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Cited by 1,672

The DOI matches its Crossref record.

Structure and Function of Lipopolysaccharide Binding Protein

Schumann, Ralf R., Leong, Steven R., Flaggs, Gail W., Gray, Patrick W., Wright, Samuel D., Mathison, John C., Tobias, Peter S., Ulevitch, Richard J.·1990·Science
DOI 10.1126/science.2402637
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Abstract

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.

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Metadata

Authors
Schumann, R. R., Leong, S. R., Flaggs, G. W., Gray, P. W., Wright, S. D., Mathison, J. C., Tobias, P. S., & Ulevitch, R. J.
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
1990-09-21
Volume
249
Issue
4975
Pages
1429-1431
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.2402637
OpenAlex
W2064626913
Cited by
1,672
References
0
FWCI
23.38
Type
journal article
Language
en
Open access
closed

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.