Results 211 to 220 of about 77,825 (245)
SARA, a FYVE Domain Protein that Recruits Smad2 to the TGFβ Receptor [PDF]
Cell, 1998 Smads transmit signals from transmembrane ser/thr kinase receptors to the nucleus. We now identify SARA (for Smad anchor for receptor activation), a FYVE domain protein that interacts directly with Smad2 and Smad3. SARA functions to recruit Smad2 to the TGFbeta receptor by controlling the subcellular localization of Smad2 and by interacting with the ...
Jeff Wrana +2 more
exaly +3 more sources
Platelets possess functional TGF-β receptors and Smad2 protein
Platelets, 2007 TGF-beta1 plays a main role in tissue repair by regulating extracellular matrix production and tissue granulation. Platelets are one of the main sources of this cytokine in the circulation. The aim of this study was to evaluate the presence of the TGF-beta receptors on platelets, the effect of TGF-beta1 on platelet aggregation and the underlying ...
P R, Lev +5 more
exaly +3 more sources
Apmis, 2007 Smad2 participates in the TGF‐β signaling pathway, where it cooperates with transcription factors to regulate expression of defined genes. The purpose of this study was to investigate the expression pattern of phosphorylated Smad2 (pSmad2) in association with clinicopathological parameters and biological markers of proliferation and invasion ...
Giorgos Liapis
exaly +4 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Expression and localization of Smad2 and Smad4 proteins in the porcine ovary
Acta Histochemica, 2014The objective of the present study was to investigate the temporal and spatial expression of Smad2 and Smad4 proteins, the downstream signaling molecules of the transforming growth factor beta (TGF-β) superfamily, in the porcine ovary. Cellular localization of Smad2 and Smad4 proteins was examined using immunohistochemistry.
Na, Xing +6 more
openaire +2 more sources
Smad2 Protein Disruption in the Central Nervous System Leads to Aberrant Cerebellar Development and Early Postnatal Ataxia in Mice [PDF]
Journal of Biological Chemistry, 2011 Smad2 is a critical mediator of TGF-β signals that are known to play an important role in a wide range of biological processes in various cell types. Its role in the development of the CNS, however, is largely unknown. Mice lacking Smad2 in the CNS (Smad2-CNS-KO) were generated by a Cre-loxP approach.
Kimitaka Tanaka +2 more
exaly +3 more sources
Andrologia, 2011
The expression and localisation of downstream signalling molecules of transforming growth factor beta superfamily, Smad2 and Smad4 proteins, was investigated in immature and mature dog testis. Cellular localisation of Smad2 and Smad4 proteins was examined using immunohistochemistry.
X-J, Zhang, J-P, He, X-X, Wen, L, Zhao
openaire +3 more sources
The expression and localisation of downstream signalling molecules of transforming growth factor beta superfamily, Smad2 and Smad4 proteins, was investigated in immature and mature dog testis. Cellular localisation of Smad2 and Smad4 proteins was examined using immunohistochemistry.
X-J, Zhang, J-P, He, X-X, Wen, L, Zhao
openaire +3 more sources
Cytokine, 2006
Insulin is known to modulate transforming growth factor-beta (TGFbeta) signaling. In this report, by using the IN Cell Analyzer 1000, the fluorescence cell imaging instrument, we demonstrated that protein tyrosine phosphatase 1B (PTP1B) could regulate TGFbeta1-induced Smad2 activation in a PI3 kinase-dependent manner.
Hong Ding, Xu Shen, Hualiang Jiang
exaly +3 more sources
Insulin is known to modulate transforming growth factor-beta (TGFbeta) signaling. In this report, by using the IN Cell Analyzer 1000, the fluorescence cell imaging instrument, we demonstrated that protein tyrosine phosphatase 1B (PTP1B) could regulate TGFbeta1-induced Smad2 activation in a PI3 kinase-dependent manner.
Hong Ding, Xu Shen, Hualiang Jiang
exaly +3 more sources
Journal of Cellular Physiology, 2001
AbstractBone tissues reportedly contain considerable amounts of activin A and follistatin, an activin A‐binding protein. In the present study, we found that follistatin strongly inhibited osteoclast formation in cocultures of mouse bone marrow cells and primary osteoblasts induced by 1α,25 dihydroxyvitamin D3, prostaglandin E2, and interleukin‐1α ...
Y, Murase +8 more
openaire +2 more sources
AbstractBone tissues reportedly contain considerable amounts of activin A and follistatin, an activin A‐binding protein. In the present study, we found that follistatin strongly inhibited osteoclast formation in cocultures of mouse bone marrow cells and primary osteoblasts induced by 1α,25 dihydroxyvitamin D3, prostaglandin E2, and interleukin‐1α ...
Y, Murase +8 more
openaire +2 more sources