pubmed-article:2402637 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2402637 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
pubmed-article:2402637 | lifeskim:mentions | umls-concept:C1416801 | lld:lifeskim |
pubmed-article:2402637 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:2402637 | pubmed:issue | 4975 | lld:pubmed |
pubmed-article:2402637 | pubmed:dateCreated | 1990-10-26 | lld:pubmed |
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pubmed-article:2402637 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2402637 | pubmed:abstractText | The primary structure of lipopolysaccharide binding protein (LBP), a trace plasma protein that binds to the lipid A moiety of bacterial lipopolysaccharides (LPSs), was deduced by sequencing cloned complementary DNA. LBP shares sequence identity with another LPS binding protein found in granulocytes, bactericidal/permeability-increasing protein, and with cholesterol ester transport protein of the plasma. LBP may control the response to LPS under physiologic conditions by forming high-affinity complexes with LPS that bind to monocytes and macrophages, which then secrete tumor necrosis factor. The identification of this pathway for LPS-induced monocyte stimulation may aid in the development of treatments for diseases in which Gram-negative sepsis or endotoxemia are involved. | lld:pubmed |
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pubmed-article:2402637 | pubmed:language | eng | lld:pubmed |
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pubmed-article:2402637 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:2402637 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2402637 | pubmed:month | Sep | lld:pubmed |
pubmed-article:2402637 | pubmed:issn | 0036-8075 | lld:pubmed |
pubmed-article:2402637 | pubmed:author | pubmed-author:GrafP DPD | lld:pubmed |
pubmed-article:2402637 | pubmed:author | pubmed-author:UlevitchR JRJ | lld:pubmed |
pubmed-article:2402637 | pubmed:author | pubmed-author:MathisonJ CJC | lld:pubmed |
pubmed-article:2402637 | pubmed:author | pubmed-author:TobiasP SPS | lld:pubmed |
pubmed-article:2402637 | pubmed:author | pubmed-author:WrightS DSD | lld:pubmed |
pubmed-article:2402637 | pubmed:author | pubmed-author:SchumannR RRR | lld:pubmed |
pubmed-article:2402637 | pubmed:author | pubmed-author:LeongS RSR | lld:pubmed |
pubmed-article:2402637 | pubmed:author | pubmed-author:FlaggsG WGW | lld:pubmed |
pubmed-article:2402637 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2402637 | pubmed:day | 21 | lld:pubmed |
pubmed-article:2402637 | pubmed:volume | 249 | lld:pubmed |
pubmed-article:2402637 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2402637 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2402637 | pubmed:pagination | 1429-31 | lld:pubmed |
pubmed-article:2402637 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:2402637 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:2402637 | pubmed:articleTitle | Structure and function of lipopolysaccharide binding protein. | lld:pubmed |
pubmed-article:2402637 | pubmed:affiliation | Department of Immunology, Research Institute of Scripps Clinic, La Jolla, CA 92037. | lld:pubmed |
pubmed-article:2402637 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2402637 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:2402637 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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