Blar i forfatter Artikler, rapporter og annet (kjemi) "Alexeeva, Marina"

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    • The escherichia coli alkA gene is activated to alleviate mutagenesis by an oxidized deoxynucleoside 

      Grøsvik, Kristin; Tesfahun, Almaz Nigatu; Muruzábal-Lecumberri, Izaskun; Haugland, Gyri Teien; Leiros, Ingar; Ruoff, Peter; Kvaløy, Jan Terje; Knævelsrud, Ingeborg; Ånensen, Hilde; Alexeeva, Marina; Sato, Kousuke; Matsuda, Akira; Alseth, Ingrun; Klungland, Arne; Bjelland, Svein (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-02-25)
      The cellular methyl donor S-adenosylmethionine (SAM) and other endo/exogenous agents methylate DNA bases non-enzymatically into products interfering with replication and transcription. An important product is 3-methyladenine (m<sup>3</sup>A), which in <i>Escherichia coli</i> is removed by m<sup>3</sup>A-DNA glycosylase I (Tag) and II (AlkA). The <i>tag</i> gene is constitutively expressed, while ...

    • Intrinsic Strand-Incision Activity of Human UNG: Implications for Nick Generation in Immunoglobulin Gene Diversification 

      Alexeeva, Marina; Moen, Marivi Nabong; Xu, Xiang Ming; Rasmussen, Anette; Leiros, Ingar; Kirpekar, Finn; Klungland, Arne; Alsøe, Lene; Nilsen, Hilde; Bjelland, Svein (Journal article; Tidsskriftartikkel; Peer reviewed, 2021-12-22)
      Uracil arises in cellular DNA by cytosine (C) deamination and erroneous replicative incorporation of deoxyuridine monophosphate opposite adenine. The former generates C ! thymine transition mutations if uracil is not removed by uracil-DNA glycosylase (UDG) and replaced by C by the base excision repair (BER) pathway. The primary human UDG is hUNG. During immunoglobulin gene diversification in ...

    • The structure of a dual-specificity tyrosine phosphorylation-regulated kinase 1A-PKC412 complex reveals disulfide-bridge formation with the anomalous catalytic loop HRD(HCD) cysteine 

      Alexeeva, Marina; Åberg, espen; Engh, Richard Alan; Rothweiler, Ulli (Journal article; Tidsskriftartikkel; Peer reviewed, 2015)
      Dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A) is a protein kinase associated with neuronal development and brain physiology. The DYRK kinases are very unusual with respect to the sequence of the catalytic loop, in which the otherwise highly conserved arginine of the HRD motif is replaced by a cysteine. This replacement, along with the proximity of a potential disulfide-bridge ...