R
Richard J. Ulevitch
Researcher at Scripps Research Institute
Publications - 240
Citations - 50508
Richard J. Ulevitch is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Innate immune system & CD14. The author has an hindex of 102, co-authored 239 publications receiving 49181 citations. Previous affiliations of Richard J. Ulevitch include French Institute of Health and Medical Research & University of Pennsylvania.
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Journal ArticleDOI
Lipopolysaccharide (LPS) signal transduction and clearance. Dual roles for LPS binding protein and membrane CD14.
TL;DR: Data show that while LPS signal transduction and LPS clearance utilize both LBP and mCD14, the pathways bifurcate after LPS binding to m CD14.
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Transfection of CD14 into 70Z/3 cells dramatically enhances the sensitivity to complexes of lipopolysaccharide (LPS) and LPS binding protein.
TL;DR: Investigation of the effect of transfection of CD14 into 70Z/3 cells on LPS responsiveness provides evidence to support the concept that the LPS receptor in cells that constitutively express CD14 may be a multiprotein complex containing CD14 and membrane protein common to a diverse group of LPS- responsive cells.
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Lipopolysaccharide (LPS) partial structures inhibit responses to LPS in a human macrophage cell line without inhibiting LPS uptake by a CD14-mediated pathway.
TL;DR: The results indicate that both stimulatory and nonstimulatory ligands can bind to CD14 in the presence of LBP; the mechanism of inhibition by dLPS is LPS- specific, yet does not involve blockade of LPS binding to CD 14; and in keeping with previous results of others, large concentrations of L PS can stimulate the cells in the absence of detectable binding toCD14.
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MD-2 and TLR4 N-Linked Glycosylations Are Important for a Functional Lipopolysaccharide Receptor *
TL;DR: The double mutant of MD-2 failed to support LPS-induced activation of an interleukin-8 (IL-8) promoter-driven luciferase reporter to induce IL-8 secretion or to activate amino-terminal c-Jun kinase (JNK).
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Activation of p38 in Stimulated Human Neutrophils: Phosphorylation of the Oxidase Component p47phoxby p38 and ERK but Not by JNK
Jamel El Benna,Jamel El Benna,Jiahuai Han,Jiahuai Han,Jeen-Woo Park,Jeen-Woo Park,Elmar Schmid,Elmar Schmid,Richard J. Ulevitch,Richard J. Ulevitch,Bernard M. Babior,Bernard M. Babior +11 more
TL;DR: The data show that p38, like ERK, can be activated in neutrophils exposed to an appropriate stimulus, and that some but not all proline-directed kinases are able to participate in the phosphorylation of a protein essential for normal neutrophil function.