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DESCRIBE <http://purl.uniprot.org/SHA-384/1827BD0EA03F2FAF9DE8D2819AC0BEB5C1939250D59A402B0674F5D20A1556C11B5756C2C04A3418DED1B2E820E699A5>
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http://purl.uniprot.org/SHA-384/1827BD0EA03F2FAF9DE8D2819AC0BEB5C1939250D59A402B0674F5D20A1556C11B5756C2C04A3418DED1B2E820E699A5
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/1827BD0EA03F2FAF9DE8D2819AC0BEB5C1939250D59A402B0674F5D20A1556C11B5756C2C04A3418DED1B2E820E699A5
http://www.w3.org/2000/01/rdf-schema#comment
"The first X-ray structure of the TMD of the alpha1GlyR solved here using GLIC as a scaffold paves the way for mechanistic investigation and design of allosteric modulators of a human receptor."
xsd:string
http://purl.uniprot.org/uniprot/#_959F4E452A99DAD8FFB66B45578A454B45AD9567913A9F0C444EDAC247D09895E8F763F5B923C7D83822D2CD9842B75E
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/1827BD0EA03F2FAF9DE8D2819AC0BEB5C1939250D59A402B0674F5D20A1556C11B5756C2C04A3418DED1B2E820E699A5
http://purl.uniprot.org/uniprot/Q14C71
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/1827BD0EA03F2FAF9DE8D2819AC0BEB5C1939250D59A402B0674F5D20A1556C11B5756C2C04A3418DED1B2E820E699A5
http://purl.uniprot.org/uniprot/#_Q14C71-mappedCitation-25730860
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/1827BD0EA03F2FAF9DE8D2819AC0BEB5C1939250D59A402B0674F5D20A1556C11B5756C2C04A3418DED1B2E820E699A5