Genistein suppressed epithelial-mesenchymal transition and migration efficacies of BG-1 ovarian cancer cells activated by estrogenic chemicals via estrogen receptor pathway and downregulation of TGF-β signaling pathway.
Ch'ŏngju, South Korea. In Phytomedicine, Nov 2015
In the protein expression of SnoN and Smad3, E2, BPA, and NP upregulated SnoN, a negative regulator of TGF-β signaling, and downregulated pSmad3, a transcription factor in the downstream pathway of TGF-β signaling pathway, suggesting that E2, BPA, and NP simultaneously lead to the downregualtion of TGF-β signaling in the process of induction of EMT and migration of BG-1 cells via ER signaling.
SnoN as a novel negative regulator of TGF-β/Smad signaling: a target for tailoring organ fibrosis.
Winnipeg, Canada. In Am J Physiol Heart Circ Physiol, Feb 2015
SnoN (and its alternatively-spliced isoforms SnoN2, SnoA, and SnoI) is one of four members of a family of negative regulators of TGF-β1 signaling that includes Ski and functional Smad-suppressing elements on chromosomes 15 and 18. SnoN has been shown to be structurally and functionally similar to Ski and has been demonstrated to directly interact with Ski to abrogate gene expression.
Methods for detection and characterization of protein S-nitrosylation.
Taipei, Taiwan. In Methods, 2013
Reversible protein S-nitrosylation, defined as the covalent addition of a nitroso moiety to the reactive thiol group on a cysteine residue, has received increasing recognition as a critical post-translational modification that exerts ubiquitous influence in a wide range of cellular pathways and physiological processes.
Protein s-nitrosylation measurement.
Gainesville, United States. In Methods Enzymol, 2012
In this review, we summarize current methods for detection of protein S-nitrosylation with a focus on the biotin switch technique and related methods.
OxyR: a molecular code for redox-related signaling.
Durham, United States. In Cell, 2002
Using the transcription factor OxyR as a model, we have generated, in vitro, several stable, posttranslational modifications of the single regulatory thiol (SH), including S-NO, S-OH, and S-SG, and shown that each occurs in vivo.