| 000 | 01684 a2200457 4500 | ||
|---|---|---|---|
| 005 | 20250513060015.0 | ||
| 264 | 0 | _c19940914 | |
| 008 | 199409s 0 0 eng d | ||
| 022 | _a0950-382X | ||
| 024 | 7 |
_a10.1111/j.1365-2958.1994.tb01011.x _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aPalzkill, T | |
| 245 | 0 | 0 |
_aEvolution of antibiotic resistance: several different amino acid substitutions in an active site loop alter the substrate profile of beta-lactamase. _h[electronic resource] |
| 260 |
_bMolecular microbiology _cApr 1994 |
||
| 300 |
_a217-29 p. _bdigital |
||
| 500 | _aPublication Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S. | ||
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 |
_aAmpicillin _xmetabolism |
| 650 | 0 | 4 |
_aAmpicillin Resistance _xgenetics |
| 650 | 0 | 4 |
_aBacterial Proteins _xbiosynthesis |
| 650 | 0 | 4 | _aBase Sequence |
| 650 | 0 | 4 | _aBinding Sites |
| 650 | 0 | 4 | _aBiological Evolution |
| 650 | 0 | 4 |
_aCeftazidime _xmetabolism |
| 650 | 0 | 4 |
_aDrug Resistance, Microbial _xgenetics |
| 650 | 0 | 4 | _aEnzyme Induction |
| 650 | 0 | 4 |
_aEscherichia coli _xenzymology |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 | _aMutagenesis |
| 650 | 0 | 4 | _aProtein Structure, Tertiary |
| 650 | 0 | 4 | _aSequence Alignment |
| 650 | 0 | 4 | _aStructure-Activity Relationship |
| 650 | 0 | 4 | _aSubstrate Specificity |
| 650 | 0 | 4 |
_abeta-Lactamases _xbiosynthesis |
| 700 | 1 | _aLe, Q Q | |
| 700 | 1 | _aVenkatachalam, K V | |
| 700 | 1 | _aLaRocco, M | |
| 700 | 1 | _aOcera, H | |
| 773 | 0 |
_tMolecular microbiology _gvol. 12 _gno. 2 _gp. 217-29 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1111/j.1365-2958.1994.tb01011.x _zAvailable from publisher's website |
| 999 |
_c8057175 _d8057175 |
||