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Q34348491-C0C69AE6-DEFF-4542-96DE-6AC251FA4C1D
Q34348491-C0C69AE6-DEFF-4542-96DE-6AC251FA4C1D
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http://www.wikidata.org/entity/statement/Q34348491-C0C69AE6-DEFF-4542-96DE-6AC251FA4C1D
Structural and thermodynamic folding characterization of triosephosphate isomerases from Trichomonas vaginalis reveals the role of destabilizing mutations following gene duplication.
P2860
Q34348491-C0C69AE6-DEFF-4542-96DE-6AC251FA4C1D
BestRank
Statement
http://www.wikidata.org/entity/statement/Q34348491-C0C69AE6-DEFF-4542-96DE-6AC251FA4C1D
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wasDerivedFrom
64aa6b9a25494985a40510f2bdcd53775e2edde8
P2860
Interaction of triosephosphate isomerase from the cell surface of Staphylococcus aureus and alpha-(1->3)-mannooligosaccharides derived from glucuronoxylomannan of Cryptococcus neoformans.