MBD4-mediated glycosylase activity on a chromatin template is enhanced by acetylation.
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Uracil DNA glycosylase activity on nucleosomal DNA depends on rotational orientation of targetsSolution structure and intramolecular exchange of methyl-cytosine binding domain protein 4 (MBD4) on DNA suggests a mechanism to scan for mCpG/TpG mismatches.Activity of FEN1 endonuclease on nucleosome substrates is dependent upon DNA sequence but not flap orientationMechanisms of base substitution mutagenesis in cancer genomes.Base excision repair in chromatin: Insights from reconstituted systems.
P2860
MBD4-mediated glycosylase activity on a chromatin template is enhanced by acetylation.
description
2008 nî lūn-bûn
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2008年の論文
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2008年論文
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2008年論文
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2008年論文
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2008年論文
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2008年論文
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2008年论文
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2008年论文
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name
MBD4-mediated glycosylase activity on a chromatin template is enhanced by acetylation.
@en
type
label
MBD4-mediated glycosylase activity on a chromatin template is enhanced by acetylation.
@en
prefLabel
MBD4-mediated glycosylase activity on a chromatin template is enhanced by acetylation.
@en
P2093
P2860
P356
P1476
MBD4-mediated glycosylase activity on a chromatin template is enhanced by acetylation
@en
P2093
Claire G Cupples
Juan Ausió
P2860
P304
P356
10.1128/MCB.00588-08
P407
P577
2008-06-02T00:00:00Z