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contains additional phosphorylation sites, C/EBP-βT188 and C/EBP-βS64 (Fig. 8B), which may be involved in modulating C/EBP-β-dependent SerpinB2 gene transcription. C/EBP-βT188 is implicated in regulating DAPK1, an IFNγ-inducible gene involved in the regulation of cell cycle and apoptosis [38], processes with which SerpinB2 has also been associated [17]. C/EBP-βS64 is important for LPS-induced transcription of the cytokines IL-6 and MCP-1 [64]. Similarly, SerpinB2 is induced by LPS and regulated in a manner similar to cytokines [29]. Given the similarities in the functional significance of these phospho-specific isoforms of C/EBP-β and SerpinB2, we investigated whether these phospho-acceptor sites may play a role in SerpinB2 gene expression. C/EBP-βT188A-transfected MEFs exhibited SerpinB2 promoter activity similar to that of wild-type C/EBP-β-transfected MEFs, whereas the expression of C/EBP-βS64A potentiated SerpinB2 promoter activity in response to LPS (Fig. 8C, right). These data suggest that phosphorylation of C/EBP-β at S64 acts to negatively regulate SerpinB2 proximal promoter activity."}

{"project":"2_test","denotations":[{"id":"23472114-17433708-87899186","span":{"begin":451,"end":453},"obj":"17433708"},{"id":"T18108","span":{"begin":451,"end":453},"obj":"17433708"}],"text":"C/EBP-β contains additional phosphorylation sites, C/EBP-βT188 and C/EBP-βS64 (Fig. 8B), which may be involved in modulating C/EBP-β-dependent SerpinB2 gene transcription. C/EBP-βT188 is implicated in regulating DAPK1, an IFNγ-inducible gene involved in the regulation of cell cycle and apoptosis [38], processes with which SerpinB2 has also been associated [17]. C/EBP-βS64 is important for LPS-induced transcription of the cytokines IL-6 and MCP-1 [64]. Similarly, SerpinB2 is induced by LPS and regulated in a manner similar to cytokines [29]. Given the similarities in the functional significance of these phospho-specific isoforms of C/EBP-β and SerpinB2, we investigated whether these phospho-acceptor sites may play a role in SerpinB2 gene expression. C/EBP-βT188A-transfected MEFs exhibited SerpinB2 promoter activity similar to that of wild-type C/EBP-β-transfected MEFs, whereas the expression of C/EBP-βS64A potentiated SerpinB2 promoter activity in response to LPS (Fig. 8C, right). These data suggest that phosphorylation of C/EBP-β at S64 acts to negatively regulate SerpinB2 proximal promoter activity."}

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C/EBP-βT188 is implicated in regulating DAPK1, an IFNγ-inducible gene involved in the regulation of cell cycle and apoptosis [38], processes with which SerpinB2 has also been associated [17]. C/EBP-βS64 is important for LPS-induced transcription of the cytokines IL-6 and MCP-1 [64]. Similarly, SerpinB2 is induced by LPS and regulated in a manner similar to cytokines [29]. Given the similarities in the functional significance of these phospho-specific isoforms of C/EBP-β and SerpinB2, we investigated whether these phospho-acceptor sites may play a role in SerpinB2 gene expression. C/EBP-βT188A-transfected MEFs exhibited SerpinB2 promoter activity similar to that of wild-type C/EBP-β-transfected MEFs, whereas the expression of C/EBP-βS64A potentiated SerpinB2 promoter activity in response to LPS (Fig. 8C, right). These data suggest that phosphorylation of C/EBP-β at S64 acts to negatively regulate SerpinB2 proximal promoter activity."}

{"project":"bionlp-st-ge-2016-coref","denotations":[{"id":"T16609","span":{"begin":28,"end":49},"obj":"Antecedent"},{"id":"T16608","span":{"begin":685,"end":713},"obj":"Anaphor"}],"relations":[{"id":"R12094","pred":"boundBy","subj":"T16608","obj":"T16609"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"C/EBP-β contains additional phosphorylation sites, C/EBP-βT188 and C/EBP-βS64 (Fig. 8B), which may be involved in modulating C/EBP-β-dependent SerpinB2 gene transcription. C/EBP-βT188 is implicated in regulating DAPK1, an IFNγ-inducible gene involved in the regulation of cell cycle and apoptosis [38], processes with which SerpinB2 has also been associated [17]. C/EBP-βS64 is important for LPS-induced transcription of the cytokines IL-6 and MCP-1 [64]. Similarly, SerpinB2 is induced by LPS and regulated in a manner similar to cytokines [29]. Given the similarities in the functional significance of these phospho-specific isoforms of C/EBP-β and SerpinB2, we investigated whether these phospho-acceptor sites may play a role in SerpinB2 gene expression. C/EBP-βT188A-transfected MEFs exhibited SerpinB2 promoter activity similar to that of wild-type C/EBP-β-transfected MEFs, whereas the expression of C/EBP-βS64A potentiated SerpinB2 promoter activity in response to LPS (Fig. 8C, right). These data suggest that phosphorylation of C/EBP-β at S64 acts to negatively regulate SerpinB2 proximal promoter activity."}

{"project":"bionlp-st-ge-2016-test-proteins","denotations":[{"id":"T16635","span":{"begin":237,"end":241},"obj":"Protein"},{"id":"T16649","span":{"begin":1081,"end":1089},"obj":"Protein"},{"id":"T16648","span":{"begin":1038,"end":1045},"obj":"Protein"},{"id":"T16647","span":{"begin":931,"end":939},"obj":"Protein"},{"id":"T16646","span":{"begin":907,"end":918},"obj":"Protein"},{"id":"T16645","span":{"begin":855,"end":862},"obj":"Protein"},{"id":"T16644","span":{"begin":799,"end":807},"obj":"Protein"},{"id":"T16643","span":{"begin":759,"end":771},"obj":"Protein"},{"id":"T16642","span":{"begin":733,"end":741},"obj":"Protein"},{"id":"T16641","span":{"begin":651,"end":659},"obj":"Protein"},{"id":"T16640","span":{"begin":639,"end":646},"obj":"Protein"},{"id":"T16639","span":{"begin":467,"end":475},"obj":"Protein"},{"id":"T16638","span":{"begin":444,"end":449},"obj":"Protein"},{"id":"T16637","span":{"begin":435,"end":439},"obj":"Protein"},{"id":"T16636","span":{"begin":324,"end":332},"obj":"Protein"},{"id":"T16634","span":{"begin":222,"end":226},"obj":"Protein"},{"id":"T16633","span":{"begin":212,"end":217},"obj":"Protein"},{"id":"T16632","span":{"begin":143,"end":151},"obj":"Protein"},{"id":"T16631","span":{"begin":125,"end":132},"obj":"Protein"},{"id":"T16630","span":{"begin":0,"end":7},"obj":"Protein"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"C/EBP-β contains additional phosphorylation sites, C/EBP-βT188 and C/EBP-βS64 (Fig. 8B), which may be involved in modulating C/EBP-β-dependent SerpinB2 gene transcription. C/EBP-βT188 is implicated in regulating DAPK1, an IFNγ-inducible gene involved in the regulation of cell cycle and apoptosis [38], processes with which SerpinB2 has also been associated [17]. C/EBP-βS64 is important for LPS-induced transcription of the cytokines IL-6 and MCP-1 [64]. Similarly, SerpinB2 is induced by LPS and regulated in a manner similar to cytokines [29]. Given the similarities in the functional significance of these phospho-specific isoforms of C/EBP-β and SerpinB2, we investigated whether these phospho-acceptor sites may play a role in SerpinB2 gene expression. C/EBP-βT188A-transfected MEFs exhibited SerpinB2 promoter activity similar to that of wild-type C/EBP-β-transfected MEFs, whereas the expression of C/EBP-βS64A potentiated SerpinB2 promoter activity in response to LPS (Fig. 8C, right). These data suggest that phosphorylation of C/EBP-β at S64 acts to negatively regulate SerpinB2 proximal promoter activity."}

{"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T17216","span":{"begin":435,"end":439},"obj":"http://www.uniprot.org/uniprot/P05231"},{"id":"T17215","span":{"begin":212,"end":217},"obj":"http://www.uniprot.org/uniprot/P53355"},{"id":"T17212","span":{"begin":1081,"end":1089},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T17211","span":{"begin":931,"end":939},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T17210","span":{"begin":799,"end":807},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T17209","span":{"begin":733,"end":741},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T17208","span":{"begin":651,"end":659},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T17207","span":{"begin":467,"end":475},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T17206","span":{"begin":324,"end":332},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T17205","span":{"begin":143,"end":151},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T17194","span":{"begin":855,"end":862},"obj":"http://www.uniprot.org/uniprot/P28033"},{"id":"T17193","span":{"begin":639,"end":646},"obj":"http://www.uniprot.org/uniprot/P28033"},{"id":"T17192","span":{"begin":125,"end":132},"obj":"http://www.uniprot.org/uniprot/P28033"},{"id":"T17191","span":{"begin":0,"end":7},"obj":"http://www.uniprot.org/uniprot/P28033"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"C/EBP-β contains additional phosphorylation sites, C/EBP-βT188 and C/EBP-βS64 (Fig. 8B), which may be involved in modulating C/EBP-β-dependent SerpinB2 gene transcription. C/EBP-βT188 is implicated in regulating DAPK1, an IFNγ-inducible gene involved in the regulation of cell cycle and apoptosis [38], processes with which SerpinB2 has also been associated [17]. C/EBP-βS64 is important for LPS-induced transcription of the cytokines IL-6 and MCP-1 [64]. Similarly, SerpinB2 is induced by LPS and regulated in a manner similar to cytokines [29]. Given the similarities in the functional significance of these phospho-specific isoforms of C/EBP-β and SerpinB2, we investigated whether these phospho-acceptor sites may play a role in SerpinB2 gene expression. C/EBP-βT188A-transfected MEFs exhibited SerpinB2 promoter activity similar to that of wild-type C/EBP-β-transfected MEFs, whereas the expression of C/EBP-βS64A potentiated SerpinB2 promoter activity in response to LPS (Fig. 8C, right). These data suggest that phosphorylation of C/EBP-β at S64 acts to negatively regulate SerpinB2 proximal promoter activity."}

{"project":"GO-BP","denotations":[{"id":"T16680","span":{"begin":444,"end":447},"obj":"http://purl.obolibrary.org/obo/GO_0004298"},{"id":"T16679","span":{"begin":287,"end":296},"obj":"http://purl.obolibrary.org/obo/GO_0097194"},{"id":"T16678","span":{"begin":287,"end":296},"obj":"http://purl.obolibrary.org/obo/GO_0006915"},{"id":"T16677","span":{"begin":272,"end":282},"obj":"http://purl.obolibrary.org/obo/GO_0007049"},{"id":"T16676","span":{"begin":258,"end":282},"obj":"http://purl.obolibrary.org/obo/GO_0071156"},{"id":"T16675","span":{"begin":258,"end":282},"obj":"http://purl.obolibrary.org/obo/GO_0045786"},{"id":"T16674","span":{"begin":258,"end":282},"obj":"http://purl.obolibrary.org/obo/GO_0007346"},{"id":"T16673","span":{"begin":258,"end":282},"obj":"http://purl.obolibrary.org/obo/GO_0045787"},{"id":"T16672","span":{"begin":258,"end":282},"obj":"http://purl.obolibrary.org/obo/GO_0032465"},{"id":"T16671","span":{"begin":258,"end":282},"obj":"http://purl.obolibrary.org/obo/GO_0010564"},{"id":"T16670","span":{"begin":258,"end":282},"obj":"http://purl.obolibrary.org/obo/GO_1901976"},{"id":"T16669","span":{"begin":258,"end":282},"obj":"http://purl.obolibrary.org/obo/GO_0051445"},{"id":"T16668","span":{"begin":258,"end":282},"obj":"http://purl.obolibrary.org/obo/GO_0051726"},{"id":"T16667","span":{"begin":961,"end":976},"obj":"http://purl.obolibrary.org/obo/GO_0032496"},{"id":"T16665","span":{"begin":949,"end":969},"obj":"http://purl.obolibrary.org/obo/GO_0014823"},{"id":"T16663","span":{"begin":258,"end":268},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T16661","span":{"begin":404,"end":417},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T16660","span":{"begin":157,"end":170},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T16658","span":{"begin":742,"end":757},"obj":"http://purl.obolibrary.org/obo/GO_0010467"},{"id":"T16655","span":{"begin":1019,"end":1034},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T16654","span":{"begin":28,"end":43},"obj":"http://purl.obolibrary.org/obo/GO_0016310"}],"text":"C/EBP-β contains additional phosphorylation sites, C/EBP-βT188 and C/EBP-βS64 (Fig. 8B), which may be involved in modulating C/EBP-β-dependent SerpinB2 gene transcription. C/EBP-βT188 is implicated in regulating DAPK1, an IFNγ-inducible gene involved in the regulation of cell cycle and apoptosis [38], processes with which SerpinB2 has also been associated [17]. C/EBP-βS64 is important for LPS-induced transcription of the cytokines IL-6 and MCP-1 [64]. Similarly, SerpinB2 is induced by LPS and regulated in a manner similar to cytokines [29]. Given the similarities in the functional significance of these phospho-specific isoforms of C/EBP-β and SerpinB2, we investigated whether these phospho-acceptor sites may play a role in SerpinB2 gene expression. C/EBP-βT188A-transfected MEFs exhibited SerpinB2 promoter activity similar to that of wild-type C/EBP-β-transfected MEFs, whereas the expression of C/EBP-βS64A potentiated SerpinB2 promoter activity in response to LPS (Fig. 8C, right). These data suggest that phosphorylation of C/EBP-β at S64 acts to negatively regulate SerpinB2 proximal promoter activity."}

{"project":"GO-MF","denotations":[{"id":"T16682","span":{"begin":444,"end":447},"obj":"http://purl.obolibrary.org/obo/GO_0004298"},{"id":"T16681","span":{"begin":435,"end":439},"obj":"http://purl.obolibrary.org/obo/GO_0005138"}],"text":"C/EBP-β contains additional phosphorylation sites, C/EBP-βT188 and C/EBP-βS64 (Fig. 8B), which may be involved in modulating C/EBP-β-dependent SerpinB2 gene transcription. C/EBP-βT188 is implicated in regulating DAPK1, an IFNγ-inducible gene involved in the regulation of cell cycle and apoptosis [38], processes with which SerpinB2 has also been associated [17]. C/EBP-βS64 is important for LPS-induced transcription of the cytokines IL-6 and MCP-1 [64]. Similarly, SerpinB2 is induced by LPS and regulated in a manner similar to cytokines [29]. Given the similarities in the functional significance of these phospho-specific isoforms of C/EBP-β and SerpinB2, we investigated whether these phospho-acceptor sites may play a role in SerpinB2 gene expression. C/EBP-βT188A-transfected MEFs exhibited SerpinB2 promoter activity similar to that of wild-type C/EBP-β-transfected MEFs, whereas the expression of C/EBP-βS64A potentiated SerpinB2 promoter activity in response to LPS (Fig. 8C, right). These data suggest that phosphorylation of C/EBP-β at S64 acts to negatively regulate SerpinB2 proximal promoter activity."}

{"project":"GO-CC","denotations":[{"id":"T16683","span":{"begin":272,"end":276},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"C/EBP-β contains additional phosphorylation sites, C/EBP-βT188 and C/EBP-βS64 (Fig. 8B), which may be involved in modulating C/EBP-β-dependent SerpinB2 gene transcription. C/EBP-βT188 is implicated in regulating DAPK1, an IFNγ-inducible gene involved in the regulation of cell cycle and apoptosis [38], processes with which SerpinB2 has also been associated [17]. C/EBP-βS64 is important for LPS-induced transcription of the cytokines IL-6 and MCP-1 [64]. Similarly, SerpinB2 is induced by LPS and regulated in a manner similar to cytokines [29]. Given the similarities in the functional significance of these phospho-specific isoforms of C/EBP-β and SerpinB2, we investigated whether these phospho-acceptor sites may play a role in SerpinB2 gene expression. C/EBP-βT188A-transfected MEFs exhibited SerpinB2 promoter activity similar to that of wild-type C/EBP-β-transfected MEFs, whereas the expression of C/EBP-βS64A potentiated SerpinB2 promoter activity in response to LPS (Fig. 8C, right). These data suggest that phosphorylation of C/EBP-β at S64 acts to negatively regulate SerpinB2 proximal promoter activity."}

{"project":"sentences","denotations":[{"id":"T16500","span":{"begin":456,"end":546},"obj":"Sentence"},{"id":"T16499","span":{"begin":364,"end":455},"obj":"Sentence"},{"id":"T16498","span":{"begin":172,"end":363},"obj":"Sentence"},{"id":"T16497","span":{"begin":0,"end":171},"obj":"Sentence"},{"id":"T16503","span":{"begin":995,"end":1117},"obj":"Sentence"},{"id":"T16502","span":{"begin":759,"end":994},"obj":"Sentence"},{"id":"T16501","span":{"begin":547,"end":758},"obj":"Sentence"},{"id":"T237","span":{"begin":0,"end":171},"obj":"Sentence"},{"id":"T238","span":{"begin":172,"end":363},"obj":"Sentence"},{"id":"T239","span":{"begin":364,"end":455},"obj":"Sentence"},{"id":"T240","span":{"begin":456,"end":546},"obj":"Sentence"},{"id":"T241","span":{"begin":547,"end":758},"obj":"Sentence"},{"id":"T242","span":{"begin":759,"end":994},"obj":"Sentence"},{"id":"T243","span":{"begin":995,"end":1117},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"C/EBP-β contains additional phosphorylation sites, C/EBP-βT188 and C/EBP-βS64 (Fig. 8B), which may be involved in modulating C/EBP-β-dependent SerpinB2 gene transcription. C/EBP-βT188 is implicated in regulating DAPK1, an IFNγ-inducible gene involved in the regulation of cell cycle and apoptosis [38], processes with which SerpinB2 has also been associated [17]. C/EBP-βS64 is important for LPS-induced transcription of the cytokines IL-6 and MCP-1 [64]. Similarly, SerpinB2 is induced by LPS and regulated in a manner similar to cytokines [29]. Given the similarities in the functional significance of these phospho-specific isoforms of C/EBP-β and SerpinB2, we investigated whether these phospho-acceptor sites may play a role in SerpinB2 gene expression. C/EBP-βT188A-transfected MEFs exhibited SerpinB2 promoter activity similar to that of wild-type C/EBP-β-transfected MEFs, whereas the expression of C/EBP-βS64A potentiated SerpinB2 promoter activity in response to LPS (Fig. 8C, right). These data suggest that phosphorylation of C/EBP-β at S64 acts to negatively regulate SerpinB2 proximal promoter activity."}

{"project":"simple1","denotations":[{"id":"T16723","span":{"begin":1081,"end":1089},"obj":"Protein"},{"id":"T16722","span":{"begin":1038,"end":1045},"obj":"Protein"},{"id":"T16721","span":{"begin":931,"end":939},"obj":"Protein"},{"id":"T16720","span":{"begin":907,"end":918},"obj":"Protein"},{"id":"T16719","span":{"begin":855,"end":862},"obj":"Protein"},{"id":"T16718","span":{"begin":799,"end":807},"obj":"Protein"},{"id":"T16717","span":{"begin":759,"end":771},"obj":"Protein"},{"id":"T16716","span":{"begin":733,"end":741},"obj":"Protein"},{"id":"T16715","span":{"begin":651,"end":659},"obj":"Protein"},{"id":"T16714","span":{"begin":639,"end":646},"obj":"Protein"},{"id":"T16713","span":{"begin":467,"end":475},"obj":"Protein"},{"id":"T16712","span":{"begin":444,"end":449},"obj":"Protein"},{"id":"T16711","span":{"begin":435,"end":439},"obj":"Protein"},{"id":"T16710","span":{"begin":324,"end":332},"obj":"Protein"},{"id":"T16709","span":{"begin":237,"end":241},"obj":"Protein"},{"id":"T16708","span":{"begin":222,"end":226},"obj":"Protein"},{"id":"T16707","span":{"begin":212,"end":217},"obj":"Protein"},{"id":"T16706","span":{"begin":143,"end":151},"obj":"Protein"},{"id":"T16705","span":{"begin":125,"end":132},"obj":"Protein"},{"id":"T16704","span":{"begin":0,"end":7},"obj":"Protein"}],"text":"C/EBP-β contains additional phosphorylation sites, C/EBP-βT188 and C/EBP-βS64 (Fig. 8B), which may be involved in modulating C/EBP-β-dependent SerpinB2 gene transcription. C/EBP-βT188 is implicated in regulating DAPK1, an IFNγ-inducible gene involved in the regulation of cell cycle and apoptosis [38], processes with which SerpinB2 has also been associated [17]. C/EBP-βS64 is important for LPS-induced transcription of the cytokines IL-6 and MCP-1 [64]. Similarly, SerpinB2 is induced by LPS and regulated in a manner similar to cytokines [29]. Given the similarities in the functional significance of these phospho-specific isoforms of C/EBP-β and SerpinB2, we investigated whether these phospho-acceptor sites may play a role in SerpinB2 gene expression. C/EBP-βT188A-transfected MEFs exhibited SerpinB2 promoter activity similar to that of wild-type C/EBP-β-transfected MEFs, whereas the expression of C/EBP-βS64A potentiated SerpinB2 promoter activity in response to LPS (Fig. 8C, right). These data suggest that phosphorylation of C/EBP-β at S64 acts to negatively regulate SerpinB2 proximal promoter activity."}

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C/EBP-βT188 is implicated in regulating DAPK1, an IFNγ-inducible gene involved in the regulation of cell cycle and apoptosis [38], processes with which SerpinB2 has also been associated [17]. C/EBP-βS64 is important for LPS-induced transcription of the cytokines IL-6 and MCP-1 [64]. Similarly, SerpinB2 is induced by LPS and regulated in a manner similar to cytokines [29]. Given the similarities in the functional significance of these phospho-specific isoforms of C/EBP-β and SerpinB2, we investigated whether these phospho-acceptor sites may play a role in SerpinB2 gene expression. C/EBP-βT188A-transfected MEFs exhibited SerpinB2 promoter activity similar to that of wild-type C/EBP-β-transfected MEFs, whereas the expression of C/EBP-βS64A potentiated SerpinB2 promoter activity in response to LPS (Fig. 8C, right). These data suggest that phosphorylation of C/EBP-β at S64 acts to negatively regulate SerpinB2 proximal promoter activity."}

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C/EBP-βT188 is implicated in regulating DAPK1, an IFNγ-inducible gene involved in the regulation of cell cycle and apoptosis [38], processes with which SerpinB2 has also been associated [17]. C/EBP-βS64 is important for LPS-induced transcription of the cytokines IL-6 and MCP-1 [64]. Similarly, SerpinB2 is induced by LPS and regulated in a manner similar to cytokines [29]. Given the similarities in the functional significance of these phospho-specific isoforms of C/EBP-β and SerpinB2, we investigated whether these phospho-acceptor sites may play a role in SerpinB2 gene expression. C/EBP-βT188A-transfected MEFs exhibited SerpinB2 promoter activity similar to that of wild-type C/EBP-β-transfected MEFs, whereas the expression of C/EBP-βS64A potentiated SerpinB2 promoter activity in response to LPS (Fig. 8C, right). These data suggest that phosphorylation of C/EBP-β at S64 acts to negatively regulate SerpinB2 proximal promoter activity."}

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