paragraph_index int64 | sec string | p_has_citation int64 | cites string | citeids list | pmid int64 | cited_id string | sentences string | all_sent_cites list | sent_len int64 | sentence_batch_index int64 | sent_has_citation float64 | qc_fail bool | cited_sentence string | cites_in_sentence list | cln_sentence string | is_cap bool | is_alpha bool | ends_wp bool | cit_qc bool | lgtm bool | __index_level_0__ int64 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 | INTRODUCTION | 1 | 14 | [
"b14",
"b17",
"b14",
"b18",
"b19",
"b20",
"b21",
"b22",
"b23",
"b24"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | The hexameric helicases studied to date bind both ssDNA and dsDNA as ring-shaped structures. | [
"14",
"17",
"14",
"18",
"19",
"20",
"21",
"22",
"23",
"24"
] | 92 | 8,900 | 0 | false | The hexameric helicases studied to date bind both ssDNA and dsDNA as ring-shaped structures. | [] | The hexameric helicases studied to date bind both ssDNA and dsDNA as ring-shaped structures. | true | true | true | true | true | 1,424 |
1 | INTRODUCTION | 1 | 14 | [
"b14",
"b17",
"b14",
"b18",
"b19",
"b20",
"b21",
"b22",
"b23",
"b24"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | In most cases ssDNA is the preferred substrate for DNA binding. | [
"14",
"17",
"14",
"18",
"19",
"20",
"21",
"22",
"23",
"24"
] | 63 | 8,901 | 0 | false | In most cases ssDNA is the preferred substrate for DNA binding. | [] | In most cases ssDNA is the preferred substrate for DNA binding. | true | true | true | true | true | 1,424 |
1 | INTRODUCTION | 1 | 14 | [
"b14",
"b17",
"b14",
"b18",
"b19",
"b20",
"b21",
"b22",
"b23",
"b24"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | As described above, the high affinity of T-antigen and E1 for dsDNA is primarily a manifestation of the presence of the OBD, and related to the assembly process for concentrating the proteins at ori. | [
"14",
"17",
"14",
"18",
"19",
"20",
"21",
"22",
"23",
"24"
] | 199 | 8,902 | 0 | false | As described above, the high affinity of T-antigen and E1 for dsDNA is primarily a manifestation of the presence of the OBD, and related to the assembly process for concentrating the proteins at ori. | [] | As described above, the high affinity of T-antigen and E1 for dsDNA is primarily a manifestation of the presence of the OBD, and related to the assembly process for concentrating the proteins at ori. | true | true | true | true | true | 1,424 |
1 | INTRODUCTION | 1 | 14 | [
"b14",
"b17",
"b14",
"b18",
"b19",
"b20",
"b21",
"b22",
"b23",
"b24"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | For T7 gp4, Escherichia coli DnaB helicase and other members of the DnaB family, ssDNA binds in a central cavity generated by oligomerization (14–17). | [
"14",
"17",
"14",
"18",
"19",
"20",
"21",
"22",
"23",
"24"
] | 150 | 8,903 | 0 | false | For T7 gp4, Escherichia coli DnaB helicase and other members of the DnaB family, ssDNA binds in a central cavity generated by oligomerization. | [
"14–17"
] | For T7 gp4, Escherichia coli DnaB helicase and other members of the DnaB family, ssDNA binds in a central cavity generated by oligomerization. | true | true | true | true | true | 1,424 |
1 | INTRODUCTION | 1 | 14 | [
"b14",
"b17",
"b14",
"b18",
"b19",
"b20",
"b21",
"b22",
"b23",
"b24"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | Binding appears unidirectional, consistent with the defined unwinding polarity of helicases (14). | [
"14",
"17",
"14",
"18",
"19",
"20",
"21",
"22",
"23",
"24"
] | 97 | 8,904 | 1 | false | Binding appears unidirectional, consistent with the defined unwinding polarity of helicases. | [
"14"
] | Binding appears unidirectional, consistent with the defined unwinding polarity of helicases. | true | true | true | true | true | 1,424 |
1 | INTRODUCTION | 1 | 14 | [
"b14",
"b17",
"b14",
"b18",
"b19",
"b20",
"b21",
"b22",
"b23",
"b24"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | Binding to replication forks, which is likely to reveal important features of the helicase mechanism, has been studied less extensively. | [
"14",
"17",
"14",
"18",
"19",
"20",
"21",
"22",
"23",
"24"
] | 136 | 8,905 | 0 | false | Binding to replication forks, which is likely to reveal important features of the helicase mechanism, has been studied less extensively. | [] | Binding to replication forks, which is likely to reveal important features of the helicase mechanism, has been studied less extensively. | true | true | true | true | true | 1,424 |
1 | INTRODUCTION | 1 | 14 | [
"b14",
"b17",
"b14",
"b18",
"b19",
"b20",
"b21",
"b22",
"b23",
"b24"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | However, DNA footprinting studies suggest that T-antigen encircle one DNA strand at a replication fork structure with interactions extending into the duplex region ahead of the fork. | [
"14",
"17",
"14",
"18",
"19",
"20",
"21",
"22",
"23",
"24"
] | 182 | 8,906 | 0 | false | However, DNA footprinting studies suggest that T-antigen encircle one DNA strand at a replication fork structure with interactions extending into the duplex region ahead of the fork. | [] | However, DNA footprinting studies suggest that T-antigen encircle one DNA strand at a replication fork structure with interactions extending into the duplex region ahead of the fork. | true | true | true | true | true | 1,424 |
1 | INTRODUCTION | 1 | 14 | [
"b14",
"b17",
"b14",
"b18",
"b19",
"b20",
"b21",
"b22",
"b23",
"b24"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | The other DNA strand is excluded from the protein complex (18,19). | [
"14",
"17",
"14",
"18",
"19",
"20",
"21",
"22",
"23",
"24"
] | 66 | 8,907 | 0 | false | The other DNA strand is excluded from the protein complex. | [
"18,19"
] | The other DNA strand is excluded from the protein complex. | true | true | true | true | true | 1,424 |
1 | INTRODUCTION | 1 | 20 | [
"b14",
"b17",
"b14",
"b18",
"b19",
"b20",
"b21",
"b22",
"b23",
"b24"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | Quantitative fluorescence titration studies with synthetic replication forks demonstrate that DnaB also excludes one strand of DNA when the substrate is engaged (20). | [
"14",
"17",
"14",
"18",
"19",
"20",
"21",
"22",
"23",
"24"
] | 166 | 8,908 | 1 | false | Quantitative fluorescence titration studies with synthetic replication forks demonstrate that DnaB also excludes one strand of DNA when the substrate is engaged. | [
"20"
] | Quantitative fluorescence titration studies with synthetic replication forks demonstrate that DnaB also excludes one strand of DNA when the substrate is engaged. | true | true | true | true | true | 1,424 |
1 | INTRODUCTION | 1 | 14 | [
"b14",
"b17",
"b14",
"b18",
"b19",
"b20",
"b21",
"b22",
"b23",
"b24"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | The requirements for oligomerization of hexameric helicases differ, although in most cases a nucleotide is required. | [
"14",
"17",
"14",
"18",
"19",
"20",
"21",
"22",
"23",
"24"
] | 116 | 8,909 | 0 | false | The requirements for oligomerization of hexameric helicases differ, although in most cases a nucleotide is required. | [] | The requirements for oligomerization of hexameric helicases differ, although in most cases a nucleotide is required. | true | true | true | true | true | 1,424 |
1 | INTRODUCTION | 1 | 21 | [
"b14",
"b17",
"b14",
"b18",
"b19",
"b20",
"b21",
"b22",
"b23",
"b24"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | T-antigen forms hexamers with ADP, ATP and non-hydrolysable analogues (21). | [
"14",
"17",
"14",
"18",
"19",
"20",
"21",
"22",
"23",
"24"
] | 75 | 8,910 | 1 | false | T-antigen forms hexamers with ADP, ATP and non-hydrolysable analogues. | [
"21"
] | T-antigen forms hexamers with ADP, ATP and non-hydrolysable analogues. | true | true | true | true | true | 1,424 |
1 | INTRODUCTION | 1 | 22 | [
"b14",
"b17",
"b14",
"b18",
"b19",
"b20",
"b21",
"b22",
"b23",
"b24"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | For bovine papillomavirus (BPV) E1 it has been reported that the enzyme purified from E.coli requires DNA for hexamerization, with or without ATP (22), but the enzyme purified from recombinant baculovirus-infected insect cells exists in a number of oligomeric states (23). | [
"14",
"17",
"14",
"18",
"19",
"20",
"21",
"22",
"23",
"24"
] | 272 | 8,911 | 1 | false | For bovine papillomavirus (BPV) E1 it has been reported that the enzyme purified from E.coli requires DNA for hexamerization, with or without ATP, but the enzyme purified from recombinant baculovirus-infected insect cells exists in a number of oligomeric states. | [
"22",
"23"
] | For bovine papillomavirus (BPV) E1 it has been reported that the enzyme purified from E.coli requires DNA for hexamerization, with or without ATP, but the enzyme purified from recombinant baculovirus-infected insect cells exists in a number of oligomeric states. | true | true | true | true | true | 1,424 |
1 | INTRODUCTION | 1 | 24 | [
"b14",
"b17",
"b14",
"b18",
"b19",
"b20",
"b21",
"b22",
"b23",
"b24"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | Similar results have been reported for HPV 11 E1 from insect cells infected with a recombinant baculovirus (24). | [
"14",
"17",
"14",
"18",
"19",
"20",
"21",
"22",
"23",
"24"
] | 112 | 8,912 | 1 | false | Similar results have been reported for HPV 11 E1 from insect cells infected with a recombinant baculovirus. | [
"24"
] | Similar results have been reported for HPV 11 E1 from insect cells infected with a recombinant baculovirus. | true | true | true | true | true | 1,424 |
2 | INTRODUCTION | 1 | 25 | [
"b25"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | The helicase mechanism can be viewed as a DNA translocase activity coupled to a base pair separation process. | [
"25"
] | 109 | 8,913 | 0 | false | The helicase mechanism can be viewed as a DNA translocase activity coupled to a base pair separation process. | [] | The helicase mechanism can be viewed as a DNA translocase activity coupled to a base pair separation process. | true | true | true | true | true | 1,425 |
2 | INTRODUCTION | 1 | 25 | [
"b25"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | However, how these processes proceed mechanistically and are coupled to each other and NTPase activity are largely unknown. | [
"25"
] | 123 | 8,914 | 0 | false | However, how these processes proceed mechanistically and are coupled to each other and NTPase activity are largely unknown. | [] | However, how these processes proceed mechanistically and are coupled to each other and NTPase activity are largely unknown. | true | true | true | true | true | 1,425 |
2 | INTRODUCTION | 1 | 25 | [
"b25"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | Mechanisms based on active and passive unwinding have been proposed but differentiating between them is problematic since they share common features, principally the modulation of protein–protein and protein–DNA interactions in a nucleotide hydrolysis cycle (25). | [
"25"
] | 263 | 8,915 | 1 | false | Mechanisms based on active and passive unwinding have been proposed but differentiating between them is problematic since they share common features, principally the modulation of protein–protein and protein–DNA interactions in a nucleotide hydrolysis cycle. | [
"25"
] | Mechanisms based on active and passive unwinding have been proposed but differentiating between them is problematic since they share common features, principally the modulation of protein–protein and protein–DNA interactions in a nucleotide hydrolysis cycle. | true | true | true | true | true | 1,425 |
2 | INTRODUCTION | 1 | 25 | [
"b25"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | Here we report the characterization of the enzymatic, oligomerization and DNA-binding properties of a helicase protein derived from the C-terminal domain of BPV E1. | [
"25"
] | 164 | 8,916 | 0 | false | Here we report the characterization of the enzymatic, oligomerization and DNA-binding properties of a helicase protein derived from the C-terminal domain of BPV E1. | [] | Here we report the characterization of the enzymatic, oligomerization and DNA-binding properties of a helicase protein derived from the C-terminal domain of BPV E1. | true | true | true | true | true | 1,425 |
2 | INTRODUCTION | 1 | 25 | [
"b25"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | The E1HD is monomeric but assembles into hexamers with ssDNA or ATP but not ADP or AMP–PNP. | [
"25"
] | 91 | 8,917 | 0 | false | The E1HD is monomeric but assembles into hexamers with ssDNA or ATP but not ADP or AMP–PNP. | [] | The E1HD is monomeric but assembles into hexamers with ssDNA or ATP but not ADP or AMP–PNP. | true | true | true | true | true | 1,425 |
2 | INTRODUCTION | 1 | 25 | [
"b25"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | The minimal DNA-binding site sizefor efficient oligomerization is ∼16 bases. | [
"25"
] | 76 | 8,918 | 0 | false | The minimal DNA-binding site sizefor efficient oligomerization is ∼16 bases. | [] | The minimal DNA-binding site sizefor efficient oligomerization is ∼16 bases. | true | true | true | true | true | 1,425 |
2 | INTRODUCTION | 1 | 25 | [
"b25"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | With ADP, AMP–PNP or without a cofactor hexamers form an exceptionally tight complex with ssDNA. | [
"25"
] | 96 | 8,919 | 0 | false | With ADP, AMP–PNP or without a cofactor hexamers form an exceptionally tight complex with ssDNA. | [] | With ADP, AMP–PNP or without a cofactor hexamers form an exceptionally tight complex with ssDNA. | true | true | true | true | true | 1,425 |
2 | INTRODUCTION | 1 | 25 | [
"b25"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | However, in the presence of ATP the half-life of the protein–ssDNA interaction is, comparatively, exceptionally short. | [
"25"
] | 118 | 8,920 | 0 | false | However, in the presence of ATP the half-life of the protein–ssDNA interaction is, comparatively, exceptionally short. | [] | However, in the presence of ATP the half-life of the protein–ssDNA interaction is, comparatively, exceptionally short. | true | true | true | true | true | 1,425 |
2 | INTRODUCTION | 1 | 25 | [
"b25"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | These results suggest that during the ATP hydrolysis cycle an ssDNA-binding site ocillates from a high to a low-affinity state whereas protein–protein interactions change from a low- to high-affinity state. | [
"25"
] | 206 | 8,921 | 0 | false | These results suggest that during the ATP hydrolysis cycle an ssDNA-binding site ocillates from a high to a low-affinity state whereas protein–protein interactions change from a low- to high-affinity state. | [] | These results suggest that during the ATP hydrolysis cycle an ssDNA-binding site ocillates from a high to a low-affinity state whereas protein–protein interactions change from a low- to high-affinity state. | true | true | true | true | true | 1,425 |
2 | INTRODUCTION | 1 | 25 | [
"b25"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | These features are indicative of an ssDNA translocase activity, thus defining a component of the helicase mechanism for this important viral protein. | [
"25"
] | 149 | 8,922 | 0 | false | These features are indicative of an ssDNA translocase activity, thus defining a component of the helicase mechanism for this important viral protein. | [] | These features are indicative of an ssDNA translocase activity, thus defining a component of the helicase mechanism for this important viral protein. | true | true | true | true | true | 1,425 |
0 | DISCUSSION | 1 | 29 | [
"b29",
"b22",
"b23",
"b31",
"b32",
"b33",
"b34",
"b35",
"b35",
"b21",
"b24"
] | 16,893,956 | pmid-3025851|pmid-3035543|pmid-8389467|pmid-8380645|pmid-2846276|pmid-8090734|pmid-16061814|pmid-16738139|pmid-14504622|pmid-8557041|pmid-16285920|pmid-10652347|pmid-2539565|pmid-9843509|pmid-9658141|pmid-9933649|pmid-10535735|pmid-10892646|pmid-9302992|pmid-15454080|pmid-15289463|pmid-15289463|pmid-9149137|pmid-113045... | The C-terminal 307 residue domain of BPV E1 (E1HD) functions as a helicase with the unwinding polarity of native E1. | [
"29",
"22",
"23",
"31",
"32",
"33",
"34",
"35",
"35",
"21",
"24"
] | 116 | 8,923 | 0 | false | The C-terminal 307 residue domain of BPV E1 (E1HD) functions as a helicase with the unwinding polarity of native E1. | [] | The C-terminal 307 residue domain of BPV E1 (E1HD) functions as a helicase with the unwinding polarity of native E1. | true | true | true | true | true | 1,426 |
0 | DISCUSSION | 1 | 29 | [
"b29",
"b22",
"b23",
"b31",
"b32",
"b33",
"b34",
"b35",
"b35",
"b21",
"b24"
] | 16,893,956 | pmid-3025851|pmid-3035543|pmid-8389467|pmid-8380645|pmid-2846276|pmid-8090734|pmid-16061814|pmid-16738139|pmid-14504622|pmid-8557041|pmid-16285920|pmid-10652347|pmid-2539565|pmid-9843509|pmid-9658141|pmid-9933649|pmid-10535735|pmid-10892646|pmid-9302992|pmid-15454080|pmid-15289463|pmid-15289463|pmid-9149137|pmid-113045... | E1HD was capable of displacing long DNA strands from duplex DNA (Figure 1d), and based on our studies we propose below a mechanism for transclocase activity and processive unwinding by a hexameric protein complex. | [
"29",
"22",
"23",
"31",
"32",
"33",
"34",
"35",
"35",
"21",
"24"
] | 213 | 8,924 | 0 | false | E1HD was capable of displacing long DNA strands from duplex DNA (Figure 1d), and based on our studies we propose below a mechanism for transclocase activity and processive unwinding by a hexameric protein complex. | [] | E1HD was capable of displacing long DNA strands from duplex DNA (Figure 1d), and based on our studies we propose below a mechanism for transclocase activity and processive unwinding by a hexameric protein complex. | true | true | true | true | true | 1,426 |
0 | DISCUSSION | 1 | 29 | [
"b29",
"b22",
"b23",
"b31",
"b32",
"b33",
"b34",
"b35",
"b35",
"b21",
"b24"
] | 16,893,956 | pmid-3025851|pmid-3035543|pmid-8389467|pmid-8380645|pmid-2846276|pmid-8090734|pmid-16061814|pmid-16738139|pmid-14504622|pmid-8557041|pmid-16285920|pmid-10652347|pmid-2539565|pmid-9843509|pmid-9658141|pmid-9933649|pmid-10535735|pmid-10892646|pmid-9302992|pmid-15454080|pmid-15289463|pmid-15289463|pmid-9149137|pmid-113045... | The enzyme is monomeric at high-protein concentrations without cofactor or with ADP. | [
"29",
"22",
"23",
"31",
"32",
"33",
"34",
"35",
"35",
"21",
"24"
] | 84 | 8,925 | 0 | false | The enzyme is monomeric at high-protein concentrations without cofactor or with ADP. | [] | The enzyme is monomeric at high-protein concentrations without cofactor or with ADP. | true | true | true | true | true | 1,426 |
0 | DISCUSSION | 1 | 29 | [
"b29",
"b22",
"b23",
"b31",
"b32",
"b33",
"b34",
"b35",
"b35",
"b21",
"b24"
] | 16,893,956 | pmid-3025851|pmid-3035543|pmid-8389467|pmid-8380645|pmid-2846276|pmid-8090734|pmid-16061814|pmid-16738139|pmid-14504622|pmid-8557041|pmid-16285920|pmid-10652347|pmid-2539565|pmid-9843509|pmid-9658141|pmid-9933649|pmid-10535735|pmid-10892646|pmid-9302992|pmid-15454080|pmid-15289463|pmid-15289463|pmid-9149137|pmid-113045... | In the presence of ATP oligomerization is highly cooperative. | [
"29",
"22",
"23",
"31",
"32",
"33",
"34",
"35",
"35",
"21",
"24"
] | 61 | 8,926 | 0 | false | In the presence of ATP oligomerization is highly cooperative. | [] | In the presence of ATP oligomerization is highly cooperative. | true | true | true | true | true | 1,426 |
0 | DISCUSSION | 1 | 29 | [
"b29",
"b22",
"b23",
"b31",
"b32",
"b33",
"b34",
"b35",
"b35",
"b21",
"b24"
] | 16,893,956 | pmid-3025851|pmid-3035543|pmid-8389467|pmid-8380645|pmid-2846276|pmid-8090734|pmid-16061814|pmid-16738139|pmid-14504622|pmid-8557041|pmid-16285920|pmid-10652347|pmid-2539565|pmid-9843509|pmid-9658141|pmid-9933649|pmid-10535735|pmid-10892646|pmid-9302992|pmid-15454080|pmid-15289463|pmid-15289463|pmid-9149137|pmid-113045... | Consistent with the properties of other members of the same helicase family the complex appears to be hexameric, as its elution volume in gel filtration was similar to the hexameric complex with ssDNA whose size we determined accurately. | [
"29",
"22",
"23",
"31",
"32",
"33",
"34",
"35",
"35",
"21",
"24"
] | 237 | 8,927 | 0 | false | Consistent with the properties of other members of the same helicase family the complex appears to be hexameric, as its elution volume in gel filtration was similar to the hexameric complex with ssDNA whose size we determined accurately. | [] | Consistent with the properties of other members of the same helicase family the complex appears to be hexameric, as its elution volume in gel filtration was similar to the hexameric complex with ssDNA whose size we determined accurately. | true | true | true | true | true | 1,426 |
0 | DISCUSSION | 1 | 29 | [
"b29",
"b22",
"b23",
"b31",
"b32",
"b33",
"b34",
"b35",
"b35",
"b21",
"b24"
] | 16,893,956 | pmid-3025851|pmid-3035543|pmid-8389467|pmid-8380645|pmid-2846276|pmid-8090734|pmid-16061814|pmid-16738139|pmid-14504622|pmid-8557041|pmid-16285920|pmid-10652347|pmid-2539565|pmid-9843509|pmid-9658141|pmid-9933649|pmid-10535735|pmid-10892646|pmid-9302992|pmid-15454080|pmid-15289463|pmid-15289463|pmid-9149137|pmid-113045... | The nucleotide requirements for oligomerization therefore resemble those for full-length E1 binding to double-stranded ori DNA, where the complexes that form in the absence of hydrolysable ATP are relatively unstable (29). | [
"29",
"22",
"23",
"31",
"32",
"33",
"34",
"35",
"35",
"21",
"24"
] | 222 | 8,928 | 1 | false | The nucleotide requirements for oligomerization therefore resemble those for full-length E1 binding to double-stranded ori DNA, where the complexes that form in the absence of hydrolysable ATP are relatively unstable. | [
"29"
] | The nucleotide requirements for oligomerization therefore resemble those for full-length E1 binding to double-stranded ori DNA, where the complexes that form in the absence of hydrolysable ATP are relatively unstable. | true | true | true | true | true | 1,426 |
0 | DISCUSSION | 1 | 29 | [
"b29",
"b22",
"b23",
"b31",
"b32",
"b33",
"b34",
"b35",
"b35",
"b21",
"b24"
] | 16,893,956 | pmid-3025851|pmid-3035543|pmid-8389467|pmid-8380645|pmid-2846276|pmid-8090734|pmid-16061814|pmid-16738139|pmid-14504622|pmid-8557041|pmid-16285920|pmid-10652347|pmid-2539565|pmid-9843509|pmid-9658141|pmid-9933649|pmid-10535735|pmid-10892646|pmid-9302992|pmid-15454080|pmid-15289463|pmid-15289463|pmid-9149137|pmid-113045... | It is curious however that hexamerization of full-length E1 itself has not been observed with ATP (22,23). | [
"29",
"22",
"23",
"31",
"32",
"33",
"34",
"35",
"35",
"21",
"24"
] | 106 | 8,929 | 0 | false | It is curious however that hexamerization of full-length E1 itself has not been observed with ATP. | [
"22,23"
] | It is curious however that hexamerization of full-length E1 itself has not been observed with ATP. | true | true | true | true | true | 1,426 |
0 | DISCUSSION | 1 | 29 | [
"b29",
"b22",
"b23",
"b31",
"b32",
"b33",
"b34",
"b35",
"b35",
"b21",
"b24"
] | 16,893,956 | pmid-3025851|pmid-3035543|pmid-8389467|pmid-8380645|pmid-2846276|pmid-8090734|pmid-16061814|pmid-16738139|pmid-14504622|pmid-8557041|pmid-16285920|pmid-10652347|pmid-2539565|pmid-9843509|pmid-9658141|pmid-9933649|pmid-10535735|pmid-10892646|pmid-9302992|pmid-15454080|pmid-15289463|pmid-15289463|pmid-9149137|pmid-113045... | It is possible that the protein concentrations required for hexamerization were not achieved in previous studies or that the experimental conditions did not favour complex stabilization. | [
"29",
"22",
"23",
"31",
"32",
"33",
"34",
"35",
"35",
"21",
"24"
] | 186 | 8,930 | 0 | false | It is possible that the protein concentrations required for hexamerization were not achieved in previous studies or that the experimental conditions did not favour complex stabilization. | [] | It is possible that the protein concentrations required for hexamerization were not achieved in previous studies or that the experimental conditions did not favour complex stabilization. | true | true | true | true | true | 1,426 |
0 | DISCUSSION | 1 | 29 | [
"b29",
"b22",
"b23",
"b31",
"b32",
"b33",
"b34",
"b35",
"b35",
"b21",
"b24"
] | 16,893,956 | pmid-3025851|pmid-3035543|pmid-8389467|pmid-8380645|pmid-2846276|pmid-8090734|pmid-16061814|pmid-16738139|pmid-14504622|pmid-8557041|pmid-16285920|pmid-10652347|pmid-2539565|pmid-9843509|pmid-9658141|pmid-9933649|pmid-10535735|pmid-10892646|pmid-9302992|pmid-15454080|pmid-15289463|pmid-15289463|pmid-9149137|pmid-113045... | Hydrolysis of available ATP is a likely explanation for our inability to observe discrete peaks in glycerol gradients (data not shown), performed over hours rather than minutes in the case of gel filtration. | [
"29",
"22",
"23",
"31",
"32",
"33",
"34",
"35",
"35",
"21",
"24"
] | 207 | 8,931 | 0 | false | Hydrolysis of available ATP is a likely explanation for our inability to observe discrete peaks in glycerol gradients (data not shown), performed over hours rather than minutes in the case of gel filtration. | [] | Hydrolysis of available ATP is a likely explanation for our inability to observe discrete peaks in glycerol gradients (data not shown), performed over hours rather than minutes in the case of gel filtration. | true | true | true | true | true | 1,426 |
0 | DISCUSSION | 1 | 29 | [
"b29",
"b22",
"b23",
"b31",
"b32",
"b33",
"b34",
"b35",
"b35",
"b21",
"b24"
] | 16,893,956 | pmid-3025851|pmid-3035543|pmid-8389467|pmid-8380645|pmid-2846276|pmid-8090734|pmid-16061814|pmid-16738139|pmid-14504622|pmid-8557041|pmid-16285920|pmid-10652347|pmid-2539565|pmid-9843509|pmid-9658141|pmid-9933649|pmid-10535735|pmid-10892646|pmid-9302992|pmid-15454080|pmid-15289463|pmid-15289463|pmid-9149137|pmid-113045... | We have also shown that oligomerization in the presence of ATP is required to assemble a catalytically robust ATPase. | [
"29",
"22",
"23",
"31",
"32",
"33",
"34",
"35",
"35",
"21",
"24"
] | 117 | 8,932 | 0 | false | We have also shown that oligomerization in the presence of ATP is required to assemble a catalytically robust ATPase. | [] | We have also shown that oligomerization in the presence of ATP is required to assemble a catalytically robust ATPase. | true | true | true | true | true | 1,426 |
0 | DISCUSSION | 1 | 33 | [
"b29",
"b22",
"b23",
"b31",
"b32",
"b33",
"b34",
"b35",
"b35",
"b21",
"b24"
] | 16,893,956 | pmid-3025851|pmid-3035543|pmid-8389467|pmid-8380645|pmid-2846276|pmid-8090734|pmid-16061814|pmid-16738139|pmid-14504622|pmid-8557041|pmid-16285920|pmid-10652347|pmid-2539565|pmid-9843509|pmid-9658141|pmid-9933649|pmid-10535735|pmid-10892646|pmid-9302992|pmid-15454080|pmid-15289463|pmid-15289463|pmid-9149137|pmid-113045... | Many AAA+ helicases proteins possess an ‘arginine finger’ (31,32), first identified in GTPases (33). | [
"29",
"22",
"23",
"31",
"32",
"33",
"34",
"35",
"35",
"21",
"24"
] | 100 | 8,933 | 1 | false | Many AAA+ helicases proteins possess an ‘arginine finger’, first identified in GTPases. | [
"31,32",
"33"
] | Many AAA+ helicases proteins possess an ‘arginine finger’, first identified in GTPases. | true | true | true | true | true | 1,426 |
0 | DISCUSSION | 1 | 29 | [
"b29",
"b22",
"b23",
"b31",
"b32",
"b33",
"b34",
"b35",
"b35",
"b21",
"b24"
] | 16,893,956 | pmid-3025851|pmid-3035543|pmid-8389467|pmid-8380645|pmid-2846276|pmid-8090734|pmid-16061814|pmid-16738139|pmid-14504622|pmid-8557041|pmid-16285920|pmid-10652347|pmid-2539565|pmid-9843509|pmid-9658141|pmid-9933649|pmid-10535735|pmid-10892646|pmid-9302992|pmid-15454080|pmid-15289463|pmid-15289463|pmid-9149137|pmid-113045... | In some multimeric ATPase complexes the finger from one subunit extends into another to interact with the ATP tri-phosphate during hydrolysis. | [
"29",
"22",
"23",
"31",
"32",
"33",
"34",
"35",
"35",
"21",
"24"
] | 142 | 8,934 | 0 | false | In some multimeric ATPase complexes the finger from one subunit extends into another to interact with the ATP tri-phosphate during hydrolysis. | [] | In some multimeric ATPase complexes the finger from one subunit extends into another to interact with the ATP tri-phosphate during hydrolysis. | true | true | true | true | true | 1,426 |
0 | DISCUSSION | 1 | 34 | [
"b29",
"b22",
"b23",
"b31",
"b32",
"b33",
"b34",
"b35",
"b35",
"b21",
"b24"
] | 16,893,956 | pmid-3025851|pmid-3035543|pmid-8389467|pmid-8380645|pmid-2846276|pmid-8090734|pmid-16061814|pmid-16738139|pmid-14504622|pmid-8557041|pmid-16285920|pmid-10652347|pmid-2539565|pmid-9843509|pmid-9658141|pmid-9933649|pmid-10535735|pmid-10892646|pmid-9302992|pmid-15454080|pmid-15289463|pmid-15289463|pmid-9149137|pmid-113045... | T-antigen has an unusual finger motif in that a lysine as well as two arginines contact the phosphate directly or indirectly through a water molecule (34). | [
"29",
"22",
"23",
"31",
"32",
"33",
"34",
"35",
"35",
"21",
"24"
] | 155 | 8,935 | 1 | false | T-antigen has an unusual finger motif in that a lysine as well as two arginines contact the phosphate directly or indirectly through a water molecule. | [
"34"
] | T-antigen has an unusual finger motif in that a lysine as well as two arginines contact the phosphate directly or indirectly through a water molecule. | true | true | true | true | true | 1,426 |
0 | DISCUSSION | 1 | 35 | [
"b29",
"b22",
"b23",
"b31",
"b32",
"b33",
"b34",
"b35",
"b35",
"b21",
"b24"
] | 16,893,956 | pmid-3025851|pmid-3035543|pmid-8389467|pmid-8380645|pmid-2846276|pmid-8090734|pmid-16061814|pmid-16738139|pmid-14504622|pmid-8557041|pmid-16285920|pmid-10652347|pmid-2539565|pmid-9843509|pmid-9658141|pmid-9933649|pmid-10535735|pmid-10892646|pmid-9302992|pmid-15454080|pmid-15289463|pmid-15289463|pmid-9149137|pmid-113045... | A conserved arginine in HPV 18 E1 is required for robust ATPase activity and is possibly an arginine finger residue (35). | [
"29",
"22",
"23",
"31",
"32",
"33",
"34",
"35",
"35",
"21",
"24"
] | 121 | 8,936 | 1 | false | A conserved arginine in HPV 18 E1 is required for robust ATPase activity and is possibly an arginine finger residue. | [
"35"
] | A conserved arginine in HPV 18 E1 is required for robust ATPase activity and is possibly an arginine finger residue. | true | true | true | true | true | 1,426 |
0 | DISCUSSION | 1 | 29 | [
"b29",
"b22",
"b23",
"b31",
"b32",
"b33",
"b34",
"b35",
"b35",
"b21",
"b24"
] | 16,893,956 | pmid-3025851|pmid-3035543|pmid-8389467|pmid-8380645|pmid-2846276|pmid-8090734|pmid-16061814|pmid-16738139|pmid-14504622|pmid-8557041|pmid-16285920|pmid-10652347|pmid-2539565|pmid-9843509|pmid-9658141|pmid-9933649|pmid-10535735|pmid-10892646|pmid-9302992|pmid-15454080|pmid-15289463|pmid-15289463|pmid-9149137|pmid-113045... | The cooperative ATPase activity we observe therefore supports the notion that the papillomavirus helicase is an arginine finger ATPase. | [
"29",
"22",
"23",
"31",
"32",
"33",
"34",
"35",
"35",
"21",
"24"
] | 135 | 8,937 | 0 | false | The cooperative ATPase activity we observe therefore supports the notion that the papillomavirus helicase is an arginine finger ATPase. | [] | The cooperative ATPase activity we observe therefore supports the notion that the papillomavirus helicase is an arginine finger ATPase. | true | true | true | true | true | 1,426 |
0 | DISCUSSION | 1 | 35 | [
"b29",
"b22",
"b23",
"b31",
"b32",
"b33",
"b34",
"b35",
"b35",
"b21",
"b24"
] | 16,893,956 | pmid-3025851|pmid-3035543|pmid-8389467|pmid-8380645|pmid-2846276|pmid-8090734|pmid-16061814|pmid-16738139|pmid-14504622|pmid-8557041|pmid-16285920|pmid-10652347|pmid-2539565|pmid-9843509|pmid-9658141|pmid-9933649|pmid-10535735|pmid-10892646|pmid-9302992|pmid-15454080|pmid-15289463|pmid-15289463|pmid-9149137|pmid-113045... | Furthermore, since E1–E2 interactions are conserved between BPV and HPV, the ATP-driven oligomerization of BPV E1HD we describe could serve as a molecular mechanism for the displacement of E2 from E1 during initiator complex assembly, as in HPV (35). | [
"29",
"22",
"23",
"31",
"32",
"33",
"34",
"35",
"35",
"21",
"24"
] | 250 | 8,938 | 1 | false | Furthermore, since E1–E2 interactions are conserved between BPV and HPV, the ATP-driven oligomerization of BPV E1HD we describe could serve as a molecular mechanism for the displacement of E2 from E1 during initiator complex assembly, as in HPV. | [
"35"
] | Furthermore, since E1–E2 interactions are conserved between BPV and HPV, the ATP-driven oligomerization of BPV E1HD we describe could serve as a molecular mechanism for the displacement of E2 from E1 during initiator complex assembly, as in HPV. | true | true | true | true | true | 1,426 |
0 | DISCUSSION | 1 | 21 | [
"b29",
"b22",
"b23",
"b31",
"b32",
"b33",
"b34",
"b35",
"b35",
"b21",
"b24"
] | 16,893,956 | pmid-3025851|pmid-3035543|pmid-8389467|pmid-8380645|pmid-2846276|pmid-8090734|pmid-16061814|pmid-16738139|pmid-14504622|pmid-8557041|pmid-16285920|pmid-10652347|pmid-2539565|pmid-9843509|pmid-9658141|pmid-9933649|pmid-10535735|pmid-10892646|pmid-9302992|pmid-15454080|pmid-15289463|pmid-15289463|pmid-9149137|pmid-113045... | It is also noteworthy that SV40 T-antigen hexamerizes with ATP, ADP and non-hydrolysable ATP analogues (21), and that HPV 11 E1 apparently forms stable hexamers without cofactors or DNA (24). | [
"29",
"22",
"23",
"31",
"32",
"33",
"34",
"35",
"35",
"21",
"24"
] | 191 | 8,939 | 1 | false | It is also noteworthy that SV40 T-antigen hexamerizes with ATP, ADP and non-hydrolysable ATP analogues, and that HPV 11 E1 apparently forms stable hexamers without cofactors or DNA. | [
"21",
"24"
] | It is also noteworthy that SV40 T-antigen hexamerizes with ATP, ADP and non-hydrolysable ATP analogues, and that HPV 11 E1 apparently forms stable hexamers without cofactors or DNA. | true | true | true | true | true | 1,426 |
0 | DISCUSSION | 1 | 29 | [
"b29",
"b22",
"b23",
"b31",
"b32",
"b33",
"b34",
"b35",
"b35",
"b21",
"b24"
] | 16,893,956 | pmid-3025851|pmid-3035543|pmid-8389467|pmid-8380645|pmid-2846276|pmid-8090734|pmid-16061814|pmid-16738139|pmid-14504622|pmid-8557041|pmid-16285920|pmid-10652347|pmid-2539565|pmid-9843509|pmid-9658141|pmid-9933649|pmid-10535735|pmid-10892646|pmid-9302992|pmid-15454080|pmid-15289463|pmid-15289463|pmid-9149137|pmid-113045... | Despite the sequence conservation and predicted structural similarity between T-antigen and E1, subtle differences may exist in the ATP hydrolysis cycle of these two viral helicases. | [
"29",
"22",
"23",
"31",
"32",
"33",
"34",
"35",
"35",
"21",
"24"
] | 182 | 8,940 | 0 | false | Despite the sequence conservation and predicted structural similarity between T-antigen and E1, subtle differences may exist in the ATP hydrolysis cycle of these two viral helicases. | [] | Despite the sequence conservation and predicted structural similarity between T-antigen and E1, subtle differences may exist in the ATP hydrolysis cycle of these two viral helicases. | true | true | true | true | true | 1,426 |
0 | DISCUSSION | 1 | 29 | [
"b29",
"b22",
"b23",
"b31",
"b32",
"b33",
"b34",
"b35",
"b35",
"b21",
"b24"
] | 16,893,956 | pmid-3025851|pmid-3035543|pmid-8389467|pmid-8380645|pmid-2846276|pmid-8090734|pmid-16061814|pmid-16738139|pmid-14504622|pmid-8557041|pmid-16285920|pmid-10652347|pmid-2539565|pmid-9843509|pmid-9658141|pmid-9933649|pmid-10535735|pmid-10892646|pmid-9302992|pmid-15454080|pmid-15289463|pmid-15289463|pmid-9149137|pmid-113045... | Within the papillomaviruses E1 proteins there may also be differences in the enzyme mechanism. | [
"29",
"22",
"23",
"31",
"32",
"33",
"34",
"35",
"35",
"21",
"24"
] | 94 | 8,941 | 0 | false | Within the papillomaviruses E1 proteins there may also be differences in the enzyme mechanism. | [] | Within the papillomaviruses E1 proteins there may also be differences in the enzyme mechanism. | true | true | true | true | true | 1,426 |
1 | DISCUSSION | 1 | 36 | [
"b36",
"b36",
"b38",
"b15",
"b18",
"b20"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | E1HD binds ssDNA as a hexamer with only one molecule of an 18 base oligonucleotide (T18) per complex. | [
"36",
"36",
"38",
"15",
"18",
"20"
] | 101 | 8,942 | 0 | false | E1HD binds ssDNA as a hexamer with only one molecule of an 18 base oligonucleotide per complex. | [
"T18"
] | E1HD binds ssDNA as a hexamer with only one molecule of an 18 base oligonucleotide per complex. | true | true | true | true | true | 1,427 |
1 | DISCUSSION | 1 | 36 | [
"b36",
"b36",
"b38",
"b15",
"b18",
"b20"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | Thirty-three bases of ssDNA were protected from nuclease digestion by the helicase and only small differences in the binding affinity of poly(dT) oligonucleotides from 16 to 30 bases were observed. | [
"36",
"36",
"38",
"15",
"18",
"20"
] | 197 | 8,943 | 0 | false | Thirty-three bases of ssDNA were protected from nuclease digestion by the helicase and only small differences in the binding affinity of poly(dT) oligonucleotides from 16 to 30 bases were observed. | [] | Thirty-three bases of ssDNA were protected from nuclease digestion by the helicase and only small differences in the binding affinity of poly(dT) oligonucleotides from 16 to 30 bases were observed. | true | true | true | true | true | 1,427 |
1 | DISCUSSION | 1 | 36 | [
"b36",
"b36",
"b38",
"b15",
"b18",
"b20"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | Formation of the hexameric complex was significantly impaired for oligonucleotides of ≤14 bp. | [
"36",
"36",
"38",
"15",
"18",
"20"
] | 93 | 8,944 | 0 | false | Formation of the hexameric complex was significantly impaired for oligonucleotides of ≤14 bp. | [] | Formation of the hexameric complex was significantly impaired for oligonucleotides of ≤14 bp. | true | true | true | true | true | 1,427 |
1 | DISCUSSION | 1 | 36 | [
"b36",
"b36",
"b38",
"b15",
"b18",
"b20"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | The 16 base DNA sequence therefore defines the extent of the ssDNA required for hexamerization, whereas the length of protected DNA indicates passage of DNA through a protein complex larger than the minimal ssDNA-binding site. | [
"36",
"36",
"38",
"15",
"18",
"20"
] | 226 | 8,945 | 0 | false | The 16 base DNA sequence therefore defines the extent of the ssDNA required for hexamerization, whereas the length of protected DNA indicates passage of DNA through a protein complex larger than the minimal ssDNA-binding site. | [] | The 16 base DNA sequence therefore defines the extent of the ssDNA required for hexamerization, whereas the length of protected DNA indicates passage of DNA through a protein complex larger than the minimal ssDNA-binding site. | true | true | true | true | true | 1,427 |
1 | DISCUSSION | 1 | 36 | [
"b36",
"b36",
"b38",
"b15",
"b18",
"b20"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | Very stable hexameric complexes formed with an 18 base oligonucleotide (T18) but these were unstable under electrophoresis conditions compared with hexamers with a T30 oligonucleotide (Figure 2b). | [
"36",
"36",
"38",
"15",
"18",
"20"
] | 196 | 8,946 | 0 | false | Very stable hexameric complexes formed with an 18 base oligonucleotide but these were unstable under electrophoresis conditions compared with hexamers with a T30 oligonucleotide (Figure 2b). | [
"T18"
] | Very stable hexameric complexes formed with an 18 base oligonucleotide but these were unstable under electrophoresis conditions compared with hexamers with a T30 oligonucleotide (Figure 2b). | true | true | true | true | true | 1,427 |
1 | DISCUSSION | 1 | 36 | [
"b36",
"b36",
"b38",
"b15",
"b18",
"b20"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | Together with the results of the protection assay, this suggests that stabilizing contacts with nucleic acid may also occur outside an essential DNA-binding site. | [
"36",
"36",
"38",
"15",
"18",
"20"
] | 162 | 8,947 | 0 | false | Together with the results of the protection assay, this suggests that stabilizing contacts with nucleic acid may also occur outside an essential DNA-binding site. | [] | Together with the results of the protection assay, this suggests that stabilizing contacts with nucleic acid may also occur outside an essential DNA-binding site. | true | true | true | true | true | 1,427 |
1 | DISCUSSION | 1 | 36 | [
"b36",
"b36",
"b38",
"b15",
"b18",
"b20"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | These results are similar to those of other well-studied hexameric helicases such, as T7 gp4, that protect 25–30 bases of ssDNA (36). | [
"36",
"36",
"38",
"15",
"18",
"20"
] | 133 | 8,948 | 1 | false | These results are similar to those of other well-studied hexameric helicases such, as T7 gp4, that protect 25–30 bases of ssDNA. | [
"36"
] | These results are similar to those of other well-studied hexameric helicases such, as T7 gp4, that protect 25–30 bases of ssDNA. | true | true | true | true | true | 1,427 |
1 | DISCUSSION | 1 | 36 | [
"b36",
"b36",
"b38",
"b15",
"b18",
"b20"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | T7 gp4 and DnaB bind short oligonucleotides (10–30 bases) in the presence of non-hydrolysable ATP analogues with Kds of 10 and 60 nM, respectively (36–38). | [
"36",
"36",
"38",
"15",
"18",
"20"
] | 155 | 8,949 | 0 | false | T7 gp4 and DnaB bind short oligonucleotides (10–30 bases) in the presence of non-hydrolysable ATP analogues with Kds of 10 and 60 nM, respectively. | [
"36–38"
] | T7 gp4 and DnaB bind short oligonucleotides in the presence of non-hydrolysable ATP analogues with Kds of 10 and 60 nM, respectively. | true | true | true | true | true | 1,427 |
1 | DISCUSSION | 1 | 36 | [
"b36",
"b36",
"b38",
"b15",
"b18",
"b20"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | Both these helicases also bind a second DNA strand with a weaker Kd, ∼40 µM in the case of DnaB. | [
"36",
"36",
"38",
"15",
"18",
"20"
] | 96 | 8,950 | 0 | false | Both these helicases also bind a second DNA strand with a weaker Kd, ∼40 µM in the case of DnaB. | [] | Both these helicases also bind a second DNA strand with a weaker Kd, ∼40 µM in the case of DnaB. | true | true | true | true | true | 1,427 |
1 | DISCUSSION | 1 | 36 | [
"b36",
"b36",
"b38",
"b15",
"b18",
"b20"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | The binding constants (Kd) that we have obtained for E1, with or without ATP, are significantly higher, between those of the primary and secondary binding sites of DnaB. | [
"36",
"36",
"38",
"15",
"18",
"20"
] | 169 | 8,951 | 0 | false | The binding constants (Kd) that we have obtained for E1, with or without ATP, are significantly higher, between those of the primary and secondary binding sites of DnaB. | [] | The binding constants (Kd) that we have obtained for E1, with or without ATP, are significantly higher, between those of the primary and secondary binding sites of DnaB. | true | true | true | true | true | 1,427 |
1 | DISCUSSION | 1 | 36 | [
"b36",
"b36",
"b38",
"b15",
"b18",
"b20"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | However, the mechanism of helicase loading on DNA is different for these enzymes. | [
"36",
"36",
"38",
"15",
"18",
"20"
] | 81 | 8,952 | 0 | false | However, the mechanism of helicase loading on DNA is different for these enzymes. | [] | However, the mechanism of helicase loading on DNA is different for these enzymes. | true | true | true | true | true | 1,427 |
1 | DISCUSSION | 1 | 36 | [
"b36",
"b36",
"b38",
"b15",
"b18",
"b20"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | E1 and T-antigen bind and assemble on DNA via the sequence-specific OBD, while specific proteins load DnaB and T7 gp4 on to ssDNA. | [
"36",
"36",
"38",
"15",
"18",
"20"
] | 130 | 8,953 | 0 | false | E1 and T-antigen bind and assemble on DNA via the sequence-specific OBD, while specific proteins load DnaB and T7 gp4 on to ssDNA. | [] | E1 and T-antigen bind and assemble on DNA via the sequence-specific OBD, while specific proteins load DnaB and T7 gp4 on to ssDNA. | true | true | true | true | true | 1,427 |
1 | DISCUSSION | 1 | 36 | [
"b36",
"b36",
"b38",
"b15",
"b18",
"b20"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | The E1HD binding to dsDNA that we observe is complex, with no clear indication of the efficient and stable hexamerization seen with ssDNA. | [
"36",
"36",
"38",
"15",
"18",
"20"
] | 138 | 8,954 | 0 | false | The E1HD binding to dsDNA that we observe is complex, with no clear indication of the efficient and stable hexamerization seen with ssDNA. | [] | The E1HD binding to dsDNA that we observe is complex, with no clear indication of the efficient and stable hexamerization seen with ssDNA. | true | true | true | true | true | 1,427 |
1 | DISCUSSION | 1 | 36 | [
"b36",
"b36",
"b38",
"b15",
"b18",
"b20"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | Although T-antigen and E1 encircle their respective ori dsDNAs as hexamers, this is performed in conjunction with the OBD. | [
"36",
"36",
"38",
"15",
"18",
"20"
] | 122 | 8,955 | 0 | false | Although T-antigen and E1 encircle their respective ori dsDNAs as hexamers, this is performed in conjunction with the OBD. | [] | Although T-antigen and E1 encircle their respective ori dsDNAs as hexamers, this is performed in conjunction with the OBD. | true | true | true | true | true | 1,427 |
1 | DISCUSSION | 1 | 36 | [
"b36",
"b36",
"b38",
"b15",
"b18",
"b20"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | T7 gp4, DnaB and T-antigen both exclude one ssDNA strand during helicase unwinding (15,18,20), and E1 is likely to function similarly. | [
"36",
"36",
"38",
"15",
"18",
"20"
] | 134 | 8,956 | 0 | false | T7 gp4, DnaB and T-antigen both exclude one ssDNA strand during helicase unwinding, and E1 is likely to function similarly. | [
"15,18,20"
] | T7 gp4, DnaB and T-antigen both exclude one ssDNA strand during helicase unwinding, and E1 is likely to function similarly. | true | true | true | true | true | 1,427 |
1 | DISCUSSION | 1 | 36 | [
"b36",
"b36",
"b38",
"b15",
"b18",
"b20"
] | 16,893,956 | pmid-7731998|pmid-12034814|pmid-7731998|pmid-1319087|pmid-9765408|pmid-9254631|pmid-9149137|pmid-9658141|pmid-9933649|pmid-11304544|pmid-8241139|pmid-8241139|pmid-8626772|pmid-9369480|pmid-1319087|pmid-9254631 | Together with the inability of E1HD to unwind DNA of pure duplex character, our dsDNA-binding data suggest that E1 is unlikely to translocate on dsDNA as a base pair separation machine. | [
"36",
"36",
"38",
"15",
"18",
"20"
] | 185 | 8,957 | 0 | false | Together with the inability of E1HD to unwind DNA of pure duplex character, our dsDNA-binding data suggest that E1 is unlikely to translocate on dsDNA as a base pair separation machine. | [] | Together with the inability of E1HD to unwind DNA of pure duplex character, our dsDNA-binding data suggest that E1 is unlikely to translocate on dsDNA as a base pair separation machine. | true | true | true | true | true | 1,427 |
2 | DISCUSSION | 1 | 36 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | E1HD forms an exceptionally stable complex with ssDNA oligonucleotides without cofactor, with ADP or with AMP–PNP. | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 114 | 8,958 | 0 | false | E1HD forms an exceptionally stable complex with ssDNA oligonucleotides without cofactor, with ADP or with AMP–PNP. | [] | E1HD forms an exceptionally stable complex with ssDNA oligonucleotides without cofactor, with ADP or with AMP–PNP. | true | true | true | true | true | 1,428 |
2 | DISCUSSION | 1 | 36 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | However, upon ATP addition the affinity for ssDNA is significantly reduced. | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 75 | 8,959 | 0 | false | However, upon ATP addition the affinity for ssDNA is significantly reduced. | [] | However, upon ATP addition the affinity for ssDNA is significantly reduced. | true | true | true | true | true | 1,428 |
2 | DISCUSSION | 1 | 36 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | The ATP-dependent kinetics of (E1HD)6–ssDNA complex dissociation we observed (Figure 6) showed an immediate phase of rapid dissociation followed by a slower rate of decay. | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 171 | 8,960 | 0 | false | The ATP-dependent kinetics of (E1HD)6–ssDNA complex dissociation we observed (Figure 6) showed an immediate phase of rapid dissociation followed by a slower rate of decay. | [] | The ATP-dependent kinetics of (E1HD)6–ssDNA complex dissociation we observed showed an immediate phase of rapid dissociation followed by a slower rate of decay. | true | true | true | true | true | 1,428 |
2 | DISCUSSION | 1 | 36 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | These observations are notable since ATP stimulates formation of the hexameric protein–DNA complex. | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 99 | 8,961 | 0 | false | These observations are notable since ATP stimulates formation of the hexameric protein–DNA complex. | [] | These observations are notable since ATP stimulates formation of the hexameric protein–DNA complex. | true | true | true | true | true | 1,428 |
2 | DISCUSSION | 1 | 36 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | With NTP compared with NDP or no cofactor T7 gp4 | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 48 | 8,962 | 0 | false | With NTP compared with NDP or no cofactor T7 gp4 | [] | With NTP compared with NDP or no cofactor T7 gp4 | true | true | false | true | false | 1,428 |
2 | DISCUSSION | 1 | 39 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | and DnaB also bind ssDNA more tightly, by orders of magnitude (36,38), and in the case of DnaB, nucleotide is not required for hexamerization (39). | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 147 | 8,963 | 1 | false | and DnaB also bind ssDNA more tightly, by orders of magnitude, and in the case of DnaB, nucleotide is not required for hexamerization. | [
"36,38",
"39"
] | and DnaB also bind ssDNA more tightly, by orders of magnitude, and in the case of DnaB, nucleotide is not required for hexamerization. | false | true | true | true | false | 1,428 |
2 | DISCUSSION | 1 | 36 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | The immediate questions that arise are how is ssDNA affinity modulated and can these results be rationalized in terms of current models for DNA unwinding? | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 154 | 8,964 | 0 | false | The immediate questions that arise are how is ssDNA affinity modulated and can these results be rationalized in terms of current models for DNA unwinding? | [] | The immediate questions that arise are how is ssDNA affinity modulated and can these results be rationalized in terms of current models for DNA unwinding? | true | true | true | true | true | 1,428 |
2 | DISCUSSION | 1 | 36 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | ssDNA complex dissociation could occur if the hexameric ring were to open or disassemble. | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 89 | 8,965 | 0 | false | ssDNA complex dissociation could occur if the hexameric ring were to open or disassemble. | [] | ssDNA complex dissociation could occur if the hexameric ring were to open or disassemble. | false | true | true | true | false | 1,428 |
2 | DISCUSSION | 1 | 36 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | We consider these possibilities unlikely since we show that ATP promotes protein complex assembly. | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 98 | 8,966 | 0 | false | We consider these possibilities unlikely since we show that ATP promotes protein complex assembly. | [] | We consider these possibilities unlikely since we show that ATP promotes protein complex assembly. | true | true | true | true | true | 1,428 |
2 | DISCUSSION | 1 | 36 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | Furthermore, the mechanism of E1 helicase loading occurs by stepwise binding to ori rather than loading of a preformed hexamer requiring a ring-opening step. | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 157 | 8,967 | 0 | false | Furthermore, the mechanism of E1 helicase loading occurs by stepwise binding to ori rather than loading of a preformed hexamer requiring a ring-opening step. | [] | Furthermore, the mechanism of E1 helicase loading occurs by stepwise binding to ori rather than loading of a preformed hexamer requiring a ring-opening step. | true | true | true | true | true | 1,428 |
2 | DISCUSSION | 1 | 36 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | Our favoured interpretation is that we have observed the ATP-dependent modulation of ssDNA-binding site affinity that is a component of the helicase transloction mechanism. | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 172 | 8,968 | 0 | false | Our favoured interpretation is that we have observed the ATP-dependent modulation of ssDNA-binding site affinity that is a component of the helicase transloction mechanism. | [] | Our favoured interpretation is that we have observed the ATP-dependent modulation of ssDNA-binding site affinity that is a component of the helicase transloction mechanism. | true | true | true | true | true | 1,428 |
2 | DISCUSSION | 1 | 34 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | The recent structures of T-antigen hexamers with and without bound nucleotide have shown large longitudinal ATP-dependent movements of a β-hairpin structure (the pre-sensor 1 β hairpin, PS1βH) within the central channel of the complex (34). | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 240 | 8,969 | 1 | false | The recent structures of T-antigen hexamers with and without bound nucleotide have shown large longitudinal ATP-dependent movements of a β-hairpin structure (the pre-sensor 1 β hairpin, PS1βH) within the central channel of the complex. | [
"34"
] | The recent structures of T-antigen hexamers with and without bound nucleotide have shown large longitudinal ATP-dependent movements of a β-hairpin structure (the pre-sensor 1 β hairpin, PS1βH) within the central channel of the complex. | true | true | true | true | true | 1,428 |
2 | DISCUSSION | 1 | 36 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | This structure is critical for ssDNA binding in both T-antigen and E1 hexamers (7,8), and along with an aromatic loop constitutes the primary ssDNA-binding site. | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 161 | 8,970 | 0 | false | This structure is critical for ssDNA binding in both T-antigen and E1 hexamers, and along with an aromatic loop constitutes the primary ssDNA-binding site. | [
"7,8"
] | This structure is critical for ssDNA binding in both T-antigen and E1 hexamers, and along with an aromatic loop constitutes the primary ssDNA-binding site. | true | true | true | true | true | 1,428 |
2 | DISCUSSION | 1 | 34 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | PS1βH movement is accompanied by changes in the dimensions of the hexameric channel, rotation of the two tiers of the hexamer relative to each other, and a large increase in the buried surface area between protomers with ATP (34). | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 230 | 8,971 | 1 | false | PS1βH movement is accompanied by changes in the dimensions of the hexameric channel, rotation of the two tiers of the hexamer relative to each other, and a large increase in the buried surface area between protomers with ATP. | [
"34"
] | PS1βH movement is accompanied by changes in the dimensions of the hexameric channel, rotation of the two tiers of the hexamer relative to each other, and a large increase in the buried surface area between protomers with ATP. | true | true | true | true | true | 1,428 |
2 | DISCUSSION | 1 | 36 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | These data also suggested that the ATP hydrolysis cycle was all-or-none, with all protomers transducing the energy of ATP hydrolysis in a concerted step. | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 153 | 8,972 | 0 | false | These data also suggested that the ATP hydrolysis cycle was all-or-none, with all protomers transducing the energy of ATP hydrolysis in a concerted step. | [] | These data also suggested that the ATP hydrolysis cycle was all-or-none, with all protomers transducing the energy of ATP hydrolysis in a concerted step. | true | true | true | true | true | 1,428 |
2 | DISCUSSION | 1 | 36 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | The initial rapid dissociation of ssDNA, we observed, upon ATP addition may represent PS1βH movement, ssDNA translocation, and its consequential release from the binding site at the end of the hydrolysis cycle. | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 210 | 8,973 | 0 | false | The initial rapid dissociation of ssDNA, we observed, upon ATP addition may represent PS1βH movement, ssDNA translocation, and its consequential release from the binding site at the end of the hydrolysis cycle. | [] | The initial rapid dissociation of ssDNA, we observed, upon ATP addition may represent PS1βH movement, ssDNA translocation, and its consequential release from the binding site at the end of the hydrolysis cycle. | true | true | true | true | true | 1,428 |
2 | DISCUSSION | 1 | 36 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | Changes in the DNA-binding site from high to low affinity must occur or the helicase would not move. | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 100 | 8,974 | 0 | false | Changes in the DNA-binding site from high to low affinity must occur or the helicase would not move. | [] | Changes in the DNA-binding site from high to low affinity must occur or the helicase would not move. | true | true | true | true | true | 1,428 |
2 | DISCUSSION | 1 | 36 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | The subsequent decrease in the ssDNA complex dissociation rate is not consistent with the rapid turnover of ATP by E1HD that we measured, albeit that ATPase activity is reduced in the prersence of ssDNA (Figure 7). | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 214 | 8,975 | 0 | false | The subsequent decrease in the ssDNA complex dissociation rate is not consistent with the rapid turnover of ATP by E1HD that we measured, albeit that ATPase activity is reduced in the prersence of ssDNA. | [
"Figure 7"
] | The subsequent decrease in the ssDNA complex dissociation rate is not consistent with the rapid turnover of ATP by E1HD that we measured, albeit that ATPase activity is reduced in the prersence of ssDNA. | true | true | true | true | true | 1,428 |
2 | DISCUSSION | 1 | 36 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | However, this may be the result of accumulating ADP, or a slow rate of ADP release from the helicase–ssDNA complex, suggesting that translocase activity itself cannot be effectively reconstituted on ssDNA alone. | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 211 | 8,976 | 0 | false | However, this may be the result of accumulating ADP, or a slow rate of ADP release from the helicase–ssDNA complex, suggesting that translocase activity itself cannot be effectively reconstituted on ssDNA alone. | [] | However, this may be the result of accumulating ADP, or a slow rate of ADP release from the helicase–ssDNA complex, suggesting that translocase activity itself cannot be effectively reconstituted on ssDNA alone. | true | true | true | true | true | 1,428 |
2 | DISCUSSION | 1 | 36 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | With T-antigen, the excluded ssDNA and a small region of dsDNA ahead of a replication fork also interact with the helicase, and all ATP modulated interactions may require coupling for efficient use of ATP and unwinding/translocation. | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 233 | 8,977 | 0 | false | With T-antigen, the excluded ssDNA and a small region of dsDNA ahead of a replication fork also interact with the helicase, and all ATP modulated interactions may require coupling for efficient use of ATP and unwinding/translocation. | [] | With T-antigen, the excluded ssDNA and a small region of dsDNA ahead of a replication fork also interact with the helicase, and all ATP modulated interactions may require coupling for efficient use of ATP and unwinding/translocation. | true | true | true | true | true | 1,428 |
2 | DISCUSSION | 1 | 19 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | With T-antigen, the excluded ssDNA has been shown to load on the outside of the helicase at high ATP concentrations (19). | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 121 | 8,978 | 1 | false | With T-antigen, the excluded ssDNA has been shown to load on the outside of the helicase at high ATP concentrations. | [
"19"
] | With T-antigen, the excluded ssDNA has been shown to load on the outside of the helicase at high ATP concentrations. | true | true | true | true | true | 1,428 |
2 | DISCUSSION | 1 | 36 | [
"b36",
"b38",
"b39",
"b34",
"b7",
"b8",
"b34",
"b19"
] | 16,893,956 | pmid-10966472|pmid-8241139|pmid-8626772|pmid-7989299|pmid-15454080|pmid-16061814|pmid-16738139|pmid-15454080|pmid-9765408 | Our observation that a small mobility difference in gel-shifts is seen for E1HD complexes loaded onto large ssDNA probes with or without ATP (Figure 5a), may indicate that ssDNA can also interact with the exterior of the E1 hexamer in a cofactor dependent manner. | [
"36",
"38",
"39",
"34",
"7",
"8",
"34",
"19"
] | 263 | 8,979 | 0 | false | Our observation that a small mobility difference in gel-shifts is seen for E1HD complexes loaded onto large ssDNA probes with or without ATP (Figure 5a), may indicate that ssDNA can also interact with the exterior of the E1 hexamer in a cofactor dependent manner. | [] | Our observation that a small mobility difference in gel-shifts is seen for E1HD complexes loaded onto large ssDNA probes with or without ATP (Figure 5a), may indicate that ssDNA can also interact with the exterior of the E1 hexamer in a cofactor dependent manner. | true | true | true | true | true | 1,428 |
3 | DISCUSSION | 0 | null | null | 16,893,956 | null | In summary, our data suggest that during the ATP-hydrolysis cycle an internal ssDNA-binding site in an E1 hexamer oscillates from a high to a low-affinity state while protein–protein interactions change from a low- to high-affinity state. | null | 238 | 8,980 | 0 | false | null | null | In summary, our data suggest that during the ATP-hydrolysis cycle an internal ssDNA-binding site in an E1 hexamer oscillates from a high to a low-affinity state while protein–protein interactions change from a low- to high-affinity state. | true | true | true | true | true | 1,429 |
3 | DISCUSSION | 0 | null | null | 16,893,956 | null | This mechanism would ensure that the complex remains tethered to DNA while processive movement along DNA proceeds. | null | 114 | 8,981 | 0 | false | null | null | This mechanism would ensure that the complex remains tethered to DNA while processive movement along DNA proceeds. | true | true | true | true | true | 1,429 |
3 | DISCUSSION | 0 | null | null | 16,893,956 | null | A complete evaluation of this proposal awaits the determination of the crystal structures of E1 or T-antigen with DNA. | null | 118 | 8,982 | 0 | false | null | null | A complete evaluation of this proposal awaits the determination of the crystal structures of E1 or T-antigen with DNA. | true | true | true | true | true | 1,429 |
3 | DISCUSSION | 0 | null | null | 16,893,956 | null | These data would also provide an answer to the intriguing question of how the path of DNA through the complex impacts on the assembly of stable hexameric structures. | null | 165 | 8,983 | 0 | false | null | null | These data would also provide an answer to the intriguing question of how the path of DNA through the complex impacts on the assembly of stable hexameric structures. | true | true | true | true | true | 1,429 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2"
] | 17,483,517 | pmid-16600018|NA | The identification of transcription factor binding sites (TFBSs) in the promoters of genes is a critical step in the delineation of the genetic regulatory network of an organism. | [
"1",
"2"
] | 178 | 8,984 | 0 | false | The identification of transcription factor binding sites (TFBSs) in the promoters of genes is a critical step in the delineation of the genetic regulatory network of an organism. | [] | The identification of transcription factor binding sites (TFBSs) in the promoters of genes is a critical step in the delineation of the genetic regulatory network of an organism. | true | true | true | true | true | 1,430 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2"
] | 17,483,517 | pmid-16600018|NA | A number of motif discovery algorithms have been developed over the past decade and a half, for the detection of cis-regulatory sites (1). | [
"1",
"2"
] | 138 | 8,985 | 1 | false | A number of motif discovery algorithms have been developed over the past decade and a half, for the detection of cis-regulatory sites. | [
"1"
] | A number of motif discovery algorithms have been developed over the past decade and a half, for the detection of cis-regulatory sites. | true | true | true | true | true | 1,430 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2"
] | 17,483,517 | pmid-16600018|NA | Most of these algorithms depend, in one way or another, on finding an optimal alignment of motif sites. | [
"1",
"2"
] | 103 | 8,986 | 0 | false | Most of these algorithms depend, in one way or another, on finding an optimal alignment of motif sites. | [] | Most of these algorithms depend, in one way or another, on finding an optimal alignment of motif sites. | true | true | true | true | true | 1,430 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2"
] | 17,483,517 | pmid-16600018|NA | In this article, we describe the web server for an improved motif discovery algorithm, the Gibbs Centroid Sampler, which finds a centroid alignment. | [
"1",
"2"
] | 148 | 8,987 | 0 | false | In this article, we describe the web server for an improved motif discovery algorithm, the Gibbs Centroid Sampler, which finds a centroid alignment. | [] | In this article, we describe the web server for an improved motif discovery algorithm, the Gibbs Centroid Sampler, which finds a centroid alignment. | true | true | true | true | true | 1,430 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2"
] | 17,483,517 | pmid-16600018|NA | The centroid alignment is the alignment that has the minimum total distance to the set of samples chosen from the a posteriori probability distribution of TFBS alignments. | [
"1",
"2"
] | 171 | 8,988 | 0 | false | The centroid alignment is the alignment that has the minimum total distance to the set of samples chosen from the a posteriori probability distribution of TFBS alignments. | [] | The centroid alignment is the alignment that has the minimum total distance to the set of samples chosen from the a posteriori probability distribution of TFBS alignments. | true | true | true | true | true | 1,430 |
0 | INTRODUCTION | 1 | 1 | [
"B1",
"B2"
] | 17,483,517 | pmid-16600018|NA | By focusing on the region of solution space containing the most posterior probability, rather than on the single solution that is most probable, this approach significantly enhances the predictive power of the algorithm. | [
"1",
"2"
] | 220 | 8,989 | 0 | false | By focusing on the region of solution space containing the most posterior probability, rather than on the single solution that is most probable, this approach significantly enhances the predictive power of the algorithm. | [] | By focusing on the region of solution space containing the most posterior probability, rather than on the single solution that is most probable, this approach significantly enhances the predictive power of the algorithm. | true | true | true | true | true | 1,430 |
0 | INTRODUCTION | 1 | 2 | [
"B1",
"B2"
] | 17,483,517 | pmid-16600018|NA | In computational experiments using simulated proteobacterial and yeast data (2), the centroid sampler showed improved specificity and positive predictive value over algorithms that report an optimal solution. | [
"1",
"2"
] | 208 | 8,990 | 1 | false | In computational experiments using simulated proteobacterial and yeast data, the centroid sampler showed improved specificity and positive predictive value over algorithms that report an optimal solution. | [
"2"
] | In computational experiments using simulated proteobacterial and yeast data, the centroid sampler showed improved specificity and positive predictive value over algorithms that report an optimal solution. | true | true | true | true | true | 1,430 |
1 | INTRODUCTION | 1 | 3 | [
"B3",
"B4 B5 B6 B7 B8",
"B3",
"B9",
"B3"
] | 17,483,517 | pmid-12824370|pmid-16269786|pmid-11160901|pmid-12368244|pmid-15466295|pmid-12933881|pmid-12824370|NA|pmid-12824370 | The Gibbs Centroid Sampler is an improved version of the Gibbs Recursive Sampler (3), which has been used extensively in the identification of TFBSs (4–8), and has been available at our Web site for some time (3,9). | [
"3",
"4–8",
"3",
"9",
"3"
] | 215 | 8,991 | 1 | false | The Gibbs Centroid Sampler is an improved version of the Gibbs Recursive Sampler, which has been used extensively in the identification of TFBSs, and has been available at our Web site for some time. | [
"3",
"4–8",
"3,9"
] | The Gibbs Centroid Sampler is an improved version of the Gibbs Recursive Sampler, which has been used extensively in the identification of TFBSs, and has been available at our Web site for some time. | true | true | true | true | true | 1,431 |
1 | INTRODUCTION | 1 | 3 | [
"B3",
"B4 B5 B6 B7 B8",
"B3",
"B9",
"B3"
] | 17,483,517 | pmid-12824370|pmid-16269786|pmid-11160901|pmid-12368244|pmid-15466295|pmid-12933881|pmid-12824370|NA|pmid-12824370 | The software currently available at the Web site retains all of the features of the previous versions, including searches for multiple motif types, multiple instances (sites) of a motif, palindromic motifs, motifs of varying widths and a heterogeneous background frequency model (see (3) for descriptions of these and ot... | [
"3",
"4–8",
"3",
"9",
"3"
] | 334 | 8,992 | 0 | false | The software currently available at the Web site retains all of the features of the previous versions, including searches for multiple motif types, multiple instances (sites) of a motif, palindromic motifs, motifs of varying widths and a heterogeneous background frequency model for descriptions of these and other featu... | [
"see (3"
] | The software currently available at the Web site retains all of the features of the previous versions, including searches for multiple motif types, multiple instances (sites) of a motif, palindromic motifs, motifs of varying widths and a heterogeneous background frequency model for descriptions of these and other featu... | true | true | true | true | true | 1,431 |
1 | INTRODUCTION | 1 | 3 | [
"B3",
"B4 B5 B6 B7 B8",
"B3",
"B9",
"B3"
] | 17,483,517 | pmid-12824370|pmid-16269786|pmid-11160901|pmid-12368244|pmid-15466295|pmid-12933881|pmid-12824370|NA|pmid-12824370 | The users’ choices of options are entered through a web form, described below, and the output is returned to the user via e-mail. | [
"3",
"4–8",
"3",
"9",
"3"
] | 129 | 8,993 | 0 | false | The users’ choices of options are entered through a web form, described below, and the output is returned to the user via e-mail. | [] | The users’ choices of options are entered through a web form, described below, and the output is returned to the user via e-mail. | true | true | true | true | true | 1,431 |
1 | INTRODUCTION | 1 | 3 | [
"B3",
"B4 B5 B6 B7 B8",
"B3",
"B9",
"B3"
] | 17,483,517 | pmid-12824370|pmid-16269786|pmid-11160901|pmid-12368244|pmid-15466295|pmid-12933881|pmid-12824370|NA|pmid-12824370 | In addition to the new algorithmic features, the Web site has been updated to include extensive tutorials on the use of the Gibbs sampling software for prokaryotic phylogenetic footprinting and for the analysis of prokaryotic co-expression data. | [
"3",
"4–8",
"3",
"9",
"3"
] | 245 | 8,994 | 0 | false | In addition to the new algorithmic features, the Web site has been updated to include extensive tutorials on the use of the Gibbs sampling software for prokaryotic phylogenetic footprinting and for the analysis of prokaryotic co-expression data. | [] | In addition to the new algorithmic features, the Web site has been updated to include extensive tutorials on the use of the Gibbs sampling software for prokaryotic phylogenetic footprinting and for the analysis of prokaryotic co-expression data. | true | true | true | true | true | 1,431 |
2 | INTRODUCTION | 1 | 10 | [
"B10",
"B11",
"B12"
] | 17,483,517 | NA|pmid-2184437|NA | A key feature of most sequence-based Gibbs sampling and expectation maximization algorithms (10,11), is the use of a probabilistic score that is maximized. | [
"10",
"11",
"12"
] | 155 | 8,995 | 0 | false | A key feature of most sequence-based Gibbs sampling and expectation maximization algorithms, is the use of a probabilistic score that is maximized. | [
"10,11"
] | A key feature of most sequence-based Gibbs sampling and expectation maximization algorithms, is the use of a probabilistic score that is maximized. | true | true | true | true | true | 1,432 |
2 | INTRODUCTION | 1 | 10 | [
"B10",
"B11",
"B12"
] | 17,483,517 | NA|pmid-2184437|NA | Typically, the alignment that has the maximum of this score is reported to the user. | [
"10",
"11",
"12"
] | 84 | 8,996 | 0 | false | Typically, the alignment that has the maximum of this score is reported to the user. | [] | Typically, the alignment that has the maximum of this score is reported to the user. | true | true | true | true | true | 1,432 |
2 | INTRODUCTION | 1 | 12 | [
"B10",
"B11",
"B12"
] | 17,483,517 | NA|pmid-2184437|NA | Previous versions of the Gibbs Sampler used the posterior probability of the alignment, called the MAP (maximum a posteriori probability) (12), as a measure of the quality of the alignment, and thus the alignment that produced the highest posterior probability (i.e. | [
"10",
"11",
"12"
] | 266 | 8,997 | 1 | false | Previous versions of the Gibbs Sampler used the posterior probability of the alignment, called the MAP (maximum a posteriori probability), as a measure of the quality of the alignment, and thus the alignment that produced the highest posterior probability (i.e. | [
"12"
] | Previous versions of the Gibbs Sampler used the posterior probability of the alignment, called the MAP (maximum a posteriori probability), as a measure of the quality of the alignment, and thus the alignment that produced the highest posterior probability (i.e. | true | true | true | true | true | 1,432 |
2 | INTRODUCTION | 1 | 10 | [
"B10",
"B11",
"B12"
] | 17,483,517 | NA|pmid-2184437|NA | the MAP alignment) was returned. | [
"10",
"11",
"12"
] | 32 | 8,998 | 0 | false | the MAP alignment) was returned. | [] | the MAP alignment) was returned. | false | true | true | true | false | 1,432 |
2 | INTRODUCTION | 1 | 10 | [
"B10",
"B11",
"B12"
] | 17,483,517 | NA|pmid-2184437|NA | The reported MAP was calculated as the logarithm of the alignment probability minus the logarithm of an empty or background alignment. | [
"10",
"11",
"12"
] | 134 | 8,999 | 0 | false | The reported MAP was calculated as the logarithm of the alignment probability minus the logarithm of an empty or background alignment. | [] | The reported MAP was calculated as the logarithm of the alignment probability minus the logarithm of an empty or background alignment. | true | true | true | true | true | 1,432 |
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