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Q28474624-AF9D1F46-78C6-45C7-B2AE-26792CD699B5
Q28474624-AF9D1F46-78C6-45C7-B2AE-26792CD699B5
BestRank
Statement
http://www.wikidata.org/entity/statement/Q28474624-AF9D1F46-78C6-45C7-B2AE-26792CD699B5
Role of a novel PH-kinase domain interface in PKB/Akt regulation: structural mechanism for allosteric inhibition
P2860
Q28474624-AF9D1F46-78C6-45C7-B2AE-26792CD699B5
BestRank
Statement
http://www.wikidata.org/entity/statement/Q28474624-AF9D1F46-78C6-45C7-B2AE-26792CD699B5
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wasDerivedFrom
ec6a22b254d21bc62b0b4f22d796be02ead1c10d
P2860
High-resolution structure of the pleckstrin homology domain of protein kinase b/akt bound to phosphatidylinositol (3,4,5)-trisphosphate