Oligomerization of Escherichia coli haemolysin (HlyA) is involved in pore formation.

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Oligomerization of Escherichia coli haemolysin (HlyA) is involved in pore formation. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1007/BF00280205
P698PubMed publication ID8232216

P2093author name stringA Ludwig
W Goebel
R Benz
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Domains of Escherichia coli hemolysin (HlyA) involved in binding of calcium and erythrocyte membranesQ36984732
The repeat domain of Escherichia coli haemolysin (HlyA) is responsible for its Ca2+-dependent binding to erythrocytesQ38346172
Transport of hemolysin across the outer membrane of Escherichia coli requires two functionsQ39975513
Escherichia coli hemolysin may damage target cell membranes by generating transmembrane poresQ40171498
Pore formation by the Escherichia coli hemolysin: evidence for an association-dissociation equilibrium of the pore-forming aggregatesQ40426473
Haemolysin of Escherichia coli: comparison of pore-forming properties between chromosome and plasmid-encoded haemolysinsQ42603156
Melittin and a chemically modified trichotoxin form alamethicin-type multi-state poresQ47956746
Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation.Q52482817
Topological and functional studies on HlyB of Escherichia coliQ54682528
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A topological model for the haemolysin translocator protein HlyDQ68005640
P433issue1-2
P921main subjectEscherichia coliQ25419
P304page(s)89-96
P577publication date1993-10-01
P1433published inMolecular Genetics and GenomicsQ15753424
P1476titleOligomerization of Escherichia coli haemolysin (HlyA) is involved in pore formation.
P478volume241