Lipopolysaccharide (LPS)-binding proteins BPI and LBP form different types of complexes with LPS.
about
The BPI/LBP family of proteins: a structural analysis of conserved regionsPurification and characterization of PLUNC from human tracheobronchial secretionsThe carboxyl-terminal domain of closely related endotoxin-binding proteins determines the target of protein-lipopolysaccharide complexesSurfactant Proteins A and D Bind CD14 by Different MechanismsrBPI(21) promotes lipopolysaccharide aggregation and exerts its antimicrobial effects by (hemi)fusion of PG-containing membranes.A neutrophil-derived anti-infective molecule: bactericidal/permeability-increasing protein.Morphology, size distribution, and aggregate structure of lipopolysaccharide and lipid A dispersions from enterobacterial origin.Deacylation of purified lipopolysaccharides by cellular and extracellular components of a sterile rabbit peritoneal inflammatory exudate.LPS-induced galectin-3 oligomerization results in enhancement of neutrophil activation.Associations between the duration of dialysis, endotoxemia, monocyte chemoattractant protein-1, and the effects of a short-dwell exchange in patients requiring continuous ambulatory peritoneal dialysis.Functional mapping of surfactant protein A.Therapeutic potential of the bactericidal/permeability-increasing protein.Effect of plasma phospholipid transfer protein deficiency on lethal endotoxemia in mice.A host beetle pheromone regulates development and behavior in the nematode Pristionchus pacificusBiophysical mechanisms of endotoxin neutralization by cationic amphiphilic peptides.Antimicrobial activity of PLUNC protects against Pseudomonas aeruginosa infection.Genetic variation in bactericidal/permeability-increasing protein influences the risk of developing rapid airflow decline after hematopoietic cell transplantation.Events at the host-microbial interface of the gastrointestinal tract. I. Adaptation to a microbial world: role of epithelial bactericidal/permeability-increasing protein.Structural and functional features of a developmentally regulated lipopolysaccharide-binding protein.Endotoxin{middle dot}albumin complexes transfer endotoxin monomers to MD-2 resulting in activation of TLR4The bactericidal/permeability-increasing protein (BPI) in infection and inflammatory disease.Hemopexin down-regulates LPS-induced proinflammatory cytokines from macrophages.LPS-binding protein protects mice from septic shock caused by LPS or gram-negative bacteria.De novo design of potent antimicrobial peptidesKukoamine B promotes TLR4-independent lipopolysaccharide uptake in murine hepatocytes.Bactericidal/permeability increasing protein: a multifaceted protein with functions beyond LPS neutralization.Isolation, characterization, and antimicrobial properties of bovine oligosaccharide-binding protein. A microbicidal granule protein of eosinophils and neutrophils.Synthetic peptides representing the N-terminal segment of surfactant protein C modulate LPS-stimulated TNF-alpha production by macrophages.Of Men Not Mice: Bactericidal/Permeability-Increasing Protein Expressed in Human Macrophages Acts as a Phagocytic Receptor and Modulates Entry and Replication of Gram-Negative Bacteria.Evaluation of lipopolysaccharide aggregation by light scattering spectroscopy.Structure-function analysis of CD14 as a soluble receptor for lipopolysaccharide.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.Mechanism of interaction of optimized Limulus-derived cyclic peptides with endotoxins: thermodynamic, biophysical and microbiological analysis.Fold-unfold transitions in the selectivity and mechanism of action of the N-terminal fragment of the bactericidal/permeability-increasing protein (rBPI(21)).Molecular cloning and characterization of spurt, a human novel gene that is retinoic acid-inducible and encodes a secretory protein specific in upper respiratory tracts.Interaction of hemoglobin with enterobacterial lipopolysaccharide and lipid A. Physicochemical characterization and biological activity.Membrane expression of soluble endotoxin-binding proteins permits lipopolysaccharide signaling in Chinese hamster ovary fibroblasts independently of CD14.Role of the degree of oligomerization in the structure and function of human surfactant protein A.The antimicrobial antiproteinase elafin binds to lipopolysaccharide and modulates macrophage responses.Identification of IL-1β and LPS as optimal activators of monolayer and alginate-encapsulated mesenchymal stromal cell immunomodulation using design of experiments and statistical methods.
P2860
Q24673162-A4548995-97F9-47A9-8951-F14A4D0E46ABQ28201914-E0EF3380-8873-4E11-835A-D527AAA53F7AQ28214380-B4F0C31C-BF97-41B9-A8B2-D00450B2E7A1Q29392656-B46271DF-3D83-4176-AE14-DD3AD731F07FQ33520240-15C36942-4DB6-4DD1-96CA-622B2FFC2222Q33593645-F1D00B12-C936-4D86-9D82-902B75D6155BQ33648669-660C5955-2B45-4A06-95A9-FF0213238A00Q33876722-DEF8FED0-E692-4FD9-AC9A-622026D007BBQ34059590-38E1E482-AC57-4FE0-A5AC-11BD1095425BQ34294329-F0A6A886-DBE9-4954-A015-3DEEE699B03FQ34326890-6E8C563E-D2CA-4BAC-BDE8-12A39BE9628EQ34519111-A15208EA-9CA5-4811-9DF3-6E0CBF152C53Q34656242-6E976476-CA91-452D-92D5-DF4342EBB5A5Q34731096-462CAB95-2C5A-49C9-B3AF-030F2BBD6502Q35051284-E9B2A9E1-1BD0-43AE-963B-427779D7FD5EQ35058932-3D41CAE8-E3F6-4413-B4F8-7C3ED368BAC1Q35849483-00BD3979-EEAA-4F12-B380-3B202071B6A1Q36069861-49248EE2-C6BE-4298-95F1-095080A52FFAQ36205838-D516D3F5-678C-4822-BED8-496C5BD5BE52Q36796331-6901DDC7-9ADA-48C5-88D8-D1CD2C87025EQ36902238-C2198161-0989-44B2-B2FD-48B83C180EB2Q37304848-69BBCF98-6690-41D1-8506-651ACA364477Q37381799-2D4C356D-12AA-4D65-9E59-F71614F737E0Q37489546-2BDE4FAC-B84E-468E-847B-973E887AA2CFQ37628894-1443404D-4FA2-4D78-A91F-624BE57C5142Q38060523-885572BC-5FF1-43CD-AC53-4D3474622B6BQ38291429-EFDDB520-5DDF-4D0F-A375-4768C30AE663Q39886078-BAC22E1D-CD8B-4CBA-93FE-E905E2D47B4EQ40460582-4E7F4E57-1E92-4F9B-ADFC-8C2A49BB9614Q40612468-3D0A61E9-FC43-4E40-8C86-1A4BDA48C0DFQ40903248-C567225E-9271-4EFE-900A-0E563CE90CCBQ42018282-37C7E704-71F5-4578-8D6D-93F5647E7A12Q42054196-87C758AE-CBC7-457B-8DE3-B1FA0DECA858Q42063076-0A32B09B-E9F9-4F6E-89A7-B92B4EB0E770Q42686992-795CDF4E-B4B6-412D-956D-2889A4925E19Q43698071-5AEFCF14-0759-4C44-ACA7-2E5EA789212DQ44410845-0E052F92-1BD4-4F1E-8165-E388C62B221BQ45198889-0F189C8C-0A45-44C5-80A3-9A84420F031BQ45236699-8E23E945-43C4-44E9-BB7A-9D6443944EC6Q48189326-482D1AC3-71DA-4AE2-ACBB-53A52DAB0F21
P2860
Lipopolysaccharide (LPS)-binding proteins BPI and LBP form different types of complexes with LPS.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh-hant
name
Lipopolysaccharide (LPS)-bindi ...... t types of complexes with LPS.
@en
type
label
Lipopolysaccharide (LPS)-bindi ...... t types of complexes with LPS.
@en
prefLabel
Lipopolysaccharide (LPS)-bindi ...... t types of complexes with LPS.
@en
P2093
P2860
P356
P1476
Lipopolysaccharide (LPS)-bindi ...... nt types of complexes with LPS
@en
P2093
P2860
P304
18682-18685
P356
10.1074/JBC.272.30.18682
P407
P577
1997-07-01T00:00:00Z