(Q28206086)

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Effects of hydrogen bonding within a damaged base pair on the activity of wild type and DNA-intercalating mutants of human alkyladenine DNA glycosylase

scientific article (publication date: 30 August 2002)

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scholarly article

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Effects of hydrogen bonding within a damaged base pair on the activity of wild type and DNA-intercalating mutants of human alkyladenine DNA glycosylase (English)

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author name string

Aarthy C Vallur

1

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Joyce A Feller

2

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Clint W Abner

3

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Robert K Tran

4

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Linda B Bloom

5

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language of work or name

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publication date

30 August 2002

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Journal of Biological Chemistry

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277

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35

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31673-8

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Initiation of base excision repair: glycosylase mechanisms and structures

1 reference

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Structural studies of human alkyladenine glycosylase and E. coli 3-methyladenine glycosylase

1 reference

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The base excision repair pathway

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Base excision repair in yeast and mammals

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Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision

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Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG

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Kinetic mechanism of damage site recognition and uracil flipping by Escherichia coli uracil DNA glycosylase

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

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

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Cloning and characterization of a 3-methyladenine DNA glycosylase cDNA from human cells whose gene maps to chromosome 16

1 reference

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Purification and characterization of human 3-methyladenine-DNA glycosylase

1 reference

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Distinct substrate preference of human and mouse N-methylpurine-DNA glycosylases.

1 reference

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1,N6-ethenoadenine is preferred over 3-methyladenine as substrate by a cloned human N-methylpurine-DNA glycosylase (3-methyladenine-DNA glycosylase)

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Escherichia coli, Saccharomyces cerevisiae, rat and human 3-methyladenine DNA glycosylases repair 1,N6-ethenoadenine when present in DNA

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Substrate specificity of human methylpurine DNA N-glycosylase

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Excision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat, and human alkylpurine DNA glycosylases

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Interaction of the recombinant human methylpurine-DNA glycosylase (MPG protein) with oligodeoxyribonucleotides containing either hypoxanthine or abasic sites

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Influence of DNA structure on hypoxanthine and 1,N(6)-ethenoadenine removal by murine 3-methyladenine DNA glycosylase.

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Base excision and DNA binding activities of human alkyladenine DNA glycosylase are sensitive to the base paired with a lesion

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Solution structure of a DNA duplex containing a replicable difluorotoluene-adenine pair

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Hydrogen bonding, base stacking, and steric effects in dna replication

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Fluorescent modification of adenosine-containing coenzymes. Biological activities and spectroscopic properties.

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LAT expression during an acute HSV infection in the mouse

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Specific interaction of wild-type and truncated mouse N-methylpurine-DNA glycosylase with ethenoadenine-containing DNA.

1 reference

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The role of leucine 191 of Escherichia coli uracil DNA glycosylase in the formation of a highly stable complex with the substrate mimic, ugi, and in uracil excision from the synthetic substrates

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Turning On uracil-DNA glycosylase using a pyrene nucleotide switch

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Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA.

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DNA repair mechanisms for the recognition and removal of damaged DNA bases.

1 reference

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Refined crystal structure of an octanucleotide duplex with I.T. mismatched base pairs

1 reference

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Crystal structure of a B-DNA dodecamer containing inosine, d(CGCIAATTCGCG), at 2.4 A resolution and its comparison with other B-DNA dodecamers

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Base pairing involving deoxyinosine: implications for probe design

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Role of electrophilic and general base catalysis in the mechanism of Escherichia coli uracil DNA glycosylase.

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21 January 2018

Identifiers

10.1074/JBC.M204475200

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