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pmc-enju-pas

bionlp-st-ge-2016-spacy-parsed

GO-BP

{"project":"GO-BP","denotations":[{"id":"T26107","span":{"begin":300,"end":310},"obj":"http://purl.obolibrary.org/obo/GO_0006412"},{"id":"T26108","span":{"begin":589,"end":599},"obj":"http://purl.obolibrary.org/obo/GO_0006412"},{"id":"T26109","span":{"begin":300,"end":319},"obj":"http://purl.obolibrary.org/obo/GO_0006412"},{"id":"T26110","span":{"begin":1065,"end":1084},"obj":"http://purl.obolibrary.org/obo/GO_0006412"},{"id":"T26111","span":{"begin":1688,"end":1707},"obj":"http://purl.obolibrary.org/obo/GO_0045289"},{"id":"T26112","span":{"begin":1688,"end":1707},"obj":"http://purl.obolibrary.org/obo/GO_0047077"},{"id":"T26113","span":{"begin":1688,"end":1707},"obj":"http://purl.obolibrary.org/obo/GO_0047712"},{"id":"T26114","span":{"begin":1688,"end":1707},"obj":"http://purl.obolibrary.org/obo/GO_0050248"},{"id":"T26115","span":{"begin":1688,"end":1707},"obj":"http://purl.obolibrary.org/obo/GO_0050397"},{"id":"T26116","span":{"begin":1779,"end":1803},"obj":"http://purl.obolibrary.org/obo/GO_0004565"},{"id":"T26117","span":{"begin":1779,"end":1803},"obj":"http://purl.obolibrary.org/obo/GO_0004336"},{"id":"T26118","span":{"begin":1779,"end":1803},"obj":"http://purl.obolibrary.org/obo/GO_1903771"},{"id":"T26119","span":{"begin":1779,"end":1803},"obj":"http://purl.obolibrary.org/obo/GO_1903770"},{"id":"T26120","span":{"begin":1779,"end":1803},"obj":"http://purl.obolibrary.org/obo/GO_0033920"},{"id":"T26121","span":{"begin":1779,"end":1803},"obj":"http://purl.obolibrary.org/obo/GO_0033929"},{"id":"T26122","span":{"begin":1779,"end":1803},"obj":"http://purl.obolibrary.org/obo/GO_0033930"}],"text":"Figure 3. Tat relieves p65 from the IκB-α inhibition. (A) Schematic representation of wild-type and mutant Tat proteins. (B) HA-IκB-α (5 µl) was incubated in presence or absence of FLAG-Tat, FLAG-Tat T,N(23,24)A, FLAG-Tat K(50,51)A, FLAG-Tat R(49–57)A or FLAG-Tat C(22,25,27)A (10 µl) using in vitro translated proteins. Wild-type and mutant Tat proteins were immunoprecipitated with anti-FLAG antibody; immunocomplexes were separated by 12% SDS–PAGE and analysed by western blotting with anti-HA and anti-FLAG antibodies. (C) 35S-methionine-labeled p65 (5 µl) was incubated with in vitro translated HA-IκB-α (5 µl) in presence or absence of FLAG-Tat or FLAG-Tat R(49–57)A (5, 10 or 20 µl). HA-IκB-α was immunoprecipitated with anti-HA antibody; immunocomplexes were separated by 12% SDS–PAGE and analysed by western blotting with anti-HA and anti-FLAG antibodies, or autoradiography (35S-Met-p65). Densitometry values (D) of the bands were expressed as fold increase above the control (lane 1). (D) The p65 DNA binding activity was analysed by EMSA using in vitro translated proteins. 32P-labeled-NF-κB double-stranded oligonucleotide was incubated with p65 (0.5 µl) in presence or absence of HA-IκB-α (1 µl), FLAG-Tat or FLAG-Tat R(49–57)A (5 and 10 µl); competition of DNA binding was performed with 10 - up to 100-fold molar excess of unlabeled NF-κB double-stranded oligonucleotide. DNA/protein complexes were run on 6% PAGE–TBE and analysed by autoradiography. (E) p50−/−p65−/−MEFs (3 × 105 cells) were transfected with pκBLuc (0.5 µg) and pSV-β-Gal (0.1 µg) with or without pRc/CMV-p65 (0.5 µg), pCMV4-HA-IκB-α (0.5 µg), p3xFLAG-Tat or p3xFLAG-Tat R(49–57)A (0.5, 1 and 2 µg). The luciferase activity was measured in cell extracts 48-h post-transfection and normalized to β-galactosidase activity. Fold activation was calculated relative to transfection of the pκBLuc plasmid alone. Values (mean ± SE, n = 3) are shown. As control of protein expression, aliquots of cell extracts (20 µg) were analysed by western blotting with anti-p65, anti-HA, anti-FLAG and anti-γ-tubulin antibodies."}

GO-MF

{"project":"GO-MF","denotations":[{"id":"T26123","span":{"begin":394,"end":402},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T26124","span":{"begin":736,"end":744},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T26125","span":{"begin":853,"end":863},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T26126","span":{"begin":2082,"end":2092},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T26127","span":{"begin":1008,"end":1019},"obj":"http://purl.obolibrary.org/obo/GO_0003677"},{"id":"T26128","span":{"begin":1272,"end":1283},"obj":"http://purl.obolibrary.org/obo/GO_0003677"},{"id":"T26129","span":{"begin":1012,"end":1019},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T26130","span":{"begin":1276,"end":1283},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T26131","span":{"begin":1688,"end":1707},"obj":"http://purl.obolibrary.org/obo/GO_0045289"},{"id":"T26132","span":{"begin":1688,"end":1707},"obj":"http://purl.obolibrary.org/obo/GO_0047077"},{"id":"T26133","span":{"begin":1688,"end":1707},"obj":"http://purl.obolibrary.org/obo/GO_0047712"},{"id":"T26134","span":{"begin":1688,"end":1707},"obj":"http://purl.obolibrary.org/obo/GO_0050248"},{"id":"T26135","span":{"begin":1688,"end":1707},"obj":"http://purl.obolibrary.org/obo/GO_0050397"},{"id":"T26136","span":{"begin":1779,"end":1803},"obj":"http://purl.obolibrary.org/obo/GO_0004565"},{"id":"T26137","span":{"begin":1779,"end":1803},"obj":"http://purl.obolibrary.org/obo/GO_0004336"},{"id":"T26138","span":{"begin":1779,"end":1803},"obj":"http://purl.obolibrary.org/obo/GO_0033920"},{"id":"T26139","span":{"begin":1779,"end":1803},"obj":"http://purl.obolibrary.org/obo/GO_0033929"},{"id":"T26140","span":{"begin":1779,"end":1803},"obj":"http://purl.obolibrary.org/obo/GO_0033930"}],"text":"Figure 3. Tat relieves p65 from the IκB-α inhibition. (A) Schematic representation of wild-type and mutant Tat proteins. (B) HA-IκB-α (5 µl) was incubated in presence or absence of FLAG-Tat, FLAG-Tat T,N(23,24)A, FLAG-Tat K(50,51)A, FLAG-Tat R(49–57)A or FLAG-Tat C(22,25,27)A (10 µl) using in vitro translated proteins. Wild-type and mutant Tat proteins were immunoprecipitated with anti-FLAG antibody; immunocomplexes were separated by 12% SDS–PAGE and analysed by western blotting with anti-HA and anti-FLAG antibodies. (C) 35S-methionine-labeled p65 (5 µl) was incubated with in vitro translated HA-IκB-α (5 µl) in presence or absence of FLAG-Tat or FLAG-Tat R(49–57)A (5, 10 or 20 µl). HA-IκB-α was immunoprecipitated with anti-HA antibody; immunocomplexes were separated by 12% SDS–PAGE and analysed by western blotting with anti-HA and anti-FLAG antibodies, or autoradiography (35S-Met-p65). Densitometry values (D) of the bands were expressed as fold increase above the control (lane 1). (D) The p65 DNA binding activity was analysed by EMSA using in vitro translated proteins. 32P-labeled-NF-κB double-stranded oligonucleotide was incubated with p65 (0.5 µl) in presence or absence of HA-IκB-α (1 µl), FLAG-Tat or FLAG-Tat R(49–57)A (5 and 10 µl); competition of DNA binding was performed with 10 - up to 100-fold molar excess of unlabeled NF-κB double-stranded oligonucleotide. DNA/protein complexes were run on 6% PAGE–TBE and analysed by autoradiography. (E) p50−/−p65−/−MEFs (3 × 105 cells) were transfected with pκBLuc (0.5 µg) and pSV-β-Gal (0.1 µg) with or without pRc/CMV-p65 (0.5 µg), pCMV4-HA-IκB-α (0.5 µg), p3xFLAG-Tat or p3xFLAG-Tat R(49–57)A (0.5, 1 and 2 µg). The luciferase activity was measured in cell extracts 48-h post-transfection and normalized to β-galactosidase activity. Fold activation was calculated relative to transfection of the pκBLuc plasmid alone. Values (mean ± SE, n = 3) are shown. As control of protein expression, aliquots of cell extracts (20 µg) were analysed by western blotting with anti-p65, anti-HA, anti-FLAG and anti-γ-tubulin antibodies."}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T26141","span":{"begin":394,"end":402},"obj":"http://purl.obolibrary.org/obo/GO_0019815"},{"id":"T26142","span":{"begin":736,"end":744},"obj":"http://purl.obolibrary.org/obo/GO_0019815"},{"id":"T26143","span":{"begin":853,"end":863},"obj":"http://purl.obolibrary.org/obo/GO_0019815"},{"id":"T26144","span":{"begin":2082,"end":2092},"obj":"http://purl.obolibrary.org/obo/GO_0019815"},{"id":"T26145","span":{"begin":394,"end":402},"obj":"http://purl.obolibrary.org/obo/GO_0042571"},{"id":"T26146","span":{"begin":736,"end":744},"obj":"http://purl.obolibrary.org/obo/GO_0042571"},{"id":"T26147","span":{"begin":853,"end":863},"obj":"http://purl.obolibrary.org/obo/GO_0042571"},{"id":"T26148","span":{"begin":2082,"end":2092},"obj":"http://purl.obolibrary.org/obo/GO_0042571"},{"id":"T26149","span":{"begin":1388,"end":1409},"obj":"http://purl.obolibrary.org/obo/GO_0001114"},{"id":"T26150","span":{"begin":1388,"end":1409},"obj":"http://purl.obolibrary.org/obo/GO_0032993"},{"id":"T26151","span":{"begin":1388,"end":1409},"obj":"http://purl.obolibrary.org/obo/GO_0097522"},{"id":"T26152","span":{"begin":1392,"end":1409},"obj":"http://purl.obolibrary.org/obo/GO_0043234"},{"id":"T26153","span":{"begin":1497,"end":1502},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T26154","span":{"begin":1724,"end":1728},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T26155","span":{"begin":1973,"end":1977},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Figure 3. Tat relieves p65 from the IκB-α inhibition. (A) Schematic representation of wild-type and mutant Tat proteins. (B) HA-IκB-α (5 µl) was incubated in presence or absence of FLAG-Tat, FLAG-Tat T,N(23,24)A, FLAG-Tat K(50,51)A, FLAG-Tat R(49–57)A or FLAG-Tat C(22,25,27)A (10 µl) using in vitro translated proteins. Wild-type and mutant Tat proteins were immunoprecipitated with anti-FLAG antibody; immunocomplexes were separated by 12% SDS–PAGE and analysed by western blotting with anti-HA and anti-FLAG antibodies. (C) 35S-methionine-labeled p65 (5 µl) was incubated with in vitro translated HA-IκB-α (5 µl) in presence or absence of FLAG-Tat or FLAG-Tat R(49–57)A (5, 10 or 20 µl). HA-IκB-α was immunoprecipitated with anti-HA antibody; immunocomplexes were separated by 12% SDS–PAGE and analysed by western blotting with anti-HA and anti-FLAG antibodies, or autoradiography (35S-Met-p65). Densitometry values (D) of the bands were expressed as fold increase above the control (lane 1). (D) The p65 DNA binding activity was analysed by EMSA using in vitro translated proteins. 32P-labeled-NF-κB double-stranded oligonucleotide was incubated with p65 (0.5 µl) in presence or absence of HA-IκB-α (1 µl), FLAG-Tat or FLAG-Tat R(49–57)A (5 and 10 µl); competition of DNA binding was performed with 10 - up to 100-fold molar excess of unlabeled NF-κB double-stranded oligonucleotide. DNA/protein complexes were run on 6% PAGE–TBE and analysed by autoradiography. (E) p50−/−p65−/−MEFs (3 × 105 cells) were transfected with pκBLuc (0.5 µg) and pSV-β-Gal (0.1 µg) with or without pRc/CMV-p65 (0.5 µg), pCMV4-HA-IκB-α (0.5 µg), p3xFLAG-Tat or p3xFLAG-Tat R(49–57)A (0.5, 1 and 2 µg). The luciferase activity was measured in cell extracts 48-h post-transfection and normalized to β-galactosidase activity. Fold activation was calculated relative to transfection of the pκBLuc plasmid alone. Values (mean ± SE, n = 3) are shown. As control of protein expression, aliquots of cell extracts (20 µg) were analysed by western blotting with anti-p65, anti-HA, anti-FLAG and anti-γ-tubulin antibodies."}

sentences

{"project":"sentences","denotations":[{"id":"T25204","span":{"begin":10,"end":320},"obj":"Sentence"},{"id":"T25205","span":{"begin":321,"end":690},"obj":"Sentence"},{"id":"T25206","span":{"begin":691,"end":898},"obj":"Sentence"},{"id":"T25207","span":{"begin":899,"end":1085},"obj":"Sentence"},{"id":"T25208","span":{"begin":1086,"end":1387},"obj":"Sentence"},{"id":"T25209","span":{"begin":1388,"end":1683},"obj":"Sentence"},{"id":"T25210","span":{"begin":1684,"end":1804},"obj":"Sentence"},{"id":"T25211","span":{"begin":1805,"end":1889},"obj":"Sentence"},{"id":"T25212","span":{"begin":1890,"end":1926},"obj":"Sentence"},{"id":"T25213","span":{"begin":1927,"end":2093},"obj":"Sentence"},{"id":"T149","span":{"begin":0,"end":9},"obj":"Sentence"},{"id":"T150","span":{"begin":10,"end":320},"obj":"Sentence"},{"id":"T151","span":{"begin":321,"end":690},"obj":"Sentence"},{"id":"T152","span":{"begin":691,"end":898},"obj":"Sentence"},{"id":"T153","span":{"begin":899,"end":1085},"obj":"Sentence"},{"id":"T154","span":{"begin":1086,"end":1387},"obj":"Sentence"},{"id":"T155","span":{"begin":1388,"end":1683},"obj":"Sentence"},{"id":"T156","span":{"begin":1684,"end":1804},"obj":"Sentence"},{"id":"T157","span":{"begin":1805,"end":1889},"obj":"Sentence"},{"id":"T158","span":{"begin":1890,"end":1926},"obj":"Sentence"},{"id":"T159","span":{"begin":1927,"end":2093},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Figure 3. Tat relieves p65 from the IκB-α inhibition. (A) Schematic representation of wild-type and mutant Tat proteins. (B) HA-IκB-α (5 µl) was incubated in presence or absence of FLAG-Tat, FLAG-Tat T,N(23,24)A, FLAG-Tat K(50,51)A, FLAG-Tat R(49–57)A or FLAG-Tat C(22,25,27)A (10 µl) using in vitro translated proteins. Wild-type and mutant Tat proteins were immunoprecipitated with anti-FLAG antibody; immunocomplexes were separated by 12% SDS–PAGE and analysed by western blotting with anti-HA and anti-FLAG antibodies. (C) 35S-methionine-labeled p65 (5 µl) was incubated with in vitro translated HA-IκB-α (5 µl) in presence or absence of FLAG-Tat or FLAG-Tat R(49–57)A (5, 10 or 20 µl). HA-IκB-α was immunoprecipitated with anti-HA antibody; immunocomplexes were separated by 12% SDS–PAGE and analysed by western blotting with anti-HA and anti-FLAG antibodies, or autoradiography (35S-Met-p65). Densitometry values (D) of the bands were expressed as fold increase above the control (lane 1). (D) The p65 DNA binding activity was analysed by EMSA using in vitro translated proteins. 32P-labeled-NF-κB double-stranded oligonucleotide was incubated with p65 (0.5 µl) in presence or absence of HA-IκB-α (1 µl), FLAG-Tat or FLAG-Tat R(49–57)A (5 and 10 µl); competition of DNA binding was performed with 10 - up to 100-fold molar excess of unlabeled NF-κB double-stranded oligonucleotide. DNA/protein complexes were run on 6% PAGE–TBE and analysed by autoradiography. (E) p50−/−p65−/−MEFs (3 × 105 cells) were transfected with pκBLuc (0.5 µg) and pSV-β-Gal (0.1 µg) with or without pRc/CMV-p65 (0.5 µg), pCMV4-HA-IκB-α (0.5 µg), p3xFLAG-Tat or p3xFLAG-Tat R(49–57)A (0.5, 1 and 2 µg). The luciferase activity was measured in cell extracts 48-h post-transfection and normalized to β-galactosidase activity. Fold activation was calculated relative to transfection of the pκBLuc plasmid alone. Values (mean ± SE, n = 3) are shown. As control of protein expression, aliquots of cell extracts (20 µg) were analysed by western blotting with anti-p65, anti-HA, anti-FLAG and anti-γ-tubulin antibodies."}

events-check-again

bionlp-st-ge-2016-reference-tees

test2

bionlp-st-ge-2016-reference

bionlp-st-ge-2016-uniprot

PMC:3333881 / 23390-25483 JSONTXT

Annnotations TAB JSON ListView MergeView

PMC:3333881 / 23390-25483 JSON TXT