| 000 | 01767 a2200529 4500 | ||
|---|---|---|---|
| 005 | 20250516053708.0 | ||
| 264 | 0 | _c20111115 | |
| 008 | 201111s 0 0 eng d | ||
| 022 | _a1476-4687 | ||
| 024 | 7 |
_a10.1038/nature10404 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aSlade, Dea | |
| 245 | 0 | 0 |
_aThe structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase. _h[electronic resource] |
| 260 |
_bNature _cSep 2011 |
||
| 300 |
_a616-20 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 |
_aActinomycetales _xenzymology |
| 650 | 0 | 4 |
_aAdenosine Diphosphate _xanalogs & derivatives |
| 650 | 0 | 4 |
_aAdenosine Diphosphate Ribose _xchemistry |
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 | _aBiocatalysis |
| 650 | 0 | 4 | _aCatalytic Domain |
| 650 | 0 | 4 | _aCrystallography, X-Ray |
| 650 | 0 | 4 | _aEvolution, Molecular |
| 650 | 0 | 4 |
_aGlycoside Hydrolases _xantagonists & inhibitors |
| 650 | 0 | 4 | _aHumans |
| 650 | 0 | 4 | _aHydrolysis |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 | _aPhylogeny |
| 650 | 0 | 4 | _aPoly (ADP-Ribose) Polymerase-1 |
| 650 | 0 | 4 |
_aPoly Adenosine Diphosphate Ribose _xchemistry |
| 650 | 0 | 4 |
_aPoly(ADP-ribose) Polymerases _xgenetics |
| 650 | 0 | 4 | _aProtein Conformation |
| 650 | 0 | 4 |
_aProteins _xmetabolism |
| 650 | 0 | 4 |
_aPyrrolidines _xpharmacology |
| 700 | 1 | _aDunstan, Mark S | |
| 700 | 1 | _aBarkauskaite, Eva | |
| 700 | 1 | _aWeston, Ria | |
| 700 | 1 | _aLafite, Pierre | |
| 700 | 1 | _aDixon, Neil | |
| 700 | 1 | _aAhel, Marijan | |
| 700 | 1 | _aLeys, David | |
| 700 | 1 | _aAhel, Ivan | |
| 773 | 0 |
_tNature _gvol. 477 _gno. 7366 _gp. 616-20 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1038/nature10404 _zAvailable from publisher's website |
| 999 |
_c21132908 _d21132908 |
||