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Mechanism of action and in vivo role of platelet-derived growth factor.
Structural and functional properties of PDGF and PDGF receptors, the mechanism whereby PDGF exerts its cellular effects, and the role ofPDGF in normal and diseased tissues are discussed.
Different signal transduction properties of KDR and Flt1, two receptors for vascular endothelial growth factor.
TGF-β signalling from cell membrane to nucleus through SMAD proteins
Inhibitory SMADs have been identified that block the activation of these pathway-restricted SMADS that direct transcription to effect the cell's response to TGF-β.
High interstitial fluid pressure — an obstacle in cancer therapy
Lowering the tumour IFP with specific signal-transduction antagonists might be a useful approach to improving anticancer drug efficacy.
TGF-beta signalling from cell membrane to nucleus through SMAD proteins.
Inhibitory SMADs have been identified that block the activation of these pathway-restricted SMADS that direct transcription to effect the cell's response to TGF-beta.
Co‐localization of NG2 proteoglycan and PDGF α‐receptor on O2A progenitor cells in the developing rat brain
- A. Nishiyama, X.‐H. Lin, N. Giese, C. Heldin, W. Stallcup
- BiologyJournal of neuroscience research
- 1 February 1996
Mapping experiments indicate that NG2‐positive, PDGF α‐receptor positive O2A cells are abundant throughout the developing central nervous system in both white and gray matter.
Identification of Smad7, a TGFbeta-inducible antagonist of TGF-beta signalling.
The identification of Smad7 is reported, which is related to Smad6 and associates stably with the TGF-beta receptor complex, but is not phosphorylated upon TGF -beta stimulation.
Identification of Smad7, a TGFβ-inducible antagonist of TGF-β signalling
The identification of Smad7 is reported, which is related to Smad6 and associates stably with the TGF-β receptor complex, but is not phosphorylated upon T GF-β stimulation.
Signal transduction via platelet-derived growth factor receptors.
TGF‐β receptor‐mediated signalling through Smad2, Smad3 and Smad4
It is shown that Smad2 and Smad3 interacted with the kinase‐deficient TGF‐β type I receptor (TβR)‐I after it was phosphorylated by TβR‐II kinase, which suggests that T GF‐β induces heteromeric complexes of Smad 2, 3 and 4, and their concomitant translocation to the nucleus, which is required for efficient TGF-β signal transduction.