F
Finn Kirpekar
Researcher at University of Southern Denmark
Publications - 79
Citations - 5135
Finn Kirpekar is an academic researcher from University of Southern Denmark. The author has contributed to research in topics: RNA & Mass spectrometry. The author has an hindex of 35, co-authored 79 publications receiving 4674 citations. Previous affiliations of Finn Kirpekar include University of Copenhagen & Norwegian University of Science and Technology.
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Journal ArticleDOI
Methylation of tRNAAsp by the DNA Methyltransferase Homolog Dnmt2
Mary G. Goll,Finn Kirpekar,Keith A. Maggert,Jeffrey A. Yoder,Chih-Lin Hsieh,Xiaoyu Zhang,Kent G. Golic,Steven E. Jacobsen,Timothy H. Bestor +8 more
TL;DR: The sequence and the structure of DNA methyltransferase-2 (DnMT2) bear close affinities to authentic DNA cytosine methyltransferases, and human DNMT2 protein restored methylation in vitro to tRNAAsp from Dnmt2-deficient strains of mouse, Arabidopsis thaliana, and Drosophila melanogaster in a manner that was dependent on preexisting patterns of modified nucleosides.
Journal ArticleDOI
Mass spectrometry of nucleic acids.
TL;DR: A survey of ESI and MALDI mass spectrometric analysis of nucleic acid oligomers and polymers, dealing with the practical aspects of the two ionization techniques, fragmentation, and applications, respectively.
Journal ArticleDOI
Infrared MALDI Mass Spectrometry of Large Nucleic Acids
TL;DR: Matrix-assisted laser desorption/ionization (MALDI) mass spectra of synthetic DNA, restriction enzyme fragments of plasmid DNA, and RNA transcripts up to a size of 2180 nucleotides are reported, which surpass all currently available techniques for the analysis of large nucleic acids.
Journal ArticleDOI
Ion stability of nucleic acids in infrared matrix-assisted laser desorption/ionization mass spectrometry.
Eckhard Nordhoff,Rainer Cramer,Michael Karas,Franz Hillenkamp,Finn Kirpekar,Karsten Kristiansen,Peter Roepstorff +6 more
TL;DR: Experiments indicate that the breakage of the N-glycosidic bond probably occurs during the desorption process due to proton transfer from the phosphodiester groups to the ionizable bases.
Journal ArticleDOI
Mammalian ALKBH8 Possesses tRNA Methyltransferase Activity Required for the Biogenesis of Multiple Wobble Uridine Modifications Implicated in Translational Decoding
Lene Songe-Møller,Erwin van den Born,Vibeke Leihne,Cathrine Broberg Vågbø,Terese Kristoffersen,Hans E. Krokan,Finn Kirpekar,Pål Ø. Falnes,Pål Ø. Falnes,Arne Klungland,Arne Klungland +10 more
TL;DR: It is shown here that ALKBh8 is a tRNA methyltransferase required for the final step in the biogenesis of mcm5U, and that the interaction of ALKBH8 with a small accessory protein, TRM112, is required to form a functional tRNAmethyltransferase.