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transactivation domain (78 amino acid residues, corresponding to residues 413–490) of VP16 was fused in frame with the N-terminus of mouse PPARδ. The VP16-PPARδ fusion cDNA was placed downstream of the human α-skeletal actin promoter (Brennan and Hardeman 1993), and upstream of the SV40 intron/poly(A) sequence. The transgene was purified and injected into C57BL/6J × CBA F1 zygotes. Transgenic mice were backcrossed with C57BL/6J for two generations. Wild-type littermates were used as controls throughout the study. On normal chow diet, the transgenic mice and control littermates used here had similar body weights. PPARδ-null mice were previously generated (Barak et al. 2002). Mice were fed either a standard chow with 4% (w/w) fat content (Harlan Teklad, Harlan, Indianapolis, Indiana, United States) or a high-fat diet containing 35% (w/w) fat content (product F3282, Bioserv, Frenchtown, New Jersey, United States) as indicated. For ligand experiments, we synthesized the GW501516 compound and mice were orally gavaged daily (10 mg/kg or vehicle alone)."}

    2_test

    {"project":"2_test","denotations":[{"id":"15328533-7678010-84708293","span":{"begin":260,"end":264},"obj":"7678010"},{"id":"15328533-11756685-84708294","span":{"begin":680,"end":684},"obj":"11756685"},{"id":"T7615","span":{"begin":260,"end":264},"obj":"7678010"},{"id":"T79960","span":{"begin":680,"end":684},"obj":"11756685"}],"text":"The transactivation domain (78 amino acid residues, corresponding to residues 413–490) of VP16 was fused in frame with the N-terminus of mouse PPARδ. The VP16-PPARδ fusion cDNA was placed downstream of the human α-skeletal actin promoter (Brennan and Hardeman 1993), and upstream of the SV40 intron/poly(A) sequence. The transgene was purified and injected into C57BL/6J × CBA F1 zygotes. Transgenic mice were backcrossed with C57BL/6J for two generations. Wild-type littermates were used as controls throughout the study. On normal chow diet, the transgenic mice and control littermates used here had similar body weights. PPARδ-null mice were previously generated (Barak et al. 2002). Mice were fed either a standard chow with 4% (w/w) fat content (Harlan Teklad, Harlan, Indianapolis, Indiana, United States) or a high-fat diet containing 35% (w/w) fat content (product F3282, Bioserv, Frenchtown, New Jersey, United States) as indicated. For ligand experiments, we synthesized the GW501516 compound and mice were orally gavaged daily (10 mg/kg or vehicle alone)."}

    craft-ca-core-ex-dev

    {"project":"craft-ca-core-ex-dev","denotations":[{"id":"T3983","span":{"begin":610,"end":614},"obj":"UBERON_EXT:body"},{"id":"T3984","span":{"begin":624,"end":629},"obj":"PR_EXT:000013057"},{"id":"T3985","span":{"begin":630,"end":634},"obj":"SO_EXT:sequence_nullness"},{"id":"T3986","span":{"begin":635,"end":639},"obj":"NCBITaxon:10088"},{"id":"T3987","span":{"begin":687,"end":691},"obj":"NCBITaxon:10088"},{"id":"T3988","span":{"begin":697,"end":700},"obj":"GO:0007631"},{"id":"T3989","span":{"begin":719,"end":723},"obj":"CHEBI_EXT:33290"},{"id":"T3990","span":{"begin":738,"end":741},"obj":"CHEBI_UBERON_EXT:triglyceride_or_adipose_tissue"},{"id":"T3991","span":{"begin":822,"end":825},"obj":"CHEBI_UBERON_EXT:triglyceride_or_adipose_tissue"},{"id":"T3992","span":{"begin":852,"end":855},"obj":"CHEBI_UBERON_EXT:triglyceride_or_adipose_tissue"},{"id":"T3993","span":{"begin":946,"end":952},"obj":"CHEBI_GO_EXT:ligand"},{"id":"T3994","span":{"begin":985,"end":993},"obj":"CHEBI:73726"},{"id":"T3995","span":{"begin":994,"end":1002},"obj":"CHEBI:36357"},{"id":"T3996","span":{"begin":1007,"end":1011},"obj":"NCBITaxon:10088"},{"id":"T4026","span":{"begin":20,"end":26},"obj":"SO_EXT:0000417"},{"id":"T4027","span":{"begin":31,"end":41},"obj":"CHEBI_SO_EXT:amino_acid"},{"id":"T4028","span":{"begin":42,"end":50},"obj":"CHEBI_EXT:residue"},{"id":"T4029","span":{"begin":69,"end":77},"obj":"CHEBI_EXT:residue"},{"id":"T4030","span":{"begin":90,"end":94},"obj":"PR_EXT:P06492"},{"id":"T4031","span":{"begin":99,"end":104},"obj":"SO_EXT:sequence_fusion_process"},{"id":"T4032","span":{"begin":105,"end":113},"obj":"SO:0001817"},{"id":"T4033","span":{"begin":123,"end":133},"obj":"CHEBI_SO_EXT:N_terminus_or_N_terminal_region"},{"id":"T4034","span":{"begin":137,"end":142},"obj":"NCBITaxon:10088"},{"id":"T4035","span":{"begin":143,"end":148},"obj":"PR_EXT:000013057"},{"id":"T4036","span":{"begin":154,"end":158},"obj":"PR_EXT:P06492"},{"id":"T4037","span":{"begin":159,"end":164},"obj":"PR_EXT:000013057"},{"id":"T4038","span":{"begin":165,"end":171},"obj":"SO_EXT:sequence_fusion_entity_or_process"},{"id":"T4039","span":{"begin":172,"end":176},"obj":"SO_EXT:cDNA"},{"id":"T4040","span":{"begin":188,"end":198},"obj":"SO_EXT:sequence_downstreamness"},{"id":"T4041","span":{"begin":206,"end":211},"obj":"NCBITaxon:9606"},{"id":"T4042","span":{"begin":212,"end":228},"obj":"PR_EXT:000003674"},{"id":"T4043","span":{"begin":214,"end":222},"obj":"UBERON:0004288"},{"id":"T4044","span":{"begin":229,"end":237},"obj":"SO_EXT:0000167"},{"id":"T4045","span":{"begin":271,"end":279},"obj":"SO_EXT:sequence_upstreamness"},{"id":"T4046","span":{"begin":287,"end":291},"obj":"NCBITaxon:10633"},{"id":"T4047","span":{"begin":292,"end":298},"obj":"SO_EXT:0000188"},{"id":"T4048","span":{"begin":299,"end":315},"obj":"SO_EXT:0000610"},{"id":"T4049","span":{"begin":304,"end":305},"obj":"CHEBI_EXT:adenine_nucleobase_or_nucleoside_or_nucleotide_molecular_entity_or_group"},{"id":"T4050","span":{"begin":321,"end":330},"obj":"SO_EXT:0000902"},{"id":"T4051","span":{"begin":380,"end":387},"obj":"CL:0000365"},{"id":"T4052","span":{"begin":389,"end":399},"obj":"SO_EXT:transgenic_entity"},{"id":"T4053","span":{"begin":400,"end":404},"obj":"NCBITaxon:10088"},{"id":"T4054","span":{"begin":457,"end":466},"obj":"SO_EXT:wild_type_entity_or_quality"},{"id":"T4055","span":{"begin":533,"end":537},"obj":"CHEBI_EXT:33290"},{"id":"T4056","span":{"begin":548,"end":558},"obj":"SO_EXT:transgenic_entity"},{"id":"T4057","span":{"begin":559,"end":563},"obj":"NCBITaxon:10088"}],"text":"The transactivation domain (78 amino acid residues, corresponding to residues 413–490) of VP16 was fused in frame with the N-terminus of mouse PPARδ. The VP16-PPARδ fusion cDNA was placed downstream of the human α-skeletal actin promoter (Brennan and Hardeman 1993), and upstream of the SV40 intron/poly(A) sequence. The transgene was purified and injected into C57BL/6J × CBA F1 zygotes. Transgenic mice were backcrossed with C57BL/6J for two generations. Wild-type littermates were used as controls throughout the study. On normal chow diet, the transgenic mice and control littermates used here had similar body weights. PPARδ-null mice were previously generated (Barak et al. 2002). Mice were fed either a standard chow with 4% (w/w) fat content (Harlan Teklad, Harlan, Indianapolis, Indiana, United States) or a high-fat diet containing 35% (w/w) fat content (product F3282, Bioserv, Frenchtown, New Jersey, United States) as indicated. For ligand experiments, we synthesized the GW501516 compound and mice were orally gavaged daily (10 mg/kg or vehicle alone)."}

    craft-ca-core-dev

    {"project":"craft-ca-core-dev","denotations":[{"id":"T3998","span":{"begin":20,"end":26},"obj":"SO:0000417"},{"id":"T3999","span":{"begin":90,"end":94},"obj":"PR:P06492"},{"id":"T4000","span":{"begin":105,"end":113},"obj":"SO:0001817"},{"id":"T4001","span":{"begin":137,"end":142},"obj":"NCBITaxon:10088"},{"id":"T4002","span":{"begin":143,"end":148},"obj":"PR:000013057"},{"id":"T4003","span":{"begin":154,"end":158},"obj":"PR:P06492"},{"id":"T4004","span":{"begin":159,"end":164},"obj":"PR:000013057"},{"id":"T4005","span":{"begin":206,"end":211},"obj":"NCBITaxon:9606"},{"id":"T4006","span":{"begin":212,"end":228},"obj":"PR:000003674"},{"id":"T4007","span":{"begin":214,"end":222},"obj":"UBERON:0004288"},{"id":"T4008","span":{"begin":229,"end":237},"obj":"SO:0000167"},{"id":"T4009","span":{"begin":287,"end":291},"obj":"NCBITaxon:10633"},{"id":"T4010","span":{"begin":292,"end":298},"obj":"SO:0000188"},{"id":"T4011","span":{"begin":299,"end":315},"obj":"SO:0000610"},{"id":"T4012","span":{"begin":321,"end":330},"obj":"SO:0000902"},{"id":"T4013","span":{"begin":380,"end":387},"obj":"CL:0000365"},{"id":"T4014","span":{"begin":400,"end":404},"obj":"NCBITaxon:10088"},{"id":"T4015","span":{"begin":533,"end":537},"obj":"CHEBI:33290"},{"id":"T4016","span":{"begin":559,"end":563},"obj":"NCBITaxon:10088"},{"id":"T4017","span":{"begin":624,"end":629},"obj":"PR:000013057"},{"id":"T4018","span":{"begin":635,"end":639},"obj":"NCBITaxon:10088"},{"id":"T4019","span":{"begin":687,"end":691},"obj":"NCBITaxon:10088"},{"id":"T4020","span":{"begin":697,"end":700},"obj":"GO:0007631"},{"id":"T4021","span":{"begin":719,"end":723},"obj":"CHEBI:33290"},{"id":"T4022","span":{"begin":985,"end":993},"obj":"CHEBI:73726"},{"id":"T4023","span":{"begin":994,"end":1002},"obj":"CHEBI:36357"},{"id":"T4024","span":{"begin":1007,"end":1011},"obj":"NCBITaxon:10088"}],"text":"The transactivation domain (78 amino acid residues, corresponding to residues 413–490) of VP16 was fused in frame with the N-terminus of mouse PPARδ. The VP16-PPARδ fusion cDNA was placed downstream of the human α-skeletal actin promoter (Brennan and Hardeman 1993), and upstream of the SV40 intron/poly(A) sequence. The transgene was purified and injected into C57BL/6J × CBA F1 zygotes. Transgenic mice were backcrossed with C57BL/6J for two generations. Wild-type littermates were used as controls throughout the study. On normal chow diet, the transgenic mice and control littermates used here had similar body weights. PPARδ-null mice were previously generated (Barak et al. 2002). Mice were fed either a standard chow with 4% (w/w) fat content (Harlan Teklad, Harlan, Indianapolis, Indiana, United States) or a high-fat diet containing 35% (w/w) fat content (product F3282, Bioserv, Frenchtown, New Jersey, United States) as indicated. For ligand experiments, we synthesized the GW501516 compound and mice were orally gavaged daily (10 mg/kg or vehicle alone)."}