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Q40339706-85BA5F7B-4D42-42C9-B5B3-411F2D0DAC0E
Q40339706-85BA5F7B-4D42-42C9-B5B3-411F2D0DAC0E
BestRank
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http://www.wikidata.org/entity/statement/Q40339706-85BA5F7B-4D42-42C9-B5B3-411F2D0DAC0E
Structure-based mutational analysis of the bovine papillomavirus E1 helicase domain identifies residues involved in the nonspecific DNA binding activity required for double trimer formation.
P2860
Q40339706-85BA5F7B-4D42-42C9-B5B3-411F2D0DAC0E
BestRank
Statement
http://www.wikidata.org/entity/statement/Q40339706-85BA5F7B-4D42-42C9-B5B3-411F2D0DAC0E
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wasDerivedFrom
eef1fa310ecfbe64a35af42049927ace27d553c8
P2860
Crystal structure of the DNA binding domain of the replication initiation protein E1 from papillomavirus