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