Literature DB >> 14510466

Identification and characterization of mammalian 5-formyluracil-DNA glycosylase.

Mayumi Matsubara1, Aya Masaoka, Tamon Tanaka, Hiroaki Terato, Yoshihiko Ohyama, Hiroshi Ide.   

Abstract

5-Formyluracil is a major oxidative thymine lesion with mutagenic and cytotoxic properties. In this study, we have partially purified and characterized a mammalian 5-formyluracil-DNA glycosylase (FDG) from rat liver. FDG was a monofunctional DNA glycosylase and removed 5-formyluracil, uracil, 5-hydroxyuracil, 5-hydroxylmethyluracil in single-stranded and double-stranded DNA. Several lines of evidence indicate that FDG is a rat SMUG1 homologue. Human SMUG1 also exhibited similar enzymatic properties.

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Year:  2003        PMID: 14510466     DOI: 10.1093/nass/3.1.233

Source DB:  PubMed          Journal:  Nucleic Acids Res Suppl


  3 in total

Review 1.  Variant base excision repair proteins: contributors to genomic instability.

Authors:  Antonia A Nemec; Susan S Wallace; Joann B Sweasy
Journal:  Semin Cancer Biol       Date:  2010-10-16       Impact factor: 15.707

Review 2.  The current state of eukaryotic DNA base damage and repair.

Authors:  Nicholas C Bauer; Anita H Corbett; Paul W Doetsch
Journal:  Nucleic Acids Res       Date:  2015-10-30       Impact factor: 16.971

3.  Ablation of SMUG1 Reduces Cell Viability and Increases UVC-Mediated Apoptosis in Hepatocarcinoma HepG2 Cells.

Authors:  Mi-Jin An; Geun-Seup Shin; Hyun-Min Lee; Jung-Woong Kim
Journal:  Genes (Basel)       Date:  2021-01-30       Impact factor: 4.096

  3 in total

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