| 000 | 01861 a2200517 4500 | ||
|---|---|---|---|
| 005 | 20250516230530.0 | ||
| 264 | 0 | _c20150206 | |
| 008 | 201502s 0 0 eng d | ||
| 022 | _a1083-351X | ||
| 024 | 7 |
_a10.1074/jbc.M114.589051 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aKidwell, Mary Anne | |
| 245 | 0 | 0 |
_aEvolutionarily conserved roles of the dicer helicase domain in regulating RNA interference processing. _h[electronic resource] |
| 260 |
_bThe Journal of biological chemistry _cOct 2014 |
||
| 300 |
_a28352-62 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 |
_aAdenosine Triphosphate _xchemistry |
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 | _aAnimals |
| 650 | 0 | 4 |
_aBaculoviridae _xgenetics |
| 650 | 0 | 4 | _aBiological Evolution |
| 650 | 0 | 4 | _aConserved Sequence |
| 650 | 0 | 4 |
_aDNA Helicases _xchemistry |
| 650 | 0 | 4 |
_aFungal Proteins _xchemistry |
| 650 | 0 | 4 | _aGene Expression Regulation, Fungal |
| 650 | 0 | 4 | _aHumans |
| 650 | 0 | 4 | _aHydrolysis |
| 650 | 0 | 4 |
_aIsoenzymes _xchemistry |
| 650 | 0 | 4 |
_aMicroRNAs _xbiosynthesis |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 | _aProtein Structure, Secondary |
| 650 | 0 | 4 | _aProtein Structure, Tertiary |
| 650 | 0 | 4 | _aRNA Interference |
| 650 | 0 | 4 |
_aRNA, Double-Stranded _xchemistry |
| 650 | 0 | 4 |
_aRecombinant Proteins _xchemistry |
| 650 | 0 | 4 |
_aRibonuclease III _xchemistry |
| 650 | 0 | 4 | _aSf9 Cells |
| 650 | 0 | 4 | _aSignal Transduction |
| 650 | 0 | 4 | _aSpodoptera |
| 650 | 0 | 4 |
_aSporothrix _xchemistry |
| 650 | 0 | 4 | _aSubstrate Specificity |
| 700 | 1 | _aChan, Jessica M | |
| 700 | 1 | _aDoudna, Jennifer A | |
| 773 | 0 |
_tThe Journal of biological chemistry _gvol. 289 _gno. 41 _gp. 28352-62 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1074/jbc.M114.589051 _zAvailable from publisher's website |
| 999 |
_c24109974 _d24109974 |
||