Structure of the hemolysin E (HlyE, ClyA, and SheA) channel in its membrane-bound form.

Structure of the hemolysin E (HlyE, ClyA, and SheA) channel in its membrane-bound form.

Item
http://www.wikidata.org/entity/Q48509335
X-ray crystal structure of the B component of Hemolysin BL fromBacillus cereusThe pesticidal Cry6Aa toxin from Bacillus thuringiensis is structurally similar to HlyE-family alpha pore-forming toxinsSpatial association with PTEX complexes defines regions for effector export into Plasmodium falciparum-infected erythrocytesAssembling the puzzle: Oligomerization of α-pore forming proteins in membranesTransport proteins promoting Escherichia coli pathogenesis.The assembly dynamics of the cytolytic pore toxin ClyA.Engineered bacterial outer membrane vesicles with enhanced functionalityCry6Aa1, a Bacillus thuringiensis nematocidal and insecticidal toxin, forms pores in planar lipid bilayers at extremely low concentrations and without the need of proteolytic processing.Formation of very large conductance channels by Bacillus cereus Nhe in Vero and GH(4) cells identifies NheA + B as the inherent pore-forming structure.Tuning the size and properties of ClyA nanopores assisted by directed evolution.Alternate SlyA and H-NS nucleoprotein complexes control hlyE expression in Escherichia coli K-12.Colicin N binds to the periphery of its receptor and translocator, outer membrane protein F.Cytotoxicity of the Bacillus cereus Nhe enterotoxin requires specific binding order of its three exoprotein components.Mutations affecting export and activity of cytolysin A from Escherichia coli.A non-classical assembly pathway of Escherichia coli pore-forming toxin cytolysin A.Molecular cloning and characterization of clyA genes in various serotypes of Salmonella enterica.Disruption of the open conductance in the β-tongue mutants of Cytolysin A.
P2860

Structure of the hemolysin E (HlyE, ClyA, and SheA) channel in its membrane-bound form.

Item
http://www.wikidata.org/entity/Q48509335
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2006 nî lūn-bûn
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Structure of the hemolysin E (HlyE, ClyA, and SheA) channel in its membrane-bound form.
@en
Structure of the hemolysin E (HlyE, ClyA, and SheA) channel in its membrane-bound form.
@nl
type
label
Structure of the hemolysin E (HlyE, ClyA, and SheA) channel in its membrane-bound form.
@en
Structure of the hemolysin E (HlyE, ClyA, and SheA) channel in its membrane-bound form.
@nl
prefLabel
Structure of the hemolysin E (HlyE, ClyA, and SheA) channel in its membrane-bound form.
@en
Structure of the hemolysin E (HlyE, ClyA, and SheA) channel in its membrane-bound form.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P356
P1433
P1476
Structure of the hemolysin E (HlyE, ClyA, and SheA) channel in its membrane-bound form.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698