Mechanisms of TGF-β Signaling from Cell Membrane to the Nucleus

By Yigong Shi, J. Massagué. 2003

5,235 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/2f024290a53f5a1f38a8221046914ad4894cc9cf

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In Molecular Biology

Citations in the corpus

TGFβ signalling in context (2012, background): “First, a large number of signal transduction regulatory factors determine the access of TGFβ ligands to signalling receptors (1), and of receptors to”
Transforming Growth Factor (TGF)-β signaling in cardiac remodeling (2010, background): “proteins [13]; Smad2 and Smad3 are activated through phosphorylation by ALK5, whereas Smad1, Smad5 and Smad8 are activated by”
Cytostatic and apoptotic actions of TGF-β in homeostasis and cancer (2003, background): “TGF-β signalling pathways The molecular events that lead from activation of cell surface TGF-β receptors to the formation of SMAD transcriptional complexes and the regulation of this entire process is now reasonably well understoo”
TGFβ–SMAD signal transduction: molecular specificity and functional flexibility (2007, background): “A hallmark of TGFβ superfamily ligands is the so-called 'cysteine knot”
TGF-&bgr; signaling and epithelial–mesenchymal transition in cancer progression (2013, background): “Smads activate or repress transcription through physical interactions with high-affinity DNA-binding transcription factors, and coactivators and corepressors, at regulatory gene sequences [10,11].”
TGFβ signalling: a complex web in cancer progression (2010, neutral): “Regulation of cell proliferation by TGFβ The effects of TGFβ are mediated by three TGFβ ligands — TGFβ1, TGFβ2 and TGFβ3 — through TGFβ type 1 and type 2 receptor”
G1 cell-cycle control and cancer (2004, background): “TGF-β activates a membrane-receptor serine/threonine kinase complex that phosphorylates the tumour suppressor proteins Smad2 and Smad3 (ref”
TGFβ in Cancer (2008, background): “…are clustered in one family branch, and bone morphogenetic proteins (BMPs), anti-muellerian hormone (AMH, also known as MIS), and various growth and differentiation factors (GDFs) are grouped into the other branch (Derynck and Akhurst, 2007; Roberts and Wakefield, 2003; Shi and Massagué, 2003).”
Smad3 as a mediator of the fibrotic response (2004, background): “This domain in R-Smads interacts with the Type I receptor, contains the SSXS phosphorylation site and mediates formation of R-Smad/Smad4 oligomers.”
Epidermal stem cells of the skin. (2006, background): “…the cytoplasmic tail of Bmpr1a, which in turns phosphorylates the R-Smad DNA-binding protein (Smad 1, 5, and 8), which in turn complexes with one of its partner Smads (typically Smad 4) to translocate to the nucleus and mediate target gene expression (Shi & Massague 2003) (Figure 6a).”