Polzien, Lisa <br/><br/>
Identification of novel in vivo phosphorylation sites of the human proapoptotic protein BAD: pore-forming activity of BAD is regulated by phosphorylation.  [electronic resource] 

 -  The Journal of biological chemistry  Oct 2009 
 - 28004-28020 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>1083-351X 
<br/><br/><label>Standard No.: </label>10.1074/jbc.M109.010702  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>14-3-3 Proteins--genetics<br/>Amino Acid Sequence<br/>Animals<br/>Cyclic AMP-Dependent Protein Kinases--metabolism<br/>Humans<br/>Ion Channels--chemistry<br/>Lipid Bilayers--metabolism<br/>Mass Spectrometry<br/>Mice<br/>Molecular Sequence Data<br/>NIH 3T3 Cells<br/>Peptides--chemistry<br/>Phosphorylation<br/>Protein Binding<br/>Proto-Oncogene Proteins c-akt--metabolism<br/>Proto-Oncogene Proteins c-bcl-2--genetics<br/>Sequence Alignment<br/>bcl-Associated Death Protein--chemistry<br/>bcl-X Protein--genetics<br/>p21-Activated Kinases--metabolism<br/>raf Kinases--genetics