Recombinant human DNA (cytosine-5) methyltransferase. II. Steady-state kinetics reveal allosteric activation by methylated dna. [electronic resource]
Producer: 20000103Description: 33011-9 p. digitalISSN:- 0021-9258
- Allosteric Regulation
- Binding Sites
- DNA (Cytosine-5-)-Methyltransferase 1
- DNA (Cytosine-5-)-Methyltransferases
- DNA Methylation
- DNA, Superhelical -- chemistry
- DNA-Binding Proteins -- chemistry
- Enzyme Activation
- Enzyme Inhibitors -- pharmacology
- Humans
- Kinetics
- Oligodeoxyribonucleotides -- chemistry
- Recombinant Proteins -- chemistry
- Ribonucleoproteins, Small Nuclear -- chemistry
- S-Adenosylhomocysteine -- pharmacology
- S-Adenosylmethionine -- chemistry
- Trinucleotide Repeats
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
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