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]
Producer: 20130426Description: 4555-66 p. digitalISSN:- 1477-9137
- Alkylation -- drug effects
- Amino Acid Sequence
- Blotting, Western
- Carrier Proteins -- chemistry
- Cluster Analysis
- Cytoplasmic Granules -- drug effects
- DNA -- metabolism
- DNA Damage
- DNA Helicases
- Fatty Acids, Unsaturated -- pharmacology
- Green Fluorescent Proteins -- metabolism
- HeLa Cells
- Humans
- Imaging, Three-Dimensional -- methods
- Isotope Labeling
- Methylnitronitrosoguanidine -- pharmacology
- Molecular Sequence Data
- Poly Adenosine Diphosphate Ribose -- metabolism
- Poly-ADP-Ribose Binding Proteins
- Protein Binding -- drug effects
- Protein Structure, Tertiary
- Protein Transport -- drug effects
- Proteomics -- methods
- RNA Helicases
- RNA Recognition Motif Proteins
- Reproducibility of Results
- Stress, Physiological -- drug effects
- Subcellular Fractions -- drug effects
- Time Factors
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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