPL binds specifically to domains DII and DVI of the first psaA intron. | false | true | true | true | false | 151 |
6 | DISCUSSION | 1 | 71 | [
"b71",
"b72",
"b69"
] | 17,012,281 | pmid-2684776|pmid-8670849|NA | Domain DII is a phylogenetically less-conserved region and was assigned as functionally unimportant because of its high degree of sequence and structure variations (71). | [
"71",
"72",
"69"
] | 169 | 877 | 1 | false | Domain DII is a phylogenetically less-conserved region and was assigned as functionally unimportant because of its high degree of sequence and structure variations. | [
"71"
] | Domain DII is a phylogenetically less-conserved region and was assigned as functionally unimportant because of its high degree of sequence and structure variations. | true | true | true | true | true | 151 |
6 | DISCUSSION | 1 | 72 | [
"b71",
"b72",
"b69"
] | 17,012,281 | pmid-2684776|pmid-8670849|NA | However, Chanfreau and Jacquier (72) could show that the so-called tertiary η–η′ interaction (see also Figure 2a) between DII and DVI of group IIA introns is responsible for a conformational change between the two catalytic transesterification steps. | [
"71",
"72",
"69"
] | 250 | 878 | 1 | false | However, Chanfreau and Jacquier could show that the so-called tertiary η–η′ interaction (see also Figure 2a) between DII and DVI of group IIA introns is responsible for a conformational change between the two catalytic transesterification steps. | [
"72"
] | However, Chanfreau and Jacquier could show that the so-called tertiary η–η′ interaction between DII and DVI of group IIA introns is responsible for a conformational change between the two catalytic transesterification steps. | true | true | true | true | true | 151 |
6 | DISCUSSION | 1 | 71 | [
"b71",
"b72",
"b69"
] | 17,012,281 | pmid-2684776|pmid-8670849|NA | Interestingly, only a few of the known group IIB introns can potentially form this interaction. | [
"71",
"72",
"69"
] | 95 | 879 | 0 | false | Interestingly, only a few of the known group IIB introns can potentially form this interaction. | [] | Interestingly, only a few of the known group IIB introns can potentially form this interaction. | true | true | true | true | true | 151 |
6 | DISCUSSION | 1 | 69 | [
"b71",
"b72",
"b69"
] | 17,012,281 | pmid-2684776|pmid-8670849|NA | It is discussed that the majority of the group IIB introns interact with protein factors to change the conformation between the first and the second step (69). | [
"71",
"72",
"69"
] | 159 | 880 | 1 | false | It is discussed that the majority of the group IIB introns interact with protein factors to change the conformation between the first and the second step. | [
"69"
] | It is discussed that the majority of the group IIB introns interact with protein factors to change the conformation between the first and the second step. | true | true | true | true | true | 151 |
6 | DISCUSSION | 1 | 71 | [
"b71",
"b72",
"b69"
] | 17,012,281 | pmid-2684776|pmid-8670849|NA | The fact that cNAPL interacts with both domains, DII and DVI, implies a role for cNAPL in this conformational change. | [
"71",
"72",
"69"
] | 117 | 881 | 0 | false | The fact that cNAPL interacts with both domains, DII and DVI, implies a role for cNAPL in this conformational change. | [] | The fact that cNAPL interacts with both domains, DII and DVI, implies a role for cNAPL in this conformational change. | true | true | true | true | true | 151 |
7 | DISCUSSION | 1 | 69 | [
"b69"
] | 17,012,281 | NA | Our experiments further demonstrated the binding of cNAPL to domain DV of the first psaA intron. | [
"69"
] | 96 | 882 | 0 | false | Our experiments further demonstrated the binding of cNAPL to domain DV of the first psaA intron. | [] | Our experiments further demonstrated the binding of cNAPL to domain DV of the first psaA intron. | true | true | true | true | true | 152 |
7 | DISCUSSION | 1 | 69 | [
"b69"
] | 17,012,281 | NA | Domain DV is the phylogenetically most conserved sequence and essential for the catalytic splicing reaction. | [
"69"
] | 108 | 883 | 0 | false | Domain DV is the phylogenetically most conserved sequence and essential for the catalytic splicing reaction. | [] | Domain DV is the phylogenetically most conserved sequence and essential for the catalytic splicing reaction. | true | true | true | true | true | 152 |
7 | DISCUSSION | 1 | 69 | [
"b69"
] | 17,012,281 | NA | DV shows numerous important tertiary interactions and contains important conserved sequence motifs (69). | [
"69"
] | 104 | 884 | 1 | false | DV shows numerous important tertiary interactions and contains important conserved sequence motifs. | [
"69"
] | DV shows numerous important tertiary interactions and contains important conserved sequence motifs. | true | true | true | true | true | 152 |
7 | DISCUSSION | 1 | 69 | [
"b69"
] | 17,012,281 | NA | Overall, we assume that cNAPL presumably has a function in the stabilization and correct folding of the catalytic core of the first psaA intron by interacting with tscA RNA and domains DV and DVI. | [
"69"
] | 196 | 885 | 0 | false | Overall, we assume that cNAPL presumably has a function in the stabilization and correct folding of the catalytic core of the first psaA intron by interacting with tscA RNA and domains DV and DVI. | [] | Overall, we assume that cNAPL presumably has a function in the stabilization and correct folding of the catalytic core of the first psaA intron by interacting with tscA RNA and domains DV and DVI. | true | true | true | true | true | 152 |
8 | DISCUSSION | 1 | 73 | [
"b73",
"b74",
"b75",
"b76",
"b77",
"b78",
"b11"
] | 17,012,281 | NA|pmid-10880449|pmid-15222765|pmid-11158540|pmid-8576143|NA|pmid-15037779 | In addition, our analyses showed that the binding of cNAPL to tscA RNA was competed efficiently by poly(U) in contrast to other RNA homopolymers. | [
"73",
"74",
"75",
"76",
"77",
"78",
"11"
] | 145 | 886 | 0 | false | In addition, our analyses showed that the binding of cNAPL to tscA RNA was competed efficiently by poly(U) in contrast to other RNA homopolymers. | [] | In addition, our analyses showed that the binding of cNAPL to tscA RNA was competed efficiently by poly(U) in contrast to other RNA homopolymers. | true | true | true | true | true | 153 |
8 | DISCUSSION | 1 | 73 | [
"b73",
"b74",
"b75",
"b76",
"b77",
"b78",
"b11"
] | 17,012,281 | NA|pmid-10880449|pmid-15222765|pmid-11158540|pmid-8576143|NA|pmid-15037779 | Moreover, cNAPL binds the 5′-UTR of U-rich chloroplast transcripts psbA, psbD, rbcL and rps4 considerably better than the nuclear transcripts Lhcb1 | [
"73",
"74",
"75",
"76",
"77",
"78",
"11"
] | 147 | 887 | 0 | false | Moreover, cNAPL binds the 5′-UTR of U-rich chloroplast transcripts psbA, psbD, rbcL and rps4 considerably better than the nuclear transcripts Lhcb1 | [] | Moreover, cNAPL binds the 5′-UTR of U-rich chloroplast transcripts psbA, psbD, rbcL and rps4 considerably better than the nuclear transcripts Lhcb1 | true | true | false | true | false | 153 |
8 | DISCUSSION | 1 | 73 | [
"b73",
"b74",
"b75",
"b76",
"b77",
"b78",
"b11"
] | 17,012,281 | NA|pmid-10880449|pmid-15222765|pmid-11158540|pmid-8576143|NA|pmid-15037779 | 5′-UTR, Lhcb1 3′-UTR, Rps18 and Tba1A. | [
"73",
"74",
"75",
"76",
"77",
"78",
"11"
] | 38 | 888 | 0 | false | 5′-UTR, Lhcb1 3′-UTR, Rps18 and Tba1A. | [] | 5′-UTR, Lhcb1 3′-UTR, Rps18 and Tba1A. | false | false | true | true | false | 153 |
8 | DISCUSSION | 1 | 73 | [
"b73",
"b74",
"b75",
"b76",
"b77",
"b78",
"b11"
] | 17,012,281 | NA|pmid-10880449|pmid-15222765|pmid-11158540|pmid-8576143|NA|pmid-15037779 | It is proven that the 5′-UTRs of chloroplast transcripts contain the cis-acting determinants for the stabilization of plastid transcripts and are essential for initiation of chloroplast translation by binding trans-acting factors (mostly encoded by nuclear genes) and by interaction with the ribosomal preinitiation complex (73). | [
"73",
"74",
"75",
"76",
"77",
"78",
"11"
] | 329 | 889 | 1 | false | It is proven that the 5′-UTRs of chloroplast transcripts contain the cis-acting determinants for the stabilization of plastid transcripts and are essential for initiation of chloroplast translation by binding trans-acting factors (mostly encoded by nuclear genes) and by interaction with the ribosomal preinitiation complex. | [
"73"
] | It is proven that the 5′-UTRs of chloroplast transcripts contain the cis-acting determinants for the stabilization of plastid transcripts and are essential for initiation of chloroplast translation by binding trans-acting factors (mostly encoded by nuclear genes) and by interaction with the ribosomal preinitiation complex. | true | true | true | true | true | 153 |
8 | DISCUSSION | 1 | 74 | [
"b73",
"b74",
"b75",
"b76",
"b77",
"b78",
"b11"
] | 17,012,281 | NA|pmid-10880449|pmid-15222765|pmid-11158540|pmid-8576143|NA|pmid-15037779 | For example, the stability of the psbD mRNA depends on a nucleus-encoded TPR protein, which is part of a high-molecular weight complex mediating its function via the psbD 5′-UTR (74). | [
"73",
"74",
"75",
"76",
"77",
"78",
"11"
] | 183 | 890 | 1 | false | For example, the stability of the psbD mRNA depends on a nucleus-encoded TPR protein, which is part of a high-molecular weight complex mediating its function via the psbD 5′-UTR. | [
"74"
] | For example, the stability of the psbD mRNA depends on a nucleus-encoded TPR protein, which is part of a high-molecular weight complex mediating its function via the psbD 5′-UTR. | true | true | true | true | true | 153 |
8 | DISCUSSION | 1 | 75 | [
"b73",
"b74",
"b75",
"b76",
"b77",
"b78",
"b11"
] | 17,012,281 | NA|pmid-10880449|pmid-15222765|pmid-11158540|pmid-8576143|NA|pmid-15037779 | For the psbA mRNA it is assumed that a multiprotein complex specifically regulates translation of this mRNA through interaction with a U-rich sequence in the 5′-UTR (75). | [
"73",
"74",
"75",
"76",
"77",
"78",
"11"
] | 170 | 891 | 1 | false | For the psbA mRNA it is assumed that a multiprotein complex specifically regulates translation of this mRNA through interaction with a U-rich sequence in the 5′-UTR. | [
"75"
] | For the psbA mRNA it is assumed that a multiprotein complex specifically regulates translation of this mRNA through interaction with a U-rich sequence in the 5′-UTR. | true | true | true | true | true | 153 |
8 | DISCUSSION | 1 | 73 | [
"b73",
"b74",
"b75",
"b76",
"b77",
"b78",
"b11"
] | 17,012,281 | NA|pmid-10880449|pmid-15222765|pmid-11158540|pmid-8576143|NA|pmid-15037779 | Furthermore, there are several proteins in Chlamydomonas binding to 5′-UTRs of chloroplast mRNAs, e.g. | [
"73",
"74",
"75",
"76",
"77",
"78",
"11"
] | 102 | 892 | 0 | false | Furthermore, there are several proteins in Chlamydomonas binding to 5′-UTRs of chloroplast mRNAs, e.g. | [] | Furthermore, there are several proteins in Chlamydomonas binding to 5′-UTRs of chloroplast mRNAs, e.g. | true | true | true | true | true | 153 |
8 | DISCUSSION | 1 | 73 | [
"b73",
"b74",
"b75",
"b76",
"b77",
"b78",
"b11"
] | 17,012,281 | NA|pmid-10880449|pmid-15222765|pmid-11158540|pmid-8576143|NA|pmid-15037779 | to 5′-UTRs of atpB, rbcL, rps7 and rps12, that so far have not been characterized and are discussed to be required for translational regulation (76,77). | [
"73",
"74",
"75",
"76",
"77",
"78",
"11"
] | 152 | 893 | 0 | false | to 5′-UTRs of atpB, rbcL, rps7 and rps12, that so far have not been characterized and are discussed to be required for translational regulation. | [
"76,77"
] | to 5′-UTRs of atpB, rbcL, rps7 and rps12, that so far have not been characterized and are discussed to be required for translational regulation. | false | true | true | true | false | 153 |
8 | DISCUSSION | 1 | 73 | [
"b73",
"b74",
"b75",
"b76",
"b77",
"b78",
"b11"
] | 17,012,281 | NA|pmid-10880449|pmid-15222765|pmid-11158540|pmid-8576143|NA|pmid-15037779 | However, the cpRNP complexes seem to be not only involved in regulation of translation, but also in distinct steps of post-transcriptional gene expression, e.g. | [
"73",
"74",
"75",
"76",
"77",
"78",
"11"
] | 160 | 894 | 0 | false | However, the cpRNP complexes seem to be not only involved in regulation of translation, but also in distinct steps of post-transcriptional gene expression, e.g. | [] | However, the cpRNP complexes seem to be not only involved in regulation of translation, but also in distinct steps of post-transcriptional gene expression, e.g. | true | true | true | true | true | 153 |
8 | DISCUSSION | 1 | 78 | [
"b73",
"b74",
"b75",
"b76",
"b77",
"b78",
"b11"
] | 17,012,281 | NA|pmid-10880449|pmid-15222765|pmid-11158540|pmid-8576143|NA|pmid-15037779 | by facilitating proper RNA folding for intron-containing RNA (78). | [
"73",
"74",
"75",
"76",
"77",
"78",
"11"
] | 66 | 895 | 1 | false | by facilitating proper RNA folding for intron-containing RNA. | [
"78"
] | by facilitating proper RNA folding for intron-containing RNA. | false | true | true | true | false | 153 |
8 | DISCUSSION | 1 | 11 | [
"b73",
"b74",
"b75",
"b76",
"b77",
"b78",
"b11"
] | 17,012,281 | NA|pmid-10880449|pmid-15222765|pmid-11158540|pmid-8576143|NA|pmid-15037779 | Recently it was demonstrated that there are two RNP complexes in C.reinhardtii that are involved in trans-splicing of psaA, one in the soluble fraction of the chloroplast and the other one associated with chloroplast membranes, which could provide a link to translation (11). | [
"73",
"74",
"75",
"76",
"77",
"78",
"11"
] | 275 | 896 | 1 | false | Recently it was demonstrated that there are two RNP complexes in C.reinhardtii that are involved in trans-splicing of psaA, one in the soluble fraction of the chloroplast and the other one associated with chloroplast membranes, which could provide a link to translation. | [
"11"
] | Recently it was demonstrated that there are two RNP complexes in C.reinhardtii that are involved in trans-splicing of psaA, one in the soluble fraction of the chloroplast and the other one associated with chloroplast membranes, which could provide a link to translation. | true | true | true | true | true | 153 |
9 | DISCUSSION | 1 | 78 | [
"b78"
] | 17,012,281 | NA | In conclusion, we have isolated a novel type of group II intron RNA-binding protein using the yeast three-hybrid system. | [
"78"
] | 120 | 897 | 0 | false | In conclusion, we have isolated a novel type of group II intron RNA-binding protein using the yeast three-hybrid system. | [] | In conclusion, we have isolated a novel type of group II intron RNA-binding protein using the yeast three-hybrid system. | true | true | true | true | true | 154 |
9 | DISCUSSION | 1 | 78 | [
"b78"
] | 17,012,281 | NA | Phylogenetic analysis indicates that the chloroplast located cNAPL protein is encoded by a nuclear gene that probably has evolved from duplication of an ancestral Nap gene. | [
"78"
] | 172 | 898 | 0 | false | Phylogenetic analysis indicates that the chloroplast located cNAPL protein is encoded by a nuclear gene that probably has evolved from duplication of an ancestral Nap gene. | [] | Phylogenetic analysis indicates that the chloroplast located cNAPL protein is encoded by a nuclear gene that probably has evolved from duplication of an ancestral Nap gene. | true | true | true | true | true | 154 |
9 | DISCUSSION | 1 | 78 | [
"b78"
] | 17,012,281 | NA | Moreover, it is proposed that cpRNP complexes are global mediators of chloroplast RNA metabolism, which connect transcription and translation in the chloroplast (78). | [
"78"
] | 166 | 899 | 1 | false | Moreover, it is proposed that cpRNP complexes are global mediators of chloroplast RNA metabolism, which connect transcription and translation in the chloroplast. | [
"78"
] | Moreover, it is proposed that cpRNP complexes are global mediators of chloroplast RNA metabolism, which connect transcription and translation in the chloroplast. | true | true | true | true | true | 154 |
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