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Q27683946-4D2A647A-8072-44FF-96E8-5D8E8CB96A0B
Q27683946-4D2A647A-8072-44FF-96E8-5D8E8CB96A0B
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http://www.wikidata.org/entity/statement/Q27683946-4D2A647A-8072-44FF-96E8-5D8E8CB96A0B
Structure of the C-terminal half of human XPB helicase and the impact of the disease-causing mutation XP11BE
P2860
Q27683946-4D2A647A-8072-44FF-96E8-5D8E8CB96A0B
BestRank
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http://www.wikidata.org/entity/statement/Q27683946-4D2A647A-8072-44FF-96E8-5D8E8CB96A0B
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8bf0e2b7b9b792d89135559f56dc7a22d15726c3
P2860
Phosphorylation of XPB helicase regulates TFIIH nucleotide excision repair activity.