The membrane attack complex of complement. Assembly, structure and cytotoxic activity.
about
Overview of C3 GlomerulopathyStructure of human C8 protein provides mechanistic insight into membrane pore formation by complement.Assembly and regulation of the membrane attack complex based on structures of C5b6 and sC5b9.Isolation, cloning and functional characterization of porcine mannose-binding lectinComplement-mediated lipopolysaccharide release and outer membrane damage in Escherichia coli J5: requirement for C9Membrane assembly of the cholesterol-dependent cytolysin pore complex.Crystal structure of the MACPF domain of human complement protein C8 alpha in complex with the C8 gamma subunitThe dual role of lipopolysaccharide as effector and target molecule.Topology of the membrane-bound form of complement protein C9 probed by glycosylation mapping, anti-peptide antibody binding, and disulfide modification.Relationship between complement membrane attack complex, chemokine (C-C motif) ligand 2 (CCL2) and vascular endothelial growth factor in mouse model of laser-induced choroidal neovascularization.Genetic modifiers of the severity of sickle cell anemia identified through a genome-wide association studyAntimicrobial peptides: properties and applicability.Identity of the segment of human complement C8 recognized by complement regulatory protein CD59.The Bacillus cereus Hbl and Nhe tripartite enterotoxin components assemble sequentially on the surface of target cells and are not interchangeable.Molecular characterization of the alpha subunit of complement component C8 (GcC8alpha) in the nurse shark (Ginglymostoma cirratum)Bacteria under stress by complement and coagulation.Mouse Cd59b but not Cd59a is upregulated to protect cells from complement attack in response to inflammatory stimulation.Role of Streptococcus pneumoniae Proteins in Evasion of Complement-Mediated Immunity.Deletion of wboA enhances activation of the lectin pathway of complement in Brucella abortus and Brucella melitensis.Affinity of the C9 molecule for the C5b-8 complex compared with that for the complex containing C9 molecules.Polymorphisms in complement genes and risk of preeclampsia in Taiyuan, China.Host immune responses to experimental infection of Plasmodium relictum (lineage SGS1) in domestic canaries (Serinus canaria).Chimeras of human complement C9 reveal the site recognized by complement regulatory protein CD59.Membrane pore formation by human complement: functional importance of the transmembrane β-hairpin (TMH) segments of C8α and C9.Interaction between complement proteins C5b-7 and erythrocyte membrane sialic acid.Complement factor C5a exerts an anti-inflammatory effect in acute pancreatitis and associated lung injury.Sex-specific variation in brown-headed cowbird immunity following acute stress: a mechanistic approach.Inhibition of complement-mediated haemolysis in paroxysmal nocturnal haemoglobinuria by heparin or low-molecular weight heparin.Baseline and post-stress seasonal changes in immunocompetence and redox state maintenance in the fishing bat Myotis vivesi.Engineering therapeutic monoclonal antibodies.Membrane attack complex generation increases as a function of time in stored blood.Biochemical characteristics of Eiseniapore, a pore-forming protein in the coelomic fluid of earthworms.Developmental corticosterone treatment does not program immune responses in zebra finches (Taeniopygia guttata).
P2860
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P2860
The membrane attack complex of complement. Assembly, structure and cytotoxic activity.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
The membrane attack complex of complement. Assembly, structure and cytotoxic activity.
@en
type
label
The membrane attack complex of complement. Assembly, structure and cytotoxic activity.
@en
prefLabel
The membrane attack complex of complement. Assembly, structure and cytotoxic activity.
@en
P1433
P1476
The membrane attack complex of complement. Assembly, structure and cytotoxic activity.
@en
P2093
P304
P356
10.1016/0300-483X(94)90253-4
P407
P577
1994-02-01T00:00:00Z