Adenine excisional repair function of MYH protein on the adenine:8-hydroxyguanine base pair in double-stranded DNA

Nucleic Acids Research

Volumn 28, Issue 24, 2000, Pages 4912-4918

  Shinmura, Kazuya ^a   Yamaguchi, Satoru ^a   Saitoh, Takayuki ^a   Takeuchi Sasaki, Mariko ^a   Kim, Su Ryang ^b   Nohmi, Takehiko ^b   Yokota, Jun ^a  

^a NATIONAL CANCER CENTER RESEARCH INSTITUTE   (Japan)

^b NATIONAL INSTITUTE OF HEALTH SCIENCES   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

8 HYDROXYGUANINE; ADENINE; BUFFER; CYTOPLASM PROTEIN; DNA; DNA GLYCOSYLTRANSFERASE; DOUBLE STRANDED DNA; GUANINE; HISTIDINE; NUCLEAR PROTEIN; SODIUM CHLORIDE;

ARTICLE; BACTERIUM MUTANT; BASE MISPAIRING; BASE PAIRING; BINDING AFFINITY; CATALYSIS; CHEMICAL REACTION; CONTROLLED STUDY; DNA CLEAVAGE; DNA DAMAGE; ENZYME ACTIVITY; ENZYME MECHANISM; ESCHERICHIA COLI; EXCISION REPAIR; GEL MOBILITY SHIFT ASSAY; GENETIC COMPLEMENTATION; HUMAN; LEPIDOPTERA; MUTAGENESIS; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN POLYMORPHISM;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; LEPIDOPTERA; SPODOPTERA FRUGIPERDA;

EID: 0034671587     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/28.24.4912     Document Type: Article

References (35)

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14. Differential subcellular localization of human MutY homolog (hMYH) and the functional activity of adenine:8-oxoguanine DNA glycosylase
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28. Principles of membrane transport
29. + ions in volume and voltage of epithelial cell nuclei
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32. DNA-dependent activation of the hMutSalpha ATPase
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34. Nuclear localization of the human mutY homologue hMYH
35. Evidence that MutY is a monofunctional glycosylase capable of forming a covalent Schiff base intermediate with substrate DNA