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Q33773458-3B1BB56B-1AF0-4592-8158-BC351C31B7A1
Q33773458-3B1BB56B-1AF0-4592-8158-BC351C31B7A1
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http://www.wikidata.org/entity/statement/Q33773458-3B1BB56B-1AF0-4592-8158-BC351C31B7A1
Mapping of the signal peptide-binding domain of Escherichia coli SecA using Förster resonance energy transfer.
P2860
Q33773458-3B1BB56B-1AF0-4592-8158-BC351C31B7A1
BestRank
Statement
http://www.wikidata.org/entity/statement/Q33773458-3B1BB56B-1AF0-4592-8158-BC351C31B7A1
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wasDerivedFrom
bbd07438eb3ffdb22ddee002f7f030dbedb5e15c
P2860
The conformation of SecA, as revealed by its protease sensitivity, is altered upon interaction with ATP, presecretory proteins, everted membrane vesicles, and phospholipids.