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DESCRIBE <http://purl.uniprot.org/SHA-384/3F9C828A0E3D578234E841C44444C1B9B469A6C8C48C30947542BE2B291F30A54A2E9C2586F610E9AD3F0D8A0491453D>
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http://purl.uniprot.org/SHA-384/3F9C828A0E3D578234E841C44444C1B9B469A6C8C48C30947542BE2B291F30A54A2E9C2586F610E9AD3F0D8A0491453D
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/3F9C828A0E3D578234E841C44444C1B9B469A6C8C48C30947542BE2B291F30A54A2E9C2586F610E9AD3F0D8A0491453D
http://www.w3.org/2000/01/rdf-schema#comment
"Our results reveal that disulphide interactions enhance intracellular accumulation of AAT mutants and implicate the oxidative ER state as a pathogenic co-factor."
xsd:string
http://purl.uniprot.org/uniprot/#_173F8743C9E9F4C361FEA57341480A6269E7B24AE44767237C24E18DCACD97A9A6D21205676FB0A830BBD388C4ED271C
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/3F9C828A0E3D578234E841C44444C1B9B469A6C8C48C30947542BE2B291F30A54A2E9C2586F610E9AD3F0D8A0491453D
http://purl.uniprot.org/uniprot/A0A0S2Z465
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/3F9C828A0E3D578234E841C44444C1B9B469A6C8C48C30947542BE2B291F30A54A2E9C2586F610E9AD3F0D8A0491453D
http://purl.uniprot.org/uniprot/#_A0A0S2Z465-mappedCitation-26647313
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/3F9C828A0E3D578234E841C44444C1B9B469A6C8C48C30947542BE2B291F30A54A2E9C2586F610E9AD3F0D8A0491453D