Disrupting a key hydrophobic pair in the oligomerization interface of the actinoporins impairs their pore-forming activity.
about
Biophysical and biochemical strategies to understand membrane binding and pore formation by sticholysins, pore-forming proteins from a sea anemone.Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation.Multigene Family of Pore-Forming Toxins from Sea Anemone Heteractis crispa.
P2860
Disrupting a key hydrophobic pair in the oligomerization interface of the actinoporins impairs their pore-forming activity.
description
2016 nî lūn-bûn
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2016年の論文
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2016年論文
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2016年論文
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2016年論文
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2016年論文
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2016年論文
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2016年论文
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2016年论文
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2016年论文
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name
Disrupting a key hydrophobic p ...... s their pore-forming activity.
@en
Disrupting a key hydrophobic p ...... s their pore-forming activity.
@nl
type
label
Disrupting a key hydrophobic p ...... s their pore-forming activity.
@en
Disrupting a key hydrophobic p ...... s their pore-forming activity.
@nl
prefLabel
Disrupting a key hydrophobic p ...... s their pore-forming activity.
@en
Disrupting a key hydrophobic p ...... s their pore-forming activity.
@nl
P2093
P2860
P356
P1433
P1476
Disrupting a key hydrophobic p ...... rs their pore-forming activity
@en
P2093
Ana J García-Sáez
Aracelys López-Castilla
Carlos Alvarez
D Peter Tieleman
Haydeé Mesa-Galloso
Jorge E Hernández-González
Karelia H Delgado-Magnero
Lohans Pedrera
Maria E Lanio
Sheila Cabezas
P2860
P304
P356
10.1002/PRO.3104
P577
2017-02-23T00:00:00Z