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Q35001178-B6B2EE31-9FCB-434D-BB85-5B0CB211566B
Q35001178-B6B2EE31-9FCB-434D-BB85-5B0CB211566B
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Statement
http://www.wikidata.org/entity/statement/Q35001178-B6B2EE31-9FCB-434D-BB85-5B0CB211566B
Purification of α-synuclein from human brain reveals an instability of endogenous multimers as the protein approaches purity.
P2860
Q35001178-B6B2EE31-9FCB-434D-BB85-5B0CB211566B
BestRank
Statement
http://www.wikidata.org/entity/statement/Q35001178-B6B2EE31-9FCB-434D-BB85-5B0CB211566B
rank
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Statement
wasDerivedFrom
d6c763c701fecafcfb5431b82562882be4acf0d6
P2860
α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer