about
Three-dimensional structure of the adenine-specific DNA methyltransferase M.Taq I in complex with the cofactor S-adenosylmethionineThe DNA (cytosine-5) methyltransferasesCircular permutation of DNA cytosine-N4 methyltransferases: in vivo coexistence in the BcnI system and in vitro probing by hybrid formationExpression of ZmMET1, a gene encoding a DNA methyltransferase from maize, is associated not only with DNA replication in actively proliferating cells, but also with altered DNA methylation status in cold-stressed quiescent cellsDsaV methyltransferase and its isoschizomers contain a conserved segment that is similar to the segment in Hhai methyltransferase that is in contact with DNA bases.The M.AluI DNA-(cytosine C5)-methyltransferase has an unusually large, partially dispensable, variable region.Functional studies of the small subunit of EcoHK31I DNA methyltransferase.Biotin-avidin microplate assay for the quantitative analysis of enzymatic methylation of DNA by DNA methyltransferases.Isolation and identification by sequence homology of a putative cytosine methyltransferase from Arabidopsis thalianaChanging the target base specificity of the EcoRV DNA methyltransferase by rational de novo protein-design.Molecular characterization of the Lactococcus lactis LlaKR2I restriction-modification system and effect of an IS982 element positioned between the restriction and modification genes.Mutational analysis of conserved residues in HhaI DNA methyltransferaseThe small subunit of M. AquI is responsible for sequence-specific DNA recognition and binding in the absence of the catalytic domain.Changing the recognition specificity of a DNA-methyltransferase by in vitro evolution.Transposon-mediated linker insertion scanning mutagenesis of the Escherichia coli McrA endonuclease.A bacterial methyltransferase M.EcoHK311 requires two proteins for in vitro methylation.Functional analysis of Gln-237 mutants of HhaI methyltransferase.The DNA binding affinity of HhaI methylase is increased by a single amino acid substitution in the catalytic center.Chemistry and biology of DNA methyltransferases.Overproduction, purification and characterization of M.EcoHK31I, a bacterial methyltransferase with two polypeptides.M.(phi)BssHII, a novel cytosine-C5-DNA-methyltransferase with target-recognizing domains at separated locations of the enzyme.Sequence comparison of the EcoHK31I and EaeI restriction-modification systems suggests an intergenic transfer of genetic material.Enzyme-mediated cytosine deamination by the bacterial methyltransferase M.MspI.The N-terminus of m5C-DNA methyltransferase MspI is involved in its topoisomerase activity.Genome-wide analysis of restriction-modification system in unicellular and filamentous cyanobacteria.Mammalian DNA cytosine-5 methyltransferase interacts with p23 protein.
P2860
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P2860
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
How M.MspI and M.HpaII decide which base to methylate.
@en
type
label
How M.MspI and M.HpaII decide which base to methylate.
@en
prefLabel
How M.MspI and M.HpaII decide which base to methylate.
@en
P2860
P356
P1476
How M.MspI and M.HpaII decide which base to methylate.
@en
P2860
P304
P356
10.1093/NAR/20.18.4811
P577
1992-09-01T00:00:00Z