Recognition of structural perturbations in DNA by human DNA(cytosine-5)methyltransferase
Author:
Publisher
Elsevier BV
Subject
Genetics,General Medicine
Reference13 articles.
1. The influence of the dT·dG mispair on the activity of the human DNA-(cytosine-5) methyltransferase;Baker;Biochem. Biophys. Res. Commun.,1987
2. The irreversible binding of azacytosine-containing DNA fragments to bacterial DNA(cytosine-5)methyltransferase;Friedman;J. Biol. Chem.,1985
3. Circular dichroism measurements show that C·C+ base pairs can coexist with A·T base pairs between antiparallel strands of an oligodeoxy-nucleotide double helix;Gray;Nucleic Acids Res.,1984
4. Bisulfite modification of nucleic acids and their constituents;Hayatsu;Prog. Nucleic Acid Res. Mol. Biol.,1976
5. Structural features and hydration of a dodecamer duplex containing two C·A mispairs;Hunter;Nucleic Acids Res.,1987
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1. Modification-dependent restriction endonuclease, MspJI, flips 5-methylcytosine out of the DNA helix;Nucleic Acids Research;2014-09-27
2. Structure of 5-hydroxymethylcytosine-specific restriction enzyme, AbaSI, in complex with DNA;Nucleic Acids Research;2014-06-03
3. Structure and mutagenesis of the DNA modification-dependent restriction endonuclease AspBHI;Scientific Reports;2014-03-07
4. Mechanism of DNA Methylation: The Double Role of DNA as a Substrate and as a Cofactor;Journal of Molecular Biology;2010-07
5. AdoMet-dependent Methyl-transfer: Glu119 Is Essential for DNA C5-Cytosine Methyltransferase M.HhaI;Journal of Molecular Biology;2007-11
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