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Q27662151-0C2F363C-9761-43AB-8DDA-913924ED9FFA
Q27662151-0C2F363C-9761-43AB-8DDA-913924ED9FFA
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http://www.wikidata.org/entity/statement/Q27662151-0C2F363C-9761-43AB-8DDA-913924ED9FFA
The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface
P2860
Q27662151-0C2F363C-9761-43AB-8DDA-913924ED9FFA
BestRank
Statement
http://www.wikidata.org/entity/statement/Q27662151-0C2F363C-9761-43AB-8DDA-913924ED9FFA
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wasDerivedFrom
c597c5668f0f0441e60c7730b08f0d75cf231038
P2860
Membrane structures of the hemifusion-inducing fusion peptide mutant G1S and the fusion-blocking mutant G1V of influenza virus hemagglutinin suggest a mechanism for pore opening in membrane fusion.