| 000 | 01419 a2200433 4500 | ||
|---|---|---|---|
| 005 | 20250513090230.0 | ||
| 264 | 0 | _c19960606 | |
| 008 | 199606s 0 0 eng d | ||
| 022 | _a0028-0836 | ||
| 024 | 7 |
_a10.1038/380727a0 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aPeat, T S | |
| 245 | 0 | 0 |
_aStructure of the UmuD' protein and its regulation in response to DNA damage. _h[electronic resource] |
| 260 |
_bNature _cApr 1996 |
||
| 300 |
_a727-30 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 |
_aBacterial Proteins _xchemistry |
| 650 | 0 | 4 | _aCloning, Molecular |
| 650 | 0 | 4 | _aCrystallography, X-Ray |
| 650 | 0 | 4 | _aDNA Damage |
| 650 | 0 | 4 | _aDNA-Directed DNA Polymerase |
| 650 | 0 | 4 | _aEscherichia coli |
| 650 | 0 | 4 | _aEscherichia coli Proteins |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 | _aProtein Conformation |
| 650 | 0 | 4 | _aProtein Folding |
| 650 | 0 | 4 |
_aRecombinant Proteins _xchemistry |
| 650 | 0 | 4 | _aSOS Response, Genetics |
| 650 | 0 | 4 | _aStructure-Activity Relationship |
| 700 | 1 | _aFrank, E G | |
| 700 | 1 | _aMcDonald, J P | |
| 700 | 1 | _aLevine, A S | |
| 700 | 1 | _aWoodgate, R | |
| 700 | 1 | _aHendrickson, W A | |
| 773 | 0 |
_tNature _gvol. 380 _gno. 6576 _gp. 727-30 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1038/380727a0 _zAvailable from publisher's website |
| 999 |
_c8613515 _d8613515 |
||