| P50 | author | Albert Jeltsch | Q30003285 |
| P2093 | author name string | M Fatemi | |
| | M Roth | |
| | F Christ | |
| P2860 | cites work | 2-Aminopurine as a fluorescent probe for DNA base flipping by methyltransferases | Q24546328 |
| | Three-dimensional structure of the adenine-specific DNA methyltransferase M.Taq I in complex with the cofactor S-adenosylmethionine | Q24562671 |
| | The DNA (cytosine-5) methyltransferases | Q24614934 |
| | The crystal structure of Haelll methyltransferase covalently complexed to DNA: An extrahelical cytosine and rearranged base pairing | Q27729758 |
| | HhaI methyltransferase flips its target base out of the DNA helix | Q27731553 |
| | Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine | Q27731970 |
| | Structure of pvu II DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment | Q27739964 |
| | Crystal structure of the DpnM DNA adenine methyltransferase from the DpnII restriction system of streptococcus pneumoniae bound to S-adenosylmethionine | Q27766381 |
| | Targeted mutation of the DNA methyltransferase gene results in embryonic lethality | Q28131773 |
| | DNA modification by methyltransferases | Q34312461 |
| | HhaI and HpaII DNA methyltransferases bind DNA mismatches, methylate uracil and block DNA repair | Q34746885 |
| | Altered DNA methylation and genome instability: a new pathway to cancer? | Q36003169 |
| | Sequence-Specific Binding of DNA by the EcoRV Restriction and Modification Enzymes with Nucleic Acid and Cofactor Analogs | Q38292360 |
| | Investigation of ionizable residues critical for sequence-specific enzymatic DNA modification: protein modification and steady-state and pre-steady-state kinetic pH analyses of EcoRI DNA methyltransferase | Q38307218 |
| | Mutational analysis of target base flipping by the EcoRV adenine-N6 DNA methyltransferase | Q38329103 |
| | Kinetics of methylation and binding of DNA by the EcoRV adenine-N6 methyltransferase | Q38339339 |
| | The Flavobacterium okeanokoites adenine-N6-specific DNA-methyltransferase M.FokI is a tandem enzyme of two independent domains with very different kinetic properties. | Q38339626 |
| | Direct real time observation of base flipping by the EcoRI DNA methyltransferase | Q38340696 |
| | DNA distortion and base flipping by the EcoRV DNA methyltransferase. A study using interference at dA and T bases and modified deoxynucleosides | Q38349483 |
| | Chemical display of thymine residues flipped out by DNA methyltransferases | Q39724595 |
| | Gametic imprinting in mammals | Q40383353 |
| | M.HhaI binds tightly to substrates containing mismatches at the target base | Q40393755 |
| | Alterations in DNA methylation may play a variety of roles in carcinogenesis | Q40410595 |
| | Structure and Function of DNA Methyltransferases | Q40475987 |
| | The cloning, purification and characterization of the Eco RV modification methylase | Q40545675 |
| | X-chromosome inactivation: molecular mechanisms and genetic consequences | Q40706784 |
| | DNA methylation and genomic imprinting | Q40754526 |
| | Effects of DNA methylation on DNA-binding proteins and gene expression. | Q40912883 |
| | The role of DNA methylation in cancer genetic and epigenetics | Q41291310 |
| | Strand-specific mismatch repair in mammalian cells | Q41602506 |
| | Targeted base stacking disruption by the EcoRI DNA methyltransferase | Q46567946 |
| | Functional roles of conserved amino acid residues in DNA methyltransferases investigated by site-directed mutagenesis of the EcoRV adenine-N6-methyltransferase | Q47892200 |
| | Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes | Q48069333 |
| | Nucleotide sequence of the FokI restriction-modification system: separate strand-specificity domains in the methyltransferase | Q48289621 |
| | New restriction endonucleases from Flavobacterium okeanokoites (FokI) and Micrococcus luteus (MluI). | Q48407304 |
| | Universal catalytic domain structure of AdoMet-dependent methyltransferases. | Q53012595 |
| | Amino acid sequence arrangements of DNA-methyltransferases | Q53753431 |
| | A model for DNA binding and enzyme action derived from crystallographic studies of the TaqI N6-adenine-methyltransferase | Q57663036 |
| P433 | issue | 28 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 19538-19544 | |
| P577 | publication date | 1999-07-01 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | On the substrate specificity of DNA methyltransferases. adenine-N6 DNA methyltransferases also modify cytosine residues at position N4 | |
| P478 | volume | 274 | |