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  • 1
    Publication Date: 2013-10-25
    Description: Epoxyeicosatrienoic acids protect cardiac cells during starvation by modulating an autophagic response Cell Death and Disease 4, e885 (October 2013). doi:10.1038/cddis.2013.418 Authors: V Samokhvalov, N Alsaleh, H E El-Sikhry, K L Jamieson, C B Chen, D G Lopaschuk, C Carter, P E Light, R Manne, J R Falck & J M Seubert
    Keywords: autophagyepoxyeicosatrienoic acidcardiac cells
    Electronic ISSN: 2041-4889
    Topics: Biology , Medicine
    Published by Springer Nature
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  • 2
    Publication Date: 2012-06-27
    Description: Organic Letters DOI: 10.1021/ol301463c
    Print ISSN: 1523-7060
    Electronic ISSN: 1523-7052
    Topics: Chemistry and Pharmacology
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  • 3
    Publication Date: 1998-02-07
    Description: Mitogen stimulation of cytoskeletal changes and c-jun amino-terminal kinases is mediated by Rac small guanine nucleotide-binding proteins. Vav, a guanosine diphosphate (GDP)-guanosine triphosphate (GTP) exchange factor for Rac that stimulates the exchange of bound GDP for GTP, bound to and was directly controlled by substrates and products of phosphoinositide (PI) 3-kinase. The PI 3-kinase substrate phosphatidylinositol-4,5-bisphosphate inhibited activation of Vav by the tyrosine kinase Lck, whereas the product phosphatidylinositol-3,4,5-trisphosphate enhanced phosphorylation and activation of Vav by Lck. Control of Vav in response to mitogens by the products of PI 3-kinase suggests a mechanism for Ras-dependent activation of Rac.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Han, J -- Luby-Phelps, K -- Das, B -- Shu, X -- Xia, Y -- Mosteller, R D -- Krishna, U M -- Falck, J R -- White, M A -- Broek, D -- CA50261/CA/NCI NIH HHS/ -- CA71443/CA/NCI NIH HHS/ -- GM31278/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 23;279(5350):558-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Norris Comprehensive Cancer Center, University of Southern California, Los Angeles, CA 90033-0800, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9438848" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Enzyme Activation ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/*metabolism ; Guanine Nucleotide Exchange Factors ; Guanosine Diphosphate/*metabolism ; Guanosine Triphosphate/metabolism ; Inositol 1,4,5-Trisphosphate/metabolism/pharmacology ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck)/metabolism ; Mutagenesis, Site-Directed ; Oncogene Proteins/chemistry/*metabolism ; Phosphatidylinositol 3-Kinases/*metabolism ; Phosphatidylinositol 4,5-Diphosphate/metabolism/pharmacology ; Phosphatidylinositol Phosphates/metabolism/pharmacology ; Phosphatidylinositols/*metabolism/pharmacology ; Phosphorylation ; Proteins/metabolism ; Proto-Oncogene Proteins c-vav ; Rats ; rac GTP-Binding Proteins ; ras Guanine Nucleotide Exchange Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 1991-02-15
    Description: In the medullary segment of the thick ascending limb of the loop of Henle (mTALH), arachidonic acid (AA) is metabolized by a cytochrome P450-dependent monooxygenase to products that affect ion transport. The linkage between changes in ion transport and AA metabolism in isolated cells of the mTALH was examined. AA produced a concentration-dependent inhibition of 86Rb uptake--an effect that was prevented by selective blockade of cytochrome P450 monooxygenases. Inhibition by cytochrome P450 blockade of the effect of AA on 86Rb uptake could be circumvented by addition of the principal products of AA metabolism in the mTALH.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Escalante, B -- Erlij, D -- Falck, J R -- McGiff, J C -- HL34300/HL/NHLBI NIH HHS/ -- R01 DK33612/DK/NIDDK NIH HHS/ -- R01 HL25394/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Feb 15;251(4995):799-802.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, New York Medical College, Valhalla 10595.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1846705" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arachidonic Acid ; Arachidonic Acids/*metabolism/physiology ; Biological Transport/physiology ; Carrier Proteins/metabolism ; Cytochrome P-450 Enzyme System/*metabolism ; Furosemide/pharmacology ; In Vitro Techniques ; Loop of Henle/drug effects/*metabolism ; Ouabain/pharmacology ; Potassium/*metabolism ; Rabbits ; Rubidium Radioisotopes ; Sodium/*metabolism ; Sodium-Potassium-Chloride Symporters ; Sodium-Potassium-Exchanging ATPase/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 2007-11-24
    Description: Inositol pyrophosphates are recognized components of cellular processes that regulate vesicle trafficking, telomere length, and apoptosis. We observed that pancreatic beta cells maintain high basal concentrations of the pyrophosphate diphosphoinositol pentakisphosphate (InsP7 or IP7). Inositol hexakisphosphate kinases (IP6Ks) that can generate IP7 were overexpressed. This overexpression stimulated exocytosis of insulin-containing granules from the readily releasable pool. Exogenously applied IP7 dose-dependently enhanced exocytosis at physiological concentrations. We determined that IP6K1 and IP6K2 were present in beta cells. RNA silencing of IP6K1, but not IP6K2, inhibited exocytosis, which suggests that IP6K1 is the critical endogenous kinase. Maintenance of high concentrations of IP7 in the pancreatic beta cell may enhance the immediate exocytotic capacity and consequently allow rapid adjustment of insulin secretion in response to increased demand.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Illies, Christopher -- Gromada, Jesper -- Fiume, Roberta -- Leibiger, Barbara -- Yu, Jia -- Juhl, Kirstine -- Yang, Shao-Nian -- Barma, Deb K -- Falck, John R -- Saiardi, Adolfo -- Barker, Christopher J -- Berggren, Per-Olof -- GM31278/GM/NIGMS NIH HHS/ -- MC_U122680443/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2007 Nov 23;318(5854):1299-302.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rolf Luft Research Center for Diabetes and Endocrinology, Karolinska Institutet, SE-171 76, Stockholm, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18033884" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cricetinae ; Electric Capacitance ; *Exocytosis ; Inositol Phosphates/*metabolism ; Insulin/*secretion ; Insulin-Secreting Cells/*metabolism/secretion ; Islets of Langerhans/metabolism ; Mice ; Patch-Clamp Techniques ; Phosphotransferases (Phosphate Group Acceptor)/genetics/metabolism ; Phytic Acid/metabolism ; RNA Interference ; Rats ; Secretory Vesicles/*metabolism ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 2008-08-23
    Description: Many bacterial pathogens rely on a conserved membrane histidine sensor kinase, QseC, to respond to host adrenergic signaling molecules and bacterial signals in order to promote the expression of virulence factors. Using a high-throughput screen, we identified a small molecule, LED209, that inhibits the binding of signals to QseC, preventing its autophosphorylation and consequently inhibiting QseC-mediated activation of virulence gene expression. LED209 is not toxic and does not inhibit pathogen growth; however, this compound markedly inhibits the virulence of several pathogens in vitro and in vivo in animals. Inhibition of signaling offers a strategy for the development of broad-spectrum antimicrobial drugs.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2605406/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2605406/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rasko, David A -- Moreira, Cristiano G -- Li, De Run -- Reading, Nicola C -- Ritchie, Jennifer M -- Waldor, Matthew K -- Williams, Noelle -- Taussig, Ron -- Wei, Shuguang -- Roth, Michael -- Hughes, David T -- Huntley, Jason F -- Fina, Maggy W -- Falck, John R -- Sperandio, Vanessa -- P01 AI055637/AI/NIAID NIH HHS/ -- P01 AI055637-010005/AI/NIAID NIH HHS/ -- P01-AI055637-03/AI/NIAID NIH HHS/ -- R01 AI053067/AI/NIAID NIH HHS/ -- R01 AI053067-06/AI/NIAID NIH HHS/ -- R01 GM31278/GM/NIGMS NIH HHS/ -- R03 NS053582/NS/NINDS NIH HHS/ -- R03 NS053582-01/NS/NINDS NIH HHS/ -- R21 AI067827/AI/NIAID NIH HHS/ -- U01 AI077853/AI/NIAID NIH HHS/ -- U01 AI077853-01/AI/NIAID NIH HHS/ -- UO1-AI77853/AI/NIAID NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2008 Aug 22;321(5892):1078-80. doi: 10.1126/science.1160354.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Texas (UT) Southwestern Medical Center, Dallas, TX 75390, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18719281" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anti-Bacterial Agents/administration & dosage/*pharmacology/therapeutic use ; Enterohemorrhagic Escherichia coli/drug ; effects/genetics/metabolism/*pathogenicity ; Escherichia coli Infections/drug therapy ; Escherichia coli Proteins/antagonists & inhibitors/genetics/*metabolism ; Francisella tularensis/drug effects/genetics/metabolism/*pathogenicity ; Gene Expression Regulation, Bacterial/drug effects ; Gram-Negative Bacterial Infections/*drug therapy ; Mice ; Norepinephrine/metabolism ; Phosphorylation ; Protein Kinases/genetics/*metabolism ; Rabbits ; Salmonella Infections, Animal/drug therapy ; Salmonella typhimurium/drug effects/genetics/metabolism/*pathogenicity ; Signal Transduction/drug effects ; Small Molecule Libraries ; Sulfonamides/administration & dosage/chemistry/*pharmacology/therapeutic use ; Tularemia/drug therapy ; Virulence Factors/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 2014-01-05
    Description: Despite the prevalence of the N-H aziridine motif in bioactive natural products and the clear advantages of this unprotected parent structure over N-protected derivatives as a synthetic building block, no practical methods have emerged for direct synthesis of this compound class from unfunctionalized olefins. Here, we present a mild, versatile method for the direct stereospecific conversion of structurally diverse mono-, di-, tri-, and tetrasubstituted olefins to N-H aziridines using O-(2,4-dinitrophenyl)hydroxylamine (DPH) via homogeneous rhodium catalysis with no external oxidants. This method is operationally simple (i.e., one-pot), scalable, and fast at ambient temperature, furnishing N-H aziridines in good-to-excellent yields. Likewise, N-alkyl aziridines are prepared from N-alkylated DPH derivatives. Quantum-mechanical calculations suggest a plausible Rh-nitrene pathway.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4175444/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4175444/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jat, Jawahar L -- Paudyal, Mahesh P -- Gao, Hongyin -- Xu, Qing-Long -- Yousufuddin, Muhammed -- Devarajan, Deepa -- Ess, Daniel H -- Kurti, Laszlo -- Falck, John R -- DK38226/DK/NIDDK NIH HHS/ -- GM31278/GM/NIGMS NIH HHS/ -- P01 DK038226/DK/NIDDK NIH HHS/ -- R01 GM031278/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2014 Jan 3;343(6166):61-5. doi: 10.1126/science.1245727.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry, Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24385626" target="_blank"〉PubMed〈/a〉
    Keywords: Alkenes/*chemistry ; Aziridines/*chemical synthesis ; Biological Products/*chemistry ; Catalysis ; Hydrogen/chemistry ; Hydroxylamines/*chemistry ; Nitrogen/chemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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