A novel inhibitor of STAT3 homodimerization selectively suppresses STAT3 activity and malignant transformation

STAT3-STAT3 dimerization, which involves reciprocal binding of the STAT3-SH2 domain to phosphorylated tyrosine-705 (Y-705), is required for STAT3 nuclear translocation, DNA binding and transcriptional regulation of downstream target genes. Here we describe a small molecule S3I-1757 capable of disrup...

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Autors principals: Zhang, Xiaolei, Sun, Ying, Pireddu, Roberta, Yang, Hua, Urlam, Murali K., Lawrence, Harshani R., Guida, Wayne C., Lawrence, Nicholas J., Sebti, Saïd M.
Format: Artigo
Idioma:Inglês
Publicat: 2013
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Article
Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC4030628/
https://ncbi.nlm.nih.gov/pubmed/23322008
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1158/0008-5472.CAN-12-3175
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