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Article

Unnatural substrates reveal the importance of 8-oxoguanine for in vivo mismatch repair by MutY

18 Nov 2007

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Identifiers

PMID: 18026095
DOI: 10.1038/nchembio.2007.40

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Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Unnatural substrates reveal the importance of 8-oxoguanine for in vivo mismatch repair by MutYPMID 18026095Read ↗

Repair of A/G and A/8-oxoG mismatches by MutY adenine DNA glycosylase.Semantic proximity Read ↗

The Mammalian Mismatch Repair Pathway Removes DNA 8-oxodGMP Incorporated from the Oxidized dNTP PoolSemantic proximity Read ↗

Multiple DNA glycosylases for repair of 8-oxoguanine and their potential in vivo functions.Semantic proximity Read ↗

MUTYH DNA glycosylase: the rationale for removing undamaged bases from the DNASemantic proximity Read ↗

Regulation of oxidative DNA damage repair: the adenine:8-oxo-guanine problem.Semantic proximity Read ↗

New insights into the mechanism of DNA mismatch repairSemantic proximity Read ↗

Catalytic contributions of key residues in the adenine glycosylase MutY revealed by pH-dependent kinetics and cellular repair assays.Semantic proximity Read ↗

Endonucleolytic Function of MutLα in Human Mismatch RepairSemantic proximity Read ↗

Mutagenesis mechanism of the major oxidative adenine lesion 7,8-dihydro-8-oxoadenine.Semantic proximity Read ↗

Structural Basis for Avoidance of Promutagenic DNA Repair by MutY Adenine DNA Glycosylase.Semantic proximity Read ↗

Repair of 8-oxoG:A mismatches by the MUTYH glycosylase: Mechanism, metals and medicine.Semantic proximity Read ↗

Unexpected non-Hoogsteen-based mutagenicity mechanism of FaPy-DNA lesions.Semantic proximity Read ↗

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