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DESCRIBE <http://purl.uniprot.org/SHA-384/E9853CE0ED6B08283F76027C36000AA87465D92CA4A9ABB72F012DD9E318B5B8A9F63032C85AC5F9C3CB5D7E82D18EB2>
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http://purl.uniprot.org/SHA-384/E9853CE0ED6B08283F76027C36000AA87465D92CA4A9ABB72F012DD9E318B5B8A9F63032C85AC5F9C3CB5D7E82D18EB2
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/E9853CE0ED6B08283F76027C36000AA87465D92CA4A9ABB72F012DD9E318B5B8A9F63032C85AC5F9C3CB5D7E82D18EB2
http://www.w3.org/2000/01/rdf-schema#comment
"CPM binding to extracellular loop 2 of the B1R results in positive allosteric modulation of B1R signaling and disruption of this interaction could provide a novel therapeutic approach to reduce pathological B1R signaling."
xsd:string
http://purl.uniprot.org/uniprot/#_057E3C4AA9A9B786CB126ACD3A987D32A8D91AFEBAE9B86B7D25EA5704E4E384C81E5BC11DD27427EE3094493F245F7E
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/E9853CE0ED6B08283F76027C36000AA87465D92CA4A9ABB72F012DD9E318B5B8A9F63032C85AC5F9C3CB5D7E82D18EB2
http://purl.uniprot.org/uniprot/A0A075E6Y0
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/E9853CE0ED6B08283F76027C36000AA87465D92CA4A9ABB72F012DD9E318B5B8A9F63032C85AC5F9C3CB5D7E82D18EB2
http://purl.uniprot.org/uniprot/#_A0A075E6Y0-mappedCitation-24108126
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/E9853CE0ED6B08283F76027C36000AA87465D92CA4A9ABB72F012DD9E318B5B8A9F63032C85AC5F9C3CB5D7E82D18EB2