Determination of the order of substrate addition to MspI DNA methyltransferase using a novel mechanism-based inhibitor.
about
Zebularine: A Novel DNA Methylation Inhibitor that Forms a Covalent Complex with DNA MethyltransferasesMechanistic insights on the inhibition of c5 DNA methyltransferases by zebularine.The fission yeast gene pmt1+ encodes a DNA methyltransferase homologueNucleoprotein-based nanoscale assemblyDNA binding and methyl transfer catalysed by mouse DNA methyltransferase.Characterisation of site-biased DNA methyltransferases: specificity, affinity and subsite relationships.The small subunit of M. AquI is responsible for sequence-specific DNA recognition and binding in the absence of the catalytic domain.Genomic structure of the human DNA methyltransferase gene.Enzyme-mediated cytosine deamination by the bacterial methyltransferase M.MspI.Potent inhibition of HhaI DNA methylase by the aglycon of 2-(1H)-pyrimidinone riboside (zebularine) at the GCGC recognition domain.2-Pyrimidinone as a probe for studying the EcoRII DNA methyltransferase-substrate interaction.
P2860
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P2860
Determination of the order of substrate addition to MspI DNA methyltransferase using a novel mechanism-based inhibitor.
description
1993 nî lūn-bûn
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1993年の論文
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1993年学术文章
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name
Determination of the order of ...... vel mechanism-based inhibitor.
@en
type
label
Determination of the order of ...... vel mechanism-based inhibitor.
@en
prefLabel
Determination of the order of ...... vel mechanism-based inhibitor.
@en
P2093
P2860
P356
P1433
P1476
Determination of the order of ...... vel mechanism-based inhibitor.
@en
P2093
P2860
P304
P356
10.1042/BJ2910493
P407
P478
291 ( Pt 2)
P577
1993-04-01T00:00:00Z