Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1 (Q27641492)

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Timothy R Waters

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Karl Haushalter

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Gregory L Verdine

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Laurence H Pearl

The main role of human thymine-DNA glycosylase is removal of thymine produced by deamination of 5-methylcytosine and not removal of ethenocytosine

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language of work or name

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June 2003

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published in

Molecular Cell

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volume

11

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issue

6

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page(s)

1647-59

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cites work

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Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions

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Crystal structure of a thwarted mismatch glycosylase DNA repair complex

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Phylogenetic evidence of a role for 5-hydroxymethyluracil-DNA glycosylase in the maintenance of 5-methylcytosine in DNA.

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Definitive identification of mammalian 5-hydroxymethyluracil DNA N-glycosylase activity as SMUG1

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Altering the pathway of immunoglobulin hypermutation by inhibiting uracil-DNA glycosylase.

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Uracil-DNA glycosylase acts by substrate autocatalysis

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Structural basis for uracil recognition by archaeal family B DNA polymerases

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A read-ahead function in archaeal DNA polymerases detects promutagenic template-strand uracil.

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1,N6-ethenoadenine and 3,N4-ethenocytosine are excised by separate human DNA glycosylases

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Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors

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An iron-sulfur cluster in the family 4 uracil-DNA glycosylases

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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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DNA glycosylases in the base excision repair of DNA

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An N -Glycosidase from Escherichia coli That Releases Free Uracil from DNA Containing Deaminated Cytosine Residues

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The role of the Escherichia coli mug protein in the removal of uracil and 3,N(4)-ethenocytosine from DNA.

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Crystal structure of human uracil-DNA glycosylase in complex with a protein inhibitor: protein mimicry of DNA

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Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis

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Efficient removal of uracil from G.U mispairs by the mismatch-specific thymine DNA glycosylase from HeLa cells

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Uracil-DNA glycosylase (UNG)-deficient mice reveal a primary role of the enzyme during DNA replication

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Excision of deaminated cytosine from the vertebrate genome: role of the SMUG1 uracil-DNA glycosylase

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3,N4-ethenocytosine, a highly mutagenic adduct, is a primary substrate for Escherichia coli double-stranded uracil-DNA glycosylase and human mismatch-specific thymine-DNA glycosylase

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A novel uracil-DNA glycosylase with broad substrate specificity and an unusual active site

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7 January 2021

The structural basis of specific base-excision repair by uracil-DNA glycosylase

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7 January 2021

Kinetic analysis of the coding properties of O6-methylguanine in DNA: the crucial role of the conformation of the phosphodiester bond

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7 January 2021

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Human thymine DNA glycosylase binds to apurinic sites in DNA but is displaced by human apurinic endonuclease 1.

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7 January 2021