Výsledky vyhledávání - "Polonca Prohinar"

Expression of Functional D299G.T399I Polymorphic Variant of TLR4 Depends More on Coexpression of MD-2 Than Does Wild-Type TLR4

Autor: Theresa L. Gioannini, Jerrold Weiss, Prasad Rallabhandi, Polonca Prohinar

Publikováno v: The Journal of Immunology. 184:4362-4367

Two missense variants (D299G and T399I) of TLR4 are cosegregated in individuals of European descent and, in a number of test systems, result in reduced responsiveness to endotoxin. How these changes within the ectodomain (ecd) of TLR4 affect TLR4 fun

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b99eda8114e877713762c59c9310f62
https://doi.org/10.4049/jimmunol.0903142

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Transfer of Monomeric Endotoxin from MD-2 to CD14

Autor: Athmane Teghanemt, Jerrold Weiss, Polonca Prohinar, Theresa L. Gioannini

Publikováno v: Journal of Biological Chemistry. 282:36250-36256

Potent Toll-like receptor 4 (TLR4)-dependent cell activation by endotoxin depends on sequential transfer of monomers of endotoxin from an aggregated form to CD14 via the lipopolysaccharide-binding protein and then to MD-2. We now show that monomeric

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6ab71fd9caf05c26c7ced8791a705c79
https://doi.org/10.1074/jbc.m705995200

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Functional activity of MD-2 polymorphic variant is significantly different in soluble and TLR4-bound forms: decreased endotoxin binding by G56R MD-2 and its rescue by TLR4 ectodomain

Autor: Jožica Vašl, Jerrold Weiss, Roman Jerala, Theresa L. Gioannini, Polonca Prohinar

Publikováno v: Journal of immunology (Baltimore, Md. : 1950). 180(9)

MD-2 is an essential component of endotoxin (LPS) sensing, binding LPS independently and when bound to the ectodomain of the membrane receptor TLR4. Natural variation of proteins involved in the LPS-recognition cascade such as the LPS-binding protein

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b7e1ff5820cd7e28d8d79088841f352
https://pubmed.ncbi.nlm.nih.gov/18424732

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Novel roles in human MD-2 of phenylalanines 121 and 126 and tyrosine 131 in activation of Toll-like receptor 4 by endotoxin

Autor: Richard Widstrom, Polonca Prohinar, Jerrold Weiss, Athmane Teghanemt, Theresa L. Gioannini, Fabio Re

Publikováno v: The Journal of biological chemistry. 283(3)

Potent mammalian cell activation by Gram-negative bacterial endotoxin requires sequential protein-endotoxin and protein-protein interactions involving lipopolysaccharide-binding protein, CD14, MD-2, and Toll-like receptor 4 (TLR4). TLR4 activation re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::433bfed5e21deed5ed6170c94998106c
https://pubmed.ncbi.nlm.nih.gov/17977838

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Transfer of monomeric endotoxin from MD-2 to CD14: characterization and functional consequences

Autor: Athmane, Teghanemt, Polonca, Prohinar, Theresa L, Gioannini, Jerrold P, Weiss

Publikováno v: The Journal of biological chemistry. 282(50)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::21c866c93395919e91334e7e0f23b5b3
https://pubmed.ncbi.nlm.nih.gov/17934216

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Endotoxin-binding proteins modulate the susceptibility of bacterial endotoxin to deacylation by acyloxyacyl hydrolase

Autor: Erika N. Levis, Jerrold Weiss, Robert S. Munford, Theresa L. Gioannini, DeSheng Zhang, Polonca Prohinar, Athmane Teghanemt

Publikováno v: The Journal of biological chemistry. 282(11)

Acyloxyacyl hydrolase (AOAH) is an eukaryotic lipase that partially deacylates and detoxifies Gram-negative bacterial lipopolysaccharides and lipooligosaccharides (LPSs or LOSs, endotoxin) within intact cells and inflammatory fluids. In cell lysates

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a4aa386646e078ec559c77654767c10
https://pubmed.ncbi.nlm.nih.gov/17227775

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Specific high affinity interactions of monomeric endotoxin.protein complexes with Toll-like receptor 4 ectodomain

Autor: Jerrold Weiss, Polonca Prohinar, Richard Widstrom, Athmane Teghanemt, Theresa L. Gioannini, Fabio Re, DeSheng Zhang

Publikováno v: The Journal of biological chemistry. 282(2)

Potent Toll-like receptor 4 (TLR4) activation by endotoxin has been intensely studied, but the molecular requirements for endotoxin interaction with TLR4 are still incompletely defined. Ligand-receptor interactions involving endotoxin and TLR4 were c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf89492446863fe8edf919d8fcb65738
https://pubmed.ncbi.nlm.nih.gov/17121827

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OmpR-dependent and OmpR-independent responses of Escherichia coli to sublethal attack by the neutrophil bactericidal/permeability increasing protein

Autor: Ines Mandic-Mulec, Jerrold Weiss, Steve A. Forst, Polonca Prohinar, Deoine Reed

Publikováno v: Molecular microbiology. 43(6)

Summary Bactericidal/permeability-increasing protein (BPI) of neutrophils is a lipopolysaccharide (LPS)-binding antibacterial protein with specificity for Gramnegative bacteria. BPI binding to the bacterial surface rapidly triggers potentially revers

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0953823c8d351d3ead7c22c89eb0e969
https://pubmed.ncbi.nlm.nih.gov/11952900

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