Myers, J K <br/><br/>
Phosphorylation of RNA polymerase II CTD fragments results in tight binding to the WW domain from the yeast prolyl isomerase Ess1.  [electronic resource] 

 -  Biochemistry  Jul 2001 
 - 8479-86 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0006-2960 
<br/><br/><label>Standard No.: </label>10.1021/bi0027884  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Circular Dichroism<br/>Enzyme Stability<br/>Ligands<br/>NIMA-Interacting Peptidylprolyl Isomerase<br/>Peptide Fragments--metabolism<br/>Peptidylprolyl Isomerase--metabolism<br/>Phosphates--metabolism<br/>Phosphorylation<br/>Phosphoserine--metabolism<br/>Protein Binding<br/>Protein Denaturation<br/>Protein Folding<br/>Protein Structure, Tertiary<br/>RNA Polymerase II--metabolism<br/>Saccharomyces cerevisiae--enzymology<br/>Saccharomyces cerevisiae Proteins<br/>Sodium Chloride--metabolism<br/>Spectrometry, Fluorescence<br/>Temperature<br/>Titrimetry<br/>Tryptophan--metabolism