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DESCRIBE <http://purl.uniprot.org/SHA-384/C5F8B730684AAC32B59715077B3265DF40C5B3735F6233619BF2FC496D41D4DFF6C7288EE8C40A70DDA6F1BB9C0E590A>
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http://purl.uniprot.org/SHA-384/C5F8B730684AAC32B59715077B3265DF40C5B3735F6233619BF2FC496D41D4DFF6C7288EE8C40A70DDA6F1BB9C0E590A
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/C5F8B730684AAC32B59715077B3265DF40C5B3735F6233619BF2FC496D41D4DFF6C7288EE8C40A70DDA6F1BB9C0E590A
http://www.w3.org/2000/01/rdf-schema#comment
"Data suggest that pH serves as an on/off switch for beta- synuclein to form aggregates/fibrils (as seem in Parkinson disease); hydrogen bonding between glutamate residues appears to be involved in fibril formation."
xsd:string
http://purl.uniprot.org/uniprot/#_6B3889F3952A003963589E1E94087023249FE02CF1CCC2B7E45C7E4377D39EE2C1888176D23AA788EAE25E0C0AAA5ED5
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/C5F8B730684AAC32B59715077B3265DF40C5B3735F6233619BF2FC496D41D4DFF6C7288EE8C40A70DDA6F1BB9C0E590A
http://purl.uniprot.org/uniprot/G4Y816
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/C5F8B730684AAC32B59715077B3265DF40C5B3735F6233619BF2FC496D41D4DFF6C7288EE8C40A70DDA6F1BB9C0E590A
http://purl.uniprot.org/uniprot/#_G4Y816-mappedCitation-28710275
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/C5F8B730684AAC32B59715077B3265DF40C5B3735F6233619BF2FC496D41D4DFF6C7288EE8C40A70DDA6F1BB9C0E590A