| 000 | 01824 a2200529 4500 | ||
|---|---|---|---|
| 005 | 20250513223701.0 | ||
| 264 | 0 | _c20001214 | |
| 008 | 200012s 0 0 eng d | ||
| 022 | _a0022-2836 | ||
| 024 | 7 |
_a10.1006/jmbi.2000.4175 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aOstermann, N | |
| 245 | 0 | 0 |
_aPotentiating AZT activation: structures of wild-type and mutant human thymidylate kinase suggest reasons for the mutants' improved kinetics with the HIV prodrug metabolite AZTMP. _h[electronic resource] |
| 260 |
_bJournal of molecular biology _cNov 2000 |
||
| 300 |
_a43-53 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 |
_aAnti-HIV Agents _xmetabolism |
| 650 | 0 | 4 | _aBinding Sites |
| 650 | 0 | 4 | _aCatalysis |
| 650 | 0 | 4 | _aCrystallography, X-Ray |
| 650 | 0 | 4 | _aDideoxynucleotides |
| 650 | 0 | 4 | _aEnzyme Stability |
| 650 | 0 | 4 |
_aEscherichia coli _xenzymology |
| 650 | 0 | 4 | _aHumans |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 |
_aMutation _xgenetics |
| 650 | 0 | 4 |
_aNucleoside-Phosphate Kinase _xchemistry |
| 650 | 0 | 4 |
_aNucleotides _xmetabolism |
| 650 | 0 | 4 | _aPhosphorylation |
| 650 | 0 | 4 |
_aProdrugs _xmetabolism |
| 650 | 0 | 4 | _aProtein Binding |
| 650 | 0 | 4 | _aProtein Conformation |
| 650 | 0 | 4 |
_aRecombinant Fusion Proteins _xchemistry |
| 650 | 0 | 4 |
_aThymine Nucleotides _xmetabolism |
| 650 | 0 | 4 |
_aZidovudine _xanalogs & derivatives |
| 700 | 1 | _aLavie, A | |
| 700 | 1 | _aPadiyar, S | |
| 700 | 1 | _aBrundiers, R | |
| 700 | 1 | _aVeit, T | |
| 700 | 1 | _aReinstein, J | |
| 700 | 1 | _aGoody, R S | |
| 700 | 1 | _aKonrad, M | |
| 700 | 1 | _aSchlichting, I | |
| 773 | 0 |
_tJournal of molecular biology _gvol. 304 _gno. 1 _gp. 43-53 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1006/jmbi.2000.4175 _zAvailable from publisher's website |
| 999 |
_c11013630 _d11013630 |
||