Complement lysis: the ultrastructure and orientation of the C5b-9 complex on target sheep erythrocyte membranes.
about
Killing of Microbes and Cancer by the Immune System with Three Mammalian Pore-Forming Killer ProteinsMolecular organization of C9 within the membrane attack complex of complement. Induction of circular C9 polymerization by the C5b-8 assemblyPermeability characteristics of complement-damaged membranes: evaluation of the membrane leak generated by the complement proteins C5b-9.Bactericidal and bacteriolytic activity of serum against gram-negative bacteria.Evidence for a two-domain structure of the terminal membrane C5b-9 complex of human complementMolecular weight of the membrane C5b-9 complex of human complement: characterization of the terminal complex as a C5b-9 monomer.Membrane attack complex of complement: distribution of subunits between the hydrocarbon phase of target membranes and water.A ring-shaped structure with a crown formed by streptolysin O on the erythrocyte membrane.Polymerization of the ninth component of complement (C9): formation of poly(C9) with a tubular ultrastructure resembling the membrane attack complex of complement.Ultrastructure of the membrane attack complex of complement: detection of the tetramolecular C9-polymerizing complex C5b-8.Staphylococcal alpha-toxin: oligomerization of hydrophilic monomers to form amphiphilic hexamers induced through contact with deoxycholate detergent micelles.Assembly of the functional membrane attack complex of human complement: formation of disulfide-linked C9 dimers.On the mechanism of membrane damage by Staphylococcus aureus alpha-toxin.Molecular composition of the terminal membrane and fluid-phase C5b-9 complexes of rabbit complement. Absence of disulphide-bonded C9 dimers in the membrane complex.Membrane attack complex of complement: generation of high-affinity phospholipid binding sites by fusion of five hydrophilic plasma proteins.Molecular nature of the complement lesion.Steady-state analysis of tracer exchange across the C5b-9 complement lesion in a biological membrane.Proteolytic modification of human complement protein C9: loss of poly(C9) and circular lesion formation without impairment of function.Difference in antigenic reactivity and ultrastructure between fluid-phase C5b-9 and the C5b-9 membrane attack complex of human complement.Mechanism of membrane damage by streptolysin-O.Membrane changes induced by exposure of Escherichia coli to human serum.Physiology and pathophysiology of complement: progress and trends.Freeze-fracture analysis of the membrane lesion of human complement.Membrane attack complex of complement: a structural analysis of its assembly.C5b-9 dimer: isolation from complement lysed cells and ultrastructural identification with complement-dependent membrane lesions.
P2860
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P2860
Complement lysis: the ultrastructure and orientation of the C5b-9 complex on target sheep erythrocyte membranes.
description
1978 nî lūn-bûn
@nan
1978年の論文
@ja
1978年学术文章
@wuu
1978年学术文章
@zh-cn
1978年学术文章
@zh-hans
1978年学术文章
@zh-my
1978年学术文章
@zh-sg
1978年學術文章
@yue
1978年學術文章
@zh
1978年學術文章
@zh-hant
name
Complement lysis: the ultrastr ...... t sheep erythrocyte membranes.
@en
Complement lysis: the ultrastr ...... t sheep erythrocyte membranes.
@nl
type
label
Complement lysis: the ultrastr ...... t sheep erythrocyte membranes.
@en
Complement lysis: the ultrastr ...... t sheep erythrocyte membranes.
@nl
prefLabel
Complement lysis: the ultrastr ...... t sheep erythrocyte membranes.
@en
Complement lysis: the ultrastr ...... t sheep erythrocyte membranes.
@nl
P2093
P2860
P1476
Complement lysis: the ultrastr ...... t sheep erythrocyte membranes.
@en
P2093
Bhakdi-Lehnen B
Bjerrum OJ
Tranum-Jensen J
P2860
P356
10.1111/J.1365-3083.1978.TB00425.X
P577
1978-01-01T00:00:00Z