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Articles by Wolfgang Voelter
Total Records ( 4 ) for Wolfgang Voelter
  Khalid Mohammed Khan , Sumbul Ahmed , Zulfiqar Ali Khan , Mubeen Rani , Shahnaz Perveen and Wolfgang Voelter
  A microwave-assisted, environmentally friendly, high-yielding, time-saving synthesis of medicinally important 3-substituted isocoumarins was carried out in a single step by direct condensation of homophthalic acid with aryol and acyl chlorides under solvent-free conditions without any solid support. The synthesised isocoumarins were structurally characterised by microanalysis, 1H NMR, EI, IR and UV.
  Khalid Mohammed Khan , Shahnaz Perveen , Safdar Hayat , Muhammad Ali , Wolfgang Voelter and Zia- Ullah
  In situ generation of hydrogen iodide from cesium iodide/methanesulfonic acid was found to be an attractive reagent combination for the conversion of alkyl, allyl, and benzyl alcohols to their corresponding iodides under mild conditions. The method is compared with that using cesium iodide/p-toluenesulfonic acid or cesium iodide/aluminium chloride.
  Khalid M. Khan , Nosheen A. Rao , Zia-Ullah , Muhammad Ali , Shahnaz Perveen , Muhammad Iqbal Choudhary , Atta-Ur-Rahman and Wolfgang Voelter
  Acridines are well-known group of compounds with a wide variety of biological properties. We describe herein an expeditious approach to prepare anilinoacridine derivatives from mefenamic acid. It is the first report of a one-pot approach to anilinoacridines in good to excellent yields.
  Rizwana Sanaullah Waraich , Cora Weigert , Hubert Kalbacher , Anita M. Hennige , Stefan Z. Lutz , Hans-Ulrich Haring , Erwin D. Schleicher , Wolfgang Voelter and Rainer Lehmann
  The activation of the protein kinase C (PKC) family of serine/threonine kinases contributes to the modulation of insulin signaling, and the PKC-dependent phosphorylation of insulin receptor substrate (IRS)-1 has been implicated in the development of insulin resistance. Here we demonstrate Ser357 of rat IRS-1 as a novel PKC-δ-dependent phosphorylation site in skeletal muscle cells upon stimulation with insulin and phorbol ester using Ser(P)357 antibodies and active and kinase dead mutants of PKC-δ. Phosphorylation of this site was simulated using IRS-1 Glu357 and shown to reduce insulin-induced tyrosine phosphorylation of IRS-1, to decrease activation of Akt, and to subsequently diminish phosphorylation of glycogen synthase kinase-3. When the phosphorylation was prevented by mutation of Ser357 to alanine, these effects of insulin were enhanced. When the adjacent Ser358, present in mouse and rat IRS-1, was mutated to alanine, which is homologous to the human sequence, the insulin-induced phosphorylation of glycogen synthase kinase-3 or tyrosine phosphorylation of IRS-1 was not increased. Moreover, both active PKC-δ and phosphorylation of Ser357 were shown to be necessary for the attenuation of insulin-stimulated Akt phosphorylation. The phosphorylation of Ser357 could lead to increased association of PKC-δ to IRS-1 upon insulin stimulation, which was demonstrated with IRS-1 Glu357. Together, these data suggest that phosphorylation of Ser357 mediates at least in part the adverse effects of PKC-δ activation on insulin action.
 
 
 
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