000 | 01688 a2200481 4500 | ||
---|---|---|---|
005 | 20250514003815.0 | ||
264 | 0 | _c20011004 | |
008 | 200110s 0 0 eng d | ||
022 | _a0006-2960 | ||
024 | 7 |
_a10.1021/bi0027884 _2doi |
|
040 |
_aNLM _beng _cNLM |
||
100 | 1 | _aMyers, J K | |
245 | 0 | 0 |
_aPhosphorylation of RNA polymerase II CTD fragments results in tight binding to the WW domain from the yeast prolyl isomerase Ess1. _h[electronic resource] |
260 |
_bBiochemistry _cJul 2001 |
||
300 |
_a8479-86 p. _bdigital |
||
500 | _aPublication Type: Journal Article; Research Support, U.S. Gov't, P.H.S. | ||
650 | 0 | 4 | _aCircular Dichroism |
650 | 0 | 4 | _aEnzyme Stability |
650 | 0 | 4 | _aLigands |
650 | 0 | 4 | _aNIMA-Interacting Peptidylprolyl Isomerase |
650 | 0 | 4 |
_aPeptide Fragments _xmetabolism |
650 | 0 | 4 |
_aPeptidylprolyl Isomerase _xmetabolism |
650 | 0 | 4 |
_aPhosphates _xmetabolism |
650 | 0 | 4 | _aPhosphorylation |
650 | 0 | 4 |
_aPhosphoserine _xmetabolism |
650 | 0 | 4 | _aProtein Binding |
650 | 0 | 4 | _aProtein Denaturation |
650 | 0 | 4 | _aProtein Folding |
650 | 0 | 4 | _aProtein Structure, Tertiary |
650 | 0 | 4 |
_aRNA Polymerase II _xmetabolism |
650 | 0 | 4 |
_aSaccharomyces cerevisiae _xenzymology |
650 | 0 | 4 | _aSaccharomyces cerevisiae Proteins |
650 | 0 | 4 |
_aSodium Chloride _xmetabolism |
650 | 0 | 4 | _aSpectrometry, Fluorescence |
650 | 0 | 4 | _aTemperature |
650 | 0 | 4 | _aTitrimetry |
650 | 0 | 4 |
_aTryptophan _xmetabolism |
700 | 1 | _aMorris, D P | |
700 | 1 | _aGreenleaf, A L | |
700 | 1 | _aOas, T G | |
773 | 0 |
_tBiochemistry _gvol. 40 _gno. 29 _gp. 8479-86 |
|
856 | 4 | 0 |
_uhttps://doi.org/10.1021/bi0027884 _zAvailable from publisher's website |
999 |
_c11384722 _d11384722 |