Related references
Note: Only part of the references are listed.Tissue type is a major modifier of the 5-hydroxymethylcytosine content of human genes
Colm E. Nestor et al.
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Retroviral restriction by APOBEC proteins
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Gene-targeted mice lacking the Ung uracil-DNA glycosylase develop B-cell lymphomas
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Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1
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Mammalian 5-Formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA glycosylase in repair of 5-formyluracil and other oxidized and deaminated base lesions
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I Elateri et al.
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Mbd4 inactivation increases C→T transition mutations and promotes gastrointestinal tumor formation
E Wong et al.
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HUNG2 is the major repair enzyme for removal of uracil from U:A matches, U:G mismatches, and U in single-stranded DNA, with hSMUG1 as a broad specificity backup
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Immunoglobulin isotype switching is inhibited and somatic hypermutation perturbed in UNG-deficient mice
C Rada et al.
CURRENT BIOLOGY (2002)
Substrate recognition by a family of uracil-DNA glycosylases: UNG, MUG, and TDG
PF Liu et al.
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Enhanced CpG mutability and tumorigenesis in MBD4-deficient mice
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Characterization of the substrate specificity of a human 5-hydroxymethyluracil glycosylase activity
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Definitive identification of mammalian 5-hydroxymethyluracil DNA N-glycosylase activity as SMUG1
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JOURNAL OF BIOLOGICAL CHEMISTRY (2001)
Excision of deaminated cytosine from the vertebrate genome: role of the SMUG1 uracil-DNA glycosylase
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An unexpectedly high excision capacity for mispaired 5-hydroxymethyluracil in human cell extracts
V Rusmintratip et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2000)
5-methylcytosine DNA glycosylase activity is also present in the human MBD4 (G/T mismatch glycosylase) and in a related avian sequence
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Uracil-DNA glycosylase (UNG)-deficient mice reveal a primary role of the enzyme during DNA replication
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5-methylcytosine-DNA glycosylase activity is present in a cloned G/T mismatch DNA glycosylase associated with the chicken embryo DNA demethylation complex
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