Intact MutY and its catalytic domain differentially contact with A/8-oxoG-containing DNA.
about
MUTYH DNA glycosylase: the rationale for removing undamaged bases from the DNAThe C-terminal domain of Escherichia coli MutY is involved in DNA binding and glycosylase activities.Physical and functional interactions between Escherichia coli MutY and endonuclease VIIIFunctional interaction of MutY homolog with proliferating cell nuclear antigen in fission yeast, Schizosaccharomyces pombe.Flipping duplex DNA inside out: a double base-flipping reaction mechanism by Escherichia coli MutY adenine glycosylase.
P2860
Intact MutY and its catalytic domain differentially contact with A/8-oxoG-containing DNA.
description
2000 nî lūn-bûn
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2000 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի դեկտեմբերին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
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2000年論文
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2000年论文
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name
Intact MutY and its catalytic domain differentially contact with A/8-oxoG-containing DNA.
@ast
Intact MutY and its catalytic domain differentially contact with A/8-oxoG-containing DNA.
@en
type
label
Intact MutY and its catalytic domain differentially contact with A/8-oxoG-containing DNA.
@ast
Intact MutY and its catalytic domain differentially contact with A/8-oxoG-containing DNA.
@en
prefLabel
Intact MutY and its catalytic domain differentially contact with A/8-oxoG-containing DNA.
@ast
Intact MutY and its catalytic domain differentially contact with A/8-oxoG-containing DNA.
@en
P2860
P356
P1476
Intact MutY and its catalytic domain differentially contact with A/8-oxoG-containing DNA.
@en
P2860
P304
P356
10.1093/NAR/28.23.4593
P407
P577
2000-12-01T00:00:00Z