@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 Protein: . @prefix hgnc: . @prefix geneProductOf: . @prefix species: . @prefix occursIn: . @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 geneProductOf: hgnc:5438; a Protein: . sub:_2 geneProductOf: hgnc:5439; a Protein: . sub:_3 occursIn: species:9606; rdf:object sub:_2; rdf:predicate belv:increases; rdf:subject sub:_1; a rdf:Statement . sub:assertion rdfs:label "p(HGNC:IFNG) -> p(HGNC:IFNGR1)" . } 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 "20131211" . sub:_4 prov:value "The extracellular domain of IFN-gamma receptor interacts with its ligand. The two regions 134-183 and 183-209 must interact in order to form a receptor capable of binding to ligand. Replacement of residues 134-209 greatly reduced the ability of the receptor to signal and ligand binding activity. IFN-gamma receptor alpha chain bind to the ligand with a single high affinity (Ka) of 1E9-1E10/M."; prov:wasQuotedFrom pubmed:8195198 . sub:_5 rdfs:label "Selventa" . sub:assertion prov:hadPrimarySource pubmed:8195198; prov:wasDerivedFrom beldoc:, sub:_4 . } sub:pubinfo { this: dct:created "2014-07-03T14:33:49.588+02:00"^^xsd:dateTime; pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 . }