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Q30353034-198EBDF5-7227-4BCB-A30B-40BADEC5B5ED
Q30353034-198EBDF5-7227-4BCB-A30B-40BADEC5B5ED
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http://www.wikidata.org/entity/statement/Q30353034-198EBDF5-7227-4BCB-A30B-40BADEC5B5ED
Effect of charged residues in the N-domain of Sup35 protein on prion [PSI+] stability and propagation.
P2860
Q30353034-198EBDF5-7227-4BCB-A30B-40BADEC5B5ED
BestRank
Statement
http://www.wikidata.org/entity/statement/Q30353034-198EBDF5-7227-4BCB-A30B-40BADEC5B5ED
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wasDerivedFrom
429947db8a02f3b2f4f08e35006ff78edb126724
P2860
Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104.