Analysis of uracil-DNA glycosylases from the murine Ung gene reveals differential expression in tissues and in embryonic development and a subcellular sorting pattern that differs from the human homologues

By Nilsen H.   Steinsbekk K.S.   Otterlei M.   Slupphaug G.   Aas P.A.   Krokan H.E.  

Nucleic Acids Research, Vol. 28, Iss. 12, 2000-06 ,pp. : 2277-2285

Oxford University Press

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Regulation of expression of nuclear and mitochondrial forms of human uracil‐DNA glycosylase

By Haug Terje   Skorpen Frank   Aas Per Arne   Malm Veslemøy   Skjelbred Camilla   Krokan Hans E.  

Nucleic Acids Research, Vol. 26, Iss. 6, 1998-03 ,pp. : 1449-1457

Oxford University Press

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Human mitochondrial uracil‐DNA glycosylase preform (UNG1) is processed to two forms one of which is resistant to inhibition by AP sites

By Bharati Sangeeta   Krokan Hans E.   Kristiansen Lena   Otterlei Marit   Slupphaug Geir  

Nucleic Acids Research, Vol. 26, Iss. 21, 1998-11 ,pp. : 4953-4959

Oxford University Press

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The Nature of Enzymes Involved in Uracil-DNA Repair: Isoform Charac-teristics of Proteins Responsible for Nuclear and Mitochondrial Genomic Integrity 1

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Current Protein and Peptide Science, Vol. 2, Iss. 4, 2001-12 ,pp. : 335-347

Bentham Science Publishers

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Nuclear and mitochondrial splice forms of human uracil‐DNA glycosylase contain a complex nuclear localisation signal and a strong classical mitochondrial localisation signal, respectively

By Otterlei Marit  

Nucleic Acids Research, Vol. 26, Iss. 20, 1998-10 ,pp. : 4611-4617

Oxford University Press

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