@prefix this: . @prefix sub: . @prefix beldoc: . @prefix rdfs: . @prefix rdf: . @prefix xsd: . @prefix dct: . @prefix dce: . @prefix pav: . @prefix np: . @prefix belv: . @prefix prov: . @prefix mesh: . @prefix go: . @prefix Protein: . @prefix rgd: . @prefix geneProductOf: . @prefix hasAgent: . @prefix occursIn: . @prefix species: . @prefix pubmed: . @prefix orcid: . sub:Head { this: np:hasAssertion sub:assertion; np:hasProvenance sub:provenance; np:hasPublicationInfo sub:pubinfo; a np:Nanopublication . } sub:assertion { sub:_1 hasAgent: sub:_2; a go:0042789 . sub:_2 geneProductOf: rgd:1304603; a Protein: . sub:_3 occursIn: mesh:D018482, species:10116; rdf:object sub:_1; rdf:predicate belv:increases; rdf:subject mesh:D015444; a rdf:Statement . sub:assertion rdfs:label "bp(MESHPP:Exercise) -> tscript(p(RGD:Nrf1))" . } sub:provenance { beldoc: dce:description "Approximately 61,000 statements."; dce:rights "Copyright (c) 2011-2012, Selventa. All rights reserved."; dce:title "BEL Framework Large Corpus Document"; pav:authoredBy sub:_5; pav:version "1.4" . sub:_4 prov:value "The magnitude of this increase was twofold (Fig. 3). An increase in PGC-1 protein of similar magnitude was seen 18 h after the fifth bout of exercise (data not shown). This finding is important because increases in mRNA do not always result in a parallel increase in protein. There was an increase in a smaller protein, which, like the full-length form, was completely competed away with a PGC-1 blocking peptide. The size of this smaller PGC-1 protein (34 kDa) is consistent with that of the smaller PGC-1 mRNA, which appears to be missing exon 8. Antibodies directed at the amino terminus (Fig. 3A) and the carboxyl terminus (Fig. 3A) recognized the shorter PGC-1 protein. It will be interesting to determine whether this smaller PGC-1 protein is in fact the translation product of the shortened PGC-1 mRNA and whether it has functional significance. Effect of exercise on expression of NRF-1 and NRF-2 NRF-1 protein binding was detected by electrophoretic mobility shift assay using an oligonucleotide containing a NRF-1 binding site from the ALA synthase promoter. NRF-2 protein binding was determined using an oligonucleotide containing the NRF-2 protein-binding site from the cytochrome oxidase subunit IV promoter. The NRF-1-specific band is shown by the arrow in Fig. 4A; quantitative analysis is shown in Fig. 4C. There was a 50% increase in NRF-1 binding in eight of nine muscles 18 h after the exercise; in other muscle, an increase was evident 12 h after exercise. This finding of an increase in NRF-1 DNA binding is in keeping with the observation of Murakami et al. (37) of a 50% increase in NRF-1 mRNA in soleus muscle of rats 6 h after a bout of running."; prov:wasQuotedFrom pubmed:12468452 . sub:_5 rdfs:label "Selventa" . sub:assertion prov:hadPrimarySource pubmed:12468452; prov:wasDerivedFrom beldoc:, sub:_4 . } sub:pubinfo { this: dct:created "2014-07-03T14:30:07.704+02:00"^^xsd:dateTime; pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 . }