Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells

@article{Tan2008ProteomicAO,
  title={Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells},
  author={Feng-wei Tan and Lifang Lu and Yun Cai and Jing-lan Wang and Yunfei Xie and Lin Wang and Yan-hua Gong and Bing-e Xu and Jun Wu and Ying Luo and Boqin Qiang and Jiangang Yuan and Xiao-qiong Sun and Xiaozhong Peng},
  journal={PROTEOMICS},
  year={2008},
  volume={8}
}
Post‐translational modification by ubiquitin (Ub) and Ub‐like modifiers is one of the most important mechanisms regulating a wide range of cellular processes in eukaryotes. Through mediating 26S proteasome‐dependent degradation of substrates, the covalent modification of proteins by multiple Ub (ubiquitination) can regulate many different cellular functions such as transcription, antigen processing, signal transduction and cell cycle. To better understand ubiquitination and its functions… 
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Proteomic analysis of ubiquitinated proteins shows that nanomolar Doxorubicin treatment of neuroblastoma cells caused dose‐dependent over‐ubiquitination of a specific set of proteins in the absence of measurable inhibition of proteasome, and these data strongly reinforce the hypothesis that Doxorbicin may also exert its effect by damaging proteins.
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