Page 25 - CBAC Newsletter 2015
P. 25

The lab is successfully working on several exciting     Urusova DV, Shim JH, Kim DJ, Jung SK, Zykova TA,
        projects and I hope to contribute to the lab projects   Carper A, Bode AM, Dong Z. Epigallocatechin-gal-
        progress with my molecular biology, biochemistry        late suppresses tumorigenesis by directly targeting
        and protein crystallography expertise, and am           Pin1. Cancer Prev Res (Phila). 2011 Sep;4(9):1366-
        currently studying how phosphorylation alters           77. Epub 2011 Jul 12. PMCID: PMC3244823
        intracellular loop conformations.
                                                                Zykova TA, Zhu F, Vakorina TI, Zhang J, Higgins LA,
        It has been established that inherited mutations        Urusova DV, Bode AM, Dong Z. T-LAK cell-origi-
        in the gene encoding the NaV1.5 sodium channel          nated protein kinase (TOPK) phosphorylation of
        including mutations in the intracellular loops, have    Prx1 at Ser-32 prevents UVB-inducedapoptosis in
        been associated with Brugada (BrS) and Long QT          RPMI7951 melanoma cells through the regulation
        syndromes (LQTS). Also, the post-translational          of Prx1 peroxidase activity. J Biol Chem. 2010 Sep
        modifications and particularly the phosphorylation      17;285(38):29138-46. Epub 2010 Jul 20.
        of these loops, may be important in acquired            PMCID: PMC2937944
        arrhythmias. I hope that my biophysical
        characterization of these purified loops will help
        to elucidate the mechanism of these effects.



        Past Work and Future Plans


        Yet, I believe that my most important research
        achievement still lies ahead. Among my past, I
        count the crystal structure of D-Serine Dehydratase
        from E.coli, which I carried out in collaboration with
        University of Wuerzburg, Germany and Daresbury
        Laboratory, UK. I crystallized the protein in two
        different crystal forms that allowed to solve the
        structure of the protein by a non-traditional method
        of multi-crystal averaging.  [see: Darya V. Urusova
        et. al. Crystal structure of D-serine dehydratase
        from Escherichia coli. Biochimica et Biophysica
        Acta (BBA) - Proteins and Proteomics. 2012; 1824:
        422-432.] PMID: 22197591



        Recent Publications


        Urusova DV, Isupov MN, Antonyuk S, Kachalova GS,
        Obmolova G, Vagin AA, Lebedev AA, Burenkov GP,
        Dauter Z, Bartunik HD, Lamzin VS, Melik-Adamyan
        WR, Mueller TD, Schnackerz KD. Crystal structure
        of D-serine dehydratase from Escherichia coli.
        Biochim Biophys Acta. 2012 Mar;1824(3):422-32.
        Epub 2011 Nov 27. PMID: 22197591





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