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and Methods\n\nAnimals.\nThe 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).\n\nGene expression analysis and physiological studies\nMouse EST clones were obtained from ATCC (Manassas, Virginia, United States), verified by sequencing, and used as Northern probes. Antibodies were obtained from Santa Cruz Biotechnology (Santa Cruz, California, United States). Total muscle protein extracts (Lin et al. 2002) and nuclear proteins (Wang et al. 2003) were prepared as described.\nPrior to the exercise performance test, the mice were accustomed to the treadmill (Columbus Instruments, Columbus, Ohio, United States) with a 5-min run at 7 m/min once per day for 2 d. The exercise test regimen was 10 m/min for the first 60 min, followed by 1 m/min increment increases at 15-min intervals. Exhaustion was defined when mice were unable to avoid repetitive electrical shocks.\n\nMuscle fiber typing and mitochondrial DNA isolation\nMuscle fiber typing was essentially performed using metachromatic dye–ATPase methods as described (Ogilvie and Feeback 1990). Muscle mitochondria were isolated (Scholte et al. 1997). Mitochondrial DNA was prepared and analyzed on 1% agarose gel.\n\nStatistical analysis\nNumber of mice for each group used in experiments is indicated in figure legends. Values are presented as mean ± SEM. A two-tailed Student's t test was used to calculate p-values."}

{"project":"2_test","denotations":[{"id":"15328533-7678010-84708293","span":{"begin":292,"end":296},"obj":"7678010"},{"id":"15328533-11756685-84708294","span":{"begin":712,"end":716},"obj":"11756685"},{"id":"15328533-12181572-84708295","span":{"begin":1420,"end":1424},"obj":"12181572"},{"id":"15328533-12705865-84708296","span":{"begin":1460,"end":1464},"obj":"12705865"},{"id":"15328533-1703671-84708297","span":{"begin":2058,"end":2062},"obj":"1703671"},{"id":"15328533-9309666-84708298","span":{"begin":2115,"end":2119},"obj":"9309666"},{"id":"T7615","span":{"begin":292,"end":296},"obj":"7678010"},{"id":"T79960","span":{"begin":712,"end":716},"obj":"11756685"},{"id":"T2356","span":{"begin":1420,"end":1424},"obj":"12181572"},{"id":"T80422","span":{"begin":1460,"end":1464},"obj":"12705865"},{"id":"T30007","span":{"begin":2058,"end":2062},"obj":"1703671"},{"id":"T52585","span":{"begin":2115,"end":2119},"obj":"9309666"}],"text":"Materials and Methods\n\nAnimals.\nThe 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).\n\nGene expression analysis and physiological studies\nMouse EST clones were obtained from ATCC (Manassas, Virginia, United States), verified by sequencing, and used as Northern probes. Antibodies were obtained from Santa Cruz Biotechnology (Santa Cruz, California, United States). Total muscle protein extracts (Lin et al. 2002) and nuclear proteins (Wang et al. 2003) were prepared as described.\nPrior to the exercise performance test, the mice were accustomed to the treadmill (Columbus Instruments, Columbus, Ohio, United States) with a 5-min run at 7 m/min once per day for 2 d. The exercise test regimen was 10 m/min for the first 60 min, followed by 1 m/min increment increases at 15-min intervals. Exhaustion was defined when mice were unable to avoid repetitive electrical shocks.\n\nMuscle fiber typing and mitochondrial DNA isolation\nMuscle fiber typing was essentially performed using metachromatic dye–ATPase methods as described (Ogilvie and Feeback 1990). Muscle mitochondria were isolated (Scholte et al. 1997). Mitochondrial DNA was prepared and analyzed on 1% agarose gel.\n\nStatistical analysis\nNumber of mice for each group used in experiments is indicated in figure legends. Values are presented as mean ± SEM. A two-tailed Student's t test was used to calculate p-values."}

{"project":"craft-ca-core-ex-dev","denotations":[{"id":"T3983","span":{"begin":642,"end":646},"obj":"UBERON_EXT:body"},{"id":"T3984","span":{"begin":656,"end":661},"obj":"PR_EXT:000013057"},{"id":"T3985","span":{"begin":662,"end":666},"obj":"SO_EXT:sequence_nullness"},{"id":"T3986","span":{"begin":667,"end":671},"obj":"NCBITaxon:10088"},{"id":"T3987","span":{"begin":719,"end":723},"obj":"NCBITaxon:10088"},{"id":"T3988","span":{"begin":729,"end":732},"obj":"GO:0007631"},{"id":"T3989","span":{"begin":751,"end":755},"obj":"CHEBI_EXT:33290"},{"id":"T3990","span":{"begin":770,"end":773},"obj":"CHEBI_UBERON_EXT:triglyceride_or_adipose_tissue"},{"id":"T3991","span":{"begin":854,"end":857},"obj":"CHEBI_UBERON_EXT:triglyceride_or_adipose_tissue"},{"id":"T3992","span":{"begin":884,"end":887},"obj":"CHEBI_UBERON_EXT:triglyceride_or_adipose_tissue"},{"id":"T3993","span":{"begin":978,"end":984},"obj":"CHEBI_GO_EXT:ligand"},{"id":"T3994","span":{"begin":1017,"end":1025},"obj":"CHEBI:73726"},{"id":"T3995","span":{"begin":1026,"end":1034},"obj":"CHEBI:36357"},{"id":"T3996","span":{"begin":1039,"end":1043},"obj":"NCBITaxon:10088"},{"id":"T4025","span":{"begin":23,"end":30},"obj":"NCBITaxon:33208"},{"id":"T4026","span":{"begin":52,"end":58},"obj":"SO_EXT:0000417"},{"id":"T4027","span":{"begin":63,"end":73},"obj":"CHEBI_SO_EXT:amino_acid"},{"id":"T4028","span":{"begin":74,"end":82},"obj":"CHEBI_EXT:residue"},{"id":"T4029","span":{"begin":101,"end":109},"obj":"CHEBI_EXT:residue"},{"id":"T4030","span":{"begin":122,"end":126},"obj":"PR_EXT:P06492"},{"id":"T4031","span":{"begin":131,"end":136},"obj":"SO_EXT:sequence_fusion_process"},{"id":"T4032","span":{"begin":137,"end":145},"obj":"SO:0001817"},{"id":"T4033","span":{"begin":155,"end":165},"obj":"CHEBI_SO_EXT:N_terminus_or_N_terminal_region"},{"id":"T4034","span":{"begin":169,"end":174},"obj":"NCBITaxon:10088"},{"id":"T4035","span":{"begin":175,"end":180},"obj":"PR_EXT:000013057"},{"id":"T4036","span":{"begin":186,"end":190},"obj":"PR_EXT:P06492"},{"id":"T4037","span":{"begin":191,"end":196},"obj":"PR_EXT:000013057"},{"id":"T4038","span":{"begin":197,"end":203},"obj":"SO_EXT:sequence_fusion_entity_or_process"},{"id":"T4039","span":{"begin":204,"end":208},"obj":"SO_EXT:cDNA"},{"id":"T4040","span":{"begin":220,"end":230},"obj":"SO_EXT:sequence_downstreamness"},{"id":"T4041","span":{"begin":238,"end":243},"obj":"NCBITaxon:9606"},{"id":"T4042","span":{"begin":244,"end":260},"obj":"PR_EXT:000003674"},{"id":"T4043","span":{"begin":246,"end":254},"obj":"UBERON:0004288"},{"id":"T4044","span":{"begin":261,"end":269},"obj":"SO_EXT:0000167"},{"id":"T4045","span":{"begin":303,"end":311},"obj":"SO_EXT:sequence_upstreamness"},{"id":"T4046","span":{"begin":319,"end":323},"obj":"NCBITaxon:10633"},{"id":"T4047","span":{"begin":324,"end":330},"obj":"SO_EXT:0000188"},{"id":"T4048","span":{"begin":331,"end":347},"obj":"SO_EXT:0000610"},{"id":"T4049","span":{"begin":336,"end":337},"obj":"CHEBI_EXT:adenine_nucleobase_or_nucleoside_or_nucleotide_molecular_entity_or_group"},{"id":"T4050","span":{"begin":353,"end":362},"obj":"SO_EXT:0000902"},{"id":"T4051","span":{"begin":412,"end":419},"obj":"CL:0000365"},{"id":"T4052","span":{"begin":421,"end":431},"obj":"SO_EXT:transgenic_entity"},{"id":"T4053","span":{"begin":432,"end":436},"obj":"NCBITaxon:10088"},{"id":"T4054","span":{"begin":489,"end":498},"obj":"SO_EXT:wild_type_entity_or_quality"},{"id":"T4055","span":{"begin":565,"end":569},"obj":"CHEBI_EXT:33290"},{"id":"T4056","span":{"begin":580,"end":590},"obj":"SO_EXT:transgenic_entity"},{"id":"T4057","span":{"begin":591,"end":595},"obj":"NCBITaxon:10088"},{"id":"T4304","span":{"begin":1100,"end":1104},"obj":"SO_EXT:0000704"},{"id":"T4305","span":{"begin":1100,"end":1115},"obj":"GO:0010467"},{"id":"T4306","span":{"begin":1129,"end":1142},"obj":"GO_PATO_EXT:physiological_process_or_quality"},{"id":"T4307","span":{"begin":1151,"end":1156},"obj":"NCBITaxon:10088"},{"id":"T4308","span":{"begin":1157,"end":1160},"obj":"SO_EXT:0000345"},{"id":"T4309","span":{"begin":1161,"end":1167},"obj":"SO_EXT:sequence_cloned_entity"},{"id":"T4310","span":{"begin":1274,"end":1280},"obj":"CHEBI_SO_EXT:molecular_probe"},{"id":"T4311","span":{"begin":1282,"end":1292},"obj":"GO:0042571"},{"id":"T4312","span":{"begin":1384,"end":1390},"obj":"UBERON_EXT:muscle_structure_or_tissue"},{"id":"T4313","span":{"begin":1391,"end":1398},"obj":"CHEBI_PR_EXT:protein"},{"id":"T4314","span":{"begin":1430,"end":1437},"obj":"GO:0005634"},{"id":"T4315","span":{"begin":1438,"end":1446},"obj":"CHEBI_PR_EXT:protein"},{"id":"T4316","span":{"begin":1538,"end":1542},"obj":"NCBITaxon:10088"},{"id":"T4317","span":{"begin":1830,"end":1834},"obj":"NCBITaxon:10088"},{"id":"T4491","span":{"begin":1887,"end":1893},"obj":"UBERON_EXT:muscle_structure_or_tissue"},{"id":"T4492","span":{"begin":1887,"end":1899},"obj":"CL:0000187"},{"id":"T4493","span":{"begin":1911,"end":1924},"obj":"GO:0005739"},{"id":"T4494","span":{"begin":1911,"end":1928},"obj":"SO:0001032"},{"id":"T4495","span":{"begin":1925,"end":1928},"obj":"CHEBI_SO_EXT:DNA"},{"id":"T4496","span":{"begin":1939,"end":1945},"obj":"UBERON_EXT:muscle_structure_or_tissue"},{"id":"T4497","span":{"begin":1939,"end":1951},"obj":"CL:0000187"},{"id":"T4498","span":{"begin":2005,"end":2008},"obj":"CHEBI_EXT:37958"},{"id":"T4499","span":{"begin":2009,"end":2015},"obj":"GO_EXT:0016887"},{"id":"T4500","span":{"begin":2065,"end":2071},"obj":"UBERON_EXT:muscle_structure_or_tissue"},{"id":"T4501","span":{"begin":2072,"end":2084},"obj":"GO:0005739"},{"id":"T4502","span":{"begin":2122,"end":2135},"obj":"GO:0005739"},{"id":"T4503","span":{"begin":2122,"end":2139},"obj":"SO:0001032"},{"id":"T4504","span":{"begin":2136,"end":2139},"obj":"CHEBI_SO_EXT:DNA"},{"id":"T4505","span":{"begin":2172,"end":2179},"obj":"CHEBI:2511"},{"id":"T4561","span":{"begin":2217,"end":2221},"obj":"NCBITaxon:10088"}],"text":"Materials and Methods\n\nAnimals.\nThe 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).\n\nGene expression analysis and physiological studies\nMouse EST clones were obtained from ATCC (Manassas, Virginia, United States), verified by sequencing, and used as Northern probes. Antibodies were obtained from Santa Cruz Biotechnology (Santa Cruz, California, United States). Total muscle protein extracts (Lin et al. 2002) and nuclear proteins (Wang et al. 2003) were prepared as described.\nPrior to the exercise performance test, the mice were accustomed to the treadmill (Columbus Instruments, Columbus, Ohio, United States) with a 5-min run at 7 m/min once per day for 2 d. The exercise test regimen was 10 m/min for the first 60 min, followed by 1 m/min increment increases at 15-min intervals. Exhaustion was defined when mice were unable to avoid repetitive electrical shocks.\n\nMuscle fiber typing and mitochondrial DNA isolation\nMuscle fiber typing was essentially performed using metachromatic dye–ATPase methods as described (Ogilvie and Feeback 1990). Muscle mitochondria were isolated (Scholte et al. 1997). Mitochondrial DNA was prepared and analyzed on 1% agarose gel.\n\nStatistical analysis\nNumber of mice for each group used in experiments is indicated in figure legends. Values are presented as mean ± SEM. A two-tailed Student's t test was used to calculate p-values."}

{"project":"craft-ca-core-dev","denotations":[{"id":"T3997","span":{"begin":23,"end":30},"obj":"NCBITaxon:33208"},{"id":"T3998","span":{"begin":52,"end":58},"obj":"SO:0000417"},{"id":"T3999","span":{"begin":122,"end":126},"obj":"PR:P06492"},{"id":"T4000","span":{"begin":137,"end":145},"obj":"SO:0001817"},{"id":"T4001","span":{"begin":169,"end":174},"obj":"NCBITaxon:10088"},{"id":"T4002","span":{"begin":175,"end":180},"obj":"PR:000013057"},{"id":"T4003","span":{"begin":186,"end":190},"obj":"PR:P06492"},{"id":"T4004","span":{"begin":191,"end":196},"obj":"PR:000013057"},{"id":"T4005","span":{"begin":238,"end":243},"obj":"NCBITaxon:9606"},{"id":"T4006","span":{"begin":244,"end":260},"obj":"PR:000003674"},{"id":"T4007","span":{"begin":246,"end":254},"obj":"UBERON:0004288"},{"id":"T4008","span":{"begin":261,"end":269},"obj":"SO:0000167"},{"id":"T4009","span":{"begin":319,"end":323},"obj":"NCBITaxon:10633"},{"id":"T4010","span":{"begin":324,"end":330},"obj":"SO:0000188"},{"id":"T4011","span":{"begin":331,"end":347},"obj":"SO:0000610"},{"id":"T4012","span":{"begin":353,"end":362},"obj":"SO:0000902"},{"id":"T4013","span":{"begin":412,"end":419},"obj":"CL:0000365"},{"id":"T4014","span":{"begin":432,"end":436},"obj":"NCBITaxon:10088"},{"id":"T4015","span":{"begin":565,"end":569},"obj":"CHEBI:33290"},{"id":"T4016","span":{"begin":591,"end":595},"obj":"NCBITaxon:10088"},{"id":"T4017","span":{"begin":656,"end":661},"obj":"PR:000013057"},{"id":"T4018","span":{"begin":667,"end":671},"obj":"NCBITaxon:10088"},{"id":"T4019","span":{"begin":719,"end":723},"obj":"NCBITaxon:10088"},{"id":"T4020","span":{"begin":729,"end":732},"obj":"GO:0007631"},{"id":"T4021","span":{"begin":751,"end":755},"obj":"CHEBI:33290"},{"id":"T4022","span":{"begin":1017,"end":1025},"obj":"CHEBI:73726"},{"id":"T4023","span":{"begin":1026,"end":1034},"obj":"CHEBI:36357"},{"id":"T4024","span":{"begin":1039,"end":1043},"obj":"NCBITaxon:10088"},{"id":"T4296","span":{"begin":1100,"end":1104},"obj":"SO:0000704"},{"id":"T4297","span":{"begin":1100,"end":1115},"obj":"GO:0010467"},{"id":"T4298","span":{"begin":1151,"end":1156},"obj":"NCBITaxon:10088"},{"id":"T4299","span":{"begin":1157,"end":1160},"obj":"SO:0000345"},{"id":"T4300","span":{"begin":1282,"end":1292},"obj":"GO:0042571"},{"id":"T4301","span":{"begin":1430,"end":1437},"obj":"GO:0005634"},{"id":"T4302","span":{"begin":1538,"end":1542},"obj":"NCBITaxon:10088"},{"id":"T4303","span":{"begin":1830,"end":1834},"obj":"NCBITaxon:10088"},{"id":"T4482","span":{"begin":1887,"end":1899},"obj":"CL:0000187"},{"id":"T4483","span":{"begin":1911,"end":1924},"obj":"GO:0005739"},{"id":"T4484","span":{"begin":1911,"end":1928},"obj":"SO:0001032"},{"id":"T4485","span":{"begin":1939,"end":1951},"obj":"CL:0000187"},{"id":"T4486","span":{"begin":2005,"end":2008},"obj":"CHEBI:37958"},{"id":"T4487","span":{"begin":2072,"end":2084},"obj":"GO:0005739"},{"id":"T4488","span":{"begin":2122,"end":2135},"obj":"GO:0005739"},{"id":"T4489","span":{"begin":2122,"end":2139},"obj":"SO:0001032"},{"id":"T4490","span":{"begin":2172,"end":2179},"obj":"CHEBI:2511"},{"id":"T4560","span":{"begin":2217,"end":2221},"obj":"NCBITaxon:10088"}],"text":"Materials and Methods\n\nAnimals.\nThe 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).\n\nGene expression analysis and physiological studies\nMouse EST clones were obtained from ATCC (Manassas, Virginia, United States), verified by sequencing, and used as Northern probes. Antibodies were obtained from Santa Cruz Biotechnology (Santa Cruz, California, United States). Total muscle protein extracts (Lin et al. 2002) and nuclear proteins (Wang et al. 2003) were prepared as described.\nPrior to the exercise performance test, the mice were accustomed to the treadmill (Columbus Instruments, Columbus, Ohio, United States) with a 5-min run at 7 m/min once per day for 2 d. The exercise test regimen was 10 m/min for the first 60 min, followed by 1 m/min increment increases at 15-min intervals. Exhaustion was defined when mice were unable to avoid repetitive electrical shocks.\n\nMuscle fiber typing and mitochondrial DNA isolation\nMuscle fiber typing was essentially performed using metachromatic dye–ATPase methods as described (Ogilvie and Feeback 1990). Muscle mitochondria were isolated (Scholte et al. 1997). Mitochondrial DNA was prepared and analyzed on 1% agarose gel.\n\nStatistical analysis\nNumber of mice for each group used in experiments is indicated in figure legends. Values are presented as mean ± SEM. A two-tailed Student's t test was used to calculate p-values."}