000 | 01795 a2200493 4500 | ||
---|---|---|---|
005 | 20250514024437.0 | ||
264 | 0 | _c20020405 | |
008 | 200204s 0 0 eng d | ||
022 | _a0022-2836 | ||
024 | 7 |
_a10.1006/jmbi.2001.5382 _2doi |
|
040 |
_aNLM _beng _cNLM |
||
100 | 1 | _aHadi, Masood Z | |
245 | 0 | 0 |
_aDeterminants in nuclease specificity of Ape1 and Ape2, human homologues of Escherichia coli exonuclease III. _h[electronic resource] |
260 |
_bJournal of molecular biology _cFeb 2002 |
||
300 |
_a853-66 p. _bdigital |
||
500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. | ||
650 | 0 | 4 | _aAmino Acid Sequence |
650 | 0 | 4 |
_aBase Pair Mismatch _xgenetics |
650 | 0 | 4 | _aBase Sequence |
650 | 0 | 4 | _aBinding Sites |
650 | 0 | 4 |
_aDNA _xgenetics |
650 | 0 | 4 | _aDNA Repair |
650 | 0 | 4 | _aDNA-(Apurinic or Apyrimidinic Site) Lyase |
650 | 0 | 4 | _aEndonucleases |
650 | 0 | 4 |
_aEscherichia coli _xenzymology |
650 | 0 | 4 |
_aExodeoxyribonucleases _xchemistry |
650 | 0 | 4 | _aHumans |
650 | 0 | 4 | _aHydrophobic and Hydrophilic Interactions |
650 | 0 | 4 | _aKinetics |
650 | 0 | 4 | _aModels, Molecular |
650 | 0 | 4 | _aMolecular Sequence Data |
650 | 0 | 4 | _aMultifunctional Enzymes |
650 | 0 | 4 | _aMutation |
650 | 0 | 4 | _aProtein Structure, Secondary |
650 | 0 | 4 | _aProtein Structure, Tertiary |
650 | 0 | 4 | _aSequence Alignment |
650 | 0 | 4 | _aSequence Homology, Amino Acid |
650 | 0 | 4 | _aSubstrate Specificity |
700 | 1 | _aGinalski, Krzysztof | |
700 | 1 | _aNguyen, Lam H | |
700 | 1 | _aWilson, David M | |
773 | 0 |
_tJournal of molecular biology _gvol. 316 _gno. 3 _gp. 853-66 |
|
856 | 4 | 0 |
_uhttps://doi.org/10.1006/jmbi.2001.5382 _zAvailable from publisher's website |
999 |
_c11774279 _d11774279 |