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Q50932976-E9DD1D16-2AE0-4319-B845-732B300D6238
Q50932976-E9DD1D16-2AE0-4319-B845-732B300D6238
BestRank
Statement
http://www.wikidata.org/entity/statement/Q50932976-E9DD1D16-2AE0-4319-B845-732B300D6238
Structural analyses of human thymidylate synthase reveal a site that may control conformational switching between active and inactive states.
P2860
Q50932976-E9DD1D16-2AE0-4319-B845-732B300D6238
BestRank
Statement
http://www.wikidata.org/entity/statement/Q50932976-E9DD1D16-2AE0-4319-B845-732B300D6238
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wasDerivedFrom
1086c0478ffad05523945ed0c79bc202972b9af0
P2860
Role of N-terminal residues in the ubiquitin-independent degradation of human thymidylate synthase.