How cells read TGF-β signals

By J. Massagué. Nature reviews. Molecular cell biology, 2000

1,246 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/da31b8e79731c82a8bfc8021c2c257ace626861e

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Citations in the corpus

TGF-β1 and angiotensin networking in cardiac remodeling (2004, background): “TGF-h1 elicits its biological responses through a heteromeric receptor complex comprising two serine–threonine kinase receptors, termed TGF-h receptor types 1 and 2 (ThR1 and ThR2) [ 89 ,90].”
TGFβ signalling in context (2012, background): “action, which results in chromatin opening and thereby allows access for canonical SMAD complexes (2) (for details, see”
A SNAIL1-SMAD3/4 transcriptional repressor complex promotes TGF-β mediated epithelial-mesenchymal transition (2009, background): “TGF-β binding to its receptors leads to phosphorylation of SMAD2/3, which partner with SMAD4 and translocate to the nucleus where SMAD transcriptional complexes control the expression of target gene”
Tumour microenvironment: TGFβ: the molecular Jekyll and Hyde of cancer (2006, neutral): “In addition to the well-characterized interactions that are known to regulate Smad activity, which are detailed in several review article”
TGF‐β activates Erk MAP kinase signalling through direct phosphorylation of ShcA (2007, background): “The kinetics of this process vary with cell type and culture conditions (Massagué, 2000).”
The Blood-Testis Barrier and Its Implications for Male Contraception (2012, background): “TGF- exerts its biological effects by first binding to the TGF- type II receptor (T RII), which then recruits the type I receptor (T RI), forming a TGF- /T RII/T RI complex, except that TGF- 2 binds to the two receptors almost at the same time with the assistance of the type III receptor, -glycan (M”
Recent advances in craniofacial morphogenesis (2006, background): “In general, TGFsignaling specificity in regulating downstream target gene expression is determined by the interaction with other factors (such as BMP, Wnt, FGF, and so on) in a temporal- and spatial-specific manner (Massague, 2000).”
TGF-β and epithelial-to-mesenchymal transitions (2005, background): “In response to TGF-b-ligand binding, TGF-b receptors type I and II form tight complexes leading to phosphorylation of Smad2 and Smad3, members of the Smad protein family (Massague, 2000).”
Signaling mechanisms of the epithelial-mesenchymal transition (2014, background): “Both ATF-2 (activating transcription factor-2, a substrate of p38 MAPK pathways) and c-Jun (a substrate of JNK) are capable of interacting with SMADs (80, 81, 89).”