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pmc-enju-pas

bionlp-st-ge-2016-test-proteins

bionlp-st-ge-2016-uniprot

GO-BP

{"project":"GO-BP","denotations":[{"id":"T11935","span":{"begin":3029,"end":3044},"obj":"http://purl.obolibrary.org/obo/GO_0032663"},{"id":"T11934","span":{"begin":3029,"end":3044},"obj":"http://purl.obolibrary.org/obo/GO_0032623"},{"id":"T11933","span":{"begin":2453,"end":2463},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T11932","span":{"begin":1314,"end":1324},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T11931","span":{"begin":1208,"end":1218},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T11930","span":{"begin":460,"end":470},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T11929","span":{"begin":386,"end":396},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T11928","span":{"begin":254,"end":266},"obj":"http://purl.obolibrary.org/obo/GO_0006954"},{"id":"T11916","span":{"begin":2551,"end":2564},"obj":"http://purl.obolibrary.org/obo/GO_0006351"}],"text":"Potentially even more relevant than the specific cytokine panel induced by GP, we found that, in the presence of other stimuli (LPS or TSST-1), GP ameliorated their pro-inflammatory immune reactions, similar to the effects in murine models of sepsis and inflammation [21-24]. Mainly, GP altered the TSST-1-induced IL-1β/IL-1RA ratio from a pro- to an anti-inflammatory profile via down-regulation of IL-1β and IL-6, at the same time there was a synergistic up-regulation of IL-1RA. In part, this change may be caused by GP-mediated modulations of the TSST-1 induced binding of NFκB, NFIL-6 and NFAT to known and up to now unknown sites within the IL-8 and IL-1RA promoter instead of the TNFα, IL-1β, IL-6 or IFNγ promoter. Accordingly, we found that the TSST-1-induced binding of NFκB to sites from the TNFα promoter negatively correlated with the GP-mediated enhancement of the TSST-1-induced IL-1RA production (r = -0.88; p \u003c 0.01; data not shown in detail). Of the four examined NFκB sites from the IL-1RA promoter, mostly the TSST-1- and LPS-induced binding to the NFκB3 and the TSST-1-induced binding to the new NFκB consensus site seemed to be increased by GP. So, while we observed a GP-mediated down-regulation of the LPS- and the TSST-1-induced NFκB binding to sites of the TNFα promoter, there was an up-regulation to NFκB3 and NFκB consensus sites of the IL-1RA promoter. These seemingly contradictory data could be explained by differences in either NFκB subunits or conserved nucleotides (#1, 2, 3, 10) within the decameric NFκB binding motif between the TNFα and the IL-1RA promoter (for NFκB3 the IL-1RA motif contains a T on position 10 instead of the conserved C in the TNFα motif, see Table 1), probably leading to differences in binding [41,42]. Despite the location of the new NFκB consensus site (-266 and -280) in the inhibitory element (-250 and -294) of the IL-1RA promoter [30], we observed no inhibition. On the other side, we found an inhibitory NFκB2/3 site (-288 and -302) towards the end of the inhibitory element, demonstrating down-regulations of the LPS- and TSST-1-induced binding, which could not be altered by GP. In our opinion, this site may therefore represent at least a part of the previoulsy described inhibitory element [30]. The GP-modulated increase in TSST-1-induced binding to the new NFκB3 and NFκB consensus site, the NFIL-6 site [32] as well as to the novel NFATP2/3 site may explain the synergistic up-regulation of the TSST-1-induced IL-1RA production. We think that this GP-modulated activation of transcription was reflected by the decrease of the IL-1β/IL-1RA ratio following GP + TSST-1 (Fig. 6). In this context, it has been postulated that in vitro a 100fold excess of IL-1RA over IL-1β might control the biological effects of IL-1 [46,47]. Since, in fact, the IL-1β/IL-1RA ratio following GP + TSST-1 is partially less than 0.01, it is not unreasonable to assume that IL-1β bioactivity is inactivated in our system. Indeed, GP reduced the TSST-1-induced, IL-1-dependent IL-2 production of murine EL-4 cells (data not shown in detail)."}

GO-MF

{"project":"GO-MF","denotations":[{"id":"T12571","span":{"begin":3029,"end":3033},"obj":"http://purl.obolibrary.org/obo/GO_0005134"},{"id":"T12570","span":{"begin":3014,"end":3018},"obj":"http://purl.obolibrary.org/obo/GO_0005149"},{"id":"T12569","span":{"begin":2785,"end":2789},"obj":"http://purl.obolibrary.org/obo/GO_0005149"},{"id":"T12567","span":{"begin":700,"end":704},"obj":"http://purl.obolibrary.org/obo/GO_0005138"},{"id":"T12566","span":{"begin":410,"end":414},"obj":"http://purl.obolibrary.org/obo/GO_0005138"},{"id":"T12561","span":{"begin":647,"end":651},"obj":"http://purl.obolibrary.org/obo/GO_0005153"},{"id":"T12547","span":{"begin":2313,"end":2320},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12546","span":{"begin":2107,"end":2114},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12545","span":{"begin":1748,"end":1755},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12544","span":{"begin":1542,"end":1549},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12543","span":{"begin":1259,"end":1266},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12542","span":{"begin":1098,"end":1105},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12541","span":{"begin":1054,"end":1061},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12540","span":{"begin":769,"end":776},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12539","span":{"begin":566,"end":573},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Potentially even more relevant than the specific cytokine panel induced by GP, we found that, in the presence of other stimuli (LPS or TSST-1), GP ameliorated their pro-inflammatory immune reactions, similar to the effects in murine models of sepsis and inflammation [21-24]. Mainly, GP altered the TSST-1-induced IL-1β/IL-1RA ratio from a pro- to an anti-inflammatory profile via down-regulation of IL-1β and IL-6, at the same time there was a synergistic up-regulation of IL-1RA. In part, this change may be caused by GP-mediated modulations of the TSST-1 induced binding of NFκB, NFIL-6 and NFAT to known and up to now unknown sites within the IL-8 and IL-1RA promoter instead of the TNFα, IL-1β, IL-6 or IFNγ promoter. Accordingly, we found that the TSST-1-induced binding of NFκB to sites from the TNFα promoter negatively correlated with the GP-mediated enhancement of the TSST-1-induced IL-1RA production (r = -0.88; p \u003c 0.01; data not shown in detail). Of the four examined NFκB sites from the IL-1RA promoter, mostly the TSST-1- and LPS-induced binding to the NFκB3 and the TSST-1-induced binding to the new NFκB consensus site seemed to be increased by GP. So, while we observed a GP-mediated down-regulation of the LPS- and the TSST-1-induced NFκB binding to sites of the TNFα promoter, there was an up-regulation to NFκB3 and NFκB consensus sites of the IL-1RA promoter. These seemingly contradictory data could be explained by differences in either NFκB subunits or conserved nucleotides (#1, 2, 3, 10) within the decameric NFκB binding motif between the TNFα and the IL-1RA promoter (for NFκB3 the IL-1RA motif contains a T on position 10 instead of the conserved C in the TNFα motif, see Table 1), probably leading to differences in binding [41,42]. Despite the location of the new NFκB consensus site (-266 and -280) in the inhibitory element (-250 and -294) of the IL-1RA promoter [30], we observed no inhibition. On the other side, we found an inhibitory NFκB2/3 site (-288 and -302) towards the end of the inhibitory element, demonstrating down-regulations of the LPS- and TSST-1-induced binding, which could not be altered by GP. In our opinion, this site may therefore represent at least a part of the previoulsy described inhibitory element [30]. The GP-modulated increase in TSST-1-induced binding to the new NFκB3 and NFκB consensus site, the NFIL-6 site [32] as well as to the novel NFATP2/3 site may explain the synergistic up-regulation of the TSST-1-induced IL-1RA production. We think that this GP-modulated activation of transcription was reflected by the decrease of the IL-1β/IL-1RA ratio following GP + TSST-1 (Fig. 6). In this context, it has been postulated that in vitro a 100fold excess of IL-1RA over IL-1β might control the biological effects of IL-1 [46,47]. Since, in fact, the IL-1β/IL-1RA ratio following GP + TSST-1 is partially less than 0.01, it is not unreasonable to assume that IL-1β bioactivity is inactivated in our system. Indeed, GP reduced the TSST-1-induced, IL-1-dependent IL-2 production of murine EL-4 cells (data not shown in detail)."}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T12574","span":{"begin":3060,"end":3065},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Potentially even more relevant than the specific cytokine panel induced by GP, we found that, in the presence of other stimuli (LPS or TSST-1), GP ameliorated their pro-inflammatory immune reactions, similar to the effects in murine models of sepsis and inflammation [21-24]. Mainly, GP altered the TSST-1-induced IL-1β/IL-1RA ratio from a pro- to an anti-inflammatory profile via down-regulation of IL-1β and IL-6, at the same time there was a synergistic up-regulation of IL-1RA. In part, this change may be caused by GP-mediated modulations of the TSST-1 induced binding of NFκB, NFIL-6 and NFAT to known and up to now unknown sites within the IL-8 and IL-1RA promoter instead of the TNFα, IL-1β, IL-6 or IFNγ promoter. Accordingly, we found that the TSST-1-induced binding of NFκB to sites from the TNFα promoter negatively correlated with the GP-mediated enhancement of the TSST-1-induced IL-1RA production (r = -0.88; p \u003c 0.01; data not shown in detail). Of the four examined NFκB sites from the IL-1RA promoter, mostly the TSST-1- and LPS-induced binding to the NFκB3 and the TSST-1-induced binding to the new NFκB consensus site seemed to be increased by GP. So, while we observed a GP-mediated down-regulation of the LPS- and the TSST-1-induced NFκB binding to sites of the TNFα promoter, there was an up-regulation to NFκB3 and NFκB consensus sites of the IL-1RA promoter. These seemingly contradictory data could be explained by differences in either NFκB subunits or conserved nucleotides (#1, 2, 3, 10) within the decameric NFκB binding motif between the TNFα and the IL-1RA promoter (for NFκB3 the IL-1RA motif contains a T on position 10 instead of the conserved C in the TNFα motif, see Table 1), probably leading to differences in binding [41,42]. Despite the location of the new NFκB consensus site (-266 and -280) in the inhibitory element (-250 and -294) of the IL-1RA promoter [30], we observed no inhibition. On the other side, we found an inhibitory NFκB2/3 site (-288 and -302) towards the end of the inhibitory element, demonstrating down-regulations of the LPS- and TSST-1-induced binding, which could not be altered by GP. In our opinion, this site may therefore represent at least a part of the previoulsy described inhibitory element [30]. The GP-modulated increase in TSST-1-induced binding to the new NFκB3 and NFκB consensus site, the NFIL-6 site [32] as well as to the novel NFATP2/3 site may explain the synergistic up-regulation of the TSST-1-induced IL-1RA production. We think that this GP-modulated activation of transcription was reflected by the decrease of the IL-1β/IL-1RA ratio following GP + TSST-1 (Fig. 6). In this context, it has been postulated that in vitro a 100fold excess of IL-1RA over IL-1β might control the biological effects of IL-1 [46,47]. Since, in fact, the IL-1β/IL-1RA ratio following GP + TSST-1 is partially less than 0.01, it is not unreasonable to assume that IL-1β bioactivity is inactivated in our system. Indeed, GP reduced the TSST-1-induced, IL-1-dependent IL-2 production of murine EL-4 cells (data not shown in detail)."}

sentences

simple1

BioNLP16_DUT

BioNLP16_Messiy

DLUT931

bionlp-st-ge-2016-test-ihmc

bionlp-st-ge-2016-spacy-parsed

bionlp-st-ge-2016-test-tees

testone

test3

PMC:1472690 / 28066-31159 JSONTXT

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PMC:1472690 / 28066-31159 JSON TXT