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100
BioInfer.d63.s0
[ { "id": "BioInfer.d63.s0__text", "type": "Sentence", "text": [ "An association was seen between E-cadherin and alpha-catenin expression, in both effusions and solid tumours, and for beta-catenin in solid tumours (range p<0. 001 to p=0.014)." ], "offsets": [ [ 0, 176 ] ] } ]
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101
BioInfer.d65.s0
[ { "id": "BioInfer.d65.s0__text", "type": "Sentence", "text": [ "An oligomeric form of simian virus 40 large T-antigen is immunologically related to the cellular tumor antigen p53." ], "offsets": [ [ 0, 115 ] ] } ]
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[]
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102
BioInfer.d65.s1
[ { "id": "BioInfer.d65.s1__text", "type": "Sentence", "text": [ "The cellular tumor antigen p53 is bound to the simian virus 40 (SV40) large T-antigen in SV40-infected and -transformed cells." ], "offsets": [ [ 0, 126 ] ] } ]
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[]
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103
BioInfer.d66.s0
[ { "id": "BioInfer.d66.s0__text", "type": "Sentence", "text": [ "Another cyclin-dependent kinase inhibitor, p27KIP1, and cyclin D increased slightly, whereas proliferating cell nuclear antigen and p130 remained unchanged." ], "offsets": [ [ 0, 156 ] ] } ]
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[]
[]
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104
BioInfer.d67.s0
[ { "id": "BioInfer.d67.s0__text", "type": "Sentence", "text": [ "A null mutation of the actin gene (ACT1) is lethal, but null mutations in the tropomyosin (TPM1), fimbrin (SAC6), Abp1p (ABP1), and capping protein (CAP1 and CAP2) genes have relatively mild or no effects." ], "offsets": [ [ 0, 205 ] ] } ]
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[]
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105
BioInfer.d68.s0
[ { "id": "BioInfer.d68.s0__text", "type": "Sentence", "text": [ "ORC1, ORC4 and Cdc6 were stable (T1/2 >2 h) and associated with a chromatin-containing fraction throughout the cell cycle." ], "offsets": [ [ 0, 122 ] ] } ]
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[]
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106
BioInfer.d68.s1
[ { "id": "BioInfer.d68.s1__text", "type": "Sentence", "text": [ "Green fluorescent protein-tagged ORC1 associated with chromatin throughout mitosis in living cells and co-localized with ORC4 in metaphase spreads." ], "offsets": [ [ 0, 147 ] ] } ]
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[]
[]
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107
BioInfer.d69.s0
[ { "id": "BioInfer.d69.s0__text", "type": "Sentence", "text": [ "A pre-treatment of cells with SGE from partially fed ticks in amounts corresponding to 1 or 3 salivary glands increased the level of both viral nucleocapsid (N) protein and phosphoprotein (P) in a dose-dependent manner." ], "offsets": [ [ 0, 219 ] ] } ]
[ { "id": "BioInfer.d69.s0.e0", "type": "Individual_protein", "text": [ "phosphoprotein" ], "offsets": [ [ 173, 187 ] ], "normalized": [] }, { "id": "BioInfer.d69.s0.e1", "type": "Individual_protein", "text": [ "P" ], "offsets": [ [ 189, 190 ] ], "normalized": [] }, { "id": "BioInfer.d69.s0.e2", "type": "Individual_protein", "text": [ "nucleocapsid", "protein" ], "offsets": [ [ 144, 156 ], [ 161, 168 ] ], "normalized": [] }, { "id": "BioInfer.d69.s0.e3", "type": "Individual_protein", "text": [ "N" ], "offsets": [ [ 158, 159 ] ], "normalized": [] } ]
[]
[]
[]
108
BioInfer.d70.s0
[ { "id": "BioInfer.d70.s0__text", "type": "Sentence", "text": [ "Aprotinin inhibited platelet aggregation induced by thrombin (0.25 U.ml-1) with IC50 200 kIU.ml-1, and inhibited the rise of cytosolic free calcium concentration in platelets stimulated by thrombin (0.1 U.ml-1) in the absence and in the presence of Ca2+ 0.5 mmol.L-1 (IC50 117 and 50 kIU.ml-1, respectively), but had no effect on the amounts of actin and myosin heavy chain associated with cytoskeletons." ], "offsets": [ [ 0, 404 ] ] } ]
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[]
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109
BioInfer.d71.s0
[ { "id": "BioInfer.d71.s0__text", "type": "Sentence", "text": [ "RAD51, RAD52, and RAD54 encode proteins that are critical to the repair of double-strand DNA breaks by homologous recombination." ], "offsets": [ [ 0, 128 ] ] } ]
[ { "id": "BioInfer.d71.s0.e0", "type": "Gene/protein/RNA", "text": [ "RAD52" ], "offsets": [ [ 7, 12 ] ], "normalized": [] }, { "id": "BioInfer.d71.s0.e1", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 0, 5 ] ], "normalized": [] }, { "id": "BioInfer.d71.s0.e2", "type": "Gene/protein/RNA", "text": [ "RAD54" ], "offsets": [ [ 18, 23 ] ], "normalized": [] } ]
[]
[]
[]
110
BioInfer.d72.s0
[ { "id": "BioInfer.d72.s0__text", "type": "Sentence", "text": [ "RAD51, RAD52, RAD57, and RAD59 were required for efficient gap repair using either chromosomal or plasmid donors." ], "offsets": [ [ 0, 113 ] ] } ]
[ { "id": "BioInfer.d72.s0.e0", "type": "Gene/protein/RNA", "text": [ "RAD59" ], "offsets": [ [ 25, 30 ] ], "normalized": [] }, { "id": "BioInfer.d72.s0.e1", "type": "Gene/protein/RNA", "text": [ "RAD52" ], "offsets": [ [ 7, 12 ] ], "normalized": [] }, { "id": "BioInfer.d72.s0.e2", "type": "Gene/protein/RNA", "text": [ "RAD57" ], "offsets": [ [ 14, 19 ] ], "normalized": [] }, { "id": "BioInfer.d72.s0.e3", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 0, 5 ] ], "normalized": [] } ]
[]
[]
[]
111
BioInfer.d73.s0
[ { "id": "BioInfer.d73.s0__text", "type": "Sentence", "text": [ "RAD51, RAD54, RAD55 and RAD57 are all required to facilitate strand invasion into otherwise inaccessible donor sequences." ], "offsets": [ [ 0, 121 ] ] } ]
[ { "id": "BioInfer.d73.s0.e0", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 0, 5 ] ], "normalized": [] }, { "id": "BioInfer.d73.s0.e1", "type": "Gene/protein/RNA", "text": [ "RAD55" ], "offsets": [ [ 14, 19 ] ], "normalized": [] }, { "id": "BioInfer.d73.s0.e2", "type": "Gene/protein/RNA", "text": [ "RAD54" ], "offsets": [ [ 7, 12 ] ], "normalized": [] }, { "id": "BioInfer.d73.s0.e3", "type": "Gene/protein/RNA", "text": [ "RAD57" ], "offsets": [ [ 24, 29 ] ], "normalized": [] } ]
[]
[]
[]
112
BioInfer.d73.s1
[ { "id": "BioInfer.d73.s1__text", "type": "Sentence", "text": [ "RAD51, RAD54, RAD55 and RAD57 are still required when the same transcribed donor is on the chromosome." ], "offsets": [ [ 0, 102 ] ] } ]
[ { "id": "BioInfer.d73.s1.e0", "type": "Gene/protein/RNA", "text": [ "RAD55" ], "offsets": [ [ 14, 19 ] ], "normalized": [] }, { "id": "BioInfer.d73.s1.e1", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 0, 5 ] ], "normalized": [] }, { "id": "BioInfer.d73.s1.e2", "type": "Gene/protein/RNA", "text": [ "RAD57" ], "offsets": [ [ 24, 29 ] ], "normalized": [] }, { "id": "BioInfer.d73.s1.e3", "type": "Gene/protein/RNA", "text": [ "RAD54" ], "offsets": [ [ 7, 12 ] ], "normalized": [] } ]
[]
[]
[]
113
BioInfer.d73.s2
[ { "id": "BioInfer.d73.s2__text", "type": "Sentence", "text": [ "Here we use physical monitoring of DNA to show that MAT switching is completely blocked at an early step in recombination in strains deleted for the DNA repair genes RAD51, RAD52, RAD54, RAD55 or RAD57." ], "offsets": [ [ 0, 202 ] ] } ]
[ { "id": "BioInfer.d73.s2.e0", "type": "Gene/protein/RNA", "text": [ "RAD55" ], "offsets": [ [ 187, 192 ] ], "normalized": [] }, { "id": "BioInfer.d73.s2.e1", "type": "Gene/protein/RNA", "text": [ "RAD52" ], "offsets": [ [ 173, 178 ] ], "normalized": [] }, { "id": "BioInfer.d73.s2.e2", "type": "Gene/protein/RNA", "text": [ "RAD57" ], "offsets": [ [ 196, 201 ] ], "normalized": [] }, { "id": "BioInfer.d73.s2.e3", "type": "Gene/protein/RNA", "text": [ "RAD51" ], "offsets": [ [ 166, 171 ] ], "normalized": [] }, { "id": "BioInfer.d73.s2.e4", "type": "Gene/protein/RNA", "text": [ "RAD54" ], "offsets": [ [ 180, 185 ] ], "normalized": [] } ]
[]
[]
[]
114
BioInfer.d75.s0
[ { "id": "BioInfer.d75.s0__text", "type": "Sentence", "text": [ "A reconstitution is described that requires not only the growth factor, its receptor with tyrosine kinase activity, and the soluble phospholipase C-gamma 1, but also the small soluble actin-binding protein profilin." ], "offsets": [ [ 0, 215 ] ] } ]
[ { "id": "BioInfer.d75.s0.e0", "type": "Gene/protein/RNA", "text": [ "phospholipase C-gamma 1" ], "offsets": [ [ 132, 155 ] ], "normalized": [] }, { "id": "BioInfer.d75.s0.e1", "type": "Protein_family_or_group", "text": [ "actin-binding protein" ], "offsets": [ [ 184, 205 ] ], "normalized": [] }, { "id": "BioInfer.d75.s0.e2", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 206, 214 ] ], "normalized": [] }, { "id": "BioInfer.d75.s0.e3", "type": "Gene/protein/RNA", "text": [ "tyrosine kinase" ], "offsets": [ [ 90, 105 ] ], "normalized": [] } ]
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115
BioInfer.d76.s0
[ { "id": "BioInfer.d76.s0__text", "type": "Sentence", "text": [ "Armadillo (Arm) repeat 10 to the COOH terminus of beta-catenin is involved in binding to CBP, whereas beta-catenin interacts directly with the CREB-binding domain of CBP." ], "offsets": [ [ 0, 170 ] ] } ]
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116
BioInfer.d77.s0
[ { "id": "BioInfer.d77.s0__text", "type": "Sentence", "text": [ "Arp2/3 complex from Acanthamoeba binds profilin and cross-links actin filaments." ], "offsets": [ [ 0, 80 ] ] } ]
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117
BioInfer.d77.s1
[ { "id": "BioInfer.d77.s1__text", "type": "Sentence", "text": [ "By analytical ultracentrifugation, rhodamine-labeled profilin binds Arp2/3 complex with a Kd of 7 microM, an affinity intermediate between the low affinity of profilin for barbed ends of actin filaments and its high affinity for actin monomers." ], "offsets": [ [ 0, 244 ] ] } ]
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[]
[]
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118
BioInfer.d77.s2
[ { "id": "BioInfer.d77.s2__text", "type": "Sentence", "text": [ "Here we show that the Arp2 subunit of the complex can be chemically cross-linked to the actin-binding site of profilin." ], "offsets": [ [ 0, 119 ] ] } ]
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[]
[]
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119
BioInfer.d78.s0
[ { "id": "BioInfer.d78.s0__text", "type": "Sentence", "text": [ "As a nuclear transport signal sequence exists in cofilin and ADF but not in actin, ADF and/or cofilin may be responsible for the nuclear import of actin in myogenic cells under certain conditions." ], "offsets": [ [ 0, 196 ] ] } ]
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[]
[]
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120
BioInfer.d78.s1
[ { "id": "BioInfer.d78.s1__text", "type": "Sentence", "text": [ "Immunofluorescence microscopy revealed that two actin-binding proteins of low molecular weight with different functional activity, ADF and cofilin, are transported into nuclei of cultured myogenic cells to form rod structures there together with actin, when the cells were incubated in medium containing dimethylsulfoxide." ], "offsets": [ [ 0, 322 ] ] } ]
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[]
[]
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121
BioInfer.d78.s2
[ { "id": "BioInfer.d78.s2__text", "type": "Sentence", "text": [ "In most cases, ADF and cofilin colocalized in the same nuclear actin rods, but ADF appeared to predominate in mononucleated cells, while cofilin was present in multinucleated myotubes." ], "offsets": [ [ 0, 184 ] ] } ]
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[]
[]
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122
BioInfer.d79.s0
[ { "id": "BioInfer.d79.s0__text", "type": "Sentence", "text": [ "A series of truncations was carried out at the C terminus of profilin, a region that has been implicated in actin binding." ], "offsets": [ [ 0, 122 ] ] } ]
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[]
[]
[ { "id": "BioInfer.d79.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d79.s0.e0", "arg2_id": "BioInfer.d79.s0.e1", "normalized": [] } ]
123
BioInfer.d79.s1
[ { "id": "BioInfer.d79.s1__text", "type": "Sentence", "text": [ "Since our earlier studies of Acanthamoeba profilins suggested the importance of PIP2 binding for suppression, we conclude that both activities are implicated and that an interplay between PIP2 binding and actin binding may be important for profilin function." ], "offsets": [ [ 0, 258 ] ] } ]
[ { "id": "BioInfer.d79.s1.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 240, 248 ] ], "normalized": [] }, { "id": "BioInfer.d79.s1.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 205, 210 ] ], "normalized": [] }, { "id": "BioInfer.d79.s1.e2", "type": "Gene/protein/RNA", "text": [ "profilins" ], "offsets": [ [ 42, 51 ] ], "normalized": [] } ]
[]
[]
[ { "id": "BioInfer.d79.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d79.s1.e0", "arg2_id": "BioInfer.d79.s1.e1", "normalized": [] } ]
124
BioInfer.d81.s0
[ { "id": "BioInfer.d81.s0__text", "type": "Sentence", "text": [ "As expected from immunofluorescence experiments, Abp1p, cofilin, and actin colocalized in immuno-EM to the dense patchlike structures but not to the cables." ], "offsets": [ [ 0, 156 ] ] } ]
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[]
[]
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125
BioInfer.d81.s1
[ { "id": "BioInfer.d81.s1__text", "type": "Sentence", "text": [ "Immuno-EM double-labeling experiments were conducted with antibodies to actin together with antibodies to the actin binding proteins Abp1p and cofilin." ], "offsets": [ [ 0, 151 ] ] } ]
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[]
[]
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126
BioInfer.d82.s0
[ { "id": "BioInfer.d82.s0__text", "type": "Sentence", "text": [ "A similar phenotype was seen in testes treated with cytochalasin B and has been noted previously in mutants at the twinstar locus, a gene that encodes a Drosophila member of the cofilin/ADF family of actin-severing proteins." ], "offsets": [ [ 0, 224 ] ] } ]
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[]
[]
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127
BioInfer.d83.s0
[ { "id": "BioInfer.d83.s0__text", "type": "Sentence", "text": [ "As previous studies indicated that the RVS161 and RVS167 gene products of Saccharomyces cerevisiae seem to be involved in the same cellular function, we considered the possibility of a complex between the proteins encoded by these two genes." ], "offsets": [ [ 0, 241 ] ] } ]
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[]
[]
[ { "id": "BioInfer.d83.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d83.s0.e0", "arg2_id": "BioInfer.d83.s0.e1", "normalized": [] } ]
128
BioInfer.d84.s0
[ { "id": "BioInfer.d84.s0__text", "type": "Sentence", "text": [ "As shown by in situ hybridization with cloned probes and analysis of in vitro translation products, M. occulta embryos do not accumulate high levels of alpha actin or myosin heavy chain mRNA." ], "offsets": [ [ 0, 191 ] ] } ]
[ { "id": "BioInfer.d84.s0.e0", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 167, 185 ] ], "normalized": [] }, { "id": "BioInfer.d84.s0.e1", "type": "Gene/protein/RNA", "text": [ "alpha actin" ], "offsets": [ [ 152, 163 ] ], "normalized": [] } ]
[]
[]
[]
129
BioInfer.d84.s1
[ { "id": "BioInfer.d84.s1__text", "type": "Sentence", "text": [ "In contrast, alpha actin and myosin heavy chain mRNA accumulation was not enhanced in hybrid embryos." ], "offsets": [ [ 0, 101 ] ] } ]
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[]
[]
[]
130
BioInfer.d85.s0
[ { "id": "BioInfer.d85.s0__text", "type": "Sentence", "text": [ "Associations of UBE2I with RAD52, UBL1, p53, and RAD51 proteins in a yeast two-hybrid system." ], "offsets": [ [ 0, 93 ] ] } ]
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[]
[]
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131
BioInfer.d87.s0
[ { "id": "BioInfer.d87.s0__text", "type": "Sentence", "text": [ "A truncated beta-catenin disrupts the interaction between E-cadherin and alpha-catenin: a cause of loss of intercellular adhesiveness in human cancer cell lines." ], "offsets": [ [ 0, 161 ] ] } ]
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[]
[]
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132
BioInfer.d87.s1
[ { "id": "BioInfer.d87.s1__text", "type": "Sentence", "text": [ "However, the recombinant fusion protein containing wild-type beta-catenin precipitated alpha-catenin from these cells." ], "offsets": [ [ 0, 118 ] ] } ]
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[]
[]
[]
133
BioInfer.d87.s2
[ { "id": "BioInfer.d87.s2__text", "type": "Sentence", "text": [ "These results suggest that the dysfunction of E-cadherin in these cell lines is due primarily to its failure to interact with alpha-catenin, and that this defect results from the mutation in beta-catenin." ], "offsets": [ [ 0, 204 ] ] } ]
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[]
[]
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134
BioInfer.d87.s3
[ { "id": "BioInfer.d87.s3__text", "type": "Sentence", "text": [ "Thus, it is most likely that the association between E-cadherin and alpha-catenin is mediated by beta-catenin, and that this process is blocked by NH2-terminal deletion in beta-catenin." ], "offsets": [ [ 0, 185 ] ] } ]
[ { "id": "BioInfer.d87.s3.e0", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 68, 81 ] ], "normalized": [] }, { "id": "BioInfer.d87.s3.e1", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 53, 63 ] ], "normalized": [] }, { "id": "BioInfer.d87.s3.e2", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 97, 109 ] ], "normalized": [] }, { "id": "BioInfer.d87.s3.e3", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 172, 184 ] ], "normalized": [] } ]
[]
[]
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135
BioInfer.d87.s4
[ { "id": "BioInfer.d87.s4__text", "type": "Sentence", "text": [ "While alpha-catenin has been demonstrated to be crucial for cadherin function, the role of beta-catenin is not yet fully understood." ], "offsets": [ [ 0, 132 ] ] } ]
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[]
[]
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136
BioInfer.d88.s0
[ { "id": "BioInfer.d88.s0__text", "type": "Sentence", "text": [ "At the light microscope level, brush cells can be identified by antibodies against the actin filament crosslinking proteins villin and fimbrin that not only stain the apical tuft of microvilli and their rootlets, but also label projections emanating from the basolateral surface of these cells." ], "offsets": [ [ 0, 294 ] ] } ]
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[]
[]
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137
BioInfer.d89.s0
[ { "id": "BioInfer.d89.s0__text", "type": "Sentence", "text": [ "BACKGROUND: Although profilin is believed to be an essential regulator of the actin cytoskeleton in most cells, its precise role in mammalian cells remains unknown." ], "offsets": [ [ 0, 164 ] ] } ]
[ { "id": "BioInfer.d89.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 78, 83 ] ], "normalized": [] }, { "id": "BioInfer.d89.s0.e1", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 21, 29 ] ], "normalized": [] } ]
[]
[]
[ { "id": "BioInfer.d89.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d89.s0.e0", "arg2_id": "BioInfer.d89.s0.e1", "normalized": [] } ]
138
BioInfer.d91.s0
[ { "id": "BioInfer.d91.s0__text", "type": "Sentence", "text": [ "BACKGROUND: p27(Kip1), a cyclin-dependent kinase inhibitor, negatively regulates the G1 phase progression of the cell cycle by binding to the cyclin E/cyclin-dependent kinase 2 complex." ], "offsets": [ [ 0, 185 ] ] } ]
[ { "id": "BioInfer.d91.s0.e0", "type": "Individual_protein", "text": [ "p27" ], "offsets": [ [ 12, 15 ] ], "normalized": [] }, { "id": "BioInfer.d91.s0.e1", "type": "Individual_protein", "text": [ "cyclin E" ], "offsets": [ [ 142, 150 ] ], "normalized": [] }, { "id": "BioInfer.d91.s0.e2", "type": "Individual_protein", "text": [ "Kip1" ], "offsets": [ [ 16, 20 ] ], "normalized": [] }, { "id": "BioInfer.d91.s0.e3", "type": "Individual_protein", "text": [ "cyclin-dependent kinase 2" ], "offsets": [ [ 151, 176 ] ], "normalized": [] }, { "id": "BioInfer.d91.s0.e4", "type": "Protein_family_or_group", "text": [ "cyclin-dependent kinase inhibitor" ], "offsets": [ [ 25, 58 ] ], "normalized": [] } ]
[]
[]
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139
BioInfer.d92.s0
[ { "id": "BioInfer.d92.s0__text", "type": "Sentence", "text": [ "Because beta-catenin is known to interact with alpha-catenin, which binds to actin, we generated a fusion molecule consisting of the ectodomain of E-cadherin and the actin binding site of alpha-catenin." ], "offsets": [ [ 0, 202 ] ] } ]
[ { "id": "BioInfer.d92.s0.e0", "type": "Individual_protein", "text": [ "beta-catenin" ], "offsets": [ [ 8, 20 ] ], "normalized": [] }, { "id": "BioInfer.d92.s0.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 166, 171 ] ], "normalized": [] }, { "id": "BioInfer.d92.s0.e2", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 188, 201 ] ], "normalized": [] }, { "id": "BioInfer.d92.s0.e3", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 77, 82 ] ], "normalized": [] }, { "id": "BioInfer.d92.s0.e4", "type": "Individual_protein", "text": [ "E-cadherin" ], "offsets": [ [ 147, 157 ] ], "normalized": [] }, { "id": "BioInfer.d92.s0.e5", "type": "Individual_protein", "text": [ "alpha-catenin" ], "offsets": [ [ 47, 60 ] ], "normalized": [] } ]
[]
[]
[ { "id": "BioInfer.d92.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d92.s0.e0", "arg2_id": "BioInfer.d92.s0.e5", "normalized": [] }, { "id": "BioInfer.d92.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d92.s0.e1", "arg2_id": "BioInfer.d92.s0.e2", "normalized": [] }, { "id": "BioInfer.d92.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d92.s0.e2", "arg2_id": "BioInfer.d92.s0.e4", "normalized": [] }, { "id": "BioInfer.d92.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d92.s0.e3", "arg2_id": "BioInfer.d92.s0.e5", "normalized": [] } ]
140
BioInfer.d94.s0
[ { "id": "BioInfer.d94.s0__text", "type": "Sentence", "text": [ "Because both proteins exchange rapidly between actin molecules, low concentrations of profilin can overcome the inhibitory effects of high concentrations of thymosin beta 4 on the nucleotide exchange." ], "offsets": [ [ 0, 200 ] ] } ]
[ { "id": "BioInfer.d94.s0.e0", "type": "Individual_protein", "text": [ "profilin" ], "offsets": [ [ 86, 94 ] ], "normalized": [] }, { "id": "BioInfer.d94.s0.e1", "type": "Individual_protein", "text": [ "thymosin beta 4" ], "offsets": [ [ 157, 172 ] ], "normalized": [] }, { "id": "BioInfer.d94.s0.e2", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 47, 52 ] ], "normalized": [] } ]
[]
[]
[ { "id": "BioInfer.d94.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d94.s0.e0", "arg2_id": "BioInfer.d94.s0.e1", "normalized": [] }, { "id": "BioInfer.d94.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d94.s0.e0", "arg2_id": "BioInfer.d94.s0.e2", "normalized": [] }, { "id": "BioInfer.d94.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d94.s0.e1", "arg2_id": "BioInfer.d94.s0.e2", "normalized": [] } ]
141
BioInfer.d95.s0
[ { "id": "BioInfer.d95.s0__text", "type": "Sentence", "text": [ "Because other researchers have shown that the RAD51 and RAD52 proteins interact, RAD51 on a high copy number plasmid was tested and found to suppress the rad52-20 allele, but RAD 54, 55 and 57 did not suppress." ], "offsets": [ [ 0, 210 ] ] } ]
[ { "id": "BioInfer.d95.s0.e0", "type": "Gene", "text": [ "RAD51" ], "offsets": [ [ 81, 86 ] ], "normalized": [] }, { "id": "BioInfer.d95.s0.e1", "type": "Gene", "text": [ "RAD 54" ], "offsets": [ [ 175, 181 ] ], "normalized": [] }, { "id": "BioInfer.d95.s0.e2", "type": "Gene", "text": [ "RAD", "57" ], "offsets": [ [ 175, 178 ], [ 190, 192 ] ], "normalized": [] }, { "id": "BioInfer.d95.s0.e3", "type": "Gene", "text": [ "RAD", "55" ], "offsets": [ [ 175, 178 ], [ 183, 185 ] ], "normalized": [] }, { "id": "BioInfer.d95.s0.e4", "type": "Gene", "text": [ "RAD51" ], "offsets": [ [ 46, 51 ] ], "normalized": [] }, { "id": "BioInfer.d95.s0.e5", "type": "Gene", "text": [ "RAD52" ], "offsets": [ [ 56, 61 ] ], "normalized": [] }, { "id": "BioInfer.d95.s0.e6", "type": "Gene", "text": [ "rad52-20" ], "offsets": [ [ 154, 162 ] ], "normalized": [] } ]
[]
[]
[ { "id": "BioInfer.d95.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d95.s0.e0", "arg2_id": "BioInfer.d95.s0.e1", "normalized": [] }, { "id": "BioInfer.d95.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d95.s0.e0", "arg2_id": "BioInfer.d95.s0.e2", "normalized": [] }, { "id": "BioInfer.d95.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d95.s0.e0", "arg2_id": "BioInfer.d95.s0.e3", "normalized": [] }, { "id": "BioInfer.d95.s0.i3", "type": "PPI", "arg1_id": "BioInfer.d95.s0.e0", "arg2_id": "BioInfer.d95.s0.e6", "normalized": [] }, { "id": "BioInfer.d95.s0.i4", "type": "PPI", "arg1_id": "BioInfer.d95.s0.e4", "arg2_id": "BioInfer.d95.s0.e5", "normalized": [] } ]
142
BioInfer.d96.s0
[ { "id": "BioInfer.d96.s0__text", "type": "Sentence", "text": [ "Between day 1 and day 3 in culture, the specific synthetic activities of total proteins and of electrophoretically purified myosin heavy chain and actin ([14C] phenylalanine incorporation into protein, in disintegrations per minute per microgram protein) decreased (-19%,-32%, and -73%, respectively)." ], "offsets": [ [ 0, 301 ] ] } ]
[ { "id": "BioInfer.d96.s0.e0", "type": "Gene/protein/RNA", "text": [ "myosin heavy chain" ], "offsets": [ [ 124, 142 ] ], "normalized": [] }, { "id": "BioInfer.d96.s0.e1", "type": "Gene/protein/RNA", "text": [ "actin" ], "offsets": [ [ 147, 152 ] ], "normalized": [] } ]
[]
[]
[]
143
BioInfer.d97.s0
[ { "id": "BioInfer.d97.s0__text", "type": "Sentence", "text": [ "Binding of talin to actin occurs at a maximal molar ratio of 1:3 as determined by fluorescencetitration under G-buffer conditions." ], "offsets": [ [ 0, 130 ] ] } ]
[ { "id": "BioInfer.d97.s0.e0", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 20, 25 ] ], "normalized": [] }, { "id": "BioInfer.d97.s0.e1", "type": "Individual_protein", "text": [ "talin" ], "offsets": [ [ 11, 16 ] ], "normalized": [] } ]
[]
[]
[ { "id": "BioInfer.d97.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d97.s0.e0", "arg2_id": "BioInfer.d97.s0.e1", "normalized": [] } ]
144
BioInfer.d97.s1
[ { "id": "BioInfer.d97.s1__text", "type": "Sentence", "text": [ "Platelet talin binds to actin in vitro and hence is an actin binding protein." ], "offsets": [ [ 0, 77 ] ] } ]
[ { "id": "BioInfer.d97.s1.e0", "type": "Individual_protein", "text": [ "Platelet talin" ], "offsets": [ [ 0, 14 ] ], "normalized": [] }, { "id": "BioInfer.d97.s1.e1", "type": "Individual_protein", "text": [ "actin" ], "offsets": [ [ 24, 29 ] ], "normalized": [] }, { "id": "BioInfer.d97.s1.e2", "type": "Protein_family_or_group", "text": [ "actin binding protein" ], "offsets": [ [ 55, 76 ] ], "normalized": [] } ]
[]
[]
[ { "id": "BioInfer.d97.s1.i0", "type": "PPI", "arg1_id": "BioInfer.d97.s1.e0", "arg2_id": "BioInfer.d97.s1.e1", "normalized": [] }, { "id": "BioInfer.d97.s1.i1", "type": "PPI", "arg1_id": "BioInfer.d97.s1.e0", "arg2_id": "BioInfer.d97.s1.e2", "normalized": [] } ]
145
BioInfer.d99.s0
[ { "id": "BioInfer.d99.s0__text", "type": "Sentence", "text": [ "Biochemical analyses revealed a strong induction of VEGF-receptor-2 (flk-1/KDR) tyrosine-autophosphorylation by VEGF which was maximal after 5 minutes and was followed by receptor downregulation." ], "offsets": [ [ 0, 195 ] ] } ]
[ { "id": "BioInfer.d99.s0.e0", "type": "Individual_protein", "text": [ "VEGF-receptor-2" ], "offsets": [ [ 52, 67 ] ], "normalized": [] }, { "id": "BioInfer.d99.s0.e1", "type": "Individual_protein", "text": [ "VEGF" ], "offsets": [ [ 112, 116 ] ], "normalized": [] }, { "id": "BioInfer.d99.s0.e2", "type": "Individual_protein", "text": [ "KDR" ], "offsets": [ [ 75, 78 ] ], "normalized": [] }, { "id": "BioInfer.d99.s0.e3", "type": "Individual_protein", "text": [ "flk-1" ], "offsets": [ [ 69, 74 ] ], "normalized": [] } ]
[]
[]
[ { "id": "BioInfer.d99.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d99.s0.e0", "arg2_id": "BioInfer.d99.s0.e1", "normalized": [] }, { "id": "BioInfer.d99.s0.i1", "type": "PPI", "arg1_id": "BioInfer.d99.s0.e1", "arg2_id": "BioInfer.d99.s0.e2", "normalized": [] }, { "id": "BioInfer.d99.s0.i2", "type": "PPI", "arg1_id": "BioInfer.d99.s0.e1", "arg2_id": "BioInfer.d99.s0.e3", "normalized": [] } ]
146
BioInfer.d100.s0
[ { "id": "BioInfer.d100.s0__text", "type": "Sentence", "text": [ "Biochemical complementation experiments also indicate that the PRP9 and PRP11 proteins interact." ], "offsets": [ [ 0, 96 ] ] } ]
[ { "id": "BioInfer.d100.s0.e0", "type": "Individual_protein", "text": [ "PRP11" ], "offsets": [ [ 72, 77 ] ], "normalized": [] }, { "id": "BioInfer.d100.s0.e1", "type": "Individual_protein", "text": [ "PRP9" ], "offsets": [ [ 63, 67 ] ], "normalized": [] } ]
[]
[]
[ { "id": "BioInfer.d100.s0.i0", "type": "PPI", "arg1_id": "BioInfer.d100.s0.e0", "arg2_id": "BioInfer.d100.s0.e1", "normalized": [] } ]
147
BioInfer.d100.s1
[ { "id": "BioInfer.d100.s1__text", "type": "Sentence", "text": [ "Four yeast spliceosomal proteins (PRP5, PRP9, PRP11, and PRP21) interact to promote U2 snRNP binding to pre-mRNA." ], "offsets": [ [ 0, 113 ] ] } ]
[ { "id": "BioInfer.d100.s1.e0", "type": "Individual_protein", "text": [ "PRP5" ], "offsets": [ [ 34, 38 ] ], "normalized": [] }, { "id": "BioInfer.d100.s1.e1", "type": "Individual_protein", "text": [ "U2 snRNP" ], "offsets": [ [ 84, 92 ] ], "normalized": [] }, { "id": "BioInfer.d100.s1.e2", "type": "Individual_protein", "text": [ "PRP21" ], "offsets": [ [ 57, 62 ] ], "normalized": [] }, { "id": "BioInfer.d100.s1.e3", "type": "Individual_protein", "text": [ "PRP9" ], "offsets": [ [ 40, 44 ] ], "normalized": [] }, { "id": "BioInfer.d100.s1.e4", "type": "Individual_protein", "text": [ "PRP11" ], "offsets": [ [ 46, 51 ] ], "normalized": [] } ]
[]
[]
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148
BioInfer.d100.s2
[ { "id": "BioInfer.d100.s2__text", "type": "Sentence", "text": [ "Here, we show that PRP5 (a DEAD box helicase-like protein), PRP9, and PRP11 are each required for the U2 snRNP to bind to the pre-spliceosome during spliceosome assembly in vitro." ], "offsets": [ [ 0, 179 ] ] } ]
[ { "id": "BioInfer.d100.s2.e0", "type": "Individual_protein", "text": [ "PRP9" ], "offsets": [ [ 60, 64 ] ], "normalized": [] }, { "id": "BioInfer.d100.s2.e1", "type": "Individual_protein", "text": [ "PRP5" ], "offsets": [ [ 19, 23 ] ], "normalized": [] }, { "id": "BioInfer.d100.s2.e2", "type": "Individual_protein", "text": [ "PRP11" ], "offsets": [ [ 70, 75 ] ], "normalized": [] }, { "id": "BioInfer.d100.s2.e3", "type": "Individual_protein", "text": [ "U2 snRNP" ], "offsets": [ [ 102, 110 ] ], "normalized": [] }, { "id": "BioInfer.d100.s2.e4", "type": "Individual_protein", "text": [ "DEAD box helicase" ], "offsets": [ [ 27, 44 ] ], "normalized": [] } ]
[]
[]
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149
BioInfer.d102.s0
[ { "id": "BioInfer.d102.s0__text", "type": "Sentence", "text": [ "Birch pollen profilin and actin can be copurified as a complex, and purified recombinant birch profilin can be used as an affinity matrix to obtain birch pollen actin." ], "offsets": [ [ 0, 167 ] ] } ]
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150
BioInfer.d102.s1
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151
BioInfer.d102.s2
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152
BioInfer.d103.s0
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153
BioInfer.d104.s0
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154
BioInfer.d105.s0
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155
BioInfer.d106.s0
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156
BioInfer.d107.s0
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157
BioInfer.d108.s0
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158
BioInfer.d111.s0
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159
BioInfer.d112.s0
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160
BioInfer.d113.s0
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161
BioInfer.d113.s1
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162
BioInfer.d113.s2
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163
BioInfer.d114.s0
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164
BioInfer.d115.s0
[ { "id": "BioInfer.d115.s0__text", "type": "Sentence", "text": [ "SNF11, a new component of the yeast SNF-SWI complex that interacts with a conserved region of SNF2." ], "offsets": [ [ 0, 99 ] ] } ]
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165
BioInfer.d115.s1
[ { "id": "BioInfer.d115.s1__text", "type": "Sentence", "text": [ "SNF11 interacts with SNF2 in vitro and copurifies with the SNF-SWI complex from yeast cells." ], "offsets": [ [ 0, 92 ] ] } ]
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166
BioInfer.d116.s0
[ { "id": "BioInfer.d116.s0__text", "type": "Sentence", "text": [ "Bud-site selection directs both cell polarity and the cytoskeletal orientation during budding and is determined by at least five genes: BUD1/RSR1, BUD2, BUD3, BUD4 and BUD5." ], "offsets": [ [ 0, 173 ] ] } ]
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[]
[]
[]
167
BioInfer.d117.s0
[ { "id": "BioInfer.d117.s0__text", "type": "Sentence", "text": [ "By 1 h the cells were well spread with straight actin bundles many of which ended at more central sites terminating on patches containing vinculin and talin; thus the cells assemble typical stress fibers but do not appear to polarize." ], "offsets": [ [ 0, 234 ] ] } ]
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168
BioInfer.d118.s0
[ { "id": "BioInfer.d118.s0__text", "type": "Sentence", "text": [ "By indirect immunofluorescence, both R. rickettsii and Listeria monocytogenes actin tails were shown to contain the cytoskeletal proteins vasodilator-stimulated phosphoprotein profilin, vinculin, and filamin." ], "offsets": [ [ 0, 208 ] ] } ]
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[]
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169
BioInfer.d119.s0
[ { "id": "BioInfer.d119.s0__text", "type": "Sentence", "text": [ "By site-directed mutagenesis of profilin II from Dictyostelium discoideum the point mutations K114E and W3N were generated by PCR thus changing actin and poly-(L)-proline-binding activity respectively." ], "offsets": [ [ 0, 201 ] ] } ]
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170
BioInfer.d119.s1
[ { "id": "BioInfer.d119.s1__text", "type": "Sentence", "text": [ "The K114E profilin exhibited a profound decrease in its ability to interact with actin, whereas binding to poly-(L)-proline was essentially unchanged." ], "offsets": [ [ 0, 150 ] ] } ]
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171
BioInfer.d121.s0
[ { "id": "BioInfer.d121.s0__text", "type": "Sentence", "text": [ "By this method, it was shown that four of these large RNA species are polycistronic transcripts containing sequences from two genes: one species contains nucleocapsid protein (NP) and phosphoprotein (P) gene sequences; another, P and membrane protein (M) gene sequences; another, M and fusion protein (F0) gene sequences; and another, F0 and hemagglutinin-neuraminidase protein (HN) gene sequences." ], "offsets": [ [ 0, 398 ] ] } ]
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[]
[]
[]
172
BioInfer.d122.s0
[ { "id": "BioInfer.d122.s0__text", "type": "Sentence", "text": [ "By two-hybrid screening we have identified two partners that directly associate with TIF34: PRT1, a previously characterized eIF3 subunit, and a novel protein of 33 kDa (eIF3-p33) which is part of the eIF3 complex and has an RNA binding domain." ], "offsets": [ [ 0, 244 ] ] } ]
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[]
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173
BioInfer.d122.s1
[ { "id": "BioInfer.d122.s1__text", "type": "Sentence", "text": [ "Our results provide support for both physical and functional interactions between three subunits, TIF34, PRT1 and p33, in the eIF3 complex." ], "offsets": [ [ 0, 139 ] ] } ]
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174
BioInfer.d123.s0
[ { "id": "BioInfer.d123.s0__text", "type": "Sentence", "text": [ "By using a chromatin immunoprecipitation (ChIP) assay, we observed that histone H4, and not histone H3, was acetylated from the endogenous p21/waf1 promoter in vivo, implying that CBP/p300, and not the SAGA complex, was critical in complexing with E2A in up-regulation of p21/waf1 in HTLV-1-infected cells." ], "offsets": [ [ 0, 306 ] ] } ]
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175
BioInfer.d124.s0
[ { "id": "BioInfer.d124.s0__text", "type": "Sentence", "text": [ "Cadherins are essential for embryonic morphogenesis since they mediate calcium-dependent cell-cell adhesion and can modulate beta-catenin signaling." ], "offsets": [ [ 0, 148 ] ] } ]
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176
BioInfer.d124.s1
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BioInfer.d126.s0
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BioInfer.d131.s0
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BioInfer.d134.s0
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BioInfer.d134.s1
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BioInfer.d135.s0
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BioInfer.d135.s1
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BioInfer.d135.s2
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BioInfer.d136.s0
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BioInfer.d137.s0
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BioInfer.d139.s0
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BioInfer.d139.s1
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BioInfer.d140.s2
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195
BioInfer.d141.s0
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196
BioInfer.d142.s0
[ { "id": "BioInfer.d142.s0__text", "type": "Sentence", "text": [ "Chick embryo fibroblasts contain about 75-100 microM unpolymerized actin and at least four proteins which can bind actin monomers, actin depolymerizing factor (ADF), gelsolin, profilin, and thymosin beta4 (Tbeta4)." ], "offsets": [ [ 0, 214 ] ] } ]
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197
BioInfer.d143.s0
[ { "id": "BioInfer.d143.s0__text", "type": "Sentence", "text": [ "Class II profilins had higher affinity for poly-l-proline and sequestered more monomeric actin than did class I profilins." ], "offsets": [ [ 0, 122 ] ] } ]
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198
BioInfer.d143.s1
[ { "id": "BioInfer.d143.s1__text", "type": "Sentence", "text": [ "The actin-sequestering activity of both maize profilin classes was found to be dependent on the concentration of free calcium." ], "offsets": [ [ 0, 126 ] ] } ]
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199
BioInfer.d143.s2
[ { "id": "BioInfer.d143.s2__text", "type": "Sentence", "text": [ "We propose a model in which profilin alters cellular concentrations of actin polymers in response to fluctuations in cytosolic calcium concentration." ], "offsets": [ [ 0, 149 ] ] } ]
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