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Q30403510-87D41B5C-B4AC-4C70-9A5A-F62E8FA7A9D8
Q30403510-87D41B5C-B4AC-4C70-9A5A-F62E8FA7A9D8
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http://www.wikidata.org/entity/statement/Q30403510-87D41B5C-B4AC-4C70-9A5A-F62E8FA7A9D8
Folding dynamics of phenylalanine hydroxylase depends on the enzyme's metallation state: the native metal, iron, protects against aggregate intermediates.
P2860
Q30403510-87D41B5C-B4AC-4C70-9A5A-F62E8FA7A9D8
BestRank
Statement
http://www.wikidata.org/entity/statement/Q30403510-87D41B5C-B4AC-4C70-9A5A-F62E8FA7A9D8
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wasDerivedFrom
936ee6a32d3300b2d987a89b6801952262363796
P2860
Predicted effects of missense mutations on native-state stability account for phenotypic outcome in phenylketonuria, a paradigm of misfolding diseases.