| 000 | 01871 a2200517 4500 | ||
|---|---|---|---|
| 005 | 20250514050219.0 | ||
| 264 | 0 | _c20030212 | |
| 008 | 200302s 0 0 eng d | ||
| 022 | _a0021-9258 | ||
| 024 | 7 |
_a10.1074/jbc.M209294200 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aLi, Jiaxu | |
| 245 | 0 | 0 |
_aAssociation of the histone methyltransferase Set2 with RNA polymerase II plays a role in transcription elongation. _h[electronic resource] |
| 260 |
_bThe Journal of biological chemistry _cDec 2002 |
||
| 300 |
_a49383-8 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, U.S. Gov't, P.H.S. | ||
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 | _aElectrophoresis, Polyacrylamide Gel |
| 650 | 0 | 4 |
_aEscherichia coli _xmetabolism |
| 650 | 0 | 4 | _aGene Deletion |
| 650 | 0 | 4 |
_aGlutathione Transferase _xmetabolism |
| 650 | 0 | 4 | _aHeLa Cells |
| 650 | 0 | 4 | _aHistone Methyltransferases |
| 650 | 0 | 4 | _aHistone-Lysine N-Methyltransferase |
| 650 | 0 | 4 | _aHumans |
| 650 | 0 | 4 | _aMass Spectrometry |
| 650 | 0 | 4 | _aMethylation |
| 650 | 0 | 4 |
_aMethyltransferases _xmetabolism |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 | _aMutation |
| 650 | 0 | 4 | _aPhenotype |
| 650 | 0 | 4 | _aPhosphorylation |
| 650 | 0 | 4 | _aProtein Binding |
| 650 | 0 | 4 | _aProtein Methyltransferases |
| 650 | 0 | 4 | _aProtein Structure, Tertiary |
| 650 | 0 | 4 |
_aRNA Polymerase II _xmetabolism |
| 650 | 0 | 4 |
_aSaccharomyces cerevisiae _xmetabolism |
| 650 | 0 | 4 |
_aSaccharomyces cerevisiae Proteins _xmetabolism |
| 650 | 0 | 4 | _aSequence Homology, Amino Acid |
| 650 | 0 | 4 | _aTranscription, Genetic |
| 650 | 0 | 4 |
_aUracil _xanalogs & derivatives |
| 700 | 1 | _aMoazed, Danesh | |
| 700 | 1 | _aGygi, Steven P | |
| 773 | 0 |
_tThe Journal of biological chemistry _gvol. 277 _gno. 51 _gp. 49383-8 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1074/jbc.M209294200 _zAvailable from publisher's website |
| 999 |
_c12191123 _d12191123 |
||