Lipopolysaccharide (LPS)-binding protein accelerates the binding of LPS to CD14. - Wikidata - awgldk - TriplyDB

Lipopolysaccharide (LPS)-binding protein accelerates the binding of LPS to CD14.

Lipopolysaccharide (LPS)-binding protein accelerates the binding of LPS to CD14.

http://www.wikidata.org/entity/Q38313210

about

Lipoteichoic acid (LTA) of Streptococcus pneumoniae and Staphylococcus aureus activates immune cells via Toll-like receptor (TLR)-2, lipopolysaccharide-binding protein (LBP), and CD14, whereas TLR-4 and MD-2 are not involved Lipopolysaccharide-binding protein mediates CD14-independent intercalation of lipopolysaccharide into phospholipid membranes CD14 is a cell-activating receptor for bacterial peptidoglycan Lipopolysaccharide-binding protein and phospholipid transfer protein release lipopolysaccharides from gram-negative bacterial membranes Physical contact between lipopolysaccharide and toll-like receptor 4 revealed by genetic complementation Innate recognition of bacteria in human milk is mediated by a milk-derived highly expressed pattern recognition receptor, soluble CD14 Physicochemical characterization of the endotoxins from Coxiella burnetii strain Priscilla in relation to their bioactivities Rodent models of neuroinflammation for Alzheimer's disease Postulates for validating TLR4 agonists Kinetics of Local and Systemic Leucocyte and Cytokine Reaction of Calves to Intrabronchial Infection with Chlamydia psittaci Bacterial lipopolysaccharide inhibits dengue virus infection of primary human monocytes/macrophages by blockade of virus entry via a CD14-dependent mechanism.The Crystal Structure of Human Soluble CD14 Reveals a Bent Solenoid with a Hydrophobic Amino-Terminal Pocket Evidence of a trimolecular complex involving LPS, LPS binding protein and soluble CD14 as an effector of LPS response The carboxyl-terminal domain of closely related endotoxin-binding proteins determines the target of protein-lipopolysaccharide complexes Plasma lipopolysaccharide-binding protein is found associated with a particle containing apolipoprotein A-I, phospholipid, and factor H-related proteins Signal transduction by the lipopolysaccharide receptor, Toll-like receptor-4 Local secretion of urocortin 1 promotes microvascular permeability during lipopolysaccharide-induced inflammation Hypertensive rats are susceptible to TLR4-mediated signaling following exposure to combustion source particulate matter Protein kinase C eta mediates lipopolysaccharide-induced nitric-oxide synthase expression in primary astrocytes The attenuated inflammation of MPL is due to the lack of CD14-dependent tight dimerization of the TLR4/MD2 complex at the plasma membrane Sepsis: in search of cure.Portable microfluidic chip for detection of Escherichia coli in produce and blood Induction of the cyclic nucleotide phosphodiesterase PDE4B is essential for LPS-activated TNF-alpha responses Structural analysis of two glycosphingolipids from the lipopolysaccharide-lacking bacterium Sphingomonas capsulata.Structural and biological characterization of highly purified hepta-acyl lipid A present in the lipopolysaccharide of the Salmonella enterica sv. Minnesota Re deep rough mutant strain R595.Construction of acetate auxotrophs of Neisseria meningitidis to study host-meningococcal endotoxin interactions.Antagonism by ethanol of endotoxin-induced tissue factor activation in relation to the depressed endotoxin binding to monocyte-like U937 cells.Visualization of the molecular dynamics of lipopolysaccharide on the plasma membrane of murine macrophages by total internal reflection fluorescence microscopy.Toll, a new piece in the puzzle of innate immunity.Vibrio cholerae proteome-wide screen for immunostimulatory proteins identifies phosphatidylserine decarboxylase as a novel Toll-like receptor 4 agonist.Soluble CD36 ectodomain binds negatively charged diacylglycerol ligands and acts as a co-receptor for TLR2.The macrophage LBP gene is an LXR target that promotes macrophage survival and atherosclerosis.The dual role of lipopolysaccharide as effector and target molecule.The human host defense peptide LL-37 interacts with Neisseria meningitidis capsular polysaccharides and inhibits inflammatory mediators release.Soluble CD14 activates monocytic cells independently of lipopolysaccharide Lipopolysaccharide and its analog antagonists display differential serum factor dependencies for induction of cytokine genes in murine macrophages.LPS-induced cytokine levels are repressed by elevated expression of HSP70 in rats: possible role of NF-kappaB Changes in endotoxin-binding proteins during major elective surgery: important role for soluble CD14 in regulation of biological activity of systemic endotoxin Human lactoferrin interacts with soluble CD14 and inhibits expression of endothelial adhesion molecules, E-selectin and ICAM-1, induced by the CD14-lipopolysaccharide complex.Interaction of surfactant protein A with lipopolysaccharide and regulation of inflammatory cytokines in the THP-1 monocytic cell line

P2860

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P2860

Lipopolysaccharide (LPS)-binding protein accelerates the binding of LPS to CD14.

http://www.wikidata.org/entity/Q38313210

description

1994 nî lūn-bûn

@nan

1994年の論文

@ja

1994年論文

@yue

1994年論文

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1994年論文

@zh-hk

1994年論文

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1994年論文

@zh-tw

1994年论文

@wuu

1994年论文

@zh

1994年论文

@zh-cn

name

Lipopolysaccharide (LPS)-binding protein accelerates the binding of LPS to CD14.

@en

type

label

Lipopolysaccharide (LPS)-binding protein accelerates the binding of LPS to CD14.

@en

prefLabel

Lipopolysaccharide (LPS)-binding protein accelerates the binding of LPS to CD14.

@en

P1433

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P2860

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P1433

Journal of Experimental Medicine

P1476

Lipopolysaccharide (LPS)-binding protein accelerates the binding of LPS to CD14.

@en

P2093

D A Johnson

http://www.w3.org/2001/XMLSchema#string

D S Miller

http://www.w3.org/2001/XMLSchema#string

E Hailman

http://www.w3.org/2001/XMLSchema#string

H S Lichenstein

http://www.w3.org/2001/XMLSchema#string

L A Busse

http://www.w3.org/2001/XMLSchema#string

M Kelley

http://www.w3.org/2001/XMLSchema#string

M M Wurfel

http://www.w3.org/2001/XMLSchema#string

M M Zukowski

http://www.w3.org/2001/XMLSchema#string

S D Wright

http://www.w3.org/2001/XMLSchema#string

P2860

Lipopolysaccharide (LPS) binding protein opsonizes LPS-bearing particles for recognition by a novel receptor on macrophages

The monocyte differentiation antigen, CD14, is anchored to the cell membrane by a phosphatidylinositol linkage

Structure and function of lipopolysaccharide binding protein

Isolation of Chinese hamster cell mutants deficient in dihydrofolate reductase activity

Monocyte antigen CD14 is a phospholipid anchored membrane protein

Lipopolysaccharide (LPS) partial structures inhibit responses to LPS in a human macrophage cell line without inhibiting LPS uptake by a CD14-mediated pathway

CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding protein

Possible role of flanking nucleotides in recognition of the AUG initiator codon by eukaryotic ribosomes

Endotoxin-mediated endothelial cell injury and activation: role of soluble CD14.

Complement receptor type three (CD11b/CD18) of human polymorphonuclear leukocytes recognizes fibrinogen.

P304

269-277

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P31

scholarly article

P356

10.1084/JEM.179.1.269

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P407

P433

1

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P478

179

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P577

1994-01-01T00:00:00Z

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P5875

277492352

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7505800

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P921

lipopolysaccharide

P932

2191344

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