Phosphorylation of transglutaminase 2 (TG2) at serine-216 has a role in TG2 mediated activation of nuclear factor-kappa B and in the downregulation of PTEN
<p>Abstract</p> <p>Background</p> <p>Transglutaminase 2 (TG2) and its phosphorylation have been consistently found to be upregulated in a number of cancer cell types. At the molecular level, TG2 has been associated with the activation of nuclear factor-kappa B (NF-κB),...
Main Authors: | Wang Yi, Ande Sudharsana R, Mishra Suresh |
---|---|
Format: | Article |
Language: | English |
Published: |
BMC
2012-07-01
|
Series: | BMC Cancer |
Subjects: | |
Online Access: | http://www.biomedcentral.com/1471-2407/12/277 |
Similar Items
-
Characterization of the interaction and phosphorylation mechanisms of serine/arginine-rich splicing factor 3 by SR protein kinase 2.
Published: (2013) -
Cross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residues
by: Lei eShi, et al.
Published: (2014-09-01) -
Binding specificity and phosphorylation mechanism of serineargnine kinase 2 (SRPK2) towards Its substrates.
Published: (2014) -
Regulation of protein tyrosine kinase ZAP-70 by serine phosphorylation
by: Yang, Yaoming
Published: (2003) -
Manganese-Dependent Serine/Threonine/Tyrosine Kinase From Arabidopsis Thaliana : Role Of Serine And Threonine Residues In The Regulation Of Kinase Activity
by: Reddy, Mamatha M
Published: (2008)