1 r serine kinases that phosphorylate Smad2 or Smad3 proteins.

2 ietin receptor (EpoR) or a dominant negative Smad3 protein and to generate cells expressing two diffe

3 tion and nuclear transportation of Smad2 and Smad3 proteins as well as stimulation of transcriptional

4 ibited impaired phosphorylation of SMAD2 and SMAD3 proteins at their linker regions, which negatively

5 n-resistant esophageal cancer cell line, the Smad3-protein complexes contained the SnoN oncoprotein.

6 wth arrest, TGF-beta enhanced the ability of Smad3-protein complexes to bind c-myc regulatory element

7 the nucleocytoplasmic shuttling of Smad2 and Smad3 proteins, demonstrate that continued nucleocytopla

8 e inhibitory effect by overexpression of the Smad3 protein, demonstrates that Smad3 is essential in m

9 ling, but the physiological relevance of the Smad3 protein in signaling by TGF-beta receptors has not

10                                            A Smad3 protein in which the three C-terminal serines have

11                                      Loss of Smad3 protein is a specific feature of pediatric T-cell

12 ether, our results suggest that the level of Smad3 protein is an important determinant of the progres

13 in quiescent cells and a significant drop in Smad3 protein levels in proliferating cells.

14 ot analyses revealed increased expression of Smad3 protein levels in the kidney cortex in response to

15                          However, changes in Smad3 protein levels were also paralleled by changes in

16         In human glomerular mesangial cells, Smad3 protein levels were specifically reduced by 24 h o

17   However, the molecular regulation of Smad2/Smad3 proteins stability remains a mystery.

18 pecifically with the MH2 domain of SMAD2 and SMAD3 proteins to regulate TGF-beta1-responsive genes su

19    Mechanistically, GAS5 competitively bound Smad3 protein via multiple RNA Smad-binding elements (rS

20                                              Smad3 protein was absent in T-cell ALL but present in pr