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Q30580764-A6E6D01A-6855-4FBA-B985-0DB7B77D4F91
Q30580764-A6E6D01A-6855-4FBA-B985-0DB7B77D4F91
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http://www.wikidata.org/entity/statement/Q30580764-A6E6D01A-6855-4FBA-B985-0DB7B77D4F91
Architecture of the nitric-oxide synthase holoenzyme reveals large conformational changes and a calmodulin-driven release of the FMN domain
P2860
Q30580764-A6E6D01A-6855-4FBA-B985-0DB7B77D4F91
BestRank
Statement
http://www.wikidata.org/entity/statement/Q30580764-A6E6D01A-6855-4FBA-B985-0DB7B77D4F91
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f7c3c88c4c2f34cb3c191dd44b8435f7d7f1fa95
P2860
Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitric-oxide synthase flavoproteins.