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    • Several versions

    Roles of coactosin-like protein (CLP) and 5-lipoxygenase-activating protein (FLAP) in cellular leukotriene biosynthesis

    Basavarajappa, Devaraj, Wan, Min, Lukic, Ana, Steinhilber, Dieter, Samuelsson, Bengt, Rådmark, Olof
    Proceedings of the National Academy of Sciences of the United States of America, 05 August 2014, Vol.111(31), pp.11371-6 [Peer Reviewed Journal]

    • Article

    Dimerization of human 5-lipoxygenase

    Häfner, Ann-Kathrin
    Cernescu, Mihaela, Hofmann, Bettina, Ermisch, Michael, Hörnig, Michael, Metzner, Julia, Schneider, Gisbert, Brutschy, Bernhard, Steinhilber, Dieter
    Biological Chemistry. - 2011/392/12/1097-1111
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    Title: Dimerization of human 5-lipoxygenase
    Author: Häfner, Ann-Kathrin
    Contributor: Cernescu, Mihaela; Hofmann, Bettina; Ermisch, Michael; Hörnig, Michael; Metzner, Julia; Schneider, Gisbert; Brutschy, Bernhard; Steinhilber, Dieter
    Subject: diamide - 5-lipoxygenase - LILBID - leukotrienes - molecular modeling
    Description: Human 5-lipoxygenase (5-LO) can form dimers as shown here via native gel electrophoresis, gel filtration chromatography and LILBID (laser induced liquid bead ion desorption) mass spectrometry. After glutathionylation of 5-LO by diamide/glutathione treatment, dimeric 5-LO was no longer detectable and 5-LO almost exclusively exists in the monomeric form which showed full catalytic activity. Incubation of 5-LO with diamide alone led to a disulfide-bridged dimer and to oligomer formation which displays a strongly reduced catalytic activity. The bioinformatic analysis of the 5-LO surface for putative protein-protein interaction domains and molecular modeling of the dimer interface suggests a head to tail orientation of the dimer which also explains the localization of previously reported ATP binding sites. This interface domain was confirmed by the observation that 5-LO dimer formation and inhibition of activity by diamide was largely prevented when four cysteines (C159S, C300S, C416S, C418S) in this domain were mutated to serines
    Linked entry: Biological Chemistry. - 2011/392/12/1097-1111
    Host document: Biological Chemistry
    Identifier: 10.1515/BC.2011.200 (DOI)

    • Several versions

    Selective Non-Steroidal Glucocorticoid Receptor Agonists Attenuate Inflammation but Do Not Impair Intestinal Epithelial Cell Restitution In Vitro (SEGRAs and Intestinal Epithelial Repair)

    Reuter, Kerstin C, Loitsch, Stefan M, Dignass, Axel U, Steinhilber, Dieter, Stein, Jürgen
    PLoS ONE, 2012, Vol.7(1), p.e29756 [Peer Reviewed Journal]

    • Several versions

    CD69 Is a TGF-β/1α,25-dihydroxyvitamin D 3 Target Gene in Monocytes

    Wöbke, Thea K, Von Knethen, Andreas, Steinhilber, Dieter, Sorg, Bernd L
    PLoS ONE, 2013, Vol.8(5) [Peer Reviewed Journal]

    • Several versions

    Post-Transcriptional Regulation of 5-Lipoxygenase mRNA Expression via Alternative Splicing and Nonsense-Mediated mRNA Decay (5-Lipoxygenase and Alternative Splicing)

    Ochs, Meike J, Sorg, Bernd L, Pufahl, Laura, Grez, Manuel, Suess, Beatrix, Steinhilber, Dieter
    PLoS ONE, 2012, Vol.7(2), p.e31363 [Peer Reviewed Journal]

    • Several versions

    Identification and Characterization of a New Protein Isoform of Human 5-Lipoxygenase

    Häfner, Ann-Kathrin, Beilstein, Kim, Graab, Philipp, Ball, Ann-Katrin, Saul, Meike J, Hofmann, Bettina, Steinhilber, Dieter
    PLoS ONE, 2016, Vol.11(11) [Peer Reviewed Journal]

    • Several versions

    The Histone Demethylase PHF8 Is Essential for Endothelial Cell Migration

    Gu, Lunda, Hitzel, Juliane, Moll, Franziska, Kruse, Christoph, Malik, Randa Abdel, Preussner, Jens, Looso, Mario, Leisegang, Matthias S, Steinhilber, Dieter, Brandes, Ralf P, Fork, Christian
    PLoS ONE, 2016, Vol.11(1) [Peer Reviewed Journal]

    • Several versions

    Loss of FADS2 Function Severely Impairs the Use of HeLa Cells as an In Vitro Model for Host Response Studies Involving Fatty Acid Effects

    Jaudszus, Anke, Degen, Christian, Barth, Stephan W, Klempt, Martin, Schlörmann, Wiebke, Roth, Alexander, Rohrer, Carsten, Sauerwein, Helga, Sachse, Konrad, Jahreis, Gerhard
    PLoS ONE, 2014, Vol.9(12) [Peer Reviewed Journal]

    • Article

    5-lipoxygenase mRNA and protein isoforms

    Ochs, Meike J, Suess, Beatrix, Steinhilber, Dieter
    Basic & clinical pharmacology & toxicology, January 2014, Vol.114(1), pp.78-82 [Peer Reviewed Journal]
    MEDLINE/PubMed (U.S. National Library of Medicine)
    Title: 5-lipoxygenase mRNA and protein isoforms
    Author: Ochs, Meike J; Suess, Beatrix; Steinhilber, Dieter
    Subject: Arachidonate 5-Lipoxygenase -- Genetics ; RNA, Messenger -- Genetics
    Description: 5-Lipoxygenase (5-LO) catalyses the two initial steps in the biosynthesis of leukotrienes, a group of inflammatory lipid mediators derived from arachidonic acid. An increased level of leukotrienes is associated with chronic inflammatory diseases such as asthma or atherosclerosis. In this MiniReview, we focus on recent findings regarding alternative splice variants of 5-LO with a special emphasis on two potential protein isoforms expressed in human B-lymphocytes which might be of interest as new drug targets.
    Is part of: Basic & clinical pharmacology & toxicology, January 2014, Vol.114(1), pp.78-82
    Identifier: 1742-7843 (E-ISSN); 24020397 Version (PMID); 10.1111/bcpt.12115 (DOI)

    • Several versions

    MicroRNA Involved in Inflammation: Control of Eicosanoid Pathway

    Ochs, Meike J, Steinhilber, Dieter, Suess, Beatrix
    Frontiers in pharmacology, 2011, Vol.2, pp.39 [Peer Reviewed Journal]