PubMed:2826446 JSONTXT

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":22,"end":31},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":167,"end":176},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":178,"end":187},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":347,"end":356},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":639,"end":648},"obj":"Glycan_Motif"},{"id":"T6","span":{"begin":1041,"end":1050},"obj":"Glycan_Motif"},{"id":"T7","span":{"begin":1209,"end":1218},"obj":"Glycan_Motif"},{"id":"T8","span":{"begin":1267,"end":1276},"obj":"Glycan_Motif"},{"id":"T9","span":{"begin":1410,"end":1419},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00031MO"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00031MO"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00031MO"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00031MO"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00031MO"},{"id":"A6","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00031MO"},{"id":"A7","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00031MO"},{"id":"A8","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00031MO"},{"id":"A9","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00031MO"}],"text":"Simian virus 40 large T antigen DNA helicase. Characterization of the ATPase-dependent DNA unwinding activity and its substrate requirements.\nThe ATPase of SV40 large T antigen (T antigen) which is essential for the replication of SV40 minichromosomes was recently shown to be functionally related to a newly discovered DNA helicase activity. The T antigen helicase unwinds DNA duplices of several kilobase pairs in a reaction depending on the presence of hydrolyzable ribo- or deoxyribonucleoside triphosphates. The in vitro rate of movement through duplex DNA was found to be about 100 base pairs/min at 37 degrees C. For DNA unwinding, T antigen requires a 3'-single strand extension of a partially double-stranded substrate and invades the double strand section processively, in a 3' to 5' direction. The minimum length of the single-stranded tail was determined to be less than 5 nucleotides. Unwinding studies in the presence of the Escherichia coli single strand-specific DNA-binding protein and competition experiments indicate that T antigen helicase binds preferentially at the single-stranded/double-stranded DNA junction. This DNA structure is therefore proposed to serve as an entry site for the T antigen helicase. Previously reported data suggest that T antigen is the replicative helicase of the SV40 minichromosome. The results presented here are consistent with these findings and imply that T antigen migrates actively and processively along the template for the leading strand."}

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":22,"end":31},"obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"T2","span":{"begin":167,"end":176},"obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"T3","span":{"begin":178,"end":187},"obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"T4","span":{"begin":347,"end":356},"obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"T5","span":{"begin":639,"end":648},"obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"T6","span":{"begin":1041,"end":1050},"obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"T7","span":{"begin":1209,"end":1218},"obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"T8","span":{"begin":1267,"end":1276},"obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"T9","span":{"begin":1410,"end":1419},"obj":"http://www.glycoepitope.jp/epitopes/EP0020"}],"text":"Simian virus 40 large T antigen DNA helicase. Characterization of the ATPase-dependent DNA unwinding activity and its substrate requirements.\nThe ATPase of SV40 large T antigen (T antigen) which is essential for the replication of SV40 minichromosomes was recently shown to be functionally related to a newly discovered DNA helicase activity. The T antigen helicase unwinds DNA duplices of several kilobase pairs in a reaction depending on the presence of hydrolyzable ribo- or deoxyribonucleoside triphosphates. The in vitro rate of movement through duplex DNA was found to be about 100 base pairs/min at 37 degrees C. For DNA unwinding, T antigen requires a 3'-single strand extension of a partially double-stranded substrate and invades the double strand section processively, in a 3' to 5' direction. The minimum length of the single-stranded tail was determined to be less than 5 nucleotides. Unwinding studies in the presence of the Escherichia coli single strand-specific DNA-binding protein and competition experiments indicate that T antigen helicase binds preferentially at the single-stranded/double-stranded DNA junction. This DNA structure is therefore proposed to serve as an entry site for the T antigen helicase. Previously reported data suggest that T antigen is the replicative helicase of the SV40 minichromosome. The results presented here are consistent with these findings and imply that T antigen migrates actively and processively along the template for the leading strand."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":45},"obj":"Sentence"},{"id":"T2","span":{"begin":46,"end":141},"obj":"Sentence"},{"id":"T3","span":{"begin":142,"end":342},"obj":"Sentence"},{"id":"T4","span":{"begin":343,"end":512},"obj":"Sentence"},{"id":"T5","span":{"begin":513,"end":619},"obj":"Sentence"},{"id":"T6","span":{"begin":620,"end":804},"obj":"Sentence"},{"id":"T7","span":{"begin":805,"end":897},"obj":"Sentence"},{"id":"T8","span":{"begin":898,"end":1133},"obj":"Sentence"},{"id":"T9","span":{"begin":1134,"end":1228},"obj":"Sentence"},{"id":"T10","span":{"begin":1229,"end":1332},"obj":"Sentence"},{"id":"T11","span":{"begin":1333,"end":1497},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":45},"obj":"Sentence"},{"id":"T2","span":{"begin":46,"end":141},"obj":"Sentence"},{"id":"T3","span":{"begin":142,"end":342},"obj":"Sentence"},{"id":"T4","span":{"begin":343,"end":512},"obj":"Sentence"},{"id":"T5","span":{"begin":513,"end":619},"obj":"Sentence"},{"id":"T6","span":{"begin":620,"end":804},"obj":"Sentence"},{"id":"T7","span":{"begin":805,"end":897},"obj":"Sentence"},{"id":"T8","span":{"begin":898,"end":1133},"obj":"Sentence"},{"id":"T9","span":{"begin":1134,"end":1228},"obj":"Sentence"},{"id":"T10","span":{"begin":1229,"end":1332},"obj":"Sentence"},{"id":"T11","span":{"begin":1333,"end":1497},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Simian virus 40 large T antigen DNA helicase. Characterization of the ATPase-dependent DNA unwinding activity and its substrate requirements.\nThe ATPase of SV40 large T antigen (T antigen) which is essential for the replication of SV40 minichromosomes was recently shown to be functionally related to a newly discovered DNA helicase activity. The T antigen helicase unwinds DNA duplices of several kilobase pairs in a reaction depending on the presence of hydrolyzable ribo- or deoxyribonucleoside triphosphates. The in vitro rate of movement through duplex DNA was found to be about 100 base pairs/min at 37 degrees C. For DNA unwinding, T antigen requires a 3'-single strand extension of a partially double-stranded substrate and invades the double strand section processively, in a 3' to 5' direction. The minimum length of the single-stranded tail was determined to be less than 5 nucleotides. Unwinding studies in the presence of the Escherichia coli single strand-specific DNA-binding protein and competition experiments indicate that T antigen helicase binds preferentially at the single-stranded/double-stranded DNA junction. This DNA structure is therefore proposed to serve as an entry site for the T antigen helicase. Previously reported data suggest that T antigen is the replicative helicase of the SV40 minichromosome. The results presented here are consistent with these findings and imply that T antigen migrates actively and processively along the template for the leading strand."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":22,"end":31},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T2","span":{"begin":167,"end":176},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T3","span":{"begin":178,"end":187},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T4","span":{"begin":347,"end":356},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T5","span":{"begin":639,"end":648},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T6","span":{"begin":1041,"end":1050},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T7","span":{"begin":1209,"end":1218},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T8","span":{"begin":1267,"end":1276},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T9","span":{"begin":1410,"end":1419},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"}],"text":"Simian virus 40 large T antigen DNA helicase. Characterization of the ATPase-dependent DNA unwinding activity and its substrate requirements.\nThe ATPase of SV40 large T antigen (T antigen) which is essential for the replication of SV40 minichromosomes was recently shown to be functionally related to a newly discovered DNA helicase activity. The T antigen helicase unwinds DNA duplices of several kilobase pairs in a reaction depending on the presence of hydrolyzable ribo- or deoxyribonucleoside triphosphates. The in vitro rate of movement through duplex DNA was found to be about 100 base pairs/min at 37 degrees C. For DNA unwinding, T antigen requires a 3'-single strand extension of a partially double-stranded substrate and invades the double strand section processively, in a 3' to 5' direction. The minimum length of the single-stranded tail was determined to be less than 5 nucleotides. Unwinding studies in the presence of the Escherichia coli single strand-specific DNA-binding protein and competition experiments indicate that T antigen helicase binds preferentially at the single-stranded/double-stranded DNA junction. This DNA structure is therefore proposed to serve as an entry site for the T antigen helicase. Previously reported data suggest that T antigen is the replicative helicase of the SV40 minichromosome. The results presented here are consistent with these findings and imply that T antigen migrates actively and processively along the template for the leading strand."}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":378,"end":386},"obj":"HP_0009609"}],"text":"Simian virus 40 large T antigen DNA helicase. Characterization of the ATPase-dependent DNA unwinding activity and its substrate requirements.\nThe ATPase of SV40 large T antigen (T antigen) which is essential for the replication of SV40 minichromosomes was recently shown to be functionally related to a newly discovered DNA helicase activity. The T antigen helicase unwinds DNA duplices of several kilobase pairs in a reaction depending on the presence of hydrolyzable ribo- or deoxyribonucleoside triphosphates. The in vitro rate of movement through duplex DNA was found to be about 100 base pairs/min at 37 degrees C. For DNA unwinding, T antigen requires a 3'-single strand extension of a partially double-stranded substrate and invades the double strand section processively, in a 3' to 5' direction. The minimum length of the single-stranded tail was determined to be less than 5 nucleotides. Unwinding studies in the presence of the Escherichia coli single strand-specific DNA-binding protein and competition experiments indicate that T antigen helicase binds preferentially at the single-stranded/double-stranded DNA junction. This DNA structure is therefore proposed to serve as an entry site for the T antigen helicase. Previously reported data suggest that T antigen is the replicative helicase of the SV40 minichromosome. The results presented here are consistent with these findings and imply that T antigen migrates actively and processively along the template for the leading strand."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":22,"end":31},"obj":"Glycan"},{"id":"T2","span":{"begin":167,"end":176},"obj":"Glycan"},{"id":"T3","span":{"begin":178,"end":187},"obj":"Glycan"},{"id":"T4","span":{"begin":347,"end":356},"obj":"Glycan"},{"id":"T5","span":{"begin":639,"end":648},"obj":"Glycan"},{"id":"T6","span":{"begin":1041,"end":1050},"obj":"Glycan"},{"id":"T7","span":{"begin":1209,"end":1218},"obj":"Glycan"},{"id":"T8","span":{"begin":1267,"end":1276},"obj":"Glycan"},{"id":"T9","span":{"begin":1410,"end":1419},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A10","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A11","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A12","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A13","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A14","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A15","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A16","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A17","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A9","pred":"glycosmos_id","subj":"T9","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A18","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"}],"text":"Simian virus 40 large T antigen DNA helicase. Characterization of the ATPase-dependent DNA unwinding activity and its substrate requirements.\nThe ATPase of SV40 large T antigen (T antigen) which is essential for the replication of SV40 minichromosomes was recently shown to be functionally related to a newly discovered DNA helicase activity. The T antigen helicase unwinds DNA duplices of several kilobase pairs in a reaction depending on the presence of hydrolyzable ribo- or deoxyribonucleoside triphosphates. The in vitro rate of movement through duplex DNA was found to be about 100 base pairs/min at 37 degrees C. For DNA unwinding, T antigen requires a 3'-single strand extension of a partially double-stranded substrate and invades the double strand section processively, in a 3' to 5' direction. The minimum length of the single-stranded tail was determined to be less than 5 nucleotides. Unwinding studies in the presence of the Escherichia coli single strand-specific DNA-binding protein and competition experiments indicate that T antigen helicase binds preferentially at the single-stranded/double-stranded DNA junction. This DNA structure is therefore proposed to serve as an entry site for the T antigen helicase. Previously reported data suggest that T antigen is the replicative helicase of the SV40 minichromosome. The results presented here are consistent with these findings and imply that T antigen migrates actively and processively along the template for the leading strand."}

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":22,"end":31},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":167,"end":176},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":178,"end":187},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":347,"end":356},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":639,"end":648},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":1041,"end":1050},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T7","span":{"begin":1209,"end":1218},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T8","span":{"begin":1267,"end":1276},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T9","span":{"begin":1410,"end":1419},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A7","pred":"glycoepitope_id","subj":"T7","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A8","pred":"glycoepitope_id","subj":"T8","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A9","pred":"glycoepitope_id","subj":"T9","obj":"http://www.glycoepitope.jp/epitopes/EP0020"}],"text":"Simian virus 40 large T antigen DNA helicase. Characterization of the ATPase-dependent DNA unwinding activity and its substrate requirements.\nThe ATPase of SV40 large T antigen (T antigen) which is essential for the replication of SV40 minichromosomes was recently shown to be functionally related to a newly discovered DNA helicase activity. The T antigen helicase unwinds DNA duplices of several kilobase pairs in a reaction depending on the presence of hydrolyzable ribo- or deoxyribonucleoside triphosphates. The in vitro rate of movement through duplex DNA was found to be about 100 base pairs/min at 37 degrees C. For DNA unwinding, T antigen requires a 3'-single strand extension of a partially double-stranded substrate and invades the double strand section processively, in a 3' to 5' direction. The minimum length of the single-stranded tail was determined to be less than 5 nucleotides. Unwinding studies in the presence of the Escherichia coli single strand-specific DNA-binding protein and competition experiments indicate that T antigen helicase binds preferentially at the single-stranded/double-stranded DNA junction. This DNA structure is therefore proposed to serve as an entry site for the T antigen helicase. Previously reported data suggest that T antigen is the replicative helicase of the SV40 minichromosome. The results presented here are consistent with these findings and imply that T antigen migrates actively and processively along the template for the leading strand."}

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":0,"end":15},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":939,"end":955},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"1891767"},{"id":"A2","pred":"db_id","subj":"T2","obj":"562"}],"text":"Simian virus 40 large T antigen DNA helicase. Characterization of the ATPase-dependent DNA unwinding activity and its substrate requirements.\nThe ATPase of SV40 large T antigen (T antigen) which is essential for the replication of SV40 minichromosomes was recently shown to be functionally related to a newly discovered DNA helicase activity. The T antigen helicase unwinds DNA duplices of several kilobase pairs in a reaction depending on the presence of hydrolyzable ribo- or deoxyribonucleoside triphosphates. The in vitro rate of movement through duplex DNA was found to be about 100 base pairs/min at 37 degrees C. For DNA unwinding, T antigen requires a 3'-single strand extension of a partially double-stranded substrate and invades the double strand section processively, in a 3' to 5' direction. The minimum length of the single-stranded tail was determined to be less than 5 nucleotides. Unwinding studies in the presence of the Escherichia coli single strand-specific DNA-binding protein and competition experiments indicate that T antigen helicase binds preferentially at the single-stranded/double-stranded DNA junction. This DNA structure is therefore proposed to serve as an entry site for the T antigen helicase. Previously reported data suggest that T antigen is the replicative helicase of the SV40 minichromosome. The results presented here are consistent with these findings and imply that T antigen migrates actively and processively along the template for the leading strand."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":677,"end":686},"obj":"Body_part"},{"id":"T2","span":{"begin":847,"end":851},"obj":"Body_part"},{"id":"T4","span":{"begin":1124,"end":1132},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_2000106"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0002415"},{"id":"A3","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_4000164"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0007651"}],"text":"Simian virus 40 large T antigen DNA helicase. Characterization of the ATPase-dependent DNA unwinding activity and its substrate requirements.\nThe ATPase of SV40 large T antigen (T antigen) which is essential for the replication of SV40 minichromosomes was recently shown to be functionally related to a newly discovered DNA helicase activity. The T antigen helicase unwinds DNA duplices of several kilobase pairs in a reaction depending on the presence of hydrolyzable ribo- or deoxyribonucleoside triphosphates. The in vitro rate of movement through duplex DNA was found to be about 100 base pairs/min at 37 degrees C. For DNA unwinding, T antigen requires a 3'-single strand extension of a partially double-stranded substrate and invades the double strand section processively, in a 3' to 5' direction. The minimum length of the single-stranded tail was determined to be less than 5 nucleotides. Unwinding studies in the presence of the Escherichia coli single strand-specific DNA-binding protein and competition experiments indicate that T antigen helicase binds preferentially at the single-stranded/double-stranded DNA junction. This DNA structure is therefore proposed to serve as an entry site for the T antigen helicase. Previously reported data suggest that T antigen is the replicative helicase of the SV40 minichromosome. The results presented here are consistent with these findings and imply that T antigen migrates actively and processively along the template for the leading strand."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":45},"obj":"Sentence"},{"id":"T2","span":{"begin":46,"end":141},"obj":"Sentence"},{"id":"T3","span":{"begin":142,"end":342},"obj":"Sentence"},{"id":"T4","span":{"begin":343,"end":512},"obj":"Sentence"},{"id":"T5","span":{"begin":513,"end":619},"obj":"Sentence"},{"id":"T6","span":{"begin":620,"end":804},"obj":"Sentence"},{"id":"T7","span":{"begin":805,"end":897},"obj":"Sentence"},{"id":"T8","span":{"begin":898,"end":1133},"obj":"Sentence"},{"id":"T9","span":{"begin":1134,"end":1228},"obj":"Sentence"},{"id":"T10","span":{"begin":1229,"end":1332},"obj":"Sentence"},{"id":"T11","span":{"begin":1333,"end":1497},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":45},"obj":"Sentence"},{"id":"T2","span":{"begin":46,"end":141},"obj":"Sentence"},{"id":"T3","span":{"begin":142,"end":342},"obj":"Sentence"},{"id":"T4","span":{"begin":343,"end":512},"obj":"Sentence"},{"id":"T5","span":{"begin":513,"end":619},"obj":"Sentence"},{"id":"T6","span":{"begin":620,"end":804},"obj":"Sentence"},{"id":"T7","span":{"begin":805,"end":897},"obj":"Sentence"},{"id":"T8","span":{"begin":898,"end":1133},"obj":"Sentence"},{"id":"T9","span":{"begin":1134,"end":1228},"obj":"Sentence"},{"id":"T10","span":{"begin":1229,"end":1332},"obj":"Sentence"},{"id":"T11","span":{"begin":1333,"end":1497},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Simian virus 40 large T antigen DNA helicase. Characterization of the ATPase-dependent DNA unwinding activity and its substrate requirements.\nThe ATPase of SV40 large T antigen (T antigen) which is essential for the replication of SV40 minichromosomes was recently shown to be functionally related to a newly discovered DNA helicase activity. The T antigen helicase unwinds DNA duplices of several kilobase pairs in a reaction depending on the presence of hydrolyzable ribo- or deoxyribonucleoside triphosphates. The in vitro rate of movement through duplex DNA was found to be about 100 base pairs/min at 37 degrees C. For DNA unwinding, T antigen requires a 3'-single strand extension of a partially double-stranded substrate and invades the double strand section processively, in a 3' to 5' direction. The minimum length of the single-stranded tail was determined to be less than 5 nucleotides. Unwinding studies in the presence of the Escherichia coli single strand-specific DNA-binding protein and competition experiments indicate that T antigen helicase binds preferentially at the single-stranded/double-stranded DNA junction. This DNA structure is therefore proposed to serve as an entry site for the T antigen helicase. Previously reported data suggest that T antigen is the replicative helicase of the SV40 minichromosome. The results presented here are consistent with these findings and imply that T antigen migrates actively and processively along the template for the leading strand."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":45},"obj":"Sentence"},{"id":"T2","span":{"begin":46,"end":141},"obj":"Sentence"},{"id":"T3","span":{"begin":142,"end":342},"obj":"Sentence"},{"id":"T4","span":{"begin":343,"end":512},"obj":"Sentence"},{"id":"T5","span":{"begin":513,"end":804},"obj":"Sentence"},{"id":"T6","span":{"begin":805,"end":897},"obj":"Sentence"},{"id":"T7","span":{"begin":898,"end":1133},"obj":"Sentence"},{"id":"T8","span":{"begin":1134,"end":1228},"obj":"Sentence"},{"id":"T9","span":{"begin":1229,"end":1332},"obj":"Sentence"},{"id":"T10","span":{"begin":1333,"end":1497},"obj":"Sentence"}],"text":"Simian virus 40 large T antigen DNA helicase. Characterization of the ATPase-dependent DNA unwinding activity and its substrate requirements.\nThe ATPase of SV40 large T antigen (T antigen) which is essential for the replication of SV40 minichromosomes was recently shown to be functionally related to a newly discovered DNA helicase activity. The T antigen helicase unwinds DNA duplices of several kilobase pairs in a reaction depending on the presence of hydrolyzable ribo- or deoxyribonucleoside triphosphates. The in vitro rate of movement through duplex DNA was found to be about 100 base pairs/min at 37 degrees C. For DNA unwinding, T antigen requires a 3'-single strand extension of a partially double-stranded substrate and invades the double strand section processively, in a 3' to 5' direction. The minimum length of the single-stranded tail was determined to be less than 5 nucleotides. Unwinding studies in the presence of the Escherichia coli single strand-specific DNA-binding protein and competition experiments indicate that T antigen helicase binds preferentially at the single-stranded/double-stranded DNA junction. This DNA structure is therefore proposed to serve as an entry site for the T antigen helicase. Previously reported data suggest that T antigen is the replicative helicase of the SV40 minichromosome. The results presented here are consistent with these findings and imply that T antigen migrates actively and processively along the template for the leading strand."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":22,"end":31},"obj":"Glycan"},{"id":"T2","span":{"begin":167,"end":176},"obj":"Glycan"},{"id":"T3","span":{"begin":178,"end":187},"obj":"Glycan"},{"id":"T4","span":{"begin":347,"end":356},"obj":"Glycan"},{"id":"T5","span":{"begin":639,"end":648},"obj":"Glycan"},{"id":"T6","span":{"begin":1041,"end":1050},"obj":"Glycan"},{"id":"T7","span":{"begin":1209,"end":1218},"obj":"Glycan"},{"id":"T8","span":{"begin":1267,"end":1276},"obj":"Glycan"},{"id":"T9","span":{"begin":1410,"end":1419},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A9","pred":"glycosmos_id","subj":"T9","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A10","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A11","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A12","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A13","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A14","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A15","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A16","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A17","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A18","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"}],"text":"Simian virus 40 large T antigen DNA helicase. Characterization of the ATPase-dependent DNA unwinding activity and its substrate requirements.\nThe ATPase of SV40 large T antigen (T antigen) which is essential for the replication of SV40 minichromosomes was recently shown to be functionally related to a newly discovered DNA helicase activity. The T antigen helicase unwinds DNA duplices of several kilobase pairs in a reaction depending on the presence of hydrolyzable ribo- or deoxyribonucleoside triphosphates. The in vitro rate of movement through duplex DNA was found to be about 100 base pairs/min at 37 degrees C. For DNA unwinding, T antigen requires a 3'-single strand extension of a partially double-stranded substrate and invades the double strand section processively, in a 3' to 5' direction. The minimum length of the single-stranded tail was determined to be less than 5 nucleotides. Unwinding studies in the presence of the Escherichia coli single strand-specific DNA-binding protein and competition experiments indicate that T antigen helicase binds preferentially at the single-stranded/double-stranded DNA junction. This DNA structure is therefore proposed to serve as an entry site for the T antigen helicase. Previously reported data suggest that T antigen is the replicative helicase of the SV40 minichromosome. The results presented here are consistent with these findings and imply that T antigen migrates actively and processively along the template for the leading strand."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":22,"end":31},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":167,"end":176},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":178,"end":187},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":347,"end":356},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":639,"end":648},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":1041,"end":1050},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T7","span":{"begin":1209,"end":1218},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T8","span":{"begin":1267,"end":1276},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T9","span":{"begin":1410,"end":1419},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A7","pred":"glycoepitope_id","subj":"T7","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A8","pred":"glycoepitope_id","subj":"T8","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A9","pred":"glycoepitope_id","subj":"T9","obj":"http://www.glycoepitope.jp/epitopes/EP0020"}],"text":"Simian virus 40 large T antigen DNA helicase. Characterization of the ATPase-dependent DNA unwinding activity and its substrate requirements.\nThe ATPase of SV40 large T antigen (T antigen) which is essential for the replication of SV40 minichromosomes was recently shown to be functionally related to a newly discovered DNA helicase activity. The T antigen helicase unwinds DNA duplices of several kilobase pairs in a reaction depending on the presence of hydrolyzable ribo- or deoxyribonucleoside triphosphates. The in vitro rate of movement through duplex DNA was found to be about 100 base pairs/min at 37 degrees C. For DNA unwinding, T antigen requires a 3'-single strand extension of a partially double-stranded substrate and invades the double strand section processively, in a 3' to 5' direction. The minimum length of the single-stranded tail was determined to be less than 5 nucleotides. Unwinding studies in the presence of the Escherichia coli single strand-specific DNA-binding protein and competition experiments indicate that T antigen helicase binds preferentially at the single-stranded/double-stranded DNA junction. This DNA structure is therefore proposed to serve as an entry site for the T antigen helicase. Previously reported data suggest that T antigen is the replicative helicase of the SV40 minichromosome. The results presented here are consistent with these findings and imply that T antigen migrates actively and processively along the template for the leading strand."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":0,"end":15},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":939,"end":955},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"1891767"},{"id":"A2","pred":"db_id","subj":"T2","obj":"562"}],"text":"Simian virus 40 large T antigen DNA helicase. Characterization of the ATPase-dependent DNA unwinding activity and its substrate requirements.\nThe ATPase of SV40 large T antigen (T antigen) which is essential for the replication of SV40 minichromosomes was recently shown to be functionally related to a newly discovered DNA helicase activity. The T antigen helicase unwinds DNA duplices of several kilobase pairs in a reaction depending on the presence of hydrolyzable ribo- or deoxyribonucleoside triphosphates. The in vitro rate of movement through duplex DNA was found to be about 100 base pairs/min at 37 degrees C. For DNA unwinding, T antigen requires a 3'-single strand extension of a partially double-stranded substrate and invades the double strand section processively, in a 3' to 5' direction. The minimum length of the single-stranded tail was determined to be less than 5 nucleotides. Unwinding studies in the presence of the Escherichia coli single strand-specific DNA-binding protein and competition experiments indicate that T antigen helicase binds preferentially at the single-stranded/double-stranded DNA junction. This DNA structure is therefore proposed to serve as an entry site for the T antigen helicase. Previously reported data suggest that T antigen is the replicative helicase of the SV40 minichromosome. The results presented here are consistent with these findings and imply that T antigen migrates actively and processively along the template for the leading strand."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":677,"end":686},"obj":"Body_part"},{"id":"T2","span":{"begin":847,"end":851},"obj":"Body_part"},{"id":"T4","span":{"begin":1124,"end":1132},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_2000106"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0002415"},{"id":"A3","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_4000164"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0007651"}],"text":"Simian virus 40 large T antigen DNA helicase. Characterization of the ATPase-dependent DNA unwinding activity and its substrate requirements.\nThe ATPase of SV40 large T antigen (T antigen) which is essential for the replication of SV40 minichromosomes was recently shown to be functionally related to a newly discovered DNA helicase activity. The T antigen helicase unwinds DNA duplices of several kilobase pairs in a reaction depending on the presence of hydrolyzable ribo- or deoxyribonucleoside triphosphates. The in vitro rate of movement through duplex DNA was found to be about 100 base pairs/min at 37 degrees C. For DNA unwinding, T antigen requires a 3'-single strand extension of a partially double-stranded substrate and invades the double strand section processively, in a 3' to 5' direction. The minimum length of the single-stranded tail was determined to be less than 5 nucleotides. Unwinding studies in the presence of the Escherichia coli single strand-specific DNA-binding protein and competition experiments indicate that T antigen helicase binds preferentially at the single-stranded/double-stranded DNA junction. This DNA structure is therefore proposed to serve as an entry site for the T antigen helicase. Previously reported data suggest that T antigen is the replicative helicase of the SV40 minichromosome. The results presented here are consistent with these findings and imply that T antigen migrates actively and processively along the template for the leading strand."}