Nuclear protein isoforms: implications for cancer diagnosis and therapy

Fei Shen, Kashif Z. Kirmani, Zhimin Xiao, Benjamin H. Thirlby, Robert J. Hickey, Linda H. Malkas

Research output: Contribution to journalReview article

16 Scopus citations


Post-translational modifications (PTMs) of nuclear proteins play essential roles in the regulation of gene transcription and signal transduction pathways. Numerous studies have demonstrated a correlation between specific nuclear protein isoforms and cellular malignant process. This communication reviews the impact of major PTM events such as phosphorylation, acetylation, methylation, ubiquitination, and sumoylation on several important nuclear proteins including p53, histones, proliferating cellular nuclear antigen (PCNA), and retinoblastoma protein (Rb) in the process. In addition, the implications of the PTMs as cancer biomarkers and therapeutic targets are considered.

Original languageEnglish (US)
Pages (from-to)756-760
Number of pages5
JournalJournal of Cellular Biochemistry
Issue number3
StatePublished - Mar 1 2011


  • Acetylation
  • Methylation
  • Nuclear protein isoforms
  • Phosphorylation
  • Sumoylation
  • Ubiquintination

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

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  • Cite this

    Shen, F., Kirmani, K. Z., Xiao, Z., Thirlby, B. H., Hickey, R. J., & Malkas, L. H. (2011). Nuclear protein isoforms: implications for cancer diagnosis and therapy. Journal of Cellular Biochemistry, 112(3), 756-760.