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Q37424978-796B1E84-C9E0-46C2-81D6-449FFD2503EE
Q37424978-796B1E84-C9E0-46C2-81D6-449FFD2503EE
BestRank
Statement
http://www.wikidata.org/entity/statement/Q37424978-796B1E84-C9E0-46C2-81D6-449FFD2503EE
Thermal Unfolding of the Pertussis Toxin S1 Subunit Facilitates Toxin Translocation to the Cytosol by the Mechanism of Endoplasmic Reticulum-Associated Degradation.
P2860
Q37424978-796B1E84-C9E0-46C2-81D6-449FFD2503EE
BestRank
Statement
http://www.wikidata.org/entity/statement/Q37424978-796B1E84-C9E0-46C2-81D6-449FFD2503EE
rank
NormalRank
type
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Statement
wasDerivedFrom
83156bf2562731d824d86b9fc83a3f967d0c6f0a
P2860
Order-disorder-order transitions mediate the activation of cholera toxin.