THE MECHANISM OF ACTION OF PROTECTIN (CD59), A HOMOLOGOUS RESTRICTION FACTOR OF THE HUMAN-COMPLEMENT SYSTEM

THE MECHANISM OF ACTION OF PROTECTIN (CD59), A HOMOLOGOUS RESTRICTION FACTOR OF THE HUMAN-COMPLEMENT SYSTEM

Sonraí bibleagrafaíochta
Príomhchruthaitheoirí:	Meri, S, Morgan, B, Davies, A, Daniels, R, Olavesen, M, Waldmann, H, Lachmann, P
Formáid:	Journal article
Foilsithe / Cruthaithe:	1990

Míreanna comhchosúla

Human protectin (CD59), an 18,000-20,000 MW complement lysis restricting factor, inhibits C5b-8 catalysed insertion of C9 into lipid bilayers.
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Distribution of protectin (CD59), a complement membrane attack inhibitor, in normal human tissues.
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CD59, an LY-6-like protein expressed in human lymphoid cells, regulates the action of the complement membrane attack complex on homologous cells.
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Transfection of human CD59 complementary DNA into rat cells confers resistance to human complement.
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The glycosylation of the complement regulatory protein, human erythrocyte CD59.
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The glycosylation of the complement regulatory protein, human erythrocyte CD59.
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A humanized monovalent CD3 antibody which can activate homologous complement.
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Mutational analysis of the active site and antibody epitopes of the complement-inhibitory glycoprotein, CD59.
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Expression of the membrane complement regulatory proteins (CD55 and CD59) in human thymus.
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High level transcription of the complement regulatory protein CD59 requires an enhancer located in intron 1.
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The CD59 antigen--a multifunctional molecule.
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The complement inhibitor CD59 is required for GABAergic synaptic transmission in the dentate gyrus
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Structural Basis for Recognition of the Pore-Forming Toxin Intermedilysin by Human Complement Receptor CD59
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Circulating Protectin D1 and Neutrophils Extracellular Traps in the Diagnosis and Progression of Acute Pancreatitis
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Structural studies of human CD59 and its ligands
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Both Freshly Prepared and Frozen-Stored Amniotic Membrane Cells Express the Complement Inhibitor CD59
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Expressão de proteínas reguladoras do complemento CD55, CD59, CD35 e CD46 na artrite reumatoide Expression of complement regulatory proteins CD55, CD59, CD35, and CD46 in rheumatoid arthritis
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Gene structure of human CD59 and demonstration that discrete mRNAs are generated by alternative polyadenylation.
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Expression levels of complement regulatory proteins (CD35, CD55 and CD59) on peripheral blood cells of patients with chronic kidney disease
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Protectin DX Exhibits Protective Effects in Mouse Model of Lipopolysaccharide-Induced Acute Lung Injury
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Erythroid-specific expression of human CD59 and transfer to vascular endothelial cells.
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Altered Expression of Complement Regulatory Proteins CD35, CD46, CD55, and CD59 on Leukocyte Subsets in Individuals Suffering From Coronary Artery Disease
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Intracellular complement activation—An alarm raising mechanism?
de réir: Reichhardt, M, et al.
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Cell- and tissue-specific expression of a human CD59 minigene in transgenic mice.
de réir: Diamond, L, et al.
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SARS-CoV-2 hijacks host CD55, CD59 and factor H to impair antibody-dependent complement-mediated lysis
de réir: Laura Gebetsberger, et al.
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Increased expression of complement regulators CD55 and CD59 on peripheral blood cells in patients with EAHEC O104:H4 infection.
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Protectin DX Relieve Hyperoxia‐induced Lung Injury by Protecting Pulmonary Endothelial Glycocalyx
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Protectin conjugates in tissue regeneration 1 alleviates sepsis-induced acute lung injury by inhibiting ferroptosis
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Protectin DX increases survival in a mouse model of sepsis by ameliorating inflammation and modulating macrophage phenotype
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Maternal dietary omega-3 fatty acid intake increases resolvin and protectin levels in the rat placenta
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Complement regulator CD59 prevents peripheral organ injury in rats made seropositive for neuromyelitis optica immunoglobulin G
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NANOG confers resistance to complement-dependent cytotoxicity in immune-edited tumor cells through up-regulating CD59
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Kinetic analysis of the interaction between the complement regulators CD46 and CD55 and components of the alternative pathway of complement
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High-resolution structures of bacterially expressed soluble human CD59
de réir: Leath, K, et al.
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High-resolution structures of bacterially expressed soluble human CD59.
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