Interaction of SP-A (surfactant protein A) with bacterial rough lipopolysaccharide (Re-LPS), and effects of SP-A on the binding of Re-LPS to CD14 and LPS-binding protein. - Wikidata - awgldk - TriplyDB

Interaction of SP-A (surfactant protein A) with bacterial rough lipopolysaccharide (Re-LPS), and effects of SP-A on the binding of Re-LPS to CD14 and LPS-binding protein.

Interaction of SP-A (surfactant protein A) with bacterial rough lipopolysaccharide (Re-LPS), and effects of SP-A on the binding of Re-LPS to CD14 and LPS-binding protein.

http://www.wikidata.org/entity/Q42018282

about

CD6 binds to pathogen-associated molecular patterns and protects from LPS-induced septic shock Effect of cysteine 85 on biochemical properties and biological function of human surfactant protein A variants Elucidation of Lipid Binding Sites on Lung Surfactant Protein A Using X-ray Crystallography, Mutagenesis, and Molecular Dynamics Simulations SP-R210 (Myo18A) Isoforms as Intrinsic Modulators of Macrophage Priming and Activation rBPI(21) promotes lipopolysaccharide aggregation and exerts its antimicrobial effects by (hemi)fusion of PG-containing membranes.Aggregation behavior of an ultra-pure lipopolysaccharide that stimulates TLR-4 receptors.Introduction of a lysine residue promotes aggregation of temporin L in lipopolysaccharides and augmentation of its antiendotoxin property.Structural and functional differences among human surfactant proteins SP-A1, SP-A2 and co-expressed SP-A1/SP-A2: role of supratrimeric oligomerization.Synthetic peptides representing the N-terminal segment of surfactant protein C modulate LPS-stimulated TNF-alpha production by macrophages.Surfactant protein A forms extensive lattice-like structures on 1,2-dipalmitoylphosphatidylcholine/rough-lipopolysaccharide-mixed monolayers.Surfactant protein A directly interacts with TLR4 and MD-2 and regulates inflammatory cellular response. Importance of supratrimeric oligomerization.Bacterial lipopolysaccharide promotes destabilization of lung surfactant-like films SP-A permeabilizes lipopolysaccharide membranes by forming protein aggregates that extract lipids from the membrane Surfactant protein A signaling pathways in human uterine smooth muscle cells.Pulmonary surfactant protein A-induced changes in the molecular conformation of bacterial deep-rough LPS lead to reduced activity on human macrophages.Squalene ameliorates atherosclerotic lesions through the reduction of CD36 scavenger receptor expression in macrophages.Surfactant Protein A Prevents IFN-γ/IFN-γ Receptor Interaction and Attenuates Classical Activation of Human Alveolar Macrophages.Role of clathrin-mediated endocytosis of surfactant protein A by alveolar macrophages in intracellular signaling.The Role of Collectins and Galectins in Lung Innate Immune Defense

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P2860

Interaction of SP-A (surfactant protein A) with bacterial rough lipopolysaccharide (Re-LPS), and effects of SP-A on the binding of Re-LPS to CD14 and LPS-binding protein.

http://www.wikidata.org/entity/Q42018282

description

2005 nî lūn-bûn

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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2005年论文

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name

Interaction of SP-A (surfactan ...... CD14 and LPS-binding protein.

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Interaction of SP-A (surfactan ...... CD14 and LPS-binding protein.

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type

label

Interaction of SP-A (surfactan ...... CD14 and LPS-binding protein.

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Interaction of SP-A (surfactan ...... CD14 and LPS-binding protein.

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prefLabel

Interaction of SP-A (surfactan ...... CD14 and LPS-binding protein.

@en

Interaction of SP-A (surfactan ...... CD14 and LPS-binding protein.

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P1433

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P1433

Biochemical Journal

P1476

Interaction of SP-A (surfactan ...... CD14 and LPS-binding protein.

@en

P2093

Fernando Sánchez-Barbero

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

Ignacio García-Verdugo

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Katrin Soldau

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Peter S Tobias

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P2860

MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4

Crystal structure of trimeric carbohydrate recognition and neck domains of surfactant protein A

Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution

Production of the acute-phase protein lipopolysaccharide-binding protein by respiratory type II epithelial cells: implications for local defense to bacterial endotoxins

Defensins: antimicrobial peptides of innate immunity

By binding SIRPalpha or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation

Surfactant Proteins A and D Bind CD14 by Different Mechanisms

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

Recognition of gram-negative bacteria and endotoxin by the innate immune system.

Tlr4: central component of the sole mammalian LPS sensor.

P304

115-124

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scholarly article

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10.1042/BJ20050529

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P433

Pt 1

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P478

391

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Cristina Casals

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2005-10-01T00:00:00Z

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15932345

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lipopolysaccharide

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1237145

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