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Q27666570-544B48BC-893E-40C0-8BA1-AB681C85E3A3
Q27666570-544B48BC-893E-40C0-8BA1-AB681C85E3A3
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http://www.wikidata.org/entity/statement/Q27666570-544B48BC-893E-40C0-8BA1-AB681C85E3A3
Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC
P2860
Q27666570-544B48BC-893E-40C0-8BA1-AB681C85E3A3
BestRank
Statement
http://www.wikidata.org/entity/statement/Q27666570-544B48BC-893E-40C0-8BA1-AB681C85E3A3
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wasDerivedFrom
4dfbd58407061d5ad804983e4a880d6e58044ff6
P2860
Conserved glycines in the C terminus of MinC proteins are implicated in their functionality as cell division inhibitors.