000 01548 a2200397 4500
005 20250513205247.0
264 0 _c20010301
008 200103s 0 0 eng d
022 _a0264-6021
024 7 _a10.1042/0264-6021:3470519
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aXu-Welliver, M
245 0 0 _aPoint mutations at multiple sites including highly conserved amino acids maintain activity, but render O6-alkylguanine-DNA alkyltransferase insensitive to O6-benzylguanine.
_h[electronic resource]
260 _bThe Biochemical journal
_cApr 2000
300 _a519-26 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
650 0 4 _aAmino Acid Sequence
650 0 4 _aAmino Acid Substitution
_xgenetics
650 0 4 _aAntineoplastic Agents
_xpharmacology
650 0 4 _aBinding Sites
650 0 4 _aConserved Sequence
_xgenetics
650 0 4 _aDNA Repair
_xdrug effects
650 0 4 _aDrug Resistance
_xgenetics
650 0 4 _aEscherichia coli
650 0 4 _aGene Library
650 0 4 _aGuanine
_xanalogs & derivatives
650 0 4 _aHumans
650 0 4 _aMethylnitronitrosoguanidine
_xpharmacology
650 0 4 _aMolecular Sequence Data
650 0 4 _aO(6)-Methylguanine-DNA Methyltransferase
_xchemistry
650 0 4 _aPoint Mutation
_xgenetics
650 0 4 _aSequence Alignment
700 1 _aPegg, A E
773 0 _tThe Biochemical journal
_gvol. 347
_gno. Pt 2
_gp. 519-26
856 4 0 _uhttps://doi.org/10.1042/0264-6021:3470519
_zAvailable from publisher's website
999 _c10703052
_d10703052