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DESCRIBE <http://purl.uniprot.org/SHA-384/AF652FCD2C434D27B29100566BA0726A1D61F53E757683DCD357DC79D7CF6E7CF09F5DBE8F22D7531E216E671AD7BBB2>
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http://purl.uniprot.org/SHA-384/AF652FCD2C434D27B29100566BA0726A1D61F53E757683DCD357DC79D7CF6E7CF09F5DBE8F22D7531E216E671AD7BBB2
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/AF652FCD2C434D27B29100566BA0726A1D61F53E757683DCD357DC79D7CF6E7CF09F5DBE8F22D7531E216E671AD7BBB2
http://www.w3.org/2000/01/rdf-schema#comment
"generation and aggregation of phosphorylated C-terminal fragments of TDP-43 play a primary role in the formation of inclusions and resultant loss of normal TDP-43 localization leading to neuronal degeneration in TDP-43 proteinopathy."
xsd:string
http://purl.uniprot.org/uniprot/#_0D658D0A5DCEF8F0A4F3AD3052808EDAAD042E0669C08FB3FB83B8386B4B5B1E11EE5B86A95754E75E01924B923BFBAC
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/AF652FCD2C434D27B29100566BA0726A1D61F53E757683DCD357DC79D7CF6E7CF09F5DBE8F22D7531E216E671AD7BBB2
http://purl.uniprot.org/uniprot/Q9H256
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/AF652FCD2C434D27B29100566BA0726A1D61F53E757683DCD357DC79D7CF6E7CF09F5DBE8F22D7531E216E671AD7BBB2
http://purl.uniprot.org/uniprot/#_Q9H256-mappedCitation-19515851
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/AF652FCD2C434D27B29100566BA0726A1D61F53E757683DCD357DC79D7CF6E7CF09F5DBE8F22D7531E216E671AD7BBB2