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bio-NER-relations

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Knowledgator Engineering 141

[ { "id": "170", "type": "<BB_NULL_STR>", "text": [ "Here, we show that GerE binds near the sigK transcriptional start site, to act as a repressor." ], "offsets": [ [ 0, 94 ] ] } ]

[ { "id": "169-agent-4", "type": "agent", "text": [ "GerE" ], "offsets": [ [ 19, 23 ] ], "normalized": [] }, { "id": "169-target-8", "type": "target", "text": [ "sigK" ], "offsets": [ [ 39, 43 ] ], "normalized": [] } ]

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[ { "id": "171", "type": "genic_interaction", "arg1_id": "169-agent-4", "arg2_id": "169-target-8", "normalized": [] } ]

[ { "id": "173", "type": "<BB_NULL_STR>", "text": [ "We show that GerE binds to two sites that span the -35 region of the cotD promoter." ], "offsets": [ [ 0, 83 ] ] } ]

[ { "id": "172-agent-3", "type": "agent", "text": [ "GerE" ], "offsets": [ [ 13, 17 ] ], "normalized": [] }, { "id": "172-target-15", "type": "target", "text": [ "cotD" ], "offsets": [ [ 69, 73 ] ], "normalized": [] } ]

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[ { "id": "174", "type": "genic_interaction", "arg1_id": "172-agent-3", "arg2_id": "172-target-15", "normalized": [] } ]

[ { "id": "176", "type": "<BB_NULL_STR>", "text": [ "The ald promoter, like the sigE promoter, is believed to be recognized by sigmaA RNA polymerase, suggesting that sigmaK may inhibit sigmaA activity late in sporulation." ], "offsets": [ [ 0, 168 ] ] } ]

[ { "id": "175-agent-13", "type": "agent", "text": [ "sigmaA" ], "offsets": [ [ 74, 80 ] ], "normalized": [] }, { "id": "175-agent-18", "type": "agent", "text": [ "sigmaK" ], "offsets": [ [ 113, 119 ] ], "normalized": [] }, { "id": "175-target-1", "type": "target", "text": [ "ald" ], "offsets": [ [ 4, 7 ] ], "normalized": [] }, { "id": "175-target-21", "type": "target", "text": [ "sigmaA" ], "offsets": [ [ 132, 138 ] ], "normalized": [] } ]

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[ { "id": "177", "type": "genic_interaction", "arg1_id": "175-agent-13", "arg2_id": "175-target-1", "normalized": [] }, { "id": "178", "type": "genic_interaction", "arg1_id": "175-agent-18", "arg2_id": "175-target-21", "normalized": [] } ]

[ { "id": "180", "type": "<BB_NULL_STR>", "text": [ "During endospore formation in Bacillus subtilis, the DNA binding protein GerE stimulates transcription from several promoters that are used by RNA polymerase containing sigmaK" ], "offsets": [ [ 0, 175 ] ] } ]

[ { "id": "179-agent-9", "type": "agent", "text": [ "GerE" ], "offsets": [ [ 73, 77 ] ], "normalized": [] }, { "id": "179-target-22", "type": "target", "text": [ "sigmaK" ], "offsets": [ [ 169, 175 ] ], "normalized": [] } ]

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[ { "id": "181", "type": "genic_interaction", "arg1_id": "179-agent-9", "arg2_id": "179-target-22", "normalized": [] } ]

[ { "id": "183", "type": "<BB_NULL_STR>", "text": [ "The -10 and -35 sequences of the sigmaB- and sigmaF-dependent promoters of katX overlap, and the transcriptional start points used by EsigmaB and EsigmaF differ by only one nucleotide." ], "offsets": [ [ 0, 184 ] ] } ]

[ { "id": "182-agent-7", "type": "agent", "text": [ "sigmaB" ], "offsets": [ [ 33, 39 ] ], "normalized": [] }, { "id": "182-agent-9", "type": "agent", "text": [ "sigmaF" ], "offsets": [ [ 45, 51 ] ], "normalized": [] }, { "id": "182-target-13", "type": "target", "text": [ "katX" ], "offsets": [ [ 75, 79 ] ], "normalized": [] } ]

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[ { "id": "184", "type": "genic_interaction", "arg1_id": "182-agent-7", "arg2_id": "182-target-13", "normalized": [] }, { "id": "185", "type": "genic_interaction", "arg1_id": "182-agent-9", "arg2_id": "182-target-13", "normalized": [] } ]

[ { "id": "187", "type": "<BB_NULL_STR>", "text": [ "DNase I footprinting showed that SpoIIID binds strongly to two sites in the cotC promoter region, binds weakly to one site in the cotX promoter, and does not bind specifically to cotB." ], "offsets": [ [ 0, 184 ] ] } ]

[ { "id": "186-agent-5", "type": "agent", "text": [ "SpoIIID" ], "offsets": [ [ 33, 40 ] ], "normalized": [] }, { "id": "186-target-13", "type": "target", "text": [ "cotC" ], "offsets": [ [ 76, 80 ] ], "normalized": [] }, { "id": "186-target-23", "type": "target", "text": [ "cotX" ], "offsets": [ [ 130, 134 ] ], "normalized": [] }, { "id": "186-target-31", "type": "target", "text": [ "cotB" ], "offsets": [ [ 179, 183 ] ], "normalized": [] } ]

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[ { "id": "188", "type": "genic_interaction", "arg1_id": "186-agent-5", "arg2_id": "186-target-13", "normalized": [] }, { "id": "189", "type": "genic_interaction", "arg1_id": "186-agent-5", "arg2_id": "186-target-23", "normalized": [] }, { "id": "190", "type": "genic_interaction", "arg1_id": "186-agent-5", "arg2_id": "186-target-31", "normalized": [] } ]

[ { "id": "192", "type": "<BB_NULL_STR>", "text": [ "However, the mutant was unable to stimulate transcription by final sigma(A)-RNA polymerase from the Spo0A-dependent spoIIG operon promoter." ], "offsets": [ [ 0, 139 ] ] } ]

[ { "id": "191-agent-15", "type": "agent", "text": [ "Spo0A" ], "offsets": [ [ 100, 105 ] ], "normalized": [] }, { "id": "191-agent-10", "type": "agent", "text": [ "sigma(A)" ], "offsets": [ [ 67, 75 ] ], "normalized": [] }, { "id": "191-target-17", "type": "target", "text": [ "spoIIG" ], "offsets": [ [ 116, 122 ] ], "normalized": [] }, { "id": "191-target-10", "type": "target", "text": [ "sigma(A)" ], "offsets": [ [ 67, 75 ] ], "normalized": [] } ]

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[ { "id": "193", "type": "genic_interaction", "arg1_id": "191-agent-15", "arg2_id": "191-target-17", "normalized": [] }, { "id": "194", "type": "genic_interaction", "arg1_id": "191-agent-10", "arg2_id": "191-target-17", "normalized": [] }, { "id": "195", "type": "genic_interaction", "arg1_id": "191-agent-15", "arg2_id": "191-target-10", "normalized": [] } ]

[ { "id": "197", "type": "<BB_NULL_STR>", "text": [ "Therefore, ftsY is solely expressed during sporulation from a sigma(K)- and GerE-controlled promoter that is located immediately upstream of ftsY inside the smc gene." ], "offsets": [ [ 0, 166 ] ] } ]

[ { "id": "196-agent-9", "type": "agent", "text": [ "sigma(K)" ], "offsets": [ [ 62, 70 ] ], "normalized": [] }, { "id": "196-agent-11", "type": "agent", "text": [ "GerE" ], "offsets": [ [ 76, 80 ] ], "normalized": [] }, { "id": "196-target-1", "type": "target", "text": [ "ftsY" ], "offsets": [ [ 11, 15 ] ], "normalized": [] } ]

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[ { "id": "198", "type": "genic_interaction", "arg1_id": "196-agent-9", "arg2_id": "196-target-1", "normalized": [] }, { "id": "199", "type": "genic_interaction", "arg1_id": "196-agent-11", "arg2_id": "196-target-1", "normalized": [] } ]

[ { "id": "201", "type": "<BB_NULL_STR>", "text": [ "The ydaP gene might belong to the increasing number of sigmaB-dependent genes whose orthologues are under the control of sigmas in Escherichia coli, indicating that both regulons may fulfil similar functions." ], "offsets": [ [ 0, 208 ] ] } ]

[ { "id": "200-agent-10", "type": "agent", "text": [ "sigmaB" ], "offsets": [ [ 55, 61 ] ], "normalized": [] }, { "id": "200-target-1", "type": "target", "text": [ "ydaP" ], "offsets": [ [ 4, 8 ] ], "normalized": [] } ]

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[ { "id": "202", "type": "genic_interaction", "arg1_id": "200-agent-10", "arg2_id": "200-target-1", "normalized": [] } ]

[ { "id": "204", "type": "<BB_NULL_STR>", "text": [ "This indicates that the yvyD gene product, being a member of both the sigmaB and sigmaH regulons, might negatively regulate the activity of the sigmaL regulon." ], "offsets": [ [ 0, 159 ] ] } ]

[ { "id": "203-agent-13", "type": "agent", "text": [ "sigmaB" ], "offsets": [ [ 70, 76 ] ], "normalized": [] }, { "id": "203-agent-15", "type": "agent", "text": [ "sigmaH" ], "offsets": [ [ 81, 87 ] ], "normalized": [] }, { "id": "203-agent-4", "type": "agent", "text": [ "yvyD" ], "offsets": [ [ 24, 28 ] ], "normalized": [] }, { "id": "203-target-4", "type": "target", "text": [ "yvyD" ], "offsets": [ [ 24, 28 ] ], "normalized": [] }, { "id": "203-target-24", "type": "target", "text": [ "sigmaL" ], "offsets": [ [ 144, 150 ] ], "normalized": [] } ]

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[ { "id": "205", "type": "genic_interaction", "arg1_id": "203-agent-13", "arg2_id": "203-target-4", "normalized": [] }, { "id": "206", "type": "genic_interaction", "arg1_id": "203-agent-15", "arg2_id": "203-target-4", "normalized": [] }, { "id": "207", "type": "genic_interaction", "arg1_id": "203-agent-4", "arg2_id": "203-target-24", "normalized": [] } ]

[ { "id": "209", "type": "<BB_NULL_STR>", "text": [ "In that respect sigB is similar to the previously described gene gsiB which is also a member of the sigmaB regulon." ], "offsets": [ [ 0, 115 ] ] } ]

[ { "id": "208-agent-19", "type": "agent", "text": [ "sigmaB" ], "offsets": [ [ 100, 106 ] ], "normalized": [] }, { "id": "208-target-11", "type": "target", "text": [ "gsiB" ], "offsets": [ [ 65, 69 ] ], "normalized": [] }, { "id": "208-target-3", "type": "target", "text": [ "sigB" ], "offsets": [ [ 16, 20 ] ], "normalized": [] } ]

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[ { "id": "210", "type": "genic_interaction", "arg1_id": "208-agent-19", "arg2_id": "208-target-11", "normalized": [] }, { "id": "211", "type": "genic_interaction", "arg1_id": "208-agent-19", "arg2_id": "208-target-3", "normalized": [] } ]

[ { "id": "213", "type": "<BB_NULL_STR>", "text": [ "The addition of ClpX to in vitro transcription reactions resulted in the stimulation of RNAP holoenzyme activity, but sigmaH-RNAP was observed to be more sensitive to ClpX-dependent stimulation than sigmaA-RNAP." ], "offsets": [ [ 0, 211 ] ] } ]

[ { "id": "212-agent-27", "type": "agent", "text": [ "ClpX" ], "offsets": [ [ 167, 171 ] ], "normalized": [] }, { "id": "212-agent-3", "type": "agent", "text": [ "ClpX" ], "offsets": [ [ 16, 20 ] ], "normalized": [] }, { "id": "212-target-18", "type": "target", "text": [ "sigmaH" ], "offsets": [ [ 118, 124 ] ], "normalized": [] }, { "id": "212-target-31", "type": "target", "text": [ "sigmaA" ], "offsets": [ [ 199, 205 ] ], "normalized": [] } ]

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[ { "id": "214", "type": "genic_interaction", "arg1_id": "212-agent-27", "arg2_id": "212-target-18", "normalized": [] }, { "id": "215", "type": "genic_interaction", "arg1_id": "212-agent-27", "arg2_id": "212-target-31", "normalized": [] }, { "id": "216", "type": "genic_interaction", "arg1_id": "212-agent-3", "arg2_id": "212-target-18", "normalized": [] }, { "id": "217", "type": "genic_interaction", "arg1_id": "212-agent-3", "arg2_id": "212-target-31", "normalized": [] } ]

[ { "id": "219", "type": "<BB_NULL_STR>", "text": [ "Transcription of the cotB, cotC, and cotX genes by final sigma(K) RNA polymerase is activated by a small, DNA-binding protein called GerE." ], "offsets": [ [ 0, 138 ] ] } ]

[ { "id": "218-agent-10", "type": "agent", "text": [ "sigma(K)" ], "offsets": [ [ 57, 65 ] ], "normalized": [] }, { "id": "218-agent-21", "type": "agent", "text": [ "GerE" ], "offsets": [ [ 133, 137 ] ], "normalized": [] }, { "id": "218-target-3", "type": "target", "text": [ "cotB" ], "offsets": [ [ 21, 25 ] ], "normalized": [] }, { "id": "218-target-4", "type": "target", "text": [ "cotC" ], "offsets": [ [ 27, 31 ] ], "normalized": [] }, { "id": "218-target-6", "type": "target", "text": [ "cotX" ], "offsets": [ [ 37, 41 ] ], "normalized": [] } ]

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[ { "id": "220", "type": "genic_interaction", "arg1_id": "218-agent-10", "arg2_id": "218-target-3", "normalized": [] }, { "id": "221", "type": "genic_interaction", "arg1_id": "218-agent-10", "arg2_id": "218-target-4", "normalized": [] }, { "id": "222", "type": "genic_interaction", "arg1_id": "218-agent-10", "arg2_id": "218-target-6", "normalized": [] }, { "id": "223", "type": "genic_interaction", "arg1_id": "218-agent-21", "arg2_id": "218-target-3", "normalized": [] }, { "id": "224", "type": "genic_interaction", "arg1_id": "218-agent-21", "arg2_id": "218-target-4", "normalized": [] }, { "id": "225", "type": "genic_interaction", "arg1_id": "218-agent-21", "arg2_id": "218-target-6", "normalized": [] } ]

[ { "id": "227", "type": "<BB_NULL_STR>", "text": [ "In vitro transcription experiments suggest that the differential pattern of cot gene expression results from the combined action of GerE and another transcription factor, SpoIIID." ], "offsets": [ [ 0, 179 ] ] } ]

[ { "id": "226-agent-19", "type": "agent", "text": [ "GerE" ], "offsets": [ [ 132, 136 ] ], "normalized": [] }, { "id": "226-agent-24", "type": "agent", "text": [ "SpoIIID" ], "offsets": [ [ 171, 178 ] ], "normalized": [] }, { "id": "226-target-10", "type": "target", "text": [ "cot" ], "offsets": [ [ 76, 79 ] ], "normalized": [] } ]

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[ { "id": "228", "type": "genic_interaction", "arg1_id": "226-agent-19", "arg2_id": "226-target-10", "normalized": [] }, { "id": "229", "type": "genic_interaction", "arg1_id": "226-agent-24", "arg2_id": "226-target-10", "normalized": [] } ]

[ { "id": "231", "type": "<BB_NULL_STR>", "text": [ "A low concentration of GerE activated cotB transcription by final sigma(K) RNA polymerase, whereas a higher concentration was needed to activate transcription of cotX or cotC." ], "offsets": [ [ 0, 175 ] ] } ]

[ { "id": "230-agent-4", "type": "agent", "text": [ "GerE" ], "offsets": [ [ 23, 27 ] ], "normalized": [] }, { "id": "230-agent-10", "type": "agent", "text": [ "sigma(K)" ], "offsets": [ [ 66, 74 ] ], "normalized": [] }, { "id": "230-target-6", "type": "target", "text": [ "cotB" ], "offsets": [ [ 38, 42 ] ], "normalized": [] }, { "id": "230-target-10", "type": "target", "text": [ "sigma(K)" ], "offsets": [ [ 66, 74 ] ], "normalized": [] }, { "id": "230-target-23", "type": "target", "text": [ "cotX" ], "offsets": [ [ 162, 166 ] ], "normalized": [] }, { "id": "230-target-25", "type": "target", "text": [ "cotC" ], "offsets": [ [ 170, 174 ] ], "normalized": [] } ]

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[ { "id": "232", "type": "genic_interaction", "arg1_id": "230-agent-4", "arg2_id": "230-target-6", "normalized": [] }, { "id": "233", "type": "genic_interaction", "arg1_id": "230-agent-4", "arg2_id": "230-target-10", "normalized": [] }, { "id": "234", "type": "genic_interaction", "arg1_id": "230-agent-10", "arg2_id": "230-target-6", "normalized": [] }, { "id": "235", "type": "genic_interaction", "arg1_id": "230-agent-4", "arg2_id": "230-target-23", "normalized": [] }, { "id": "236", "type": "genic_interaction", "arg1_id": "230-agent-4", "arg2_id": "230-target-25", "normalized": [] } ]

[ { "id": "238", "type": "<BB_NULL_STR>", "text": [ "SpoIIID at low concentration repressed cotC transcription, whereas a higher concentration only partially repressed cotX transcription and had little effect on cotB transcription." ], "offsets": [ [ 0, 178 ] ] } ]

[ { "id": "237-agent-0", "type": "agent", "text": [ "SpoIIID" ], "offsets": [ [ 0, 7 ] ], "normalized": [] }, { "id": "237-target-5", "type": "target", "text": [ "cotC" ], "offsets": [ [ 39, 43 ] ], "normalized": [] }, { "id": "237-target-14", "type": "target", "text": [ "cotX" ], "offsets": [ [ 115, 119 ] ], "normalized": [] }, { "id": "237-target-21", "type": "target", "text": [ "cotB" ], "offsets": [ [ 159, 163 ] ], "normalized": [] } ]

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[ { "id": "239", "type": "genic_interaction", "arg1_id": "237-agent-0", "arg2_id": "237-target-5", "normalized": [] }, { "id": "240", "type": "genic_interaction", "arg1_id": "237-agent-0", "arg2_id": "237-target-14", "normalized": [] }, { "id": "241", "type": "genic_interaction", "arg1_id": "237-agent-0", "arg2_id": "237-target-21", "normalized": [] } ]

[ { "id": "243", "type": "<BB_NULL_STR>", "text": [ "We demonstrated that katX is also a sigmaB-dependent general stress gene, since it is strongly induced by heat, salt and ethanol stress, as well as by energy depletion." ], "offsets": [ [ 0, 168 ] ] } ]

[ { "id": "242-agent-7", "type": "agent", "text": [ "sigmaB" ], "offsets": [ [ 36, 42 ] ], "normalized": [] }, { "id": "242-target-3", "type": "target", "text": [ "katX" ], "offsets": [ [ 21, 25 ] ], "normalized": [] } ]

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[ { "id": "244", "type": "genic_interaction", "arg1_id": "242-agent-7", "arg2_id": "242-target-3", "normalized": [] } ]

[ { "id": "246", "type": "<BB_NULL_STR>", "text": [ "sigmaF is controlled by a regulatory cascade involving an anti-sigma factor, SpoIIAB, an anti-anti-sigma factor, SpoIIAA, and a membrane-bound phosphatase, SpoIIE, which converts the inactive, phosphorylated form of SpoIIAA back to the active form." ], "offsets": [ [ 0, 248 ] ] } ]

[ { "id": "245-agent-11", "type": "agent", "text": [ "SpoIIAB" ], "offsets": [ [ 77, 84 ] ], "normalized": [] }, { "id": "245-agent-15", "type": "agent", "text": [ "SpoIIAA" ], "offsets": [ [ 113, 120 ] ], "normalized": [] }, { "id": "245-agent-20", "type": "agent", "text": [ "SpoIIE" ], "offsets": [ [ 156, 162 ] ], "normalized": [] }, { "id": "245-target-0", "type": "target", "text": [ "sigmaF" ], "offsets": [ [ 0, 6 ] ], "normalized": [] }, { "id": "245-target-28", "type": "target", "text": [ "SpoIIAA" ], "offsets": [ [ 216, 223 ] ], "normalized": [] } ]

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[ { "id": "247", "type": "genic_interaction", "arg1_id": "245-agent-11", "arg2_id": "245-target-0", "normalized": [] }, { "id": "248", "type": "genic_interaction", "arg1_id": "245-agent-15", "arg2_id": "245-target-0", "normalized": [] }, { "id": "249", "type": "genic_interaction", "arg1_id": "245-agent-20", "arg2_id": "245-target-0", "normalized": [] }, { "id": "250", "type": "genic_interaction", "arg1_id": "245-agent-20", "arg2_id": "245-target-28", "normalized": [] } ]

[ { "id": "252", "type": "<BB_NULL_STR>", "text": [ "Unlike the case for other sigma(54)-dependent genes, rocG has no UAS; instead, its expression depends on a sequence located 1.5 kilobases downstream of the rocG promoter, beyond the end of the rocG coding region." ], "offsets": [ [ 0, 212 ] ] } ]

[ { "id": "251-agent-5", "type": "agent", "text": [ "sigma(54)" ], "offsets": [ [ 26, 35 ] ], "normalized": [] }, { "id": "251-target-8", "type": "target", "text": [ "rocG" ], "offsets": [ [ 53, 57 ] ], "normalized": [] } ]

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[ { "id": "253", "type": "genic_interaction", "arg1_id": "251-agent-5", "arg2_id": "251-target-8", "normalized": [] } ]

[ { "id": "255", "type": "<BB_NULL_STR>", "text": [ "Although spo0H is transcriptionally regulated by the key regulatory device that controls sporulation initiation, the Spo0 phosphorelay, there is considerable evidence implicating a mechanism of post-translational control that governs the activity and concentration of sigmaH." ], "offsets": [ [ 0, 275 ] ] } ]

[ { "id": "254-agent-15", "type": "agent", "text": [ "Spo0" ], "offsets": [ [ 117, 121 ] ], "normalized": [] }, { "id": "254-target-1", "type": "target", "text": [ "spo0H" ], "offsets": [ [ 9, 14 ] ], "normalized": [] } ]

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[ { "id": "256", "type": "genic_interaction", "arg1_id": "254-agent-15", "arg2_id": "254-target-1", "normalized": [] } ]

[ { "id": "258", "type": "<BB_NULL_STR>", "text": [ "In the mother cell compartment of sporulating cells, expression of the sigE gene, encoding the earlier-acting sigma factor, sigmaE, is negatively regulated by the later-acting sigma factor, sigmaK." ], "offsets": [ [ 0, 197 ] ] } ]

[ { "id": "257-agent-27", "type": "agent", "text": [ "sigmaK" ], "offsets": [ [ 190, 196 ] ], "normalized": [] }, { "id": "257-target-11", "type": "target", "text": [ "sigE" ], "offsets": [ [ 71, 75 ] ], "normalized": [] } ]

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[ { "id": "259", "type": "genic_interaction", "arg1_id": "257-agent-27", "arg2_id": "257-target-11", "normalized": [] } ]

[ { "id": "261", "type": "<BB_NULL_STR>", "text": [ "Cell-specific activation of transcription factor sigmaF during sporulation in Bacillus subtilis requires the formation of the polar septum and the activity of a serine phosphatase (SpoIIE) located in the septum." ], "offsets": [ [ 0, 211 ] ] } ]

[ { "id": "260-agent-24", "type": "agent", "text": [ "SpoIIE" ], "offsets": [ [ 181, 187 ] ], "normalized": [] }, { "id": "260-target-5", "type": "target", "text": [ "sigmaF" ], "offsets": [ [ 49, 55 ] ], "normalized": [] } ]

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[ { "id": "262", "type": "genic_interaction", "arg1_id": "260-agent-24", "arg2_id": "260-target-5", "normalized": [] } ]

[ { "id": "264", "type": "<BB_NULL_STR>", "text": [ "The SpoIIE phosphatase indirectly activates sigmaF by dephosphorylating a protein (SpoIIAA-P) in the pathway that controls the activity of the transcription factor." ], "offsets": [ [ 0, 164 ] ] } ]

[ { "id": "263-agent-1", "type": "agent", "text": [ "SpoIIE" ], "offsets": [ [ 4, 10 ] ], "normalized": [] }, { "id": "263-agent-10", "type": "agent", "text": [ "SpoIIAA-P" ], "offsets": [ [ 83, 92 ] ], "normalized": [] }, { "id": "263-target-5", "type": "target", "text": [ "sigmaF" ], "offsets": [ [ 44, 50 ] ], "normalized": [] }, { "id": "263-target-10", "type": "target", "text": [ "SpoIIAA-P" ], "offsets": [ [ 83, 92 ] ], "normalized": [] } ]

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[ { "id": "265", "type": "genic_interaction", "arg1_id": "263-agent-1", "arg2_id": "263-target-5", "normalized": [] }, { "id": "266", "type": "genic_interaction", "arg1_id": "263-agent-1", "arg2_id": "263-target-10", "normalized": [] }, { "id": "267", "type": "genic_interaction", "arg1_id": "263-agent-10", "arg2_id": "263-target-5", "normalized": [] } ]

[ { "id": "269", "type": "<BB_NULL_STR>", "text": [ "Three new sigmaB-dependent genes (ydaE, ydaG and yfkM) encoding proteins with still unknown functions were also described." ], "offsets": [ [ 0, 122 ] ] } ]

[ { "id": "268-agent-2", "type": "agent", "text": [ "sigmaB" ], "offsets": [ [ 10, 16 ] ], "normalized": [] }, { "id": "268-target-5", "type": "target", "text": [ "ydaE" ], "offsets": [ [ 34, 38 ] ], "normalized": [] }, { "id": "268-target-6", "type": "target", "text": [ "ydaG" ], "offsets": [ [ 40, 44 ] ], "normalized": [] }, { "id": "268-target-8", "type": "target", "text": [ "yfkM" ], "offsets": [ [ 49, 53 ] ], "normalized": [] } ]

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[ { "id": "270", "type": "genic_interaction", "arg1_id": "268-agent-2", "arg2_id": "268-target-5", "normalized": [] }, { "id": "271", "type": "genic_interaction", "arg1_id": "268-agent-2", "arg2_id": "268-target-6", "normalized": [] }, { "id": "272", "type": "genic_interaction", "arg1_id": "268-agent-2", "arg2_id": "268-target-8", "normalized": [] } ]

[ { "id": "274", "type": "<BB_NULL_STR>", "text": [ "These results suggest that a rising level of GerE in sporulating cells may first activate cotD transcription from the upstream site then repress transcription as the downstream site becomes occupied." ], "offsets": [ [ 0, 199 ] ] } ]

[ { "id": "273-agent-8", "type": "agent", "text": [ "GerE" ], "offsets": [ [ 45, 49 ] ], "normalized": [] }, { "id": "273-target-15", "type": "target", "text": [ "cotD" ], "offsets": [ [ 90, 94 ] ], "normalized": [] } ]

[]

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[ { "id": "275", "type": "genic_interaction", "arg1_id": "273-agent-8", "arg2_id": "273-target-15", "normalized": [] }, { "id": "276", "type": "genic_interaction", "arg1_id": "273-agent-8", "arg2_id": "273-target-15", "normalized": [] } ]

[ { "id": "278", "type": "<BB_NULL_STR>", "text": [ "The class includes AsiA form bacteriophage T4, which inhibits Escherichia coli sigma 70; FlgM, present in both gram-positive and gram-negative bacteria, which inhibits the flagella sigma factor sigma 28; SpoIIAB, which inhibits the sporulation-specific sigma factor, sigma F and sigma G, of Bacillus subtilis; RbsW of B. subtilis, which inhibits stress response sigma factor sigma B; and DnaK, a general regulator of the heat shock response, which in bacteria inhibits the heat shock sigma factor sigma 32." ], "offsets": [ [ 0, 506 ] ] } ]

[ { "id": "277-agent-26", "type": "agent", "text": [ "SpoIIAB" ], "offsets": [ [ 204, 211 ] ], "normalized": [] }, { "id": "277-agent-11", "type": "agent", "text": [ "FlgM" ], "offsets": [ [ 89, 93 ] ], "normalized": [] }, { "id": "277-agent-38", "type": "agent", "text": [ "RbsW" ], "offsets": [ [ 310, 314 ] ], "normalized": [] }, { "id": "277-agent-49", "type": "agent", "text": [ "DnaK" ], "offsets": [ [ 388, 392 ] ], "normalized": [] }, { "id": "277-target-33", "type": "target", "text": [ "sigma F" ], "offsets": [ [ 267, 274 ] ], "normalized": [] }, { "id": "277-target-35", "type": "target", "text": [ "sigma G" ], "offsets": [ [ 279, 286 ] ], "normalized": [] }, { "id": "277-target-25", "type": "target", "text": [ "sigma 28" ], "offsets": [ [ 194, 202 ] ], "normalized": [] }, { "id": "277-target-47", "type": "target", "text": [ "sigma B" ], "offsets": [ [ 375, 382 ] ], "normalized": [] }, { "id": "277-target-67", "type": "target", "text": [ "sigma 32" ], "offsets": [ [ 497, 505 ] ], "normalized": [] } ]

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[ { "id": "279", "type": "genic_interaction", "arg1_id": "277-agent-26", "arg2_id": "277-target-33", "normalized": [] }, { "id": "280", "type": "genic_interaction", "arg1_id": "277-agent-26", "arg2_id": "277-target-35", "normalized": [] }, { "id": "281", "type": "genic_interaction", "arg1_id": "277-agent-11", "arg2_id": "277-target-25", "normalized": [] }, { "id": "282", "type": "genic_interaction", "arg1_id": "277-agent-38", "arg2_id": "277-target-47", "normalized": [] }, { "id": "283", "type": "genic_interaction", "arg1_id": "277-agent-49", "arg2_id": "277-target-67", "normalized": [] } ]

[ { "id": "285", "type": "<BB_NULL_STR>", "text": [ "We have shown previously that the transcription of degR is driven by an alternative sigma factor, sigmaD." ], "offsets": [ [ 0, 105 ] ] } ]

[ { "id": "284-agent-16", "type": "agent", "text": [ "sigmaD" ], "offsets": [ [ 98, 104 ] ], "normalized": [] }, { "id": "284-target-8", "type": "target", "text": [ "degR" ], "offsets": [ [ 51, 55 ] ], "normalized": [] } ]

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[]

[ { "id": "286", "type": "genic_interaction", "arg1_id": "284-agent-16", "arg2_id": "284-target-8", "normalized": [] } ]

[ { "id": "288", "type": "<BB_NULL_STR>", "text": [ "Finally, we show that proper localization of SpoIVA required the expression of one or more genes which, like spoIVA, are under the control of the mother cell transcription factor sigmaE." ], "offsets": [ [ 0, 186 ] ] } ]

[ { "id": "287-agent-29", "type": "agent", "text": [ "sigmaE" ], "offsets": [ [ 179, 185 ] ], "normalized": [] }, { "id": "287-target-18", "type": "target", "text": [ "spoIVA" ], "offsets": [ [ 109, 115 ] ], "normalized": [] } ]

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[]

[ { "id": "289", "type": "genic_interaction", "arg1_id": "287-agent-29", "arg2_id": "287-target-18", "normalized": [] } ]

[ { "id": "291", "type": "<BB_NULL_STR>", "text": [ "In addition to the typical sigmaB-dependent, stress- and starvation-inducible pattern, yvyD is also induced in response to amino acid depletion." ], "offsets": [ [ 0, 144 ] ] } ]

[ { "id": "290-agent-5", "type": "agent", "text": [ "sigmaB" ], "offsets": [ [ 27, 33 ] ], "normalized": [] }, { "id": "290-target-11", "type": "target", "text": [ "yvyD" ], "offsets": [ [ 87, 91 ] ], "normalized": [] } ]

[]

[]

[ { "id": "292", "type": "genic_interaction", "arg1_id": "290-agent-5", "arg2_id": "290-target-11", "normalized": [] } ]

[ { "id": "294", "type": "<BB_NULL_STR>", "text": [ "Our data demonstrate that the CtsR protein acts as a global repressor of the clpC operon, as well as other class III heat shock genes, by preventing unstressed transcription from either the sigmaB- or sigmaA-dependent promoter and might be inactivated or dissociate under inducing stress conditions." ], "offsets": [ [ 0, 299 ] ] } ]

[ { "id": "293-agent-5", "type": "agent", "text": [ "CtsR" ], "offsets": [ [ 30, 34 ] ], "normalized": [] }, { "id": "293-agent-32", "type": "agent", "text": [ "sigmaB" ], "offsets": [ [ 190, 196 ] ], "normalized": [] }, { "id": "293-agent-34", "type": "agent", "text": [ "sigmaA" ], "offsets": [ [ 201, 207 ] ], "normalized": [] }, { "id": "293-target-14", "type": "target", "text": [ "clpC" ], "offsets": [ [ 77, 81 ] ], "normalized": [] } ]

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[ { "id": "295", "type": "genic_interaction", "arg1_id": "293-agent-5", "arg2_id": "293-target-14", "normalized": [] }, { "id": "296", "type": "genic_interaction", "arg1_id": "293-agent-32", "arg2_id": "293-target-14", "normalized": [] }, { "id": "297", "type": "genic_interaction", "arg1_id": "293-agent-34", "arg2_id": "293-target-14", "normalized": [] } ]

[ { "id": "299", "type": "<BB_NULL_STR>", "text": [ "The sspH and sspL genes are recognized primarily by the forespore-specific sigma factor for RNA polymerase, sigmaG; the sspN-tlp operon is recognized equally well by sigmaG and the other forespore-specific sigma factor, sigmaF." ], "offsets": [ [ 0, 227 ] ] } ]

[ { "id": "298-agent-16", "type": "agent", "text": [ "sigmaG" ], "offsets": [ [ 108, 114 ] ], "normalized": [] }, { "id": "298-agent-26", "type": "agent", "text": [ "sigmaG" ], "offsets": [ [ 166, 172 ] ], "normalized": [] }, { "id": "298-agent-33", "type": "agent", "text": [ "sigmaF" ], "offsets": [ [ 220, 226 ] ], "normalized": [] }, { "id": "298-target-1", "type": "target", "text": [ "sspH" ], "offsets": [ [ 4, 8 ] ], "normalized": [] }, { "id": "298-target-18", "type": "target", "text": [ "sspN" ], "offsets": [ [ 120, 124 ] ], "normalized": [] }, { "id": "298-target-3", "type": "target", "text": [ "sspL" ], "offsets": [ [ 13, 17 ] ], "normalized": [] }, { "id": "298-target-19", "type": "target", "text": [ "tlp" ], "offsets": [ [ 125, 128 ] ], "normalized": [] } ]

[]

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[ { "id": "300", "type": "genic_interaction", "arg1_id": "298-agent-16", "arg2_id": "298-target-1", "normalized": [] }, { "id": "301", "type": "genic_interaction", "arg1_id": "298-agent-26", "arg2_id": "298-target-18", "normalized": [] }, { "id": "302", "type": "genic_interaction", "arg1_id": "298-agent-16", "arg2_id": "298-target-3", "normalized": [] }, { "id": "303", "type": "genic_interaction", "arg1_id": "298-agent-26", "arg2_id": "298-target-19", "normalized": [] }, { "id": "304", "type": "genic_interaction", "arg1_id": "298-agent-33", "arg2_id": "298-target-18", "normalized": [] }, { "id": "305", "type": "genic_interaction", "arg1_id": "298-agent-33", "arg2_id": "298-target-19", "normalized": [] } ]

[ { "id": "307", "type": "<BB_NULL_STR>", "text": [ "GerE binds to a site on one of these promoters, cotX, that overlaps its -35 region." ], "offsets": [ [ 0, 83 ] ] } ]

[ { "id": "306-agent-0", "type": "agent", "text": [ "GerE" ], "offsets": [ [ 0, 4 ] ], "normalized": [] }, { "id": "306-target-10", "type": "target", "text": [ "cotX" ], "offsets": [ [ 48, 52 ] ], "normalized": [] } ]

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[]

[ { "id": "308", "type": "genic_interaction", "arg1_id": "306-agent-0", "arg2_id": "306-target-10", "normalized": [] } ]

[ { "id": "310", "type": "<BB_NULL_STR>", "text": [ "The sigma W regulon includes a penicillin binding protein (PBP4*) and a co-transcribed amino acid racemase (RacX), homologues of signal peptide peptidase (YteI), flotillin (YuaG), ABC transporters (YknXYZ), non-haem bromoperoxidase (YdjP), epoxide hydrolase (YfhM) and three small peptides with structural similarities to bacteriocin precursor polypeptides." ], "offsets": [ [ 0, 357 ] ] } ]

[ { "id": "309-agent-1", "type": "agent", "text": [ "sigma W" ], "offsets": [ [ 4, 11 ] ], "normalized": [] }, { "id": "309-target-8", "type": "target", "text": [ "PBP4*" ], "offsets": [ [ 59, 64 ] ], "normalized": [] }, { "id": "309-target-15", "type": "target", "text": [ "RacX" ], "offsets": [ [ 108, 112 ] ], "normalized": [] }, { "id": "309-target-21", "type": "target", "text": [ "YteI" ], "offsets": [ [ 155, 159 ] ], "normalized": [] }, { "id": "309-target-23", "type": "target", "text": [ "YuaG" ], "offsets": [ [ 173, 177 ] ], "normalized": [] }, { "id": "309-target-26", "type": "target", "text": [ "YknXYZ" ], "offsets": [ [ 198, 204 ] ], "normalized": [] }, { "id": "309-target-29", "type": "target", "text": [ "YdjP" ], "offsets": [ [ 233, 237 ] ], "normalized": [] }, { "id": "309-target-32", "type": "target", "text": [ "YfhM" ], "offsets": [ [ 259, 263 ] ], "normalized": [] } ]

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[ { "id": "311", "type": "genic_interaction", "arg1_id": "309-agent-1", "arg2_id": "309-target-8", "normalized": [] }, { "id": "312", "type": "genic_interaction", "arg1_id": "309-agent-1", "arg2_id": "309-target-15", "normalized": [] }, { "id": "313", "type": "genic_interaction", "arg1_id": "309-agent-1", "arg2_id": "309-target-21", "normalized": [] }, { "id": "314", "type": "genic_interaction", "arg1_id": "309-agent-1", "arg2_id": "309-target-23", "normalized": [] }, { "id": "315", "type": "genic_interaction", "arg1_id": "309-agent-1", "arg2_id": "309-target-26", "normalized": [] }, { "id": "316", "type": "genic_interaction", "arg1_id": "309-agent-1", "arg2_id": "309-target-29", "normalized": [] }, { "id": "317", "type": "genic_interaction", "arg1_id": "309-agent-1", "arg2_id": "309-target-32", "normalized": [] } ]

[ { "id": "BioInfer.d0.s0__text", "type": "Sentence", "text": [ "alpha-catenin inhibits beta-catenin signaling by preventing formation of a beta-catenin*T-cell factor*DNA complex." ], "offsets": [ [ 0, 114 ] ] } ]

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[ { "id": "BioInfer.d1.s0__text", "type": "Sentence", "text": [ "A binary complex of birch profilin and skeletal muscle actin could be isolated by gel chromatography." ], "offsets": [ [ 0, 101 ] ] } ]

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[ { "id": "BioInfer.d1.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d1.s0.e0", "arg2_id": "BioInfer.d1.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d1.s1__text", "type": "Sentence", "text": [ "Birch profilin increased the critical concentration required for muscle and brain actin polymerization in a concentration-dependent manner, supporting the notion of the formation of a heterologous complex between the plant protein and animal actin." ], "offsets": [ [ 0, 248 ] ] } ]

[ { "id": "BioInfer.d1.s1.e0", "type": "Individual_protein", "text": [ "brain actin" ], "offsets": [ [ 76, 87 ] ], "normalized": [] }, { "id": "BioInfer.d1.s1.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 6, 14 ] ], "normalized": [] }, { "id": "BioInfer.d1.s1.e2", "type": "Individual_protein", "text": [ "muscle", "actin" ], "offsets": [ [ 65, 71 ], [ 82, 87 ] ], "normalized": [] }, { "id": "BioInfer.d1.s1.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 242, 247 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d1.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d1.s1.e0", "arg2_id": "BioInfer.d1.s1.e1", "normalized": [] }, { "id": "BioInfer.d1.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d1.s1.e1", "arg2_id": "BioInfer.d1.s1.e2", "normalized": [] }, { "id": "BioInfer.d1.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d1.s1.e1", "arg2_id": "BioInfer.d1.s1.e3", "normalized": [] } ]

[ { "id": "BioInfer.d1.s2__text", "type": "Sentence", "text": [ "Interaction of plant profilin with mammalian actin." ], "offsets": [ [ 0, 51 ] ] } ]

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[ { "id": "BioInfer.d1.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d1.s2.e0", "arg2_id": "BioInfer.d1.s2.e1", "normalized": [] } ]

[ { "id": "BioInfer.d1.s3__text", "type": "Sentence", "text": [ "In viscometric assays, the birch protein was seen to modulate actin filament formation analogous to animal profilin." ], "offsets": [ [ 0, 116 ] ] } ]

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[ { "id": "BioInfer.d1.s3.i0", "type": "PPI", "arg1_id": "BioInfer.d1.s3.e0", "arg2_id": "BioInfer.d1.s3.e1", "normalized": [] } ]

[ { "id": "BioInfer.d1.s4__text", "type": "Sentence", "text": [ "These data indicate that the actin-binding domains in plant and animal profilins are functionally highly conserved, although the overall sequence similarity is less than 25%." ], "offsets": [ [ 0, 174 ] ] } ]

[ { "id": "BioInfer.d1.s4.e0", "type": "Protein_family_or_group", "text": [ "profilins" ], "offsets": [ [ 71, 80 ] ], "normalized": [] }, { "id": "BioInfer.d1.s4.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 29, 34 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d1.s4.i0", "type": "PPI", "arg1_id": "BioInfer.d1.s4.e0", "arg2_id": "BioInfer.d1.s4.e1", "normalized": [] } ]

[ { "id": "BioInfer.d2.s0__text", "type": "Sentence", "text": [ "Abnormal immunoreactivity in the tumor tissue was observed in 18 patients (34.0%) for E-cadherin, in 35 (66.0%) for alpha-catenin, in 20 (37.7%) for beta-catenin, and in 37 (69.8%) for gamma-catenin." ], "offsets": [ [ 0, 199 ] ] } ]

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[ { "id": "BioInfer.d3.s0__text", "type": "Sentence", "text": [ "Absence of alpha-syntrophin leads to structurally aberrant neuromuscular synapses deficient in utrophin." ], "offsets": [ [ 0, 104 ] ] } ]

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[ { "id": "BioInfer.d3.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d3.s0.e0", "arg2_id": "BioInfer.d3.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d3.s1__text", "type": "Sentence", "text": [ "Thus, alpha-syntrophin has an important role in synapse formation and in the organization of utrophin, acetylcholine receptor, and acetylcholinesterase at the neuromuscular synapse." ], "offsets": [ [ 0, 181 ] ] } ]

[ { "id": "BioInfer.d3.s1.e0", "type": "Individual_protein", "text": [ "acetylcholine receptor" ], "offsets": [ [ 103, 125 ] ], "normalized": [] }, { "id": "BioInfer.d3.s1.e1", "type": "Individual_protein", "text": [ "acetylcholinesterase" ], "offsets": [ [ 131, 151 ] ], "normalized": [] }, { "id": "BioInfer.d3.s1.e2", "type": "Individual_protein", "text": [ "utrophin" ], "offsets": [ [ 93, 101 ] ], "normalized": [] }, { "id": "BioInfer.d3.s1.e3", "type": "Individual_protein", "text": [ "alpha-syntrophin" ], "offsets": [ [ 6, 22 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d4.s0__text", "type": "Sentence", "text": [ "Abundance of actin, talin, alpha 5 and beta 1 integrins, pp125 focal adhesion kinase, and alpha-catenin is not affected by the differential calreticulin expression." ], "offsets": [ [ 0, 164 ] ] } ]

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[ { "id": "BioInfer.d5.s0__text", "type": "Sentence", "text": [ "Acanthamoeba actin and profilin can be cross-linked between glutamic acid 364 of actin and lysine 115 of profilin." ], "offsets": [ [ 0, 114 ] ] } ]

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[ { "id": "BioInfer.d5.s1__text", "type": "Sentence", "text": [ "Acanthamoeba profilin was cross-linked to actin via a zero-length isopeptide bond using carbodiimide." ], "offsets": [ [ 0, 101 ] ] } ]

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[ { "id": "BioInfer.d5.s2__text", "type": "Sentence", "text": [ "Since the NH2 terminus of profilin is blocked, Edman degradation gave only the sequence of the conjugated actin CNBr fragment beginning with Trp-356." ], "offsets": [ [ 0, 149 ] ] } ]

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[ { "id": "BioInfer.d6.s0__text", "type": "Sentence", "text": [ "Acanthamoeba profilin affects the mechanical properties of nonfilamentous actin." ], "offsets": [ [ 0, 80 ] ] } ]

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[ { "id": "BioInfer.d6.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d6.s0.e0", "arg2_id": "BioInfer.d6.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d6.s1__text", "type": "Sentence", "text": [ "In contrast, profilin had little effect on the rigidity and viscosity of actin filaments." ], "offsets": [ [ 0, 89 ] ] } ]

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[ { "id": "BioInfer.d6.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d6.s1.e0", "arg2_id": "BioInfer.d6.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d6.s2__text", "type": "Sentence", "text": [ "We speculate that nonfilamentous actin and profilin, both of which form shear-sensitive structures, can be modeled as flocculant materials." ], "offsets": [ [ 0, 139 ] ] } ]

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[ { "id": "BioInfer.d7.s0__text", "type": "Sentence", "text": [ "Acanthamoeba profilin has similar but weaker effects on muscle actin, requiring 5 to 10 times more profilin than with amoeba actin." ], "offsets": [ [ 0, 131 ] ] } ]

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[ { "id": "BioInfer.d7.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d7.s0.e1", "arg2_id": "BioInfer.d7.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d7.s1__text", "type": "Sentence", "text": [ "Acanthamoeba profilin strongly inhibits in a concentration-dependent fashion the rate and extent of Acanthamoeba actin polymerization in 50 mM KCl." ], "offsets": [ [ 0, 147 ] ] } ]

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[ { "id": "BioInfer.d7.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d7.s1.e0", "arg2_id": "BioInfer.d7.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d7.s2__text", "type": "Sentence", "text": [ "Addition of profilin to polymerized actin causes it to depolymerize until a new steady-state, dependent on profilin concentration, is achieved." ], "offsets": [ [ 0, 143 ] ] } ]

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[ { "id": "BioInfer.d7.s3__text", "type": "Sentence", "text": [ "Mechanism of action of Acanthamoeba profilin: demonstration of actin species specificity and regulation by micromolar concentrations of MgCl2." ], "offsets": [ [ 0, 142 ] ] } ]

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[ { "id": "BioInfer.d7.s4__text", "type": "Sentence", "text": [ "MgCl2 strongly inhibits these effects of profilin, most likely by binding to the high-affinity divalent cation site on the actin." ], "offsets": [ [ 0, 129 ] ] } ]

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[ { "id": "BioInfer.d7.s4.i0", "type": "PPI", "arg1_id": "BioInfer.d7.s4.e0", "arg2_id": "BioInfer.d7.s4.e1", "normalized": [] } ]

[ { "id": "BioInfer.d8.s0__text", "type": "Sentence", "text": [ "Accordingly, beta-catenin is also found in these structures, again in the absence of alpha-catenin." ], "offsets": [ [ 0, 99 ] ] } ]

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[ { "id": "BioInfer.d8.s1__text", "type": "Sentence", "text": [ "In addition to its presence in cell-cell adhesion sites, we have found beta-catenin, but not alpha-catenin, in the Z-discs of heart and skeletal striated muscles." ], "offsets": [ [ 0, 162 ] ] } ]

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[ { "id": "BioInfer.d8.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d8.s1.e0", "arg2_id": "BioInfer.d8.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d9.s0__text", "type": "Sentence", "text": [ "A chimera consisting of the alpha-catenin-binding region of beta-catenin linked to the amino terminus of alpha-catenin 57-264 behaves as a monomer in solution, as expected, since beta-catenin binding disrupts the alpha-catenin dimer." ], "offsets": [ [ 0, 233 ] ] } ]

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[ { "id": "BioInfer.d9.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d9.s0.e0", "arg2_id": "BioInfer.d9.s0.e2", "normalized": [] }, { "id": "BioInfer.d9.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d9.s0.e0", "arg2_id": "BioInfer.d9.s0.e4", "normalized": [] }, { "id": "BioInfer.d9.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d9.s0.e1", "arg2_id": "BioInfer.d9.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d10.s0__text", "type": "Sentence", "text": [ "Acidic domain of the phosphoprotein (P) of vesicular stomatitis virus differentially interacts with homologous and heterologous nucleocapsid protein (N)." ], "offsets": [ [ 0, 153 ] ] } ]

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[ { "id": "BioInfer.d10.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d10.s0.e0", "arg2_id": "BioInfer.d10.s0.e1", "normalized": [] }, { "id": "BioInfer.d10.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d10.s0.e0", "arg2_id": "BioInfer.d10.s0.e2", "normalized": [] }, { "id": "BioInfer.d10.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d10.s0.e1", "arg2_id": "BioInfer.d10.s0.e3", "normalized": [] }, { "id": "BioInfer.d10.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d10.s0.e2", "arg2_id": "BioInfer.d10.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d11.s0__text", "type": "Sentence", "text": [ "A common feature of these talin-positive domains is the deep membrane infoldings, where bundles of actin filaments are inserted into the membrane." ], "offsets": [ [ 0, 146 ] ] } ]

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[ { "id": "BioInfer.d12.s0__text", "type": "Sentence", "text": [ "A core activity associated with the N terminus of the yeast RAD52 protein is revealed by RAD51 overexpression suppression of C-terminal rad52 truncation alleles." ], "offsets": [ [ 0, 161 ] ] } ]

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[ { "id": "BioInfer.d14.s0__text", "type": "Sentence", "text": [ "Actin-binding proteins such as profilin and gelsolin bind to phosphatidylinositol (PI) 4,5-bisphosphate (PI 4,5-P2) and regulate the concentration of monomeric actin." ], "offsets": [ [ 0, 166 ] ] } ]

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[ { "id": "BioInfer.d14.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d14.s0.e0", "arg2_id": "BioInfer.d14.s0.e2", "normalized": [] }, { "id": "BioInfer.d14.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d14.s0.e1", "arg2_id": "BioInfer.d14.s0.e2", "normalized": [] }, { "id": "BioInfer.d14.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d14.s0.e2", "arg2_id": "BioInfer.d14.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d14.s1__text", "type": "Sentence", "text": [ "These studies suggest that profilin and gelsolin may control the generation of 3-OH phosphorylated phosphoinositides, which in turn may regulate the actin polymerization." ], "offsets": [ [ 0, 170 ] ] } ]

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[ { "id": "BioInfer.d14.s2__text", "type": "Sentence", "text": [ "This effect is specific to profilin and gelsolin because other cytoskeletal proteins such as tau or actin do not affect PI 3-kinase activity." ], "offsets": [ [ 0, 141 ] ] } ]

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[ { "id": "BioInfer.d14.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d14.s2.e1", "arg2_id": "BioInfer.d14.s2.e2", "normalized": [] }, { "id": "BioInfer.d14.s2.i1", "type": "PPI", "arg1_id": "BioInfer.d14.s2.e1", "arg2_id": "BioInfer.d14.s2.e3", "normalized": [] } ]

[ { "id": "BioInfer.d16.s0__text", "type": "Sentence", "text": [ "Actin-depolymerizing factor (ADF) and cofilin define a family of actin-binding proteins essential for the rapid turnover of filamentous actin in vivo." ], "offsets": [ [ 0, 150 ] ] } ]

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[ { "id": "BioInfer.d16.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d16.s0.e0", "arg2_id": "BioInfer.d16.s0.e4", "normalized": [] }, { "id": "BioInfer.d16.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d16.s0.e1", "arg2_id": "BioInfer.d16.s0.e4", "normalized": [] }, { "id": "BioInfer.d16.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d16.s0.e2", "arg2_id": "BioInfer.d16.s0.e4", "normalized": [] }, { "id": "BioInfer.d16.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d16.s0.e3", "arg2_id": "BioInfer.d16.s0.e4", "normalized": [] } ]

[ { "id": "BioInfer.d17.s0__text", "type": "Sentence", "text": [ "Actin expression was reduced by 25-50%, relative to that of myosin heavy chain, in smooth muscle of KO mice, without any change in the relative distribution of the actin isoforms." ], "offsets": [ [ 0, 179 ] ] } ]

[ { "id": "BioInfer.d17.s0.e0", "type": "Gene/protein/RNA", "text": [ "Actin" ], "offsets": [ [ 0, 5 ] ], "normalized": [] }, { "id": "BioInfer.d17.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 164, 169 ] ], "normalized": [] }, { "id": "BioInfer.d17.s0.e2", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 60, 78 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d17.s1__text", "type": "Sentence", "text": [ "We conclude that the faster Vus of smooth muscle of the KO mouse is consistent with, but does not prove without further study, physiological regulation of the crossbridge cycle by calponin." ], "offsets": [ [ 0, 189 ] ] } ]

[ { "id": "BioInfer.d17.s1.e0", "type": "Gene/protein/RNA", "text": [ "calponin" ], "offsets": [ [ 180, 188 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d18.s0__text", "type": "Sentence", "text": [ "Actin isoforms from different species were also compared, and the effect of profilin on the thermal stability of actin was studied." ], "offsets": [ [ 0, 131 ] ] } ]

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[ { "id": "BioInfer.d18.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d18.s0.e1", "arg2_id": "BioInfer.d18.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d20.s0__text", "type": "Sentence", "text": [ "Active, Ser133-phosphorylated CREB effects transcription of CRE-dependent genes via interaction with the 265-kDa co-activator protein CREB-binding-protein, CBP, which bridges the CRE/CREB complex to components of the basal transcriptional apparatus." ], "offsets": [ [ 0, 249 ] ] } ]

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[ { "id": "BioInfer.d20.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d20.s0.e0", "arg2_id": "BioInfer.d20.s0.e1", "normalized": [] }, { "id": "BioInfer.d20.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d20.s0.e0", "arg2_id": "BioInfer.d20.s0.e2", "normalized": [] }, { "id": "BioInfer.d20.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d20.s0.e1", "arg2_id": "BioInfer.d20.s0.e3", "normalized": [] }, { "id": "BioInfer.d20.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d20.s0.e2", "arg2_id": "BioInfer.d20.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d21.s0__text", "type": "Sentence", "text": [ "Actophorin and profilin have opposite effects on the rate of exchange of nucleotide bound to actin monomers." ], "offsets": [ [ 0, 108 ] ] } ]

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[ { "id": "BioInfer.d24.s0__text", "type": "Sentence", "text": [ "Addition of EGTA (3 mM) to the extracellular media completely inhibited the cleavage of actin-binding protein, talin, and pp60src in response to A23187 (1 microM)." ], "offsets": [ [ 0, 163 ] ] } ]

[ { "id": "BioInfer.d24.s0.e0", "type": "Gene/protein/RNA", "text": [ "pp60src" ], "offsets": [ [ 122, 129 ] ], "normalized": [] }, { "id": "BioInfer.d24.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin-binding protein" ], "offsets": [ [ 88, 109 ] ], "normalized": [] }, { "id": "BioInfer.d24.s0.e2", "type": "Gene/protein/RNA", "text": [ "talin" ], "offsets": [ [ 111, 116 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d25.s0__text", "type": "Sentence", "text": [ "Adherens junction proteins (N-cadherin, E-cadherin, alpha-catenin, beta-catenin, plakoglobin, and actin) and the proliferation marker Ki-67 were localized in the cultures by fluorescence microscopy, and in vitro wound healing was compared." ], "offsets": [ [ 0, 239 ] ] } ]

[ { "id": "BioInfer.d25.s0.e0", "type": "Gene/protein/RNA", "text": [ "plakoglobin" ], "offsets": [ [ 81, 92 ] ], "normalized": [] }, { "id": "BioInfer.d25.s0.e1", "type": "Gene/protein/RNA", "text": [ "E-cadherin" ], "offsets": [ [ 40, 50 ] ], "normalized": [] }, { "id": "BioInfer.d25.s0.e2", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 52, 65 ] ], "normalized": [] }, { "id": "BioInfer.d25.s0.e3", "type": "Gene/protein/RNA", "text": [ "N-cadherin" ], "offsets": [ [ 28, 38 ] ], "normalized": [] }, { "id": "BioInfer.d25.s0.e4", "type": "Gene/protein/RNA", "text": [ "Ki-67" ], "offsets": [ [ 134, 139 ] ], "normalized": [] }, { "id": "BioInfer.d25.s0.e5", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 98, 103 ] ], "normalized": [] }, { "id": "BioInfer.d25.s0.e6", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 67, 79 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d26.s0__text", "type": "Sentence", "text": [ "A distinct modulating domain in glucocorticoid receptor monomers in the repression of activity of the transcription factor AP-1." ], "offsets": [ [ 0, 128 ] ] } ]

[ { "id": "BioInfer.d26.s0.e0", "type": "Individual_protein", "text": [ "AP-1" ], "offsets": [ [ 123, 127 ] ], "normalized": [] }, { "id": "BioInfer.d26.s0.e1", "type": "Individual_protein", "text": [ "glucocorticoid receptor" ], "offsets": [ [ 32, 55 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d26.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d26.s0.e0", "arg2_id": "BioInfer.d26.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d27.s0__text", "type": "Sentence", "text": [ "ADP-ribosylation of actin at Arg 177 by Clostridium perfringens iota toxin increased the nucleotide dissociation rate from 2.2 x 10(-3) s-1 to 4.5 x 10(-3) s-1 without affecting the profilin-induced stimulation of nucleotide exchange." ], "offsets": [ [ 0, 234 ] ] } ]

[ { "id": "BioInfer.d27.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 20, 25 ] ], "normalized": [] }, { "id": "BioInfer.d27.s0.e1", "type": "Individual_protein", "text": [ "iota toxin" ], "offsets": [ [ 64, 74 ] ], "normalized": [] }, { "id": "BioInfer.d27.s0.e2", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 182, 190 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d27.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d27.s0.e0", "arg2_id": "BioInfer.d27.s0.e1", "normalized": [] }, { "id": "BioInfer.d27.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d27.s0.e1", "arg2_id": "BioInfer.d27.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d27.s1__text", "type": "Sentence", "text": [ "In contrast, ADP-ribosylation of actin at Arg95/Arg372 induced by turkey erythrocyte transferase decreased the nucleotide dissociation rate to 1.5 x 10(3) s-1 and inhibited the profilin-induced stimulation of nucleotide exchange." ], "offsets": [ [ 0, 229 ] ] } ]

[ { "id": "BioInfer.d27.s1.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 177, 185 ] ], "normalized": [] }, { "id": "BioInfer.d27.s1.e1", "type": "Individual_protein", "text": [ "erythrocyte transferase" ], "offsets": [ [ 73, 96 ] ], "normalized": [] }, { "id": "BioInfer.d27.s1.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 33, 38 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d27.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d27.s1.e1", "arg2_id": "BioInfer.d27.s1.e2", "normalized": [] } ]

[ { "id": "BioInfer.d28.s0__text", "type": "Sentence", "text": [ "After 24 or 48 hours of shear, staining for VE-cadherin, alpha-catenin, and beta-catenin was intense and peripheral, forming a band of \"dashes\" (adherens plaques) that colocalized with the ends of stress fibers that inserted along the lateral membranes of cells." ], "offsets": [ [ 0, 262 ] ] } ]

[ { "id": "BioInfer.d28.s0.e0", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 76, 88 ] ], "normalized": [] }, { "id": "BioInfer.d28.s0.e1", "type": "Gene/protein/RNA", "text": [ "VE-cadherin" ], "offsets": [ [ 44, 55 ] ], "normalized": [] }, { "id": "BioInfer.d28.s0.e2", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 57, 70 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d28.s1__text", "type": "Sentence", "text": [ "Cells were fixed and stained with antibodies to vascular endothelial (VE) cadherin, alpha-catenin, beta-catenin, or plakoglobin." ], "offsets": [ [ 0, 128 ] ] } ]

[ { "id": "BioInfer.d28.s1.e0", "type": "Gene/protein/RNA", "text": [ "vascular endothelial", "cadherin" ], "offsets": [ [ 48, 68 ], [ 74, 82 ] ], "normalized": [] }, { "id": "BioInfer.d28.s1.e1", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 99, 111 ] ], "normalized": [] }, { "id": "BioInfer.d28.s1.e2", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 84, 97 ] ], "normalized": [] }, { "id": "BioInfer.d28.s1.e3", "type": "Gene/protein/RNA", "text": [ "plakoglobin" ], "offsets": [ [ 116, 127 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d29.s0__text", "type": "Sentence", "text": [ "After digestion of the 60 kDa fragment with cyanogen bromide, the N-terminal 21-amino acid sequence of one of the resulting peptides was found to show sequence similarity to a region near the actin-binding site (amino acid residues 260-281) of yeast fimbrin." ], "offsets": [ [ 0, 258 ] ] } ]

[ { "id": "BioInfer.d29.s0.e0", "type": "Individual_protein", "text": [ "fimbrin" ], "offsets": [ [ 250, 257 ] ], "normalized": [] }, { "id": "BioInfer.d29.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 192, 197 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d29.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d29.s0.e0", "arg2_id": "BioInfer.d29.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d30.s0__text", "type": "Sentence", "text": [ "After elution of the three actin-binding proteins, actin and profilin were recovered from the DNase I column with 2 M urea solution." ], "offsets": [ [ 0, 132 ] ] } ]

[ { "id": "BioInfer.d30.s0.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 51, 56 ] ], "normalized": [] }, { "id": "BioInfer.d30.s0.e1", "type": "Gene/protein/RNA", "text": [ "DNase I" ], "offsets": [ [ 94, 101 ] ], "normalized": [] }, { "id": "BioInfer.d30.s0.e2", "type": "Gene/protein/RNA", "text": [ "actin-binding proteins" ], "offsets": [ [ 27, 49 ] ], "normalized": [] }, { "id": "BioInfer.d30.s0.e3", "type": "Gene/protein/RNA", "text": [ "profilin" ], "offsets": [ [ 61, 69 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d31.s0__text", "type": "Sentence", "text": [ "After in vitro labelling of isolated rat liver nuclei, the following ADP-ribosylated and unmodified histones were identified by HPLC and gel electrophoresis: histone H1(0), four histone H1 subfractions, histone H2A.1, histone H2A.2, oxidized histone H2A.2, histone H2A.X, histone H2A.Z, histone H2B, three histone H3 variants and histone H4." ], "offsets": [ [ 0, 341 ] ] } ]

[ { "id": "BioInfer.d31.s0.e0", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 330, 337 ] ], "normalized": [] }, { "id": "BioInfer.d31.s0.e1", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 306, 313 ] ], "normalized": [] }, { "id": "BioInfer.d31.s0.e2", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 158, 165 ] ], "normalized": [] }, { "id": "BioInfer.d31.s0.e3", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 218, 225 ] ], "normalized": [] }, { "id": "BioInfer.d31.s0.e4", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 203, 210 ] ], "normalized": [] }, { "id": "BioInfer.d31.s0.e5", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 178, 185 ] ], "normalized": [] }, { "id": "BioInfer.d31.s0.e6", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 257, 264 ] ], "normalized": [] }, { "id": "BioInfer.d31.s0.e7", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 287, 294 ] ], "normalized": [] }, { "id": "BioInfer.d31.s0.e8", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 272, 279 ] ], "normalized": [] }, { "id": "BioInfer.d31.s0.e9", "type": "Individual_protein", "text": [ "H3" ], "offsets": [ [ 314, 316 ] ], "normalized": [] }, { "id": "BioInfer.d31.s0.e10", "type": "Individual_protein", "text": [ "H2B" ], "offsets": [ [ 295, 298 ] ], "normalized": [] }, { "id": "BioInfer.d31.s0.e11", "type": "Individual_protein", "text": [ "H4" ], "offsets": [ [ 338, 340 ] ], "normalized": [] }, { "id": "BioInfer.d31.s0.e12", "type": "Protein_family_or_group", "text": [ "histone" ], "offsets": [ [ 242, 249 ] ], "normalized": [] }, { "id": "BioInfer.d31.s0.e13", "type": "Individual_protein", "text": [ "H2A.1" ], "offsets": [ [ 211, 216 ] ], "normalized": [] }, { "id": "BioInfer.d31.s0.e14", "type": "Individual_protein", "text": [ "H1" ], "offsets": [ [ 186, 188 ] ], "normalized": [] }, { "id": "BioInfer.d31.s0.e15", "type": "Individual_protein", "text": [ "H1(0)" ], "offsets": [ [ 166, 171 ] ], "normalized": [] }, { "id": "BioInfer.d31.s0.e16", "type": "Gene/protein/RNA", "text": [ "histones" ], "offsets": [ [ 100, 108 ] ], "normalized": [] }, { "id": "BioInfer.d31.s0.e17", "type": "Individual_protein", "text": [ "H2A.Z" ], "offsets": [ [ 280, 285 ] ], "normalized": [] }, { "id": "BioInfer.d31.s0.e18", "type": "Individual_protein", "text": [ "H2A.X" ], "offsets": [ [ 265, 270 ] ], "normalized": [] }, { "id": "BioInfer.d31.s0.e19", "type": "Individual_protein", "text": [ "H2A.2" ], "offsets": [ [ 250, 255 ] ], "normalized": [] }, { "id": "BioInfer.d31.s0.e20", "type": "Individual_protein", "text": [ "H2A.2" ], "offsets": [ [ 226, 231 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d31.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d31.s0.e0", "arg2_id": "BioInfer.d31.s0.e11", "normalized": [] }, { "id": "BioInfer.d31.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d31.s0.e1", "arg2_id": "BioInfer.d31.s0.e9", "normalized": [] }, { "id": "BioInfer.d31.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d31.s0.e2", "arg2_id": "BioInfer.d31.s0.e15", "normalized": [] }, { "id": "BioInfer.d31.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d31.s0.e3", "arg2_id": "BioInfer.d31.s0.e20", "normalized": [] }, { "id": "BioInfer.d31.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d31.s0.e4", "arg2_id": "BioInfer.d31.s0.e13", "normalized": [] }, { "id": "BioInfer.d31.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d31.s0.e5", "arg2_id": "BioInfer.d31.s0.e14", "normalized": [] }, { "id": "BioInfer.d31.s0.i6", "type": "PPI", "arg1_id": "BioInfer.d31.s0.e6", "arg2_id": "BioInfer.d31.s0.e18", "normalized": [] }, { "id": "BioInfer.d31.s0.i7", "type": "PPI", "arg1_id": "BioInfer.d31.s0.e7", "arg2_id": "BioInfer.d31.s0.e10", "normalized": [] }, { "id": "BioInfer.d31.s0.i8", "type": "PPI", "arg1_id": "BioInfer.d31.s0.e8", "arg2_id": "BioInfer.d31.s0.e17", "normalized": [] }, { "id": "BioInfer.d31.s0.i9", "type": "PPI", "arg1_id": "BioInfer.d31.s0.e12", "arg2_id": "BioInfer.d31.s0.e19", "normalized": [] } ]

[ { "id": "BioInfer.d32.s0__text", "type": "Sentence", "text": [ "A further outcome of this study is that the actin filament core bundles in microvilli of chicken pigment epithelial cells are presumed to contain a crosslinking protein, which is not immunologically related to either villin, fimbrin or myosin I of the intestinal brush border." ], "offsets": [ [ 0, 276 ] ] } ]

[ { "id": "BioInfer.d32.s0.e0", "type": "Gene/protein/RNA", "text": [ "myosin I" ], "offsets": [ [ 236, 244 ] ], "normalized": [] }, { "id": "BioInfer.d32.s0.e1", "type": "Gene/protein/RNA", "text": [ "fimbrin" ], "offsets": [ [ 225, 232 ] ], "normalized": [] }, { "id": "BioInfer.d32.s0.e2", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 44, 49 ] ], "normalized": [] }, { "id": "BioInfer.d32.s0.e3", "type": "Gene/protein/RNA", "text": [ "villin" ], "offsets": [ [ 217, 223 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d33.s0__text", "type": "Sentence", "text": [ "A highly significant correlation was observed between the loss of expression of E-cadherin, alpha-catenin and gamma-catenin, but not beta-catenin, with increased TNM stage (p <0.05)." ], "offsets": [ [ 0, 182 ] ] } ]

[ { "id": "BioInfer.d33.s0.e0", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 92, 105 ] ], "normalized": [] }, { "id": "BioInfer.d33.s0.e1", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 80, 90 ] ], "normalized": [] }, { "id": "BioInfer.d33.s0.e2", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 133, 145 ] ], "normalized": [] }, { "id": "BioInfer.d33.s0.e3", "type": "Individual_protein", "text": [ "gamma-catenin" ], "offsets": [ [ 110, 123 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d33.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d33.s0.e0", "arg2_id": "BioInfer.d33.s0.e1", "normalized": [] }, { "id": "BioInfer.d33.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d33.s0.e0", "arg2_id": "BioInfer.d33.s0.e2", "normalized": [] }, { "id": "BioInfer.d33.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d33.s0.e0", "arg2_id": "BioInfer.d33.s0.e3", "normalized": [] }, { "id": "BioInfer.d33.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d33.s0.e1", "arg2_id": "BioInfer.d33.s0.e2", "normalized": [] }, { "id": "BioInfer.d33.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d33.s0.e1", "arg2_id": "BioInfer.d33.s0.e3", "normalized": [] }, { "id": "BioInfer.d33.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d33.s0.e2", "arg2_id": "BioInfer.d33.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d33.s1__text", "type": "Sentence", "text": [ "Loss of normal surface E-cadherin, alpha-catenin, beta-catenin and gamma-catenin expression was found in 52/68 (76.4%) tumors, 57/68 (83.8%) tumors, 54/68 (79.4%) tumors and 54/68 (79.4%) tumors (p <0.001)." ], "offsets": [ [ 0, 206 ] ] } ]

[ { "id": "BioInfer.d33.s1.e0", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 50, 62 ] ], "normalized": [] }, { "id": "BioInfer.d33.s1.e1", "type": "Gene/protein/RNA", "text": [ "E-cadherin" ], "offsets": [ [ 23, 33 ] ], "normalized": [] }, { "id": "BioInfer.d33.s1.e2", "type": "Gene/protein/RNA", "text": [ "gamma-catenin" ], "offsets": [ [ 67, 80 ] ], "normalized": [] }, { "id": "BioInfer.d33.s1.e3", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 35, 48 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d33.s2__text", "type": "Sentence", "text": [ "MATERIALS AND METHODS: We used an avidin-biotin immunoperoxidase technique to examine the cellular localization of alpha-catenin, beta-catenin, gamma-catenin and E-cadherin in 68 TCC and 14 normal bladder biopsies." ], "offsets": [ [ 0, 214 ] ] } ]

[ { "id": "BioInfer.d33.s2.e0", "type": "Gene/protein/RNA", "text": [ "avidin" ], "offsets": [ [ 34, 40 ] ], "normalized": [] }, { "id": "BioInfer.d33.s2.e1", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 130, 142 ] ], "normalized": [] }, { "id": "BioInfer.d33.s2.e2", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 115, 128 ] ], "normalized": [] }, { "id": "BioInfer.d33.s2.e3", "type": "Gene/protein/RNA", "text": [ "E-cadherin" ], "offsets": [ [ 162, 172 ] ], "normalized": [] }, { "id": "BioInfer.d33.s2.e4", "type": "Gene/protein/RNA", "text": [ "gamma-catenin" ], "offsets": [ [ 144, 157 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d33.s3__text", "type": "Sentence", "text": [ "RESULTS: E-cadherin, alpha-catenin, beta-catenin and gamma-catenin were expressed in a normal membranous pattern in all normal bladder epithelium specimens." ], "offsets": [ [ 0, 156 ] ] } ]

[ { "id": "BioInfer.d33.s3.e0", "type": "Gene/protein/RNA", "text": [ "alpha-catenin" ], "offsets": [ [ 21, 34 ] ], "normalized": [] }, { "id": "BioInfer.d33.s3.e1", "type": "Gene/protein/RNA", "text": [ "gamma-catenin" ], "offsets": [ [ 53, 66 ] ], "normalized": [] }, { "id": "BioInfer.d33.s3.e2", "type": "Gene/protein/RNA", "text": [ "E-cadherin" ], "offsets": [ [ 9, 19 ] ], "normalized": [] }, { "id": "BioInfer.d33.s3.e3", "type": "Gene/protein/RNA", "text": [ "beta-catenin" ], "offsets": [ [ 36, 48 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d34.s0__text", "type": "Sentence", "text": [ "AIMS: To investigate the disturbance of intercellular adhesion in adenoid cystic carcinoma (ACC), we examined the ultrastructural localization of E-cadherin (E-cad), alpha-catenin (alpha-cat) and beta-catenin (beta-cat) in ACC, and compared it with that in the normal labial gland." ], "offsets": [ [ 0, 281 ] ] } ]

[ { "id": "BioInfer.d34.s0.e0", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 146, 156 ] ], "normalized": [] }, { "id": "BioInfer.d34.s0.e1", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 196, 208 ] ], "normalized": [] }, { "id": "BioInfer.d34.s0.e2", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 166, 179 ] ], "normalized": [] }, { "id": "BioInfer.d34.s0.e3", "type": "Individual_protein", "text": [ "beta-cat" ], "offsets": [ [ 210, 218 ] ], "normalized": [] }, { "id": "BioInfer.d34.s0.e4", "type": "Individual_protein", "text": [ "alpha-cat" ], "offsets": [ [ 181, 190 ] ], "normalized": [] }, { "id": "BioInfer.d34.s0.e5", "type": "Individual_protein", "text": [ "E-cad" ], "offsets": [ [ 158, 163 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d35.s0__text", "type": "Sentence", "text": [ "Aip1p interacts with cofilin to disassemble actin filaments." ], "offsets": [ [ 0, 60 ] ] } ]

[ { "id": "BioInfer.d35.s0.e0", "type": "Individual_protein", "text": [ "Aip1p" ], "offsets": [ [ 0, 5 ] ], "normalized": [] }, { "id": "BioInfer.d35.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 44, 49 ] ], "normalized": [] }, { "id": "BioInfer.d35.s0.e2", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 21, 28 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d35.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d35.s0.e0", "arg2_id": "BioInfer.d35.s0.e1", "normalized": [] }, { "id": "BioInfer.d35.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d35.s0.e0", "arg2_id": "BioInfer.d35.s0.e2", "normalized": [] }, { "id": "BioInfer.d35.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d35.s0.e1", "arg2_id": "BioInfer.d35.s0.e2", "normalized": [] } ]

[ { "id": "BioInfer.d35.s1__text", "type": "Sentence", "text": [ "Aip1p localizes to cortical actin patches in yeast cells, and this localization is disrupted by specific actin and cofilin mutations." ], "offsets": [ [ 0, 133 ] ] } ]

[ { "id": "BioInfer.d35.s1.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 28, 33 ] ], "normalized": [] }, { "id": "BioInfer.d35.s1.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 105, 110 ] ], "normalized": [] }, { "id": "BioInfer.d35.s1.e2", "type": "Individual_protein", "text": [ "Aip1p" ], "offsets": [ [ 0, 5 ] ], "normalized": [] }, { "id": "BioInfer.d35.s1.e3", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 115, 122 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d35.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d35.s1.e0", "arg2_id": "BioInfer.d35.s1.e1", "normalized": [] }, { "id": "BioInfer.d35.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d35.s1.e0", "arg2_id": "BioInfer.d35.s1.e2", "normalized": [] }, { "id": "BioInfer.d35.s1.i2", "type": "PPI", "arg1_id": "BioInfer.d35.s1.e0", "arg2_id": "BioInfer.d35.s1.e3", "normalized": [] } ]

[ { "id": "BioInfer.d35.s2__text", "type": "Sentence", "text": [ "A two-hybrid-based approach using cofilin and actin mutants identified residues necessary for the interaction of actin, cofilin, and Aip1p in an apparent ternary complex." ], "offsets": [ [ 0, 170 ] ] } ]

[ { "id": "BioInfer.d35.s2.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 46, 51 ] ], "normalized": [] }, { "id": "BioInfer.d35.s2.e1", "type": "Gene/protein/RNA", "text": [ "cofilin" ], "offsets": [ [ 34, 41 ] ], "normalized": [] }, { "id": "BioInfer.d35.s2.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 113, 118 ] ], "normalized": [] }, { "id": "BioInfer.d35.s2.e3", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 120, 127 ] ], "normalized": [] }, { "id": "BioInfer.d35.s2.e4", "type": "Individual_protein", "text": [ "Aip1p" ], "offsets": [ [ 133, 138 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d35.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d35.s2.e2", "arg2_id": "BioInfer.d35.s2.e3", "normalized": [] }, { "id": "BioInfer.d35.s2.i1", "type": "PPI", "arg1_id": "BioInfer.d35.s2.e2", "arg2_id": "BioInfer.d35.s2.e4", "normalized": [] }, { "id": "BioInfer.d35.s2.i2", "type": "PPI", "arg1_id": "BioInfer.d35.s2.e3", "arg2_id": "BioInfer.d35.s2.e4", "normalized": [] } ]

[ { "id": "BioInfer.d35.s3__text", "type": "Sentence", "text": [ "Here, we report that Aip1p also interacts with the ubiquitous actin depolymerizing factor cofilin." ], "offsets": [ [ 0, 98 ] ] } ]

[ { "id": "BioInfer.d35.s3.e0", "type": "Individual_protein", "text": [ "actin depolymerizing factor" ], "offsets": [ [ 62, 89 ] ], "normalized": [] }, { "id": "BioInfer.d35.s3.e1", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 90, 97 ] ], "normalized": [] }, { "id": "BioInfer.d35.s3.e2", "type": "Individual_protein", "text": [ "Aip1p" ], "offsets": [ [ 21, 26 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d35.s3.i0", "type": "PPI", "arg1_id": "BioInfer.d35.s3.e0", "arg2_id": "BioInfer.d35.s3.e1", "normalized": [] }, { "id": "BioInfer.d35.s3.i1", "type": "PPI", "arg1_id": "BioInfer.d35.s3.e1", "arg2_id": "BioInfer.d35.s3.e2", "normalized": [] } ]

[ { "id": "BioInfer.d35.s4__text", "type": "Sentence", "text": [ "We conclude that Aip1p is a cofilin-associated protein that enhances the filament disassembly activity of cofilin and restricts cofilin localization to cortical actin patches." ], "offsets": [ [ 0, 175 ] ] } ]

[ { "id": "BioInfer.d35.s4.e0", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 106, 113 ] ], "normalized": [] }, { "id": "BioInfer.d35.s4.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 161, 166 ] ], "normalized": [] }, { "id": "BioInfer.d35.s4.e2", "type": "Individual_protein", "text": [ "Aip1p" ], "offsets": [ [ 17, 22 ] ], "normalized": [] }, { "id": "BioInfer.d35.s4.e3", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 128, 135 ] ], "normalized": [] }, { "id": "BioInfer.d35.s4.e4", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 28, 35 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d35.s4.i0", "type": "PPI", "arg1_id": "BioInfer.d35.s4.e0", "arg2_id": "BioInfer.d35.s4.e2", "normalized": [] }, { "id": "BioInfer.d35.s4.i1", "type": "PPI", "arg1_id": "BioInfer.d35.s4.e1", "arg2_id": "BioInfer.d35.s4.e2", "normalized": [] }, { "id": "BioInfer.d35.s4.i2", "type": "PPI", "arg1_id": "BioInfer.d35.s4.e1", "arg2_id": "BioInfer.d35.s4.e3", "normalized": [] }, { "id": "BioInfer.d35.s4.i3", "type": "PPI", "arg1_id": "BioInfer.d35.s4.e2", "arg2_id": "BioInfer.d35.s4.e4", "normalized": [] } ]

[ { "id": "BioInfer.d36.s0__text", "type": "Sentence", "text": [ "A LIMK2 mutant with replacement of threonine 505 by valine abolished LIMK2 activities for cofilin phosphorylation and actin cytoskeletal changes, whereas replacement by glutamate enhanced the protein kinase activity and stress fiber formation by LIMK2." ], "offsets": [ [ 0, 252 ] ] } ]

[ { "id": "BioInfer.d36.s0.e0", "type": "Individual_protein", "text": [ "protein kinase" ], "offsets": [ [ 192, 206 ] ], "normalized": [] }, { "id": "BioInfer.d36.s0.e1", "type": "Individual_protein", "text": [ "LIMK2" ], "offsets": [ [ 246, 251 ] ], "normalized": [] }, { "id": "BioInfer.d36.s0.e2", "type": "Individual_protein", "text": [ "cofilin" ], "offsets": [ [ 90, 97 ] ], "normalized": [] }, { "id": "BioInfer.d36.s0.e3", "type": "Individual_protein", "text": [ "LIMK2" ], "offsets": [ [ 2, 7 ] ], "normalized": [] }, { "id": "BioInfer.d36.s0.e4", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 118, 123 ] ], "normalized": [] }, { "id": "BioInfer.d36.s0.e5", "type": "Individual_protein", "text": [ "LIMK2" ], "offsets": [ [ 69, 74 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d36.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d36.s0.e0", "arg2_id": "BioInfer.d36.s0.e1", "normalized": [] }, { "id": "BioInfer.d36.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d36.s0.e2", "arg2_id": "BioInfer.d36.s0.e3", "normalized": [] }, { "id": "BioInfer.d36.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d36.s0.e2", "arg2_id": "BioInfer.d36.s0.e5", "normalized": [] }, { "id": "BioInfer.d36.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d36.s0.e3", "arg2_id": "BioInfer.d36.s0.e4", "normalized": [] }, { "id": "BioInfer.d36.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d36.s0.e4", "arg2_id": "BioInfer.d36.s0.e5", "normalized": [] } ]

[ { "id": "BioInfer.d37.s0__text", "type": "Sentence", "text": [ "All of the experimental data were quantitatively accounted for on the basis of a 1:1 complex between profilin and monomeric actin with a Kr between 4 and 9 microM, the same value obtained previously in the absence of MgCl2." ], "offsets": [ [ 0, 223 ] ] } ]

[ { "id": "BioInfer.d37.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 101, 109 ] ], "normalized": [] }, { "id": "BioInfer.d37.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 124, 129 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d37.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d37.s0.e0", "arg2_id": "BioInfer.d37.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d37.s1__text", "type": "Sentence", "text": [ "The interaction of Acanthamoeba actin and Acanthamoeba profilin was evaluated as a function of ionic conditions." ], "offsets": [ [ 0, 112 ] ] } ]

[ { "id": "BioInfer.d37.s1.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 32, 37 ] ], "normalized": [] }, { "id": "BioInfer.d37.s1.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 55, 63 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d37.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d37.s1.e0", "arg2_id": "BioInfer.d37.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d39.s0__text", "type": "Sentence", "text": [ "Although binding patterns of different sera were not identical, almost all sera caused IgG binding to platelet components of 87-90 kD, 140 kD (identified as vinculin) and 220-240 kD (tentatively identified as talin and actin-binding protein)." ], "offsets": [ [ 0, 242 ] ] } ]

[ { "id": "BioInfer.d39.s0.e0", "type": "Individual_protein", "text": [ "IgG" ], "offsets": [ [ 87, 90 ] ], "normalized": [] }, { "id": "BioInfer.d39.s0.e1", "type": "Individual_protein", "text": [ "actin-binding protein" ], "offsets": [ [ 219, 240 ] ], "normalized": [] }, { "id": "BioInfer.d39.s0.e2", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 209, 214 ] ], "normalized": [] }, { "id": "BioInfer.d39.s0.e3", "type": "Individual_protein", "text": [ "vinculin" ], "offsets": [ [ 157, 165 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d39.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d39.s0.e0", "arg2_id": "BioInfer.d39.s0.e1", "normalized": [] }, { "id": "BioInfer.d39.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d39.s0.e0", "arg2_id": "BioInfer.d39.s0.e2", "normalized": [] }, { "id": "BioInfer.d39.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d39.s0.e0", "arg2_id": "BioInfer.d39.s0.e3", "normalized": [] } ]

[ { "id": "BioInfer.d41.s0__text", "type": "Sentence", "text": [ "Although profilin released actin at the appropriate time to stimulate actin assembly during exposure to chemoattractants, the concentration of profilin in PMN was insufficient to explain the high unpolymerized actin content in unstimulated PMN and the quantity of actin released from profilin too small to account for the large shifts from unpolymerized to polymerized actin associated with maximal chemoattractant stimulation." ], "offsets": [ [ 0, 427 ] ] } ]

[ { "id": "BioInfer.d41.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 9, 17 ] ], "normalized": [] }, { "id": "BioInfer.d41.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 264, 269 ] ], "normalized": [] }, { "id": "BioInfer.d41.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 70, 75 ] ], "normalized": [] }, { "id": "BioInfer.d41.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 27, 32 ] ], "normalized": [] }, { "id": "BioInfer.d41.s0.e4", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 210, 215 ] ], "normalized": [] }, { "id": "BioInfer.d41.s0.e5", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 143, 151 ] ], "normalized": [] }, { "id": "BioInfer.d41.s0.e6", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 369, 374 ] ], "normalized": [] }, { "id": "BioInfer.d41.s0.e7", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 284, 292 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d41.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d41.s0.e0", "arg2_id": "BioInfer.d41.s0.e2", "normalized": [] }, { "id": "BioInfer.d41.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d41.s0.e0", "arg2_id": "BioInfer.d41.s0.e3", "normalized": [] }, { "id": "BioInfer.d41.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d41.s0.e1", "arg2_id": "BioInfer.d41.s0.e6", "normalized": [] }, { "id": "BioInfer.d41.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d41.s0.e1", "arg2_id": "BioInfer.d41.s0.e7", "normalized": [] }, { "id": "BioInfer.d41.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d41.s0.e2", "arg2_id": "BioInfer.d41.s0.e3", "normalized": [] }, { "id": "BioInfer.d41.s0.i5", "type": "PPI", "arg1_id": "BioInfer.d41.s0.e4", "arg2_id": "BioInfer.d41.s0.e5", "normalized": [] } ]

[ { "id": "BioInfer.d41.s1__text", "type": "Sentence", "text": [ "Determination of the total profilin and actin concentrations in PMN revealed that the molar ratio of profilin to actin was 1 to 5.2." ], "offsets": [ [ 0, 132 ] ] } ]

[ { "id": "BioInfer.d41.s1.e0", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 40, 45 ] ], "normalized": [] }, { "id": "BioInfer.d41.s1.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 113, 118 ] ], "normalized": [] }, { "id": "BioInfer.d41.s1.e2", "type": "Gene/protein/RNA", "text": [ "profilin" ], "offsets": [ [ 27, 35 ] ], "normalized": [] }, { "id": "BioInfer.d41.s1.e3", "type": "Gene/protein/RNA", "text": [ "profilin" ], "offsets": [ [ 101, 109 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d41.s2__text", "type": "Sentence", "text": [ "We examined the role of the actin monomer sequestering protein, profilin, in the regulation of PMN actin filament assembly during chemoattractant stimulation using a Triton extraction method." ], "offsets": [ [ 0, 191 ] ] } ]

[ { "id": "BioInfer.d41.s2.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 64, 72 ] ], "normalized": [] }, { "id": "BioInfer.d41.s2.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 28, 33 ] ], "normalized": [] }, { "id": "BioInfer.d41.s2.e2", "type": "Individual_protein", "text": [ "PMN actin" ], "offsets": [ [ 95, 104 ] ], "normalized": [] } ]

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[ { "id": "BioInfer.d41.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d41.s2.e0", "arg2_id": "BioInfer.d41.s2.e1", "normalized": [] }, { "id": "BioInfer.d41.s2.i1", "type": "PPI", "arg1_id": "BioInfer.d41.s2.e0", "arg2_id": "BioInfer.d41.s2.e2", "normalized": [] } ]

[ { "id": "BioInfer.d43.s0__text", "type": "Sentence", "text": [ "Although co-localization of glucokinase with actin filaments was not clearly demonstrated in the pancreatic beta-cell line MIN6, islet glucokinase was found to be present in both the nucleus and the cytoplasm, though predominantly in the nucleus." ], "offsets": [ [ 0, 246 ] ] } ]

[ { "id": "BioInfer.d43.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 45, 50 ] ], "normalized": [] }, { "id": "BioInfer.d43.s0.e1", "type": "Individual_protein", "text": [ "glucokinase" ], "offsets": [ [ 28, 39 ] ], "normalized": [] }, { "id": "BioInfer.d43.s0.e2", "type": "Gene/protein/RNA", "text": [ "islet glucokinase" ], "offsets": [ [ 129, 146 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d43.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d43.s0.e0", "arg2_id": "BioInfer.d43.s0.e1", "normalized": [] } ]

[ { "id": "BioInfer.d43.s1__text", "type": "Sentence", "text": [ "A portion of glucokinase appeared to be co-localized with actin filaments in the cytoplasm of cultured rat hepatocytes incubated with 25 mM glucose." ], "offsets": [ [ 0, 148 ] ] } ]

[ { "id": "BioInfer.d43.s1.e0", "type": "Individual_protein", "text": [ "glucokinase" ], "offsets": [ [ 13, 24 ] ], "normalized": [] }, { "id": "BioInfer.d43.s1.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 58, 63 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d43.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d43.s1.e0", "arg2_id": "BioInfer.d43.s1.e1", "normalized": [] } ]

[ { "id": "BioInfer.d43.s2__text", "type": "Sentence", "text": [ "Co-localization of glucokinase with actin filaments." ], "offsets": [ [ 0, 52 ] ] } ]

[ { "id": "BioInfer.d43.s2.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 36, 41 ] ], "normalized": [] }, { "id": "BioInfer.d43.s2.e1", "type": "Individual_protein", "text": [ "glucokinase" ], "offsets": [ [ 19, 30 ] ], "normalized": [] } ]

[]

[]

[ { "id": "BioInfer.d43.s2.i0", "type": "PPI", "arg1_id": "BioInfer.d43.s2.e0", "arg2_id": "BioInfer.d43.s2.e1", "normalized": [] } ]