Article citationsMore>>

Hazan-Halevy, I., Harris, D., Liu, Z., Liu, J., Li, P., Chen, X., Shanker, S., Ferrajoli, A., Keating, M.J. and Estrov, Z. (2010) STAT3 Is Constitutively Phosphorylated on Serine 727 Residues, Binds DNA, and Activates Transcription in CLL Cells. Blood, 115, 2852-2863.
http://dx.doi.org/10.1182/blood-2009-10-230060

has been cited by the following article:

• TITLE: STAT3 Signaling in Cancer

  AUTHORS: Ioannis Gkouveris, Nikolaos Nikitakis, John Sauk

  KEYWORDS: STAT3, Signaling, Cancer, Dual Role, Tyrosine and Serine Phosphorylation

  JOURNAL NAME: Journal of Cancer Therapy, Vol.6 No.8, August 10, 2015

  ABSTRACT: In recent years, signal transducers and activators of transcription (STAT) proteins have been recognized as cytoplasmic transcription factors that mediate extracellular signaling to the nucleus controlling fundamental functions, such as cell proliferation, apoptosis, differentiation, immune responses and angiogenesis. Among them, STAT3 is a major player, aberrant activation of which is involved in several diseases, including cancer. Among other upstream regulators, IL-6/Jak signaling can activate STAT3 and its role appears to be critical in various types of cancer. Although STAT3 has been traditionally recognized as amoncogene, more recently the dual role of STAT3 in cancer, either tumor inductive or suppressive, has been appreciated. The importance and differential effect of STAT3 on tyrosine or serine residues are also a matter of continuing debate. Interestingly, recent findings suggesting that STAT3 plays an important role in cancer stem cell regulation have gained significant attention. This review summarizes current literature focusing on the significance of STAT3 in several diseases as well as in cancer. Understanding the complexity of STAT3 function has the potential to elucidate important molecular aspects of cancer with significant therapeutic implications.