000 01673 a2200433 4500
005 20250513194710.0
264 0 _c20000103
008 200001s 0 0 eng d
022 _a0021-9258
024 7 _a10.1074/jbc.274.46.33011
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aBacolla, A
245 0 0 _aRecombinant human DNA (cytosine-5) methyltransferase. II. Steady-state kinetics reveal allosteric activation by methylated dna.
_h[electronic resource]
260 _bThe Journal of biological chemistry
_cNov 1999
300 _a33011-9 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
650 0 4 _aAllosteric Regulation
650 0 4 _aBinding Sites
650 0 4 _aDNA (Cytosine-5-)-Methyltransferase 1
650 0 4 _aDNA (Cytosine-5-)-Methyltransferases
650 0 4 _aDNA Methylation
650 0 4 _aDNA, Superhelical
_xchemistry
650 0 4 _aDNA-Binding Proteins
_xchemistry
650 0 4 _aEnzyme Activation
650 0 4 _aEnzyme Inhibitors
_xpharmacology
650 0 4 _aHumans
650 0 4 _aKinetics
650 0 4 _aOligodeoxyribonucleotides
_xchemistry
650 0 4 _aRecombinant Proteins
_xchemistry
650 0 4 _aRibonucleoproteins, Small Nuclear
_xchemistry
650 0 4 _aS-Adenosylhomocysteine
_xpharmacology
650 0 4 _aS-Adenosylmethionine
_xchemistry
650 0 4 _aTrinucleotide Repeats
700 1 _aPradhan, S
700 1 _aRoberts, R J
700 1 _aWells, R D
773 0 _tThe Journal of biological chemistry
_gvol. 274
_gno. 46
_gp. 33011-9
856 4 0 _uhttps://doi.org/10.1074/jbc.274.46.33011
_zAvailable from publisher's website
999 _c10508507
_d10508507