Isabelle, Maxim <br/><br/>
Quantitative proteomics and dynamic imaging reveal that G3BP-mediated stress granule assembly is poly(ADP-ribose)-dependent following exposure to MNNG-induced DNA alkylation.  [electronic resource] 

 -  Journal of cell science  Oct 2012 
 - 4555-66 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>1477-9137 
<br/><br/><label>Standard No.: </label>10.1242/jcs.106963  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Alkylation--drug effects<br/>Amino Acid Sequence<br/>Blotting, Western<br/>Carrier Proteins--chemistry<br/>Cluster Analysis<br/>Cytoplasmic Granules--drug effects<br/>DNA--metabolism<br/>DNA Damage<br/>DNA Helicases<br/>Fatty Acids, Unsaturated--pharmacology<br/>Green Fluorescent Proteins--metabolism<br/>HeLa Cells<br/>Humans<br/>Imaging, Three-Dimensional--methods<br/>Isotope Labeling<br/>Methylnitronitrosoguanidine--pharmacology<br/>Molecular Sequence Data<br/>Poly Adenosine Diphosphate Ribose--metabolism<br/>Poly-ADP-Ribose Binding Proteins<br/>Protein Binding--drug effects<br/>Protein Structure, Tertiary<br/>Protein Transport--drug effects<br/>Proteomics--methods<br/>RNA Helicases<br/>RNA Recognition Motif Proteins<br/>Reproducibility of Results<br/>Stress, Physiological--drug effects<br/>Subcellular Fractions--drug effects<br/>Time Factors